Entry
stringlengths 6
10
| Entry Name
stringlengths 5
11
| Sequence
stringlengths 2
35.2k
| EC number
stringlengths 7
118
⌀ | Cofactor
stringlengths 38
1.77k
⌀ | Gene Ontology (biological process)
stringlengths 18
11.3k
⌀ | Gene Ontology (cellular component)
stringlengths 17
1.75k
⌀ | Gene Ontology (molecular function)
stringlengths 24
2.09k
⌀ | Pfam
stringlengths 8
232
⌀ | Gene3D
stringlengths 10
250
⌀ | Protein families
stringlengths 9
237
⌀ | Post-translational modification
stringlengths 16
8.52k
⌀ | Subcellular location [CC]
stringlengths 29
6.18k
⌀ | Catalytic activity
stringlengths 64
35.7k
⌀ | Kinetics
stringlengths 69
11.7k
⌀ | Pathway
stringlengths 27
908
⌀ | pH dependence
stringlengths 64
955
⌀ | Temperature dependence
stringlengths 70
1.16k
⌀ | Function [CC]
stringlengths 17
15.3k
⌀ | Organism
stringlengths 8
196
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|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
P02639
|
S10A1_BOVIN
|
MGSELETAMETLINVFHAHSGKEGDKYKLSKKELKELLQTELSGFLDAQKDADAVDKVMKELDENGDGEVDFQEYVVLVAALTVACNNFFWENS
| null | null |
positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of cell population proliferation [GO:0008284]; regulation of heart contraction [GO:0008016]
|
cytoplasm [GO:0005737]; extracellular space [GO:0005615]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; sarcoplasmic reticulum [GO:0016529]
|
calcium ion binding [GO:0005509]; calcium-dependent protein binding [GO:0048306]; RAGE receptor binding [GO:0050786]; S100 protein binding [GO:0044548]
|
PF00036;PF01023;
|
1.10.238.10;
|
S-100 family
|
PTM: Glutathionylated; glutathionylation increases affinity to calcium about 10-fold. {ECO:0000250|UniProtKB:P23297}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P23297}. Sarcoplasmic reticulum {ECO:0000250|UniProtKB:P23297}. Mitochondrion {ECO:0000250|UniProtKB:P56565}.
| null | null | null | null | null |
FUNCTION: Small calcium binding protein that plays important roles in several biological processes such as Ca(2+) homeostasis, chondrocyte biology and cardiomyocyte regulation. In response to an increase in intracellular Ca(2+) levels, binds calcium which triggers conformational changes. These changes allow interactions with specific target proteins and modulate their activity. Regulates a network in cardiomyocytes controlling sarcoplasmic reticulum Ca(2+) cycling and mitochondrial function through interaction with the ryanodine receptors RYR1 and RYR2, sarcoplasmic reticulum Ca(2+)-ATPase/ATP2A2 and mitochondrial F1-ATPase. Facilitates diastolic Ca(2+) dissociation and myofilament mechanics in order to improve relaxation during diastole. {ECO:0000250|UniProtKB:P23297}.
|
Bos taurus (Bovine)
|
P02640
|
VILI_CHICK
|
MVELSKKVTGKLDKTTPGIQIWRIENMEMVPVPTKSYGNFYEGDCYVLLSTRKTGSGFSYNIHYWLGKNSSQDEQGAAAIYTTQMDEYLGSVAVQHREVQGHESETFRAYFKQGLIYKQGGVASGMKHVETNTYNVQRLLHVKGKKNVVAAEVEMSWKSFNLGDVFLLDLGQLIIQWNGPESNRAERLRAMTLAKDIRDRERAGRAKVGVVEGENEAASPELMQALTHVLGEKKNIKAATPDEQVHQALNSALKLYHVSDASGNLVIQEVAIRPLTQDMLQHEDCYILDQAGLKIFVWKGKNANKEEKQQAMSRALGFIKAKNYLASTSVETENDGSESAVFRQLFQKWTVPNQTSGLGKTHTVGKVAKVEQVKFDATTMHVKPEVAAQQKMVDDGSGEAEVWRVENQELVPVEKRWLGHFYGGDCYLVLYTYYVGPKVNRIIYIWQGRHASTDELAASAYQAVFLDQKYNNEPVQVRVTMGKEPAHLMAIFKGKMVVYENGSSRAGGTEPASSTRLFHVHGTNEYNTKAFEVPVRAASLNSNDVFVLKTPSSCYLWYGKGCSGDEREMGKMVADIISKTEKPVVAEGQEPPEFWVALGGKTSYANSKRLQEENPSVPPRLFECSNKTGRFLATEIVDFTQDDLDENDVYLLDTWDQIFFWIGKGANESEKEAAAETAQEYLRSHPGSRDLDTPIIVVKQGFEPPTFTGWFMAWDPLCWSDRKSYDELKAELGDNASIGQLVSGLTSKNEVFTATTTLVPTKLETFPLDVLVNTAAEDLPRGVDPSRKENHLSDEDFKAVFGMTRSAFANLPLWKQQNLKKEKGLF
| null | null |
actin filament capping [GO:0051693]; actin filament depolymerization [GO:0030042]; actin filament polymerization [GO:0030041]; actin filament severing [GO:0051014]; actin polymerization or depolymerization [GO:0008154]; barbed-end actin filament capping [GO:0051016]; cellular response to epidermal growth factor stimulus [GO:0071364]; cellular response to hepatocyte growth factor stimulus [GO:0035729]; cytoplasmic actin-based contraction involved in cell motility [GO:0060327]; epidermal growth factor receptor signaling pathway [GO:0007173]; positive regulation of actin filament bundle assembly [GO:0032233]; positive regulation of cell migration [GO:0030335]; positive regulation of epithelial cell migration [GO:0010634]; regulation of actin nucleation [GO:0051125]; regulation of cell shape [GO:0008360]; regulation of lamellipodium morphogenesis [GO:2000392]; regulation of wound healing [GO:0061041]; response to bacterium [GO:0009617]
|
actin cytoskeleton [GO:0015629]; actin filament bundle [GO:0032432]; cytoplasm [GO:0005737]; filopodium [GO:0030175]; filopodium tip [GO:0032433]; lamellipodium [GO:0030027]; microvillus [GO:0005902]; ruffle [GO:0001726]
|
actin filament binding [GO:0051015]; calcium ion binding [GO:0005509]; cysteine-type endopeptidase inhibitor activity involved in apoptotic process [GO:0043027]; lysophosphatidic acid binding [GO:0035727]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]; protein homodimerization activity [GO:0042803]
|
PF00626;PF02209;
|
3.40.20.10;1.10.950.10;
|
Villin/gelsolin family
|
PTM: Phosphorylated on tyrosine residues. The unphosphorylated form increases the initial rate of actin-nucleating activity, whereas the tyrosine-phosphorylated form inhibits actin-nucleating activity, enhances actin-bundling activity and enhances actin-severing activity by reducing high Ca(2+) requirements. The tyrosine-phosphorylated form does not regulate actin-capping activity. Tyrosine phosphorylation is essential for cell migration: tyrosine phosphorylation sites in the N-terminus half regulate actin reorganization and cell morphology, whereas tyrosine phosphorylation sites in the C-terminus half regulate cell migration. Tyrosine phosphorylation is induced by epidermal growth factor (EGF) and stimulates cell migration (By similarity). {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:3793760}. Cell projection, microvillus {ECO:0000269|PubMed:3793760}. Cell projection, lamellipodium {ECO:0000250}. Cell projection, ruffle {ECO:0000250}. Cell projection, filopodium tip {ECO:0000250}. Cell projection, filopodium {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Epithelial cell-specific Ca(2+)-regulated actin-modifying protein that modulates the reorganization of microvillar actin filaments. Plays a role in the actin nucleation, actin filament bundle assembly, actin filament capping and severing. Binds phosphatidylinositol 4,5-bisphosphate (PIP2) and lysophosphatidic acid (LPA); binds LPA with higher affinity than PIP2. Binding to LPA increases its phosphorylation by SRC and inhibits all actin-modifying activities. Binding to PIP2 inhibits actin-capping and -severing activities but enhances actin-bundling activity. Regulates the intestinal epithelial cell morphology, cell invasion, cell migration and apoptosis. Protects against apoptosis induced by dextran sodium sulfate (DSS) in the gastrointestinal epithelium. Appears to regulate cell death by maintaining mitochondrial integrity. Enhances hepatocyte growth factor (HGF)-induced epithelial cell motility, chemotaxis and wound repair (By similarity). Its actin-bundling activity is inhibited by tropomyosin. {ECO:0000250, ECO:0000269|PubMed:1618806, ECO:0000269|PubMed:3793760}.
|
Gallus gallus (Chicken)
|
P02641
|
TNNT3_RABIT
|
MSDEEVEHVEEQYEEEEEAQEEAPSPAEVHEPAPEVHVPEEVHEDALEDMREEEEEEEKPRPKLTAPKIPEGEKVDFDDIQKKRQNKDLMELQALIDSHFEARKKEEEELVALKERIEKRRAERAEQQRIRAEKERERQNRLAEEKARREEEDAKRRAEEDLKKKKALSSMGANYSSYLAKADQKRGKKQTAREMKKKILAERRKPLNIDHLSDEKLRDKAKELWDTLYQLETDKFEFGEKLKRQKYDIMNVRARVEMLAKFSKKAGTTAKGKVGGRWK
| null | null |
regulation of muscle contraction [GO:0006937]; sarcomere organization [GO:0045214]; skeletal muscle contraction [GO:0003009]
|
troponin complex [GO:0005861]
|
tropomyosin binding [GO:0005523]; troponin C binding [GO:0030172]; troponin I binding [GO:0031013]
|
PF00992;
|
1.20.5.350;
|
Troponin T family
| null | null | null | null | null | null | null |
FUNCTION: Troponin T is the tropomyosin-binding subunit of troponin, the thin filament regulatory complex which confers calcium-sensitivity to striated muscle actomyosin ATPase activity.
|
Oryctolagus cuniculus (Rabbit)
|
P02647
|
APOA1_HUMAN
|
MKAAVLTLAVLFLTGSQARHFWQQDEPPQSPWDRVKDLATVYVDVLKDSGRDYVSQFEGSALGKQLNLKLLDNWDSVTSTFSKLREQLGPVTQEFWDNLEKETEGLRQEMSKDLEEVKAKVQPYLDDFQKKWQEEMELYRQKVEPLRAELQEGARQKLHELQEKLSPLGEEMRDRARAHVDALRTHLAPYSDELRQRLAARLEALKENGGARLAEYHAKATEHLSTLSEKAKPALEDLRQGLLPVLESFKVSFLSALEEYTKKLNTQ
| null | null |
acylglycerol homeostasis [GO:0055090]; adrenal gland development [GO:0030325]; blood vessel endothelial cell migration [GO:0043534]; cholesterol biosynthetic process [GO:0006695]; cholesterol efflux [GO:0033344]; cholesterol homeostasis [GO:0042632]; cholesterol import [GO:0070508]; cholesterol metabolic process [GO:0008203]; cholesterol transport [GO:0030301]; endothelial cell proliferation [GO:0001935]; G protein-coupled receptor signaling pathway [GO:0007186]; glucocorticoid metabolic process [GO:0008211]; high-density lipoprotein particle assembly [GO:0034380]; high-density lipoprotein particle clearance [GO:0034384]; high-density lipoprotein particle remodeling [GO:0034375]; integrin-mediated signaling pathway [GO:0007229]; lipid storage [GO:0019915]; lipoprotein biosynthetic process [GO:0042158]; negative chemotaxis [GO:0050919]; negative regulation of cell adhesion molecule production [GO:0060354]; negative regulation of cytokine production involved in immune response [GO:0002719]; negative regulation of heterotypic cell-cell adhesion [GO:0034115]; negative regulation of inflammatory response [GO:0050728]; negative regulation of interleukin-1 beta production [GO:0032691]; negative regulation of response to cytokine stimulus [GO:0060761]; negative regulation of tumor necrosis factor-mediated signaling pathway [GO:0010804]; negative regulation of very-low-density lipoprotein particle remodeling [GO:0010903]; peptidyl-methionine modification [GO:0018206]; phosphatidylcholine biosynthetic process [GO:0006656]; phospholipid efflux [GO:0033700]; phospholipid homeostasis [GO:0055091]; positive regulation of cholesterol efflux [GO:0010875]; positive regulation of cholesterol metabolic process [GO:0090205]; positive regulation of CoA-transferase activity [GO:1905920]; positive regulation of hydrolase activity [GO:0051345]; positive regulation of phagocytosis [GO:0050766]; positive regulation of phospholipid efflux [GO:1902995]; positive regulation of Rho protein signal transduction [GO:0035025]; positive regulation of stress fiber assembly [GO:0051496]; positive regulation of substrate adhesion-dependent cell spreading [GO:1900026]; protein oxidation [GO:0018158]; protein stabilization [GO:0050821]; regulation of Cdc42 protein signal transduction [GO:0032489]; regulation of intestinal cholesterol absorption [GO:0030300]; regulation of protein phosphorylation [GO:0001932]; reverse cholesterol transport [GO:0043691]; triglyceride homeostasis [GO:0070328]; vitamin transport [GO:0051180]
|
blood microparticle [GO:0072562]; chylomicron [GO:0042627]; collagen-containing extracellular matrix [GO:0062023]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; early endosome [GO:0005769]; endocytic vesicle [GO:0030139]; endocytic vesicle lumen [GO:0071682]; endoplasmic reticulum lumen [GO:0005788]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; extracellular vesicle [GO:1903561]; high-density lipoprotein particle [GO:0034364]; low-density lipoprotein particle [GO:0034362]; plasma membrane [GO:0005886]; secretory granule lumen [GO:0034774]; spherical high-density lipoprotein particle [GO:0034366]; very-low-density lipoprotein particle [GO:0034361]
|
amyloid-beta binding [GO:0001540]; apolipoprotein A-I receptor binding [GO:0034191]; apolipoprotein receptor binding [GO:0034190]; chemorepellent activity [GO:0045499]; cholesterol binding [GO:0015485]; cholesterol transfer activity [GO:0120020]; enzyme binding [GO:0019899]; heat shock protein binding [GO:0031072]; high-density lipoprotein particle binding [GO:0008035]; high-density lipoprotein particle receptor binding [GO:0070653]; identical protein binding [GO:0042802]; phosphatidylcholine-sterol O-acyltransferase activator activity [GO:0060228]; phospholipid binding [GO:0005543]; protein homodimerization activity [GO:0042803]; signaling receptor binding [GO:0005102]
|
PF01442;
|
1.20.5.20;6.10.140.380;1.20.120.20;
|
Apolipoprotein A1/A4/E family
|
PTM: Glycosylated. {ECO:0000250}.; PTM: Palmitoylated. {ECO:0000269|PubMed:3005308}.; PTM: Phosphorylation sites are present in the extracellular medium.
|
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Participates in the reverse transport of cholesterol from tissues to the liver for excretion by promoting cholesterol efflux from tissues and by acting as a cofactor for the lecithin cholesterol acyltransferase (LCAT). As part of the SPAP complex, activates spermatozoa motility. {ECO:0000269|PubMed:1909888}.
|
Homo sapiens (Human)
|
P02648
|
APOA1_CANLF
|
MKAALLTLAVLFLTGSQARHFWQQDEPQSPWDRVKDLATVYVDAVKDSGRDYVAQFEASALGKQLNLKLLDNWDSLSSTVTKLREQIGPVTQEFWDNLEKETEVLRQEMSKDLEEVKQKVQPYLDDFQKKWQEEVELYRQKVAPLGSELREGARQKLQELQEKLSPLAEELRDRARTHVDALRAQLAPYSDDLRERLAARLEALKEGGGASLAEYHARASEQLSALGEKARPALEDLRQGLLPVLESFKVSLLAAIDEATKKLNAQ
| null | null |
acylglycerol homeostasis [GO:0055090]; cholesterol efflux [GO:0033344]; cholesterol metabolic process [GO:0008203]; lipoprotein metabolic process [GO:0042157]; peptidyl-methionine modification [GO:0018206]; phosphatidylcholine metabolic process [GO:0046470]; phospholipid efflux [GO:0033700]; positive regulation of cholesterol efflux [GO:0010875]; positive regulation of phagocytosis [GO:0050766]; positive regulation of phospholipid efflux [GO:1902995]; protein oxidation [GO:0018158]; protein stabilization [GO:0050821]; regulation of intestinal cholesterol absorption [GO:0030300]
|
chylomicron [GO:0042627]; extracellular vesicle [GO:1903561]; high-density lipoprotein particle [GO:0034364]; low-density lipoprotein particle [GO:0034362]; very-low-density lipoprotein particle [GO:0034361]
|
cholesterol transfer activity [GO:0120020]; high-density lipoprotein particle receptor binding [GO:0070653]; phosphatidylcholine-sterol O-acyltransferase activator activity [GO:0060228]; phospholipid binding [GO:0005543]; protein homodimerization activity [GO:0042803]
|
PF01442;
|
1.20.5.20;6.10.140.380;1.20.120.20;
|
Apolipoprotein A1/A4/E family
|
PTM: Palmitoylated. {ECO:0000269|PubMed:20483223}.; PTM: Glycosylated. {ECO:0000269|PubMed:20483223}.; PTM: Phosphorylation sites are present in the extracellular medium. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Participates in the reverse transport of cholesterol from tissues to the liver for excretion by promoting cholesterol efflux from tissues and by acting as a cofactor for the lecithin cholesterol acyltransferase (LCAT). As part of the SPAP complex, activates spermatozoa motility.
|
Canis lupus familiaris (Dog) (Canis familiaris)
|
P02649
|
APOE_HUMAN
|
MKVLWAALLVTFLAGCQAKVEQAVETEPEPELRQQTEWQSGQRWELALGRFWDYLRWVQTLSEQVQEELLSSQVTQELRALMDETMKELKAYKSELEEQLTPVAEETRARLSKELQAAQARLGADMEDVCGRLVQYRGEVQAMLGQSTEELRVRLASHLRKLRKRLLRDADDLQKRLAVYQAGAREGAERGLSAIRERLGPLVEQGRVRAATVGSLAGQPLQERAQAWGERLRARMEEMGSRTRDRLDEVKEQVAEVRAKLEEQAQQIRLQAEAFQARLKSWFEPLVEDMQRQWAGLVEKVQAAVGTSAAPVPSDNH
| null | null |
acylglycerol homeostasis [GO:0055090]; AMPA glutamate receptor clustering [GO:0097113]; amyloid precursor protein metabolic process [GO:0042982]; artery morphogenesis [GO:0048844]; cholesterol catabolic process [GO:0006707]; cholesterol efflux [GO:0033344]; cholesterol homeostasis [GO:0042632]; cholesterol metabolic process [GO:0008203]; chylomicron remnant clearance [GO:0034382]; cytoskeleton organization [GO:0007010]; fatty acid homeostasis [GO:0055089]; G protein-coupled receptor signaling pathway [GO:0007186]; gene expression [GO:0010467]; high-density lipoprotein particle assembly [GO:0034380]; high-density lipoprotein particle clearance [GO:0034384]; high-density lipoprotein particle remodeling [GO:0034375]; intermediate-density lipoprotein particle clearance [GO:0071831]; intracellular calcium ion homeostasis [GO:0006874]; intracellular transport [GO:0046907]; lipid transport involved in lipid storage [GO:0010877]; lipoprotein biosynthetic process [GO:0042158]; lipoprotein catabolic process [GO:0042159]; locomotory exploration behavior [GO:0035641]; long-chain fatty acid transport [GO:0015909]; long-term memory [GO:0007616]; low-density lipoprotein particle remodeling [GO:0034374]; maintenance of location in cell [GO:0051651]; melanosome organization [GO:0032438]; negative regulation of amyloid fibril formation [GO:1905907]; negative regulation of amyloid-beta formation [GO:1902430]; negative regulation of blood coagulation [GO:0030195]; negative regulation of blood vessel endothelial cell migration [GO:0043537]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of cholesterol biosynthetic process [GO:0045541]; negative regulation of endothelial cell migration [GO:0010596]; negative regulation of endothelial cell proliferation [GO:0001937]; negative regulation of gene expression [GO:0010629]; negative regulation of inflammatory response [GO:0050728]; negative regulation of long-term synaptic potentiation [GO:1900272]; negative regulation of MAP kinase activity [GO:0043407]; negative regulation of neuron apoptotic process [GO:0043524]; negative regulation of neuron projection development [GO:0010977]; negative regulation of platelet activation [GO:0010544]; negative regulation of protein metabolic process [GO:0051248]; negative regulation of protein secretion [GO:0050709]; negative regulation of smooth muscle cell proliferation [GO:0048662]; negative regulation of triglyceride metabolic process [GO:0090209]; neuron projection development [GO:0031175]; nitric oxide-cGMP-mediated signaling pathway [GO:0038060]; NMDA glutamate receptor clustering [GO:0097114]; phospholipid efflux [GO:0033700]; positive regulation by host of viral process [GO:0044794]; positive regulation of amyloid fibril formation [GO:1905908]; positive regulation of amyloid-beta clearance [GO:1900223]; positive regulation of cholesterol efflux [GO:0010875]; positive regulation of cholesterol metabolic process [GO:0090205]; positive regulation of CoA-transferase activity [GO:1905920]; positive regulation of dendritic spine development [GO:0060999]; positive regulation of dendritic spine maintenance [GO:1902952]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of endocytosis [GO:0045807]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of heparan sulfate proteoglycan binding [GO:1905860]; positive regulation of lipid biosynthetic process [GO:0046889]; positive regulation of lipid transport across blood-brain barrier [GO:1903002]; positive regulation of low-density lipoprotein particle receptor catabolic process [GO:0032805]; positive regulation of membrane protein ectodomain proteolysis [GO:0051044]; positive regulation of neuron projection development [GO:0010976]; positive regulation of nitric oxide biosynthetic process [GO:0045429]; positive regulation of phospholipid efflux [GO:1902995]; protein import [GO:0017038]; receptor-mediated endocytosis [GO:0006898]; regulation of amyloid fibril formation [GO:1905906]; regulation of amyloid precursor protein catabolic process [GO:1902991]; regulation of amyloid-beta clearance [GO:1900221]; regulation of axon extension [GO:0030516]; regulation of behavioral fear response [GO:2000822]; regulation of Cdc42 protein signal transduction [GO:0032489]; regulation of cellular response to very-low-density lipoprotein particle stimulus [GO:1905890]; regulation of cholesterol metabolic process [GO:0090181]; regulation of innate immune response [GO:0045088]; regulation of neuronal synaptic plasticity [GO:0048168]; regulation of proteasomal protein catabolic process [GO:0061136]; regulation of protein metabolic process [GO:0051246]; regulation of protein-containing complex assembly [GO:0043254]; response to caloric restriction [GO:0061771]; response to dietary excess [GO:0002021]; response to reactive oxygen species [GO:0000302]; reverse cholesterol transport [GO:0043691]; synaptic transmission, cholinergic [GO:0007271]; triglyceride homeostasis [GO:0070328]; triglyceride metabolic process [GO:0006641]; triglyceride-rich lipoprotein particle clearance [GO:0071830]; vasodilation [GO:0042311]; very-low-density lipoprotein particle clearance [GO:0034447]; very-low-density lipoprotein particle remodeling [GO:0034372]; virion assembly [GO:0019068]
|
blood microparticle [GO:0072562]; chylomicron [GO:0042627]; chylomicron remnant [GO:0034360]; clathrin-coated endocytic vesicle membrane [GO:0030669]; collagen-containing extracellular matrix [GO:0062023]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; discoidal high-density lipoprotein particle [GO:0034365]; early endosome [GO:0005769]; endocytic vesicle lumen [GO:0071682]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum lumen [GO:0005788]; extracellular exosome [GO:0070062]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; extracellular vesicle [GO:1903561]; glutamatergic synapse [GO:0098978]; Golgi apparatus [GO:0005794]; high-density lipoprotein particle [GO:0034364]; intermediate-density lipoprotein particle [GO:0034363]; lipoprotein particle [GO:1990777]; low-density lipoprotein particle [GO:0034362]; melanosome [GO:0042470]; membrane [GO:0016020]; multivesicular body, internal vesicle [GO:0097487]; neuronal cell body [GO:0043025]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; synaptic cleft [GO:0043083]; very-low-density lipoprotein particle [GO:0034361]
|
amyloid-beta binding [GO:0001540]; antioxidant activity [GO:0016209]; cholesterol transfer activity [GO:0120020]; enzyme binding [GO:0019899]; heparan sulfate proteoglycan binding [GO:0043395]; heparin binding [GO:0008201]; identical protein binding [GO:0042802]; lipid binding [GO:0008289]; lipid transporter activity [GO:0005319]; lipoprotein particle binding [GO:0071813]; low-density lipoprotein particle receptor binding [GO:0050750]; metal chelating activity [GO:0046911]; phosphatidylcholine-sterol O-acyltransferase activator activity [GO:0060228]; phospholipid binding [GO:0005543]; protein dimerization activity [GO:0046983]; protein homodimerization activity [GO:0042803]; protein-containing complex binding [GO:0044877]; signaling receptor binding [GO:0005102]; structural molecule activity [GO:0005198]; tau protein binding [GO:0048156]; very-low-density lipoprotein particle receptor binding [GO:0070326]
|
PF01442;
|
1.20.120.20;
|
Apolipoprotein A1/A4/E family
|
PTM: APOE exists as multiple glycosylated and sialylated glycoforms within cells and in plasma (PubMed:29516132). The extent of glycosylation and sialylation are tissue and context specific (PubMed:29516132). Plasma APOE undergoes desialylation and is less glycosylated and sialylated than the cellular form (PubMed:19838169, PubMed:20511397, PubMed:23234360, PubMed:2498325). Glycosylation is not required for proper expression and secretion (PubMed:2498325). O-glycosylated with core 1 or possibly core 8 glycans. Thr-307 and Ser-314 are minor glycosylation sites compared to Ser-308 (PubMed:19838169, PubMed:23234360). {ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:20511397, ECO:0000269|PubMed:23234360, ECO:0000269|PubMed:2498325, ECO:0000303|PubMed:29516132}.; PTM: Glycated in plasma VLDL of normal subjects, and of hyperglycemic diabetic patients at a higher level (2-3 fold). {ECO:0000269|PubMed:10452964}.; PTM: Phosphorylated by FAM20C in the extracellular medium. {ECO:0000269|PubMed:26091039}.; PTM: Undergoes C-terminal proteolytic processing in neurons. C-terminally truncated APOE has a tendency to form neurotoxic intracellular neurofibrillary tangle-like inclusions in neurons. {ECO:0000269|PubMed:11447277}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2498325, ECO:0000269|PubMed:30333625}. Secreted, extracellular space {ECO:0000269|PubMed:8340399}. Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:9488694}. Extracellular vesicle {ECO:0000269|PubMed:26387950}. Endosome, multivesicular body {ECO:0000269|PubMed:26387950}. Note=In the plasma, APOE is associated with chylomicrons, chylomicrons remnants, VLDL, LDL and HDL lipoproteins (PubMed:1911868, PubMed:8340399). Lipid poor oligomeric APOE is associated with the extracellular matrix in a calcium- and heparan-sulfate proteoglycans-dependent manner (PubMed:9488694). Lipidation induces the release from the extracellular matrix (PubMed:9488694). Colocalizes with CD63 and PMEL at exosomes and in intraluminal vesicles within multivesicular endosomes. {ECO:0000269|PubMed:1911868, ECO:0000269|PubMed:26387950, ECO:0000269|PubMed:8340399, ECO:0000269|PubMed:9488694}.
| null | null | null | null | null |
FUNCTION: APOE is an apolipoprotein, a protein associating with lipid particles, that mainly functions in lipoprotein-mediated lipid transport between organs via the plasma and interstitial fluids (PubMed:14754908, PubMed:1911868, PubMed:6860692). APOE is a core component of plasma lipoproteins and is involved in their production, conversion and clearance (PubMed:14754908, PubMed:1911868, PubMed:1917954, PubMed:23620513, PubMed:2762297, PubMed:6860692, PubMed:9395455). Apolipoproteins are amphipathic molecules that interact both with lipids of the lipoprotein particle core and the aqueous environment of the plasma (PubMed:2762297, PubMed:6860692, PubMed:9395455). As such, APOE associates with chylomicrons, chylomicron remnants, very low density lipoproteins (VLDL) and intermediate density lipoproteins (IDL) but shows a preferential binding to high-density lipoproteins (HDL) (PubMed:1911868, PubMed:6860692). It also binds a wide range of cellular receptors including the LDL receptor/LDLR, the LDL receptor-related proteins LRP1, LRP2 and LRP8 and the very low-density lipoprotein receptor/VLDLR that mediate the cellular uptake of the APOE-containing lipoprotein particles (PubMed:12950167, PubMed:1530612, PubMed:1917954, PubMed:20030366, PubMed:20303980, PubMed:2063194, PubMed:2762297, PubMed:7635945, PubMed:7768901, PubMed:8756331, PubMed:8939961). Finally, APOE has also a heparin-binding activity and binds heparan-sulfate proteoglycans on the surface of cells, a property that supports the capture and the receptor-mediated uptake of APOE-containing lipoproteins by cells (PubMed:23676495, PubMed:7635945, PubMed:9395455, PubMed:9488694). A main function of APOE is to mediate lipoprotein clearance through the uptake of chylomicrons, VLDLs, and HDLs by hepatocytes (PubMed:1911868, PubMed:1917954, PubMed:23676495, PubMed:29516132, PubMed:9395455). APOE is also involved in the biosynthesis by the liver of VLDLs as well as their uptake by peripheral tissues ensuring the delivery of triglycerides and energy storage in muscle, heart and adipose tissues (PubMed:2762297, PubMed:29516132). By participating in the lipoprotein-mediated distribution of lipids among tissues, APOE plays a critical role in plasma and tissues lipid homeostasis (PubMed:1917954, PubMed:2762297, PubMed:29516132). APOE is also involved in two steps of reverse cholesterol transport, the HDLs-mediated transport of cholesterol from peripheral tissues to the liver, and thereby plays an important role in cholesterol homeostasis (PubMed:14754908, PubMed:23620513, PubMed:9395455). First, it is functionally associated with ABCA1 in the biogenesis of HDLs in tissues (PubMed:14754908, PubMed:23620513). Second, it is enriched in circulating HDLs and mediates their uptake by hepatocytes (PubMed:9395455). APOE also plays an important role in lipid transport in the central nervous system, regulating neuron survival and sprouting (PubMed:25173806, PubMed:8939961). APOE is also involved in innate and adaptive immune responses, controlling for instance the survival of myeloid-derived suppressor cells (By similarity). Binds to the immune cell receptor LILRB4 (PubMed:30333625). APOE may also play a role in transcription regulation through a receptor-dependent and cholesterol-independent mechanism, that activates MAP3K12 and a non-canonical MAPK signal transduction pathway that results in enhanced AP-1-mediated transcription of APP (PubMed:28111074). {ECO:0000250|UniProtKB:P08226, ECO:0000269|PubMed:12950167, ECO:0000269|PubMed:14754908, ECO:0000269|PubMed:1530612, ECO:0000269|PubMed:1911868, ECO:0000269|PubMed:1917954, ECO:0000269|PubMed:20030366, ECO:0000269|PubMed:20303980, ECO:0000269|PubMed:2063194, ECO:0000269|PubMed:23620513, ECO:0000269|PubMed:23676495, ECO:0000269|PubMed:2762297, ECO:0000269|PubMed:28111074, ECO:0000269|PubMed:30333625, ECO:0000269|PubMed:6860692, ECO:0000269|PubMed:7635945, ECO:0000269|PubMed:7768901, ECO:0000269|PubMed:8756331, ECO:0000269|PubMed:8939961, ECO:0000269|PubMed:9395455, ECO:0000269|PubMed:9488694, ECO:0000303|PubMed:25173806, ECO:0000303|PubMed:29516132}.; FUNCTION: (Microbial infection) Through its interaction with HCV envelope glycoprotein E2, participates in the attachment of HCV to HSPGs and other receptors (LDLr, VLDLr, and SR-B1) on the cell surface and to the assembly, maturation and infectivity of HCV viral particles (PubMed:25122793, PubMed:29695434). This interaction is probably promoted via the up-regulation of cellular autophagy by the virus (PubMed:29695434). {ECO:0000269|PubMed:25122793, ECO:0000269|PubMed:29695434}.
|
Homo sapiens (Human)
|
P02650
|
APOE_RAT
|
MKALWALLLVPLLTGCLAEGELEVTDQLPGQSDQPWEQALNRFWDYLRWVQTLSDQVQEELQSSQVTQELTVLMEDTMTEVKAYKKELEEQLGPVAEETRARLAKEVQAAQARLGADMEDLRNRLGQYRNEVNTMLGQSTEELRSRLSTHLRKMRKRLMRDADDLQKRLAVYKAGAQEGAERGVSAIRERLGPLVEQGRQRTANLGAGAAQPLRDRAQALSDRIRGRLEEVGNQARDRLEEVREQMEEVRSKMEEQTQQIRLQAEIFQARIKGWFEPLVEDMQRQWANLMEKIQASVATNSIASTTVPLENQ
| null | null |
acylglycerol homeostasis [GO:0055090]; AMPA glutamate receptor clustering [GO:0097113]; amyloid precursor protein metabolic process [GO:0042982]; artery morphogenesis [GO:0048844]; cellular response to cholesterol [GO:0071397]; cellular response to ethanol [GO:0071361]; cellular response to growth factor stimulus [GO:0071363]; cellular response to interleukin-1 [GO:0071347]; cGMP-mediated signaling [GO:0019934]; cholesterol catabolic process [GO:0006707]; cholesterol efflux [GO:0033344]; cholesterol homeostasis [GO:0042632]; cholesterol metabolic process [GO:0008203]; chylomicron remnant clearance [GO:0034382]; circulatory system development [GO:0072359]; fatty acid homeostasis [GO:0055089]; G protein-coupled receptor signaling pathway [GO:0007186]; gene expression [GO:0010467]; high-density lipoprotein particle assembly [GO:0034380]; high-density lipoprotein particle clearance [GO:0034384]; high-density lipoprotein particle remodeling [GO:0034375]; intermediate-density lipoprotein particle clearance [GO:0071831]; intracellular calcium ion homeostasis [GO:0006874]; lipid homeostasis [GO:0055088]; lipid metabolic process [GO:0006629]; lipid transport [GO:0006869]; lipid transport involved in lipid storage [GO:0010877]; lipoprotein biosynthetic process [GO:0042158]; lipoprotein catabolic process [GO:0042159]; lipoprotein metabolic process [GO:0042157]; locomotory exploration behavior [GO:0035641]; long-chain fatty acid transport [GO:0015909]; long-term memory [GO:0007616]; low-density lipoprotein particle remodeling [GO:0034374]; maintenance of location in cell [GO:0051651]; melanosome organization [GO:0032438]; negative regulation of amyloid fibril formation [GO:1905907]; negative regulation of amyloid-beta formation [GO:1902430]; negative regulation of blood coagulation [GO:0030195]; negative regulation of blood vessel endothelial cell migration [GO:0043537]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of cholesterol biosynthetic process [GO:0045541]; negative regulation of endothelial cell migration [GO:0010596]; negative regulation of endothelial cell proliferation [GO:0001937]; negative regulation of gene expression [GO:0010629]; negative regulation of inflammatory response [GO:0050728]; negative regulation of long-term synaptic potentiation [GO:1900272]; negative regulation of neuron apoptotic process [GO:0043524]; negative regulation of neuron projection development [GO:0010977]; negative regulation of platelet activation [GO:0010544]; negative regulation of protein metabolic process [GO:0051248]; negative regulation of protein secretion [GO:0050709]; negative regulation of smooth muscle cell proliferation [GO:0048662]; negative regulation of triglyceride metabolic process [GO:0090209]; neuron projection development [GO:0031175]; neuron projection regeneration [GO:0031102]; nitric oxide mediated signal transduction [GO:0007263]; NMDA glutamate receptor clustering [GO:0097114]; oligodendrocyte differentiation [GO:0048709]; peripheral nervous system axon regeneration [GO:0014012]; phospholipid efflux [GO:0033700]; positive regulation by host of viral process [GO:0044794]; positive regulation of amyloid-beta clearance [GO:1900223]; positive regulation of axon extension [GO:0045773]; positive regulation of cholesterol efflux [GO:0010875]; positive regulation of cholesterol metabolic process [GO:0090205]; positive regulation of dendritic spine development [GO:0060999]; positive regulation of dendritic spine maintenance [GO:1902952]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of endocytosis [GO:0045807]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of lipid biosynthetic process [GO:0046889]; positive regulation of lipid transport across blood-brain barrier [GO:1903002]; positive regulation of low-density lipoprotein particle receptor catabolic process [GO:0032805]; positive regulation of membrane protein ectodomain proteolysis [GO:0051044]; positive regulation of neuron projection development [GO:0010976]; positive regulation of phospholipid efflux [GO:1902995]; protein import [GO:0017038]; receptor-mediated endocytosis [GO:0006898]; regulation of amyloid fibril formation [GO:1905906]; regulation of amyloid precursor protein catabolic process [GO:1902991]; regulation of amyloid-beta clearance [GO:1900221]; regulation of apoptotic process [GO:0042981]; regulation of behavioral fear response [GO:2000822]; regulation of Cdc42 protein signal transduction [GO:0032489]; regulation of cellular response to very-low-density lipoprotein particle stimulus [GO:1905890]; regulation of cholesterol metabolic process [GO:0090181]; regulation of gene expression [GO:0010468]; regulation of innate immune response [GO:0045088]; regulation of plasma lipoprotein particle levels [GO:0097006]; regulation of proteasomal protein catabolic process [GO:0061136]; regulation of protein metabolic process [GO:0051246]; regulation of protein-containing complex assembly [GO:0043254]; regulation of synapse organization [GO:0050807]; regulation of triglyceride metabolic process [GO:0090207]; response to caloric restriction [GO:0061771]; response to D-galactosamine [GO:1904421]; response to dietary excess [GO:0002021]; response to ethanol [GO:0045471]; response to insulin [GO:0032868]; response to oxidative stress [GO:0006979]; response to retinoic acid [GO:0032526]; response to tumor necrosis factor [GO:0034612]; response to zinc ion [GO:0010043]; reverse cholesterol transport [GO:0043691]; triglyceride homeostasis [GO:0070328]; triglyceride metabolic process [GO:0006641]; triglyceride-rich lipoprotein particle clearance [GO:0071830]; vasodilation [GO:0042311]; very-low-density lipoprotein particle clearance [GO:0034447]; very-low-density lipoprotein particle remodeling [GO:0034372]; virion assembly [GO:0019068]
|
cell surface [GO:0009986]; chylomicron [GO:0042627]; chylomicron remnant [GO:0034360]; dendrite [GO:0030425]; discoidal high-density lipoprotein particle [GO:0034365]; endoplasmic reticulum [GO:0005783]; endosome [GO:0005768]; extracellular exosome [GO:0070062]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; extracellular vesicle [GO:1903561]; extrinsic component of external side of plasma membrane [GO:0031232]; glutamatergic synapse [GO:0098978]; Golgi apparatus [GO:0005794]; high-density lipoprotein particle [GO:0034364]; intermediate-density lipoprotein particle [GO:0034363]; late endosome [GO:0005770]; lipoprotein particle [GO:1990777]; low-density lipoprotein particle [GO:0034362]; melanosome [GO:0042470]; multivesicular body, internal vesicle [GO:0097487]; neuronal cell body [GO:0043025]; nuclear envelope [GO:0005635]; synaptic cleft [GO:0043083]; very-low-density lipoprotein particle [GO:0034361]
|
amyloid-beta binding [GO:0001540]; antioxidant activity [GO:0016209]; cholesterol transfer activity [GO:0120020]; enzyme binding [GO:0019899]; heparan sulfate proteoglycan binding [GO:0043395]; heparin binding [GO:0008201]; hydroxyapatite binding [GO:0046848]; identical protein binding [GO:0042802]; lipid binding [GO:0008289]; lipid transporter activity [GO:0005319]; lipoprotein particle binding [GO:0071813]; low-density lipoprotein particle receptor binding [GO:0050750]; metal chelating activity [GO:0046911]; phosphatidylcholine-sterol O-acyltransferase activator activity [GO:0060228]; phospholipid binding [GO:0005543]; protein dimerization activity [GO:0046983]; protein homodimerization activity [GO:0042803]; protein-containing complex binding [GO:0044877]; signaling receptor binding [GO:0005102]; tau protein binding [GO:0048156]; very-low-density lipoprotein particle receptor binding [GO:0070326]
|
PF01442;
|
1.20.120.20;
|
Apolipoprotein A1/A4/E family
|
PTM: APOE exists as multiple glycosylated and sialylated glycoforms within cells and in plasma. The extent of glycosylation and sialylation are tissue and context specific. {ECO:0000250|UniProtKB:P02649}.; PTM: Glycated in plasma VLDL. {ECO:0000250|UniProtKB:P02649}.; PTM: Phosphorylated by FAM20C in the extracellular medium. {ECO:0000250|UniProtKB:P02649}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02649}. Secreted, extracellular space {ECO:0000250|UniProtKB:P02649}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P02649}. Extracellular vesicle {ECO:0000250|UniProtKB:P02649}. Endosome, multivesicular body {ECO:0000250|UniProtKB:P02649}. Note=In the plasma, APOE is associated with chylomicrons, chylomicrons remnants, VLDL, LDL and HDL lipoproteins. Lipid poor oligomeric APOE is associated with the extracellular matrix in a calcium- and heparan-sulfate proteoglycans-dependent manner. Lipidation induces the release from the extracellular matrix. Colocalizes with CD63 and PMEL at exosomes and in intraluminal vesicles within multivesicular endosomes. {ECO:0000250|UniProtKB:P02649}.
| null | null | null | null | null |
FUNCTION: APOE is an apolipoprotein, a protein associating with lipid particles, that mainly functions in lipoprotein-mediated lipid transport between organs via the plasma and interstitial fluids. APOE is a core component of plasma lipoproteins and is involved in their production, conversion and clearance. Apolipoproteins are amphipathic molecules that interact both with lipids of the lipoprotein particle core and the aqueous environment of the plasma. As such, APOE associates with chylomicrons, chylomicron remnants, very low density lipoproteins (VLDL) and intermediate density lipoproteins (IDL) but shows a preferential binding to high-density lipoproteins (HDL). It also binds a wide range of cellular receptors including the LDL receptor/LDLR and the very low-density lipoprotein receptor/VLDLR that mediate the cellular uptake of the APOE-containing lipoprotein particles. Finally, APOE has also a heparin-binding activity and binds heparan-sulfate proteoglycans on the surface of cells, a property that supports the capture and the receptor-mediated uptake of APOE-containing lipoproteins by cells. {ECO:0000250|UniProtKB:P02649}.
|
Rattus norvegicus (Rat)
|
P02651
|
APOA4_RAT
|
MFLKAVVLTVALVAITGTQAEVTSDQVANVMWDYFTQLSNNAKEAVEQLQKTDVTQQLNTLFQDKLGNINTYADDLQNKLVPFAVQLSGHLTKETERVREEIQKELEDLRANMMPHANKVSQMFGDNVQKLQEHLRPYATDLQAQINAQTQDMKRQLTPYIQRMQTTIQDNVENLQSSMVPFANELKEKFNQNMEGLKGQLTPRANELKATIDQNLEDLRSRLAPLAEGVQEKLNHQMEGLAFQMKKNAEELQTKVSTNIDQLQKNLAPLVEDVQSKLKGNTEGLQKSLEDLNKQLDQQVEVFRRAVEPLGDKFNMALVQQMEKFRQQLGSDSGDVESHLSFLEKNLREKVSSFMSTLQKKGSPDQPLALPLPEQVQEQVQEQVQPKPLES
| null | null |
acylglycerol homeostasis [GO:0055090]; cholesterol efflux [GO:0033344]; cholesterol homeostasis [GO:0042632]; cholesterol metabolic process [GO:0008203]; high-density lipoprotein particle remodeling [GO:0034375]; hydrogen peroxide catabolic process [GO:0042744]; innate immune response in mucosa [GO:0002227]; leukocyte cell-cell adhesion [GO:0007159]; lipid catabolic process [GO:0016042]; lipid homeostasis [GO:0055088]; lipid transport [GO:0006869]; lipoprotein metabolic process [GO:0042157]; negative regulation of plasma lipoprotein oxidation [GO:0034445]; peripheral nervous system axon regeneration [GO:0014012]; phosphatidylcholine metabolic process [GO:0046470]; phospholipid efflux [GO:0033700]; positive regulation of fatty acid biosynthetic process [GO:0045723]; positive regulation of triglyceride catabolic process [GO:0010898]; protein-lipid complex assembly [GO:0065005]; regulation of cholesterol transport [GO:0032374]; regulation of intestinal cholesterol absorption [GO:0030300]; removal of superoxide radicals [GO:0019430]; response to food [GO:0032094]; response to lipid hydroperoxide [GO:0006982]; response to stilbenoid [GO:0035634]; response to triglyceride [GO:0034014]; reverse cholesterol transport [GO:0043691]; triglyceride homeostasis [GO:0070328]; very-low-density lipoprotein particle remodeling [GO:0034372]
|
blood microparticle [GO:0072562]; cell surface [GO:0009986]; chylomicron [GO:0042627]; extracellular space [GO:0005615]; extracellular vesicle [GO:1903561]; high-density lipoprotein particle [GO:0034364]; low-density lipoprotein particle [GO:0034362]; synapse [GO:0045202]; very-low-density lipoprotein particle [GO:0034361]
|
antioxidant activity [GO:0016209]; cholesterol transfer activity [GO:0120020]; copper ion binding [GO:0005507]; identical protein binding [GO:0042802]; lipid binding [GO:0008289]; phosphatidylcholine binding [GO:0031210]; phosphatidylcholine-sterol O-acyltransferase activator activity [GO:0060228]; phospholipid binding [GO:0005543]; protein homodimerization activity [GO:0042803]
|
PF01442;
|
1.20.120.20;
|
Apolipoprotein A1/A4/E family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: May have a role in chylomicrons and VLDL secretion and catabolism. Required for efficient activation of lipoprotein lipase by ApoC-II; potent activator of LCAT. Apoa-IV is a major component of HDL and chylomicrons.
|
Rattus norvegicus (Rat)
|
P02652
|
APOA2_HUMAN
|
MKLLAATVLLLTICSLEGALVRRQAKEPCVESLVSQYFQTVTDYGKDLMEKVKSPELQAEAKSYFEKSKEQLTPLIKKAGTELVNFLSYFVELGTQPATQ
| null | null |
animal organ regeneration [GO:0031100]; cholesterol efflux [GO:0033344]; cholesterol homeostasis [GO:0042632]; cholesterol metabolic process [GO:0008203]; cholesterol transport [GO:0030301]; diacylglycerol catabolic process [GO:0046340]; high-density lipoprotein particle assembly [GO:0034380]; high-density lipoprotein particle clearance [GO:0034384]; high-density lipoprotein particle remodeling [GO:0034375]; lipoprotein metabolic process [GO:0042157]; low-density lipoprotein particle remodeling [GO:0034374]; negative regulation of cholesterol import [GO:0060621]; negative regulation of cholesterol transport [GO:0032375]; negative regulation of cholesterol transporter activity [GO:0060695]; negative regulation of cytokine production involved in immune response [GO:0002719]; negative regulation of lipase activity [GO:0060192]; negative regulation of lipid catabolic process [GO:0050995]; negative regulation of very-low-density lipoprotein particle remodeling [GO:0010903]; peptidyl-methionine modification [GO:0018206]; phosphatidylcholine biosynthetic process [GO:0006656]; phospholipid catabolic process [GO:0009395]; phospholipid efflux [GO:0033700]; positive regulation of CoA-transferase activity [GO:1905920]; positive regulation of interleukin-8 production [GO:0032757]; positive regulation of lipid catabolic process [GO:0050996]; positive regulation of phagocytosis [GO:0050766]; protein oxidation [GO:0018158]; protein stabilization [GO:0050821]; regulation of intestinal cholesterol absorption [GO:0030300]; regulation of protein stability [GO:0031647]; response to estrogen [GO:0043627]; response to glucocorticoid [GO:0051384]; response to glucose [GO:0009749]; response to xenobiotic stimulus [GO:0009410]; reverse cholesterol transport [GO:0043691]; triglyceride metabolic process [GO:0006641]; triglyceride-rich lipoprotein particle remodeling [GO:0034370]
|
blood microparticle [GO:0072562]; chylomicron [GO:0042627]; cytosol [GO:0005829]; early endosome [GO:0005769]; endoplasmic reticulum lumen [GO:0005788]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; high-density lipoprotein particle [GO:0034364]; spherical high-density lipoprotein particle [GO:0034366]; very-low-density lipoprotein particle [GO:0034361]
|
apolipoprotein receptor binding [GO:0034190]; cholesterol binding [GO:0015485]; cholesterol transfer activity [GO:0120020]; enzyme binding [GO:0019899]; heat shock protein binding [GO:0031072]; high-density lipoprotein particle binding [GO:0008035]; high-density lipoprotein particle receptor binding [GO:0070653]; lipase inhibitor activity [GO:0055102]; lipid binding [GO:0008289]; lipid transporter activity [GO:0005319]; phosphatidylcholine binding [GO:0031210]; phosphatidylcholine-sterol O-acyltransferase activator activity [GO:0060228]; phospholipid binding [GO:0005543]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; signaling receptor binding [GO:0005102]
|
PF04711;
|
6.10.250.100;
|
Apolipoprotein A2 family
|
PTM: Phosphorylation sites are present in the extracellular medium. {ECO:0000269|PubMed:26091039}.; PTM: Apolipoprotein A-II is O-glycosylated. {ECO:0000269|PubMed:23234360}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24116940}.
| null | null | null | null | null |
FUNCTION: May stabilize HDL (high density lipoprotein) structure by its association with lipids, and affect the HDL metabolism.
|
Homo sapiens (Human)
|
P02653
|
APOA2_MACMU
|
QAEEPSVESLVSQYFQTVTDYGKDLMEKVKSPELQAQAKAYFEKSKEQLTPLVKKAGTDLVNFLSYFVELRTQPATQ
| null | null |
cholesterol homeostasis [GO:0042632]; cholesterol metabolic process [GO:0008203]; cholesterol transport [GO:0030301]; high-density lipoprotein particle assembly [GO:0034380]; high-density lipoprotein particle remodeling [GO:0034375]; lipoprotein metabolic process [GO:0042157]; low-density lipoprotein particle remodeling [GO:0034374]; peptidyl-methionine modification [GO:0018206]; positive regulation of interleukin-8 production [GO:0032757]; positive regulation of phagocytosis [GO:0050766]; protein oxidation [GO:0018158]; protein stabilization [GO:0050821]; triglyceride-rich lipoprotein particle remodeling [GO:0034370]
|
blood microparticle [GO:0072562]; chylomicron [GO:0042627]; spherical high-density lipoprotein particle [GO:0034366]; very-low-density lipoprotein particle [GO:0034361]
|
apolipoprotein receptor binding [GO:0034190]; cholesterol binding [GO:0015485]; cholesterol transfer activity [GO:0120020]; high-density lipoprotein particle binding [GO:0008035]; high-density lipoprotein particle receptor binding [GO:0070653]; lipase inhibitor activity [GO:0055102]; phosphatidylcholine binding [GO:0031210]; protein heterodimerization activity [GO:0046982]
|
PF04711;
|
6.10.250.100;
|
Apolipoprotein A2 family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02652}.
| null | null | null | null | null |
FUNCTION: Apo A-II makes up about 20% of the protein of the HDL (high density lipoprotein) phospholipid-rich fraction in plasma.
|
Macaca mulatta (Rhesus macaque)
|
P02654
|
APOC1_HUMAN
|
MRLFLSLPVLVVVLSIVLEGPAPAQGTPDVSSALDKLKEFGNTLEDKARELISRIKQSELSAKMREWFSETFQKVKEKLKIDS
| null | null |
cholesterol efflux [GO:0033344]; cholesterol metabolic process [GO:0008203]; chylomicron remnant clearance [GO:0034382]; high-density lipoprotein particle remodeling [GO:0034375]; lipid metabolic process [GO:0006629]; lipoprotein metabolic process [GO:0042157]; negative regulation of cholesterol transport [GO:0032375]; negative regulation of fatty acid biosynthetic process [GO:0045717]; negative regulation of lipid catabolic process [GO:0050995]; negative regulation of lipid metabolic process [GO:0045833]; negative regulation of lipoprotein lipase activity [GO:0051005]; negative regulation of phosphatidylcholine catabolic process [GO:0010900]; negative regulation of receptor-mediated endocytosis [GO:0048261]; negative regulation of very-low-density lipoprotein particle clearance [GO:0010916]; phospholipid efflux [GO:0033700]; plasma lipoprotein particle remodeling [GO:0034369]; regulation of cholesterol transport [GO:0032374]; triglyceride metabolic process [GO:0006641]; very-low-density lipoprotein particle assembly [GO:0034379]; very-low-density lipoprotein particle clearance [GO:0034447]
|
chylomicron [GO:0042627]; endoplasmic reticulum [GO:0005783]; extracellular region [GO:0005576]; high-density lipoprotein particle [GO:0034364]; very-low-density lipoprotein particle [GO:0034361]
|
fatty acid binding [GO:0005504]; lipase inhibitor activity [GO:0055102]; phosphatidylcholine binding [GO:0031210]; phosphatidylcholine-sterol O-acyltransferase activator activity [GO:0060228]; phospholipase inhibitor activity [GO:0004859]
|
PF04691;
|
4.10.260.30;
|
Apolipoprotein C1 family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000303|PubMed:2835369}.
| null | null | null | null | null |
FUNCTION: Inhibitor of lipoprotein binding to the low density lipoprotein (LDL) receptor, LDL receptor-related protein, and very low density lipoprotein (VLDL) receptor. Associates with high density lipoproteins (HDL) and the triacylglycerol-rich lipoproteins in the plasma and makes up about 10% of the protein of the VLDL and 2% of that of HDL. Appears to interfere directly with fatty acid uptake and is also the major plasma inhibitor of cholesteryl ester transfer protein (CETP). Binds free fatty acids and reduces their intracellular esterification. Modulates the interaction of APOE with beta-migrating VLDL and inhibits binding of beta-VLDL to the LDL receptor-related protein. {ECO:0000269|PubMed:17339654, ECO:0000303|PubMed:25160599}.
|
Homo sapiens (Human)
|
P02655
|
APOC2_HUMAN
|
MGTRLLPALFLVLLVLGFEVQGTQQPQQDEMPSPTFLTQVKESLSSYWESAKTAAQNLYEKTYLPAVDEKLRDLYSKSTAAMSTYTGIFTDQVLSVLKGEE
| null | null |
cholesterol efflux [GO:0033344]; cholesterol homeostasis [GO:0042632]; chylomicron remnant clearance [GO:0034382]; chylomicron remodeling [GO:0034371]; high-density lipoprotein particle clearance [GO:0034384]; lipid catabolic process [GO:0016042]; negative regulation of cholesterol transport [GO:0032375]; negative regulation of lipid metabolic process [GO:0045833]; negative regulation of receptor-mediated endocytosis [GO:0048261]; negative regulation of very-low-density lipoprotein particle clearance [GO:0010916]; phospholipid efflux [GO:0033700]; positive regulation of fatty acid biosynthetic process [GO:0045723]; positive regulation of lipoprotein lipase activity [GO:0051006]; positive regulation of phospholipase activity [GO:0010518]; positive regulation of phospholipid catabolic process [GO:0060697]; positive regulation of triglyceride catabolic process [GO:0010898]; positive regulation of very-low-density lipoprotein particle remodeling [GO:0010902]; reverse cholesterol transport [GO:0043691]; triglyceride homeostasis [GO:0070328]; triglyceride-rich lipoprotein particle remodeling [GO:0034370]; very-low-density lipoprotein particle remodeling [GO:0034372]
|
chylomicron [GO:0042627]; early endosome [GO:0005769]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; intermediate-density lipoprotein particle [GO:0034363]; low-density lipoprotein particle [GO:0034362]; spherical high-density lipoprotein particle [GO:0034366]; very-low-density lipoprotein particle [GO:0034361]
|
lipase inhibitor activity [GO:0055102]; lipid binding [GO:0008289]; lipoprotein lipase activator activity [GO:0060230]; molecular function activator activity [GO:0140677]; phospholipase activator activity [GO:0016004]; phospholipase binding [GO:0043274]
|
PF05355;
|
1.10.1440.10;
|
Apolipoprotein C2 family
|
PTM: Proapolipoprotein C-II is synthesized as a sialic acid containing glycoprotein which is subsequently desialylated prior to its proteolytic processing. {ECO:0000269|PubMed:3525527}.; PTM: Proapolipoprotein C-II, the major form found in plasma undergoes proteolytic cleavage of its N-terminal hexapeptide to generate apolipoprotein C-II, which occurs as the minor form in plasma. {ECO:0000269|PubMed:3525527}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:3525527}.
| null | null | null | null | null |
FUNCTION: Component of chylomicrons, very low-density lipoproteins (VLDL), low-density lipoproteins (LDL), and high-density lipoproteins (HDL) in plasma. Plays an important role in lipoprotein metabolism as an activator of lipoprotein lipase. Both proapolipoprotein C-II and apolipoprotein C-II can activate lipoprotein lipase. In normolipidemic individuals, it is mainly distributed in the HDL, whereas in hypertriglyceridemic individuals, predominantly found in the VLDL and LDL. {ECO:0000269|PubMed:2209608, ECO:0000303|PubMed:22304839}.
|
Homo sapiens (Human)
|
P02656
|
APOC3_HUMAN
|
MQPRVLLVVALLALLASARASEAEDASLLSFMQGYMKHATKTAKDALSSVQESQVAQQARGWVTDGFSSLKDYWSTVKDKFSEFWDLDPEVRPTSAVAA
| null | null |
cholesterol efflux [GO:0033344]; cholesterol homeostasis [GO:0042632]; chylomicron remnant clearance [GO:0034382]; G protein-coupled receptor signaling pathway [GO:0007186]; high-density lipoprotein particle remodeling [GO:0034375]; lipoprotein metabolic process [GO:0042157]; negative regulation of cholesterol import [GO:0060621]; negative regulation of fatty acid biosynthetic process [GO:0045717]; negative regulation of high-density lipoprotein particle clearance [GO:0010987]; negative regulation of lipid catabolic process [GO:0050995]; negative regulation of lipid metabolic process [GO:0045833]; negative regulation of lipoprotein lipase activity [GO:0051005]; negative regulation of low-density lipoprotein particle clearance [GO:0010989]; negative regulation of receptor-mediated endocytosis [GO:0048261]; negative regulation of triglyceride catabolic process [GO:0010897]; negative regulation of very-low-density lipoprotein particle clearance [GO:0010916]; negative regulation of very-low-density lipoprotein particle remodeling [GO:0010903]; phospholipid efflux [GO:0033700]; regulation of Cdc42 protein signal transduction [GO:0032489]; reverse cholesterol transport [GO:0043691]; triglyceride catabolic process [GO:0019433]; triglyceride homeostasis [GO:0070328]; triglyceride metabolic process [GO:0006641]; very-low-density lipoprotein particle assembly [GO:0034379]
|
chylomicron [GO:0042627]; collagen-containing extracellular matrix [GO:0062023]; early endosome [GO:0005769]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; intermediate-density lipoprotein particle [GO:0034363]; spherical high-density lipoprotein particle [GO:0034366]; very-low-density lipoprotein particle [GO:0034361]
|
cholesterol binding [GO:0015485]; enzyme regulator activity [GO:0030234]; high-density lipoprotein particle receptor binding [GO:0070653]; lipase inhibitor activity [GO:0055102]; phospholipid binding [GO:0005543]
|
PF05778;
|
6.10.90.10;
|
Apolipoprotein C3 family
|
PTM: The most abundant glycoforms are characterized by an O-linked disaccharide galactose linked to N-acetylgalactosamine (Gal-GalNAc), further modified with up to 3 sialic acid residues. Less abundant glycoforms are characterized by more complex and fucosylated glycan moieties. O-glycosylated on Thr-94 with a core 1 or possibly core 8 glycan. {ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:23527852, ECO:0000269|PubMed:3123586}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000303|PubMed:18201179, ECO:0000303|PubMed:22510806}.
| null | null | null | null | null |
FUNCTION: Component of triglyceride-rich very low density lipoproteins (VLDL) and high density lipoproteins (HDL) in plasma (PubMed:18201179, PubMed:22510806). Plays a multifaceted role in triglyceride homeostasis (PubMed:18201179, PubMed:22510806). Intracellularly, promotes hepatic very low density lipoprotein 1 (VLDL1) assembly and secretion; extracellularly, attenuates hydrolysis and clearance of triglyceride-rich lipoproteins (TRLs) (PubMed:18201179, PubMed:22510806). Impairs the lipolysis of TRLs by inhibiting lipoprotein lipase and the hepatic uptake of TRLs by remnant receptors (PubMed:18201179, PubMed:22510806). Formed of several curved helices connected via semiflexible hinges, so that it can wrap tightly around the curved micelle surface and easily adapt to the different diameters of its natural binding partners (PubMed:18408013). {ECO:0000269|PubMed:18408013, ECO:0000303|PubMed:18201179, ECO:0000303|PubMed:22510806}.
|
Homo sapiens (Human)
|
P02662
|
CASA1_BOVIN
|
MKLLILTCLVAVALARPKHPIKHQGLPQEVLNENLLRFFVAPFPEVFGKEKVNELSKDIGSESTEDQAMEDIKQMEAESISSSEEIVPNSVEQKHIQKEDVPSERYLGYLEQLLRLKKYKVPQLEIVPNSAEERLHSMKEGIHAQQKEPMIGVNQELAYFYPELFRQFYQLDAYPSGAWYYVPLGTQYTDAPSFSDIPNPIGSENSEKTTMPLW
| null | null |
negative regulation of supramolecular fiber organization [GO:1902904]; protein stabilization [GO:0050821]; response to 11-deoxycorticosterone [GO:1903496]; response to dehydroepiandrosterone [GO:1903494]; response to estradiol [GO:0032355]; response to growth hormone [GO:0060416]; response to progesterone [GO:0032570]
|
extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; Golgi lumen [GO:0005796]
|
amyloid-beta binding [GO:0001540]; antioxidant activity [GO:0016209]
|
PF00363;
| null |
Alpha-casein family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Important role in the capacity of milk to transport calcium phosphate. {ECO:0000269|Ref.15}.; FUNCTION: Antioxidant peptide has 2,2-diphenyl-1-picrylhydrazyl (DPPH) radical scavenging activity. {ECO:0000269|Ref.15}.
|
Bos taurus (Bovine)
|
P02663
|
CASA2_BOVIN
|
MKFFIFTCLLAVALAKNTMEHVSSSEESIISQETYKQEKNMAINPSKENLCSTFCKEVVRNANEEEYSIGSSSEESAEVATEEVKITVDDKHYQKALNEINQFYQKFPQYLQYLYQGPIVLNPWDQVKRNAVPITPTLNREQLSTSEENSKKTVDMESTEVFTKKTKLTEEEKNRLNFLKKISQRYQKFALPQYLKTVYQHQKAMKPWIQPKTKVIPYVRYL
| null | null |
defense response to bacterium [GO:0042742]; response to 11-deoxycorticosterone [GO:1903496]; response to dehydroepiandrosterone [GO:1903494]; response to estradiol [GO:0032355]; response to growth hormone [GO:0060416]; response to progesterone [GO:0032570]
|
extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; Golgi lumen [GO:0005796]
|
protein homodimerization activity [GO:0042803]; zymogen binding [GO:0035375]
|
PF00363;
| null |
Alpha-casein family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Important role in the capacity of milk to transport calcium phosphate.; FUNCTION: Casocidin-I inhibits the growth of E.coli and S.carnosus.
|
Bos taurus (Bovine)
|
P02666
|
CASB_BOVIN
|
MKVLILACLVALALARELEELNVPGEIVESLSSSEESITRINKKIEKFQSEEQQQTEDELQDKIHPFAQTQSLVYPFPGPIPNSLPQNIPPLTQTPVVVPPFLQPEVMGVSKVKEAMAPKHKEMPFPKYPVEPFTESQSLTLTDVENLHLPLPLLQSWMHQPHQPLPPTVMFPPQSVLSLSQSKVLPVPQKAVPYPQRDMPIQAFLLYQEPVLGPVRGPFPIIV
| null | null |
negative regulation of canonical NF-kappaB signal transduction [GO:0043124]; negative regulation of cysteine-type endopeptidase activity [GO:2000117]; negative regulation of inflammatory response [GO:0050728]; negative regulation of lactation [GO:1903488]; negative regulation of tumor necrosis factor-mediated signaling pathway [GO:0010804]; regulation of blood pressure [GO:0008217]; response to 11-deoxycorticosterone [GO:1903496]; response to dehydroepiandrosterone [GO:1903494]; response to estradiol [GO:0032355]; response to heat [GO:0009408]; response to progesterone [GO:0032570]
|
extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; Golgi lumen [GO:0005796]
|
antioxidant activity [GO:0016209]; cysteine-type endopeptidase inhibitor activity [GO:0004869]; ion binding [GO:0043167]; metal ion binding [GO:0046872]; potassium channel inhibitor activity [GO:0019870]; protein homodimerization activity [GO:0042803]
|
PF00363;
| null |
Beta-casein family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Important role in determination of the surface properties of the casein micelles.; FUNCTION: Casoparan acts as a macrophage activator, increasing the phagocytic activity of macrophages and peroxide release from macrophages. It also acts as a bradykinin-potentiating peptide.; FUNCTION: Casohypotensin acts as a bradykinin-potentiating peptide. Induces hypotension in rats. Acts as a strong competitive inhibitor of endo-oligopeptidase A.; FUNCTION: Antioxidant peptide has antioxidant activity.
|
Bos taurus (Bovine)
|
P02668
|
CASK_BOVIN
|
MMKSFFLVVTILALTLPFLGAQEQNQEQPIRCEKDERFFSDKIAKYIPIQYVLSRYPSYGLNYYQQKPVALINNQFLPYPYYAKPAAVRSPAQILQWQVLSNTVPAKSCQAQPTTMARHPHPHLSFMAIPPKKNQDKTEIPTINTIASGEPTSTPTTEAVESTVATLEDSPEVIESPPEINTVQVTSTAV
| null | null |
lactation [GO:0007595]; protein stabilization [GO:0050821]; response to 11-deoxycorticosterone [GO:1903496]; response to dehydroepiandrosterone [GO:1903494]; response to estradiol [GO:0032355]; response to progesterone [GO:0032570]
|
extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; Golgi lumen [GO:0005796]
|
identical protein binding [GO:0042802]; zymogen binding [GO:0035375]
|
PF00997;
| null |
Kappa-casein family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Kappa-casein stabilizes micelle formation, preventing casein precipitation in milk.; FUNCTION: Casoxins A, B and C have opioid antagonist activity. Casoxin C causes biphasic ileal contractions through the binding to the complement C3a receptors.; FUNCTION: Casoplatelin inhibits platelet aggregation.
|
Bos taurus (Bovine)
|
P02669
|
CASK_SHEEP
|
MMKSFFLVVTILALTLPFLGAQEQNQEQRICCEKDERFFDDKIAKYIPIQYVLSRYPSYGLNYYQQRPVALINNQFLPYPYYAKPVAVRSPAQTLQWQVLPNAVPAKSCQDQPTAMARHPHPHLSFMAIPPKKDQDKTEIPAINTIASAEPTVHSTPTTEAVVNAVDNPEASSESIASAPETNTAQVTSTEV
| null | null |
lactation [GO:0007595]; protein stabilization [GO:0050821]
|
extracellular space [GO:0005615]
| null |
PF00997;
| null |
Kappa-casein family
|
PTM: O-glycosylated on Thr at position 156, 158 or 159.
|
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Kappa-casein stabilizes micelle formation, preventing casein precipitation in milk.
|
Ovis aries (Sheep)
|
P02670
|
CASK_CAPHI
|
MMKSFFLVVTILALTLPFLGAQEQNQEQPICCEKDERFFDDKIAKYIPIQYVLSRYPSYGLNYYQQRPVALINNQFLPYPYYAKPVAVRSPAQTLQWQVLPNTVPAKSCQDQPTTLARHPHPHLSFMAIPPKKDQDKTEVPAINTIASAEPTVHSTPTTEAIVNTVDNPEASSESIASASETNTAQVTSTEV
| null | null |
lactation [GO:0007595]; protein stabilization [GO:0050821]
|
extracellular space [GO:0005615]
| null |
PF00997;
| null |
Kappa-casein family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Kappa-casein stabilizes micelle formation, preventing casein precipitation in milk.
|
Capra hircus (Goat)
|
P02671
|
FIBA_HUMAN
|
MFSMRIVCLVLSVVGTAWTADSGEGDFLAEGGGVRGPRVVERHQSACKDSDWPFCSDEDWNYKCPSGCRMKGLIDEVNQDFTNRINKLKNSLFEYQKNNKDSHSLTTNIMEILRGDFSSANNRDNTYNRVSEDLRSRIEVLKRKVIEKVQHIQLLQKNVRAQLVDMKRLEVDIDIKIRSCRGSCSRALAREVDLKDYEDQQKQLEQVIAKDLLPSRDRQHLPLIKMKPVPDLVPGNFKSQLQKVPPEWKALTDMPQMRMELERPGGNEITRGGSTSYGTGSETESPRNPSSAGSWNSGSSGPGSTGNRNPGSSGTGGTATWKPGSSGPGSTGSWNSGSSGTGSTGNQNPGSPRPGSTGTWNPGSSERGSAGHWTSESSVSGSTGQWHSESGSFRPDSPGSGNARPNNPDWGTFEEVSGNVSPGTRREYHTEKLVTSKGDKELRTGKEKVTSGSTTTTRRSCSKTVTKTVIGPDGHKEVTKEVVTSEDGSDCPEAMDLGTLSGIGTLDGFRHRHPDEAAFFDTASTGKTFPGFFSPMLGEFVSETESRGSESGIFTNTKESSSHHPGIAEFPSRGKSSSYSKQFTSSTSYNRGDSTFESKSYKMADEAGSEADHEGTHSTKRGHAKSRPVRDCDDVLQTHPSGTQSGIFNIKLPGSSKIFSVYCDQETSLGGWLLIQQRMDGSLNFNRTWQDYKRGFGSLNDEGEGEFWLGNDYLHLLTQRGSVLRVELEDWAGNEAYAEYHFRVGSEAEGYALQVSSYEGTAGDALIEGSVEEGAEYTSHNNMQFSTFDRDADQWEENCAEVYGGGWWYNNCQAANLNGIYYPGGSYDPRNNSPYEIENGVVWVSFRGADYSLRAVRMKIRPLVTQ
| null | null |
adaptive immune response [GO:0002250]; blood coagulation, common pathway [GO:0072377]; blood coagulation, fibrin clot formation [GO:0072378]; cell-matrix adhesion [GO:0007160]; fibrinolysis [GO:0042730]; induction of bacterial agglutination [GO:0043152]; innate immune response [GO:0045087]; negative regulation of endothelial cell apoptotic process [GO:2000352]; negative regulation of extrinsic apoptotic signaling pathway via death domain receptors [GO:1902042]; plasminogen activation [GO:0031639]; platelet aggregation [GO:0070527]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of exocytosis [GO:0045921]; positive regulation of heterotypic cell-cell adhesion [GO:0034116]; positive regulation of peptide hormone secretion [GO:0090277]; positive regulation of protein secretion [GO:0050714]; positive regulation of substrate adhesion-dependent cell spreading [GO:1900026]; positive regulation of vasoconstriction [GO:0045907]; protein polymerization [GO:0051258]; protein-containing complex assembly [GO:0065003]; response to calcium ion [GO:0051592]
|
blood microparticle [GO:0072562]; cell surface [GO:0009986]; collagen-containing extracellular matrix [GO:0062023]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum lumen [GO:0005788]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; extracellular vesicle [GO:1903561]; fibrinogen complex [GO:0005577]; plasma membrane [GO:0005886]; platelet alpha granule [GO:0031091]; platelet alpha granule lumen [GO:0031093]
|
extracellular matrix structural constituent [GO:0005201]; metal ion binding [GO:0046872]; signaling receptor binding [GO:0005102]; structural molecule activity [GO:0005198]
|
PF08702;PF12160;PF00147;
|
1.20.5.50;3.90.215.10;4.10.530.10;
| null |
PTM: The alpha chain is normally not N-glycosylated (PubMed:23151259), even though glycosylation at Asn-686 was observed when a fragment of the protein was expressed in insect cells (PubMed:9689040). It is well known that heterologous expression of isolated domains can lead to adventitious protein modifications. Besides, glycosylation at Asn-686 is supported by large-scale glycoproteomics studies (PubMed:16335952, PubMed:19159218), but the evidence is still quite tenuous. Most likely, Asn-686 is not glycosylated in the healthy human body, or only with low efficiency. {ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:23151259, ECO:0000269|PubMed:9689040, ECO:0000305}.; PTM: O-glycosylated. {ECO:0000269|PubMed:23050552}.; PTM: Forms F13A-mediated cross-links between a glutamine and the epsilon-amino group of a lysine residue, forming fibronectin-fibrinogen heteropolymers.; PTM: About one-third of the alpha chains in the molecules in blood were found to be phosphorylated.; PTM: Conversion of fibrinogen to fibrin is triggered by thrombin, which cleaves fibrinopeptides A and B from alpha and beta chains, and thus exposes the N-terminal polymerization sites responsible for the formation of the soft clot. The soft clot is converted into the hard clot by factor XIIIA which catalyzes the epsilon-(gamma-glutamyl)lysine cross-linking between gamma chains (stronger) and between alpha chains (weaker) of different monomers. {ECO:0000269|PubMed:2143188}.; PTM: Phosphorylated by FAM20C in the extracellular medium. {ECO:0000269|PubMed:26091039}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19296670, ECO:0000269|PubMed:9628725}.
| null | null | null | null | null |
FUNCTION: Cleaved by the protease thrombin to yield monomers which, together with fibrinogen beta (FGB) and fibrinogen gamma (FGG), polymerize to form an insoluble fibrin matrix. Fibrin has a major function in hemostasis as one of the primary components of blood clots. In addition, functions during the early stages of wound repair to stabilize the lesion and guide cell migration during re-epithelialization. Was originally thought to be essential for platelet aggregation, based on in vitro studies using anticoagulated blood. However, subsequent studies have shown that it is not absolutely required for thrombus formation in vivo. Enhances expression of SELP in activated platelets via an ITGB3-dependent pathway. Maternal fibrinogen is essential for successful pregnancy. Fibrin deposition is also associated with infection, where it protects against IFNG-mediated hemorrhage. May also facilitate the immune response via both innate and T-cell mediated pathways. {ECO:0000250|UniProtKB:E9PV24}.
|
Homo sapiens (Human)
|
P02672
|
FIBA_BOVIN
|
MFSVRDLCLVLSLVGAIKTEDGSDPPSGDFLTEGGGVRGPRLVERQQSACKETGWPFCSDEDWNTKCPSGCRMKGLIDEVDQDFTSRINKLRDSLFNYQKNSKDSNTLTKNIVELMRGDFAKANNNDNTFKQISEDLRSRIEILRRKVIEQVQRIKVLQKNVRDQLVDMKRLEVDIDIKIRSCKGSCSRALEHKVDLEDYKNQQKQLEQVIAINLLPSRDIQYLPLIKMSTITGPVPREFKSQLQEAPLEWKALLEMQQTKMVLETFGGDGHARGDSVSQGTGLAPGSPRKPGTSSIGNVNPGSYGPGSSGTWNPGRPEPGSAGTWNPGRPEPGSAGTWNPGRPEPGSAGTWNPGRPEPGSAGTWNPGRPEPGSAGTWNTGSSGSSSFRPDSSGHGNIRPSSPDWGTFREEGSVSSGTKQEFHTGKLVTTKGDKELLIDNEKVTSGHTTTTRRSCSKVITKTVTNADGRTETTKEVVKSEDGSDCGDADFDWHHTFPSRGNLDDFFHRDKDDFFTRSSHEFDGRTGLAPEFAALGESGSSSSKTSTHSKQFVSSSTTVNRGGSAIESKHFKMEDEAESLEDLGFKGAHGTQKGHTKARPARGIHTSPLGEPSLTP
| null | null |
adaptive immune response [GO:0002250]; blood coagulation, common pathway [GO:0072377]; fibrinolysis [GO:0042730]; innate immune response [GO:0045087]; negative regulation of endothelial cell apoptotic process [GO:2000352]; negative regulation of extrinsic apoptotic signaling pathway via death domain receptors [GO:1902042]; platelet aggregation [GO:0070527]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of heterotypic cell-cell adhesion [GO:0034116]; positive regulation of peptide hormone secretion [GO:0090277]; protein polymerization [GO:0051258]
|
fibrinogen complex [GO:0005577]
|
extracellular matrix structural constituent [GO:0005201]; signaling receptor binding [GO:0005102]
|
PF08702;PF12160;
|
1.20.5.50;
| null |
PTM: Conversion of fibrinogen to fibrin is triggered by thrombin, which cleaves fibrinopeptides A and B from alpha and beta chains, and thus exposes the N-terminal polymerization sites responsible for the formation of the soft clot. The soft clot is converted into the hard clot by factor XIIIA which catalyzes the epsilon-(gamma-glutamyl)lysine cross-linking between gamma chains (stronger) and between alpha chains (weaker) of different monomers.; PTM: Forms F13A-mediated cross-links between a glutamine and the epsilon-amino group of a lysine residue, forming fibronectin-fibrinogen heteropolymers.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Cleaved by the protease thrombin to yield monomers which, together with fibrinogen beta (FGB) and fibrinogen gamma (FGG), polymerize to form an insoluble fibrin matrix. Fibrin has a major function in hemostasis as one of the primary components of blood clots. In addition, functions during the early stages of wound repair to stabilize the lesion and guide cell migration during re-epithelialization. Was originally thought to be essential for platelet aggregation, based on in vitro studies using anticoagulated blood. However, subsequent studies have shown that it is not absolutely required for thrombus formation in vivo. Enhances expression of SELP in activated platelets via an ITGB3-dependent pathway. Maternal fibrinogen is essential for successful pregnancy. Fibrin deposition is also associated with infection, where it protects against IFNG-mediated hemorrhage. May also facilitate the immune response via both innate and T-cell mediated pathways. {ECO:0000250|UniProtKB:E9PV24}.
|
Bos taurus (Bovine)
|
P02674
|
FIBA1_PETMA
|
QVCIADDISLRGPRLTEQRSAGQGSCASATADLCVHGDWGRKCPNGCRMQGLMSHAEKDIGKRIGDLTERLARLGRLYTQVHTDFRAVSDTSGQTLNEHNELEVRYSEVLRELERRIIHLQRRINMQLQQLTLLQHNIKTQVSQILRVEVDIDVALRTCKGSCARYLEYRLDKEKNLQLEKAASYIANLKFERFEEVVVEETLNRRVETSSHAFQPTHGQGTPQPGHGTHSLSATSSITSAPNFVPHRQPTYVDHGRLSNPNEVAHSASSSSTHTSSSSSPSQPVSRDSAFPLPGSNTGTSEWDFNFHDESTPGNGPRDEAAASSSAHSPSTASHDTATSTTSFSSGTSGKDVAPLGTGVTHDGGVRTSGSLMDGGSSDTGTGGVSKTTTFTGSAQGGSWSTGGSTATNTGSAQGGSWSTGGRTEPNTGSGQGGSWGTGGRTEPNTGSGQGGSWGTGGRTEPNTGSGQGGSWGTGGRTEPNTGSAQGGSWGTGGRTEPNTGSAQGGSWGTGGRTEPNTGSAQGGSWSTGGRTEPNTGSAKGGSWGTGGRTEPNTGSAKGGSWSTGGRTEPNTGSAKGGSWGTGGRTEPNTGSAQGGSWGTGGRTEPNTGSAQGGSWGTGGRTEPNTGSAQGGSWGTGGRTEPNTGSAQGGSWGTGGRTEPNTGSAQGGSWSTGGRTEPNTGSGQGGSWGTGGRTEPNTGSGQGGSWSTGGRTEPNTGSGQGGSWGTGGRTEPNTGSAQGGSWGTGGRTEPNTGSAQGGSWGTGGSTATNTGSAQGGGGYAAGGTGAQTGSGSTSTHSAHSASGGMSSLDMLPALPDFGTWDMPDHSDIFSRRRVSTSSTTSSSSGGGHAGAAAGGGGDGASRFGSLFTTDFGPEFHEEFRSMLPGASRLSSSSSSSTRSTSSTSGGKVVTESVVTKVLSNGTTITHHTKHVSTSDGTGAASDGVSPLLTGRKTKAARSRRAKATRP
| null | null |
blood coagulation, common pathway [GO:0072377]; fibrinolysis [GO:0042730]; negative regulation of endothelial cell apoptotic process [GO:2000352]; negative regulation of extrinsic apoptotic signaling pathway via death domain receptors [GO:1902042]; platelet aggregation [GO:0070527]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of heterotypic cell-cell adhesion [GO:0034116]; positive regulation of peptide hormone secretion [GO:0090277]; protein polymerization [GO:0051258]
|
fibrinogen complex [GO:0005577]
|
extracellular matrix structural constituent [GO:0005201]; signaling receptor binding [GO:0005102]
|
PF08702;
|
1.20.5.50;
| null |
PTM: Not glycosylated.; PTM: Conversion of fibrinogen to fibrin is triggered by thrombin, which cleaves fibrinopeptides A and B from alpha and beta chains, and thus exposes the N-terminal polymerization sites responsible for the formation of the soft clot. The soft clot is converted into the hard clot by factor XIIIA which catalyzes the epsilon-(gamma-glutamyl)lysine cross-linking between gamma chains (stronger) and between alpha chains (weaker) of different monomers.; PTM: Forms F13A-mediated cross-links between a glutamine and the epsilon-amino group of a lysine residue, forming fibronectin-fibrinogen heteropolymers.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12501189}.
| null | null | null | null | null |
FUNCTION: Fibrinogen has a double function: yielding monomers that polymerize into fibrin and acting as a cofactor in platelet aggregation.
|
Petromyzon marinus (Sea lamprey)
|
P02675
|
FIBB_HUMAN
|
MKRMVSWSFHKLKTMKHLLLLLLCVFLVKSQGVNDNEEGFFSARGHRPLDKKREEAPSLRPAPPPISGGGYRARPAKAAATQKKVERKAPDAGGCLHADPDLGVLCPTGCQLQEALLQQERPIRNSVDELNNNVEAVSQTSSSSFQYMYLLKDLWQKRQKQVKDNENVVNEYSSELEKHQLYIDETVNSNIPTNLRVLRSILENLRSKIQKLESDVSAQMEYCRTPCTVSCNIPVVSGKECEEIIRKGGETSEMYLIQPDSSVKPYRVYCDMNTENGGWTVIQNRQDGSVDFGRKWDPYKQGFGNVATNTDGKNYCGLPGEYWLGNDKISQLTRMGPTELLIEMEDWKGDKVKAHYGGFTVQNEANKYQISVNKYRGTAGNALMDGASQLMGENRTMTIHNGMFFSTYDRDNDGWLTSDPRKQCSKEDGGGWWYNRCHAANPNGRYYWGGQYTWDMAKHGTDDGVVWMNWKGSWYSMRKMSMKIRPFFPQQ
| null | null |
adaptive immune response [GO:0002250]; blood coagulation, fibrin clot formation [GO:0072378]; cell-matrix adhesion [GO:0007160]; cellular response to interleukin-1 [GO:0071347]; cellular response to leptin stimulus [GO:0044320]; fibrinolysis [GO:0042730]; induction of bacterial agglutination [GO:0043152]; innate immune response [GO:0045087]; negative regulation of endothelial cell apoptotic process [GO:2000352]; negative regulation of extrinsic apoptotic signaling pathway via death domain receptors [GO:1902042]; plasminogen activation [GO:0031639]; platelet aggregation [GO:0070527]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of exocytosis [GO:0045921]; positive regulation of heterotypic cell-cell adhesion [GO:0034116]; positive regulation of peptide hormone secretion [GO:0090277]; positive regulation of protein secretion [GO:0050714]; positive regulation of substrate adhesion-dependent cell spreading [GO:1900026]; positive regulation of vasoconstriction [GO:0045907]; protein polymerization [GO:0051258]; protein-containing complex assembly [GO:0065003]; response to calcium ion [GO:0051592]
|
blood microparticle [GO:0072562]; cell cortex [GO:0005938]; cell surface [GO:0009986]; collagen-containing extracellular matrix [GO:0062023]; endoplasmic reticulum [GO:0005783]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; extracellular vesicle [GO:1903561]; fibrinogen complex [GO:0005577]; plasma membrane [GO:0005886]; platelet alpha granule [GO:0031091]; platelet alpha granule lumen [GO:0031093]; synapse [GO:0045202]
|
extracellular matrix structural constituent [GO:0005201]; protein-folding chaperone binding [GO:0051087]; signaling receptor binding [GO:0005102]; structural molecule activity [GO:0005198]
|
PF08702;PF00147;
|
1.20.5.50;3.90.215.10;
| null |
PTM: Conversion of fibrinogen to fibrin is triggered by thrombin, which cleaves fibrinopeptides A and B from alpha and beta chains, and thus exposes the N-terminal polymerization sites responsible for the formation of the soft clot. The soft clot is converted into the hard clot by factor XIIIA which catalyzes the epsilon-(gamma-glutamyl)lysine cross-linking between gamma chains (stronger) and between alpha chains (weaker) of different monomers. {ECO:0000269|PubMed:2143188}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10074346, ECO:0000269|PubMed:19296670, ECO:0000269|PubMed:9628725}.
| null | null | null | null | null |
FUNCTION: Cleaved by the protease thrombin to yield monomers which, together with fibrinogen alpha (FGA) and fibrinogen gamma (FGG), polymerize to form an insoluble fibrin matrix. Fibrin has a major function in hemostasis as one of the primary components of blood clots. In addition, functions during the early stages of wound repair to stabilize the lesion and guide cell migration during re-epithelialization. Was originally thought to be essential for platelet aggregation, based on in vitro studies using anticoagulated blood. However subsequent studies have shown that it is not absolutely required for thrombus formation in vivo. Enhances expression of SELP in activated platelets. Maternal fibrinogen is essential for successful pregnancy. Fibrin deposition is also associated with infection, where it protects against IFNG-mediated hemorrhage. May also facilitate the antibacterial immune response via both innate and T-cell mediated pathways. {ECO:0000250|UniProtKB:E9PV24}.
|
Homo sapiens (Human)
|
P02676
|
FIBB_BOVIN
|
QFPTDYDEGQDDRPKVGLGARGHRPYDKKKEEAPSLRPVPPPISGGGYRARPATATVGQKKVERKPPDADGCLHADPDLGVLCPTGCKLQDTLVRQERPIRKSIEDLRNTVDSVSRTSSSTFQYITLLKNMWKGRQNQVQDNENVVNEYSSHLEKHQLYIDETVKNNIPTKLRVLRSILENLRSKIQKLESDVSTQMEYCRTPCTVTCNIPVVSGKECEKIIRNEGETSEMYLIQPEDSSKPYRVYCDMKTEKGGWTVIQNRQDGSVDFGRKWDPYKQGFGNIATNAEGKKYCGVPGEYWLGNDRISQLTNMGPTKLLIEMEDWKGDKVTALYEGFTVQNEANKYQLSVSKYKGTAGNALIEGASQLVGENRTMTIHNSMFFSTYDRDNDGWKTTDPRKQCSKEDGGGWWYNRCHAANPNGRYYWGGAYTWDMAKHGTDDGVVWMNWQGSWYSMKKMSMKIRPYFPEQ
| null | null |
adaptive immune response [GO:0002250]; blood coagulation, fibrin clot formation [GO:0072378]; cell-matrix adhesion [GO:0007160]; innate immune response [GO:0045087]; platelet aggregation [GO:0070527]; protein polymerization [GO:0051258]
|
collagen-containing extracellular matrix [GO:0062023]; extracellular space [GO:0005615]; fibrinogen complex [GO:0005577]
|
signaling receptor binding [GO:0005102]
|
PF08702;PF00147;
|
1.20.5.50;3.90.215.10;
| null |
PTM: Conversion of fibrinogen to fibrin is triggered by thrombin, which cleaves fibrinopeptides A and B from alpha and beta chains, and thus exposes the N-terminal polymerization sites responsible for the formation of the soft clot. The soft clot is converted into the hard clot by factor XIIIA which catalyzes the epsilon-(gamma-glutamyl)lysine cross-linking between gamma chains (stronger) and between alpha chains (weaker) of different monomers.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11593005}.
| null | null | null | null | null |
FUNCTION: Cleaved by the protease thrombin to yield monomers which, together with fibrinogen alpha (FGA) and fibrinogen gamma (FGG), polymerize to form an insoluble fibrin matrix. Fibrin has a major function in hemostasis as one of the primary components of blood clots. In addition, functions during the early stages of wound repair to stabilize the lesion and guide cell migration during re-epithelialization. Was originally thought to be essential for platelet aggregation, based on in vitro studies using anticoagulated blood. However subsequent studies have shown that it is not absolutely required for thrombus formation in vivo. Enhances expression of SELP in activated platelets. Maternal fibrinogen is essential for successful pregnancy. Fibrin deposition is also associated with infection, where it protects against IFNG-mediated hemorrhage. May also facilitate the antibacterial immune response via both innate and T-cell mediated pathways. {ECO:0000250|UniProtKB:E9PV24}.
|
Bos taurus (Bovine)
|
P02679
|
FIBG_HUMAN
|
MSWSLHPRNLILYFYALLFLSSTCVAYVATRDNCCILDERFGSYCPTTCGIADFLSTYQTKVDKDLQSLEDILHQVENKTSEVKQLIKAIQLTYNPDESSKPNMIDAATLKSRKMLEEIMKYEASILTHDSSIRYLQEIYNSNNQKIVNLKEKVAQLEAQCQEPCKDTVQIHDITGKDCQDIANKGAKQSGLYFIKPLKANQQFLVYCEIDGSGNGWTVFQKRLDGSVDFKKNWIQYKEGFGHLSPTGTTEFWLGNEKIHLISTQSAIPYALRVELEDWNGRTSTADYAMFKVGPEADKYRLTYAYFAGGDAGDAFDGFDFGDDPSDKFFTSHNGMQFSTWDNDNDKFEGNCAEQDGSGWWMNKCHAGHLNGVYYQGGTYSKASTPNGYDNGIIWATWKTRWYSMKKTTMKIIPFNRLTIGEGQQHHLGGAKQVRPEHPAETEYDSLYPEDDL
| null | null |
blood coagulation, fibrin clot formation [GO:0072378]; cell-matrix adhesion [GO:0007160]; cellular response to interleukin-1 [GO:0071347]; cellular response to interleukin-6 [GO:0071354]; fibrinolysis [GO:0042730]; negative regulation of endothelial cell apoptotic process [GO:2000352]; negative regulation of extrinsic apoptotic signaling pathway via death domain receptors [GO:1902042]; plasminogen activation [GO:0031639]; platelet aggregation [GO:0070527]; platelet maturation [GO:0036345]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of exocytosis [GO:0045921]; positive regulation of heterotypic cell-cell adhesion [GO:0034116]; positive regulation of peptide hormone secretion [GO:0090277]; positive regulation of protein secretion [GO:0050714]; positive regulation of substrate adhesion-dependent cell spreading [GO:1900026]; positive regulation of vasoconstriction [GO:0045907]; protein polymerization [GO:0051258]; protein secretion [GO:0009306]; protein-containing complex assembly [GO:0065003]; response to calcium ion [GO:0051592]
|
blood microparticle [GO:0072562]; cell surface [GO:0009986]; collagen-containing extracellular matrix [GO:0062023]; endoplasmic reticulum lumen [GO:0005788]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; fibrinogen complex [GO:0005577]; plasma membrane [GO:0005886]; platelet alpha granule [GO:0031091]; platelet alpha granule lumen [GO:0031093]
|
cell adhesion molecule binding [GO:0050839]; extracellular matrix structural constituent [GO:0005201]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; signaling receptor binding [GO:0005102]; structural molecule activity [GO:0005198]
|
PF08702;PF00147;
|
1.20.5.50;3.90.215.10;4.10.530.10;
| null |
PTM: Conversion of fibrinogen to fibrin is triggered by thrombin, which cleaves fibrinopeptides A and B from alpha and beta chains, and thus exposes the N-terminal polymerization sites responsible for the formation of the soft clot. The soft clot is converted into the hard clot by factor XIIIA which catalyzes the epsilon-(gamma-glutamyl)lysine cross-linking between gamma chains (stronger) and between alpha chains (weaker) of different monomers. {ECO:0000269|PubMed:2143188}.; PTM: Sulfation of C-terminal tyrosines increases affinity for thrombin. {ECO:0000269|PubMed:11307817, ECO:0000269|PubMed:1892842}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10074346, ECO:0000269|PubMed:19296670, ECO:0000269|PubMed:9628725}.
| null | null | null | null | null |
FUNCTION: Together with fibrinogen alpha (FGA) and fibrinogen beta (FGB), polymerizes to form an insoluble fibrin matrix. Has a major function in hemostasis as one of the primary components of blood clots. In addition, functions during the early stages of wound repair to stabilize the lesion and guide cell migration during re-epithelialization. Was originally thought to be essential for platelet aggregation, based on in vitro studies using anticoagulated blood. However, subsequent studies have shown that it is not absolutely required for thrombus formation in vivo. Enhances expression of SELP in activated platelets via an ITGB3-dependent pathway. Maternal fibrinogen is essential for successful pregnancy. Fibrin deposition is also associated with infection, where it protects against IFNG-mediated hemorrhage. May also facilitate the antibacterial immune response via both innate and T-cell mediated pathways. {ECO:0000250|UniProtKB:E9PV24}.
|
Homo sapiens (Human)
|
P02680
|
FIBG_RAT
|
MNWSLQLRSFILCWALLLLSPTGLAQYTATRDNCCILDERFGSYCPTTCGISDFLNSYQTDVDTDLQTLENILQRAENRTTEAKELIKAIQVYYNPDQPPKPGMIEGATQKSKKMVEEILKYEALLLTHESSIRYLQDIYTSNKQKITNLKQKVAQLEAQCQEPCKDSVRIHDTTGKDCQDIANKGAKESGLYFIRPLKATQQFLVYCEIDGSGNGWTVLQKRLDGSVDFKKNWIQYKEGFGHLSPTGTTEFWLGNEKIHLISMQSTIPYALRIQLKDWSGRTSTADYAMFRVGPESDKYRLTYAYFIGGDAGDAFDGYDFGDDPSDKFFTSHNGMHFSTWDNDNDKFEGNCAEQDGSGWWMNKCHAGHLNGVYYQGGTYSKSSTPNGYDNGIIWATWKTRWYSMKETTMKIIPFNRLSIGDGQQHHMGGSKQVSVEHEVDVEYP
| null | null |
blood coagulation, fibrin clot formation [GO:0072378]; cell-matrix adhesion [GO:0007160]; cellular response to interleukin-1 [GO:0071347]; cellular response to interleukin-6 [GO:0071354]; fibrinolysis [GO:0042730]; negative regulation of endothelial cell apoptotic process [GO:2000352]; negative regulation of extrinsic apoptotic signaling pathway via death domain receptors [GO:1902042]; plasminogen activation [GO:0031639]; platelet aggregation [GO:0070527]; platelet maturation [GO:0036345]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of exocytosis [GO:0045921]; positive regulation of heterotypic cell-cell adhesion [GO:0034116]; positive regulation of peptide hormone secretion [GO:0090277]; positive regulation of protein secretion [GO:0050714]; positive regulation of vasoconstriction [GO:0045907]; protein polymerization [GO:0051258]; protein secretion [GO:0009306]; protein-containing complex assembly [GO:0065003]; response to calcium ion [GO:0051592]
|
blood microparticle [GO:0072562]; cell cortex [GO:0005938]; cell surface [GO:0009986]; collagen-containing extracellular matrix [GO:0062023]; external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; fibrinogen complex [GO:0005577]; platelet alpha granule [GO:0031091]; synapse [GO:0045202]
|
cell adhesion molecule binding [GO:0050839]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; signaling receptor binding [GO:0005102]; structural molecule activity [GO:0005198]
|
PF08702;PF00147;
|
1.20.5.50;3.90.215.10;4.10.530.10;
| null |
PTM: Conversion of fibrinogen to fibrin is triggered by thrombin, which cleaves fibrinopeptides A and B from alpha and beta chains, and thus exposes the N-terminal polymerization sites responsible for the formation of the soft clot. The soft clot is converted into the hard clot by factor XIIIA which catalyzes the epsilon-(gamma-glutamyl)lysine cross-linking between gamma chains (stronger) and between alpha chains (weaker) of different monomers.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02679}.
| null | null | null | null | null |
FUNCTION: Together with fibrinogen alpha (FGA) and fibrinogen beta (FGB), polymerizes to form an insoluble fibrin matrix. Has a major function in hemostasis as one of the primary components of blood clots. In addition, functions during the early stages of wound repair to stabilize the lesion and guide cell migration during re-epithelialization. Was originally thought to be essential for platelet aggregation, based on in vitro studies using anticoagulated blood. However, subsequent studies have shown that it is not absolutely required for thrombus formation in vivo. Enhances expression of SELP in activated platelets via an ITGB3-dependent pathway. Maternal fibrinogen is essential for successful pregnancy. Fibrin deposition is also associated with infection, where it protects against IFNG-mediated hemorrhage. May also facilitate the antibacterial immune response via both innate and T-cell mediated pathways. {ECO:0000250|UniProtKB:E9PV24}.
|
Rattus norvegicus (Rat)
|
P02683
|
NSG1_RAT
|
MVKLGNNFAEKGTKQPLLEDGFDTIPLMTPLDVNQLQFPPPDKVVVKTKTEYEPDRKKGKARPPKIAEFTVSITEGVTERFKVSVLVLFALAFLTCVVFLVVYKVYKYDRACPDGFVLKNTQCIPEGLESYYTEQDSSAREKFYTVINHYNLAKQSITRSVSPWMSVLSEEKLSEQETEAAEKSA
| null | null |
amyloid precursor protein metabolic process [GO:0042982]; apoptotic process [GO:0006915]; clathrin coat assembly [GO:0048268]; dopamine receptor signaling pathway [GO:0007212]; endosomal transport [GO:0016197]; neurotransmitter receptor cycle [GO:0099627]; neurotransmitter receptor transport, endosome to postsynaptic membrane [GO:0098887]; positive regulation of receptor recycling [GO:0001921]; postsynaptic neurotransmitter receptor cycle [GO:0099630]; receptor recycling [GO:0001881]; regulation of long-term synaptic potentiation [GO:1900271]; spontaneous synaptic transmission [GO:0098814]; vesicle-mediated transport in synapse [GO:0099003]
|
dendrite [GO:0030425]; early endosome [GO:0005769]; early endosome membrane [GO:0031901]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; endosome [GO:0005768]; glutamatergic synapse [GO:0098978]; Golgi cisterna membrane [GO:0032580]; late endosome [GO:0005770]; lateral plasma membrane [GO:0016328]; lysosomal lumen [GO:0043202]; multivesicular body membrane [GO:0032585]; postsynaptic endosome [GO:0098845]; postsynaptic membrane [GO:0045211]; recycling endosome membrane [GO:0055038]; somatodendritic compartment [GO:0036477]; trans-Golgi network membrane [GO:0032588]
|
clathrin light chain binding [GO:0032051]; ionotropic glutamate receptor binding [GO:0035255]; signaling receptor binding [GO:0005102]
|
PF06387;
| null |
NSG family
| null |
SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:28874679}; Single-pass type II membrane protein {ECO:0000269|PubMed:28874679}. Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:28874679}. Endosome membrane {ECO:0000269|PubMed:18299352, ECO:0000269|PubMed:28874679}. Cell projection, dendrite {ECO:0000269|PubMed:12070131, ECO:0000269|PubMed:28874679}. Early endosome membrane {ECO:0000269|PubMed:12070131, ECO:0000269|PubMed:28874679}. Late endosome membrane {ECO:0000269|PubMed:28874679}. Lysosome lumen {ECO:0000269|PubMed:28874679}. Recycling endosome membrane {ECO:0000269|PubMed:12070131}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:9461575}. Golgi apparatus, Golgi stack membrane {ECO:0000269|PubMed:9461575}. Endosome, multivesicular body membrane {ECO:0000269|PubMed:9461575}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P42857}. Note=Endocytosed from the cell surface, thus enters into early endosomes, trafficks to late endosomes and degradates in lysosomes (PubMed:28874679). Endoplasmic reticulum targeting is essential for apoptosis (By similarity). Found in both stationary and motile endosomes. A previous study supports a type I membrane protein topology (By similarity). {ECO:0000250|UniProtKB:P42857, ECO:0000250|UniProtKB:Q62092, ECO:0000269|PubMed:28874679}.
| null | null | null | null | null |
FUNCTION: Plays a role in the recycling mechanism in neurons of multiple receptors, including AMPAR, APP and L1CAM and acts at the level of early endosomes to promote sorting of receptors toward a recycling pathway (PubMed:15911354, PubMed:18299352). Regulates sorting and recycling of GRIA2 through interaction with GRIP1 and then contributes to the regulation of synaptic transmission and plasticity by affecting the recycling and targeting of AMPA receptors to the synapse (PubMed:15911354). Is required for faithful sorting of L1CAM to axons by facilitating trafficking from somatodendritic early endosome or the recycling endosome (PubMed:18299352). In an other hand, induces apoptosis via the activation of CASP3 in response to DNA damage (By similarity). {ECO:0000250|UniProtKB:P42857, ECO:0000269|PubMed:15911354, ECO:0000269|PubMed:18299352}.
|
Rattus norvegicus (Rat)
|
P02686
|
MBP_HUMAN
|
MGNHAGKRELNAEKASTNSETNRGESEKKRNLGELSRTTSEDNEVFGEADANQNNGTSSQDTAVTDSKRTADPKNAWQDAHPADPGSRPHLIRLFSRDAPGREDNTFKDRPSESDELQTIQEDSAATSESLDVMASQKRPSQRHGSKYLATASTMDHARHGFLPRHRDTGILDSIGRFFGGDRGAPKRGSGKDSHHPARTAHYGSLPQKSHGRTQDENPVVHFFKNIVTPRTPPPSQGKGRGLSLSRFSWGAEGQRPGFGYGGRASDYKSAHKGFKGVDAQGTLSKIFKLGGRDSRSGSPMARR
| null | null |
axon ensheathment [GO:0008366]; central nervous system development [GO:0007417]; chemical synaptic transmission [GO:0007268]; immune response [GO:0006955]; maintenance of blood-brain barrier [GO:0035633]; MAPK cascade [GO:0000165]; membrane organization [GO:0061024]; myelination [GO:0042552]; negative regulation of heterotypic cell-cell adhesion [GO:0034115]; positive regulation of chemokine (C-X-C motif) ligand 2 production [GO:2000343]; positive regulation of interleukin-6 production [GO:0032755]; positive regulation of metalloendopeptidase activity [GO:1904685]; response to toxic substance [GO:0009636]; sensory perception of sound [GO:0007605]; substantia nigra development [GO:0021762]
|
cell periphery [GO:0071944]; cell surface [GO:0009986]; compact myelin [GO:0043218]; cytosol [GO:0005829]; internode region of axon [GO:0033269]; myelin sheath [GO:0043209]; neuronal cell body [GO:0043025]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]; synapse [GO:0045202]
|
calmodulin binding [GO:0005516]; lipid binding [GO:0008289]; protease binding [GO:0002020]; structural constituent of myelin sheath [GO:0019911]
|
PF01669;
| null |
Myelin basic protein family
|
PTM: Several charge isomers of MBP; C1 (the most cationic, least modified, and most abundant form), C2, C3, C4, C5, C6, C7, C8-A and C8-B (the least cationic form); are produced as a result of optional PTM, such as phosphorylation, deamidation of glutamine or asparagine, arginine citrullination and methylation. C8-A and C8-B contain each two mass isoforms termed C8-A(H), C8-A(L), C8-B(H) and C8-B(L), (H) standing for higher and (L) for lower molecular weight. C3, C4 and C5 are phosphorylated. The ratio of methylated arginine residues decreases during aging, making the protein more cationic. {ECO:0000269|PubMed:23828821, ECO:0000269|PubMed:2466844, ECO:0000269|PubMed:5128665}.; PTM: The N-terminal alanine is acetylated (isoform 3, isoform 4, isoform 5 and isoform 6).; PTM: Arg-241 was found to be 6% monomethylated and 60% symmetrically dimethylated.; PTM: Proteolytically cleaved in B cell lysosomes by cathepsin CTSG which degrades the major immunogenic MBP epitope and prevents the activation of MBP-specific autoreactive T cells. {ECO:0000269|PubMed:15100291}.; PTM: Phosphorylated by TAOK2, VRK2, MAPK11, MAPK12, MAPK14 and MINK1.
|
SUBCELLULAR LOCATION: Myelin membrane; Peripheral membrane protein; Cytoplasmic side. Note=Cytoplasmic side of myelin.; SUBCELLULAR LOCATION: [Isoform 3]: Nucleus {ECO:0000269|PubMed:22609403}. Note=Targeted to nucleus in oligodendrocytes.
| null | null | null | null | null |
FUNCTION: The classic group of MBP isoforms (isoform 4-isoform 14) are with PLP the most abundant protein components of the myelin membrane in the CNS. They have a role in both its formation and stabilization. The smaller isoforms might have an important role in remyelination of denuded axons in multiple sclerosis. The non-classic group of MBP isoforms (isoform 1-isoform 3/Golli-MBPs) may preferentially have a role in the early developing brain long before myelination, maybe as components of transcriptional complexes, and may also be involved in signaling pathways in T-cells and neural cells. Differential splicing events combined with optional post-translational modifications give a wide spectrum of isomers, with each of them potentially having a specialized function. Induces T-cell proliferation. {ECO:0000269|PubMed:8544862}.
|
Homo sapiens (Human)
|
P02687
|
MBP_BOVIN
|
AAQKRPSQRSKYLASASTMDHARHGFLPRHRDTGILDSLGRFFGSDRGAPKRGSGKDGHHAARTTHYGSLPQKAQGHRPQDENPVVHFFKNIVTPRTPPPSQGKGRGLSLSRFSWGAEGQKPGFGYGGRASDYKSAHKGLKGHDAQGTLSKIFKLGGRDSRSGSPMARR
| null | null |
myelination [GO:0042552]
|
cell periphery [GO:0071944]; compact myelin [GO:0043218]; internode region of axon [GO:0033269]; myelin sheath [GO:0043209]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]
|
calmodulin binding [GO:0005516]; lipid binding [GO:0008289]; phospholipid binding [GO:0005543]; structural constituent of myelin sheath [GO:0019911]
|
PF01669;
| null |
Myelin basic protein family
|
PTM: At least 6 charge isomers; C1 (the most cationic and least modified form), C2, C3, C4, C5 and C6 (the least cationic form); are produced as a result of optional post-translational modifications, such as phosphorylation of serine or threonine residues, deamidation of glutamine or asparagine residues, citrullination and methylation of arginine residues. {ECO:0000269|PubMed:1700979, ECO:0000269|PubMed:22420465, ECO:0000269|PubMed:23828821, ECO:0000269|PubMed:4994464}.; PTM: Phosphorylated by TAOK2, VRK2, MAPK11, MAPK12, MAPK14 and MINK1. {ECO:0000250}.; PTM: Proteolytically cleaved in B cell lysosomes by cathepsin CTSG which degrades the major immunogenic MBP epitope and prevents the activation of MBP-specific autoreactive T cells. {ECO:0000250|UniProtKB:P02686}.
|
SUBCELLULAR LOCATION: Myelin membrane; Peripheral membrane protein; Cytoplasmic side. Note=Cytoplasmic side of myelin.
| null | null | null | null | null |
FUNCTION: Is, with PLP, the most abundant protein component of the myelin membrane in the CNS. Has a role in both the formation and stabilization of this compact multilayer arrangement of bilayers. Each splice variant and charge isomer may have a specialized function in the assembly of an optimized, biochemically functional myelin membrane (By similarity). {ECO:0000250}.
|
Bos taurus (Bovine)
|
P02688
|
MBP_RAT
|
MASQKRPSQRHGSKYLATASTMDHARHGFLPRHRDTGILDSIGRFFSGDRGAPKRGSGKVPWLKQSRSPLPSHARSRPGLCHMYKDSHTRTTHYGSLPQKSQRTQDENPVVHFFKNIVTPRTPPPSQGKGRGLSLSRFSWGAEGQKPGFGYGGRASDYKSAHKGFKGAYDAQGTLSKIFKLGGRDSRSGSPMARR
| null | null |
maintenance of blood-brain barrier [GO:0035633]; MAPK cascade [GO:0000165]; membrane organization [GO:0061024]; myelination [GO:0042552]; negative regulation of axonogenesis [GO:0050771]; negative regulation of heterotypic cell-cell adhesion [GO:0034115]; positive regulation of chemokine (C-X-C motif) ligand 2 production [GO:2000343]; positive regulation of interleukin-6 production [GO:0032755]; response to fatty acid [GO:0070542]; response to mercury ion [GO:0046689]; response to progesterone [GO:0032570]; response to toxic substance [GO:0009636]; response to tumor necrosis factor [GO:0034612]; sensory perception of sound [GO:0007605]
|
cell periphery [GO:0071944]; cell projection [GO:0042995]; cell surface [GO:0009986]; compact myelin [GO:0043218]; internode region of axon [GO:0033269]; myelin sheath [GO:0043209]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]
|
calmodulin binding [GO:0005516]; protease binding [GO:0002020]; structural constituent of myelin sheath [GO:0019911]
|
PF01669;
| null |
Myelin basic protein family
|
PTM: As in other animals, several charge isomers may be produced as a result of optional post-translational modifications, such as phosphorylation of serine or threonine residues, deamidation of glutamine or asparagine residues, citrullination and methylation of arginine residues. {ECO:0000269|PubMed:4141893, ECO:0000269|Ref.10}.; PTM: Arg-131 was found to be 44% monomethylated and 11% symmetrically dimethylated.; PTM: Phosphorylated by TAOK2, VRK2, MAPK11, MAPK12, MAPK14 and MINK1. {ECO:0000250}.; PTM: Proteolytically cleaved in B cell lysosomes by cathepsin CTSG which degrades the major immunogenic MBP epitope and prevents the activation of MBP-specific autoreactive T cells. {ECO:0000250|UniProtKB:P02686}.
|
SUBCELLULAR LOCATION: Myelin membrane; Peripheral membrane protein; Cytoplasmic side. Note=Cytoplasmic side of myelin.
| null | null | null | null | null |
FUNCTION: Is, with PLP, the most abundant protein component of the myelin membrane in the CNS. Has a role in both the formation and stabilization of this compact multilayer arrangement of bilayers. Each splice variant and charge isomer may have a specialized function in the assembly of an optimized, biochemically functional myelin membrane (By similarity). {ECO:0000250}.
|
Rattus norvegicus (Rat)
|
P02689
|
MYP2_HUMAN
|
MSNKFLGTWKLVSSENFDDYMKALGVGLATRKLGNLAKPTVIISKKGDIITIRTESTFKNTEISFKLGQEFEETTADNRKTKSIVTLQRGSLNQVQRWDGKETTIKRKLVNGKMVAECKMKGVVCTRIYEKV
| null | null |
fatty acid transport [GO:0015908]; membrane organization [GO:0061024]
|
cytosol [GO:0005829]; extracellular exosome [GO:0070062]; myelin sheath [GO:0043209]; nucleus [GO:0005634]
|
cholesterol binding [GO:0015485]; fatty acid binding [GO:0005504]
|
PF00061;
|
2.40.128.20;
|
Calycin superfamily, Fatty-acid binding protein (FABP) family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: May play a role in lipid transport protein in Schwann cells. May bind cholesterol. {ECO:0000269|PubMed:20421974}.
|
Homo sapiens (Human)
|
P02690
|
MYP2_BOVIN
|
MSNKFLGTWKLVSSENFDEYMKALGVGLATRKLGNLAKPRVIISKKGDIITIRTESPFKNTEISFKLGQEFEETTADNRKTKSTVTLARGSLNQVQKWDGNETTIKRKLVDGKMVVECKMKDVVCTRIYEKV
| null | null |
fatty acid transport [GO:0015908]; membrane organization [GO:0061024]
|
cytosol [GO:0005829]; myelin sheath [GO:0043209]; nucleus [GO:0005634]
|
cholesterol binding [GO:0015485]; fatty acid binding [GO:0005504]
|
PF00061;
|
2.40.128.20;
|
Calycin superfamily, Fatty-acid binding protein (FABP) family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: May play a role in lipid transport protein in Schwann cells. May bind cholesterol.
|
Bos taurus (Bovine)
|
P02692
|
FABPL_RAT
|
MNFSGKYQVQSQENFEPFMKAMGLPEDLIQKGKDIKGVSEIVHEGKKVKLTITYGSKVIHNEFTLGEECELETMTGEKVKAVVKMEGDNKMVTTFKGIKSVTEFNGDTITNTMTLGDIVYKRVSKRI
| null | null |
cellular response to hydrogen peroxide [GO:0070301]; cellular response to hypoxia [GO:0071456]; fatty acid transport [GO:0015908]; intestinal absorption [GO:0050892]; long-chain fatty acid transport [GO:0015909]; negative regulation of apoptotic process [GO:0043066]; positive regulation of fatty acid beta-oxidation [GO:0032000]; response to vitamin B3 [GO:0033552]
|
apical cortex [GO:0045179]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; peroxisomal matrix [GO:0005782]; protein-containing complex [GO:0032991]
|
antioxidant activity [GO:0016209]; bile acid binding [GO:0032052]; chromatin binding [GO:0003682]; fatty acid binding [GO:0005504]; heterocyclic compound binding [GO:1901363]; long-chain fatty acid transporter activity [GO:0005324]; lysophospholipid:sodium symporter activity [GO:0051978]; oleic acid binding [GO:0070538]; phospholipid binding [GO:0005543]
|
PF14651;
|
2.40.128.20;
|
Calycin superfamily, Fatty-acid binding protein (FABP) family
|
PTM: Deamidation and transpeptidation at the beta carboxyl of Asn-105 forms an isoaspartyl residue found in an isoform of the DE-III fraction. This rearrangement gives rise to an extra negative charge carried by the acid form. {ECO:0000269|PubMed:8117116}.
|
SUBCELLULAR LOCATION: Cytoplasm.
| null | null | null | null | null |
FUNCTION: Plays a role in lipoprotein-mediated cholesterol uptake in hepatocytes (By similarity). Binds cholesterol (PubMed:25732850). Binds free fatty acids and their coenzyme A derivatives, bilirubin, and some other small molecules in the cytoplasm. May be involved in intracellular lipid transport (By similarity). {ECO:0000250|UniProtKB:P82289, ECO:0000269|PubMed:25732850}.
|
Rattus norvegicus (Rat)
|
P02693
|
FABPI_RAT
|
MAFDGTWKVDRNENYEKFMEKMGINVVKRKLGAHDNLKLTITQEGNKFTVKESSNFRNIDVVFELGVDFAYSLADGTELTGTWTMEGNKLVGKFKRVDNGKELIAVREISGNELIQTYTYEGVEAKRIFKKE
| null | null |
fatty acid metabolic process [GO:0006631]; fatty acid transport [GO:0015908]; intestinal absorption [GO:0050892]; intestinal lipid absorption [GO:0098856]; long-chain fatty acid transport [GO:0015909]
|
apical cortex [GO:0045179]; cytosol [GO:0005829]; microvillus [GO:0005902]; nucleus [GO:0005634]
|
fatty acid binding [GO:0005504]; long-chain fatty acid binding [GO:0036041]; long-chain fatty acid transporter activity [GO:0005324]
|
PF00061;
|
2.40.128.20;
|
Calycin superfamily, Fatty-acid binding protein (FABP) family
| null |
SUBCELLULAR LOCATION: Cytoplasm.
| null | null | null | null | null |
FUNCTION: FABPs are thought to play a role in the intracellular transport of long-chain fatty acids and their acyl-CoA esters. FABP2 is probably involved in triglyceride-rich lipoprotein synthesis. Binds saturated long-chain fatty acids with a high affinity, but binds with a lower affinity to unsaturated long-chain fatty acids. FABP2 may also help maintain energy homeostasis by functioning as a lipid sensor (By similarity). {ECO:0000250}.
|
Rattus norvegicus (Rat)
|
P02696
|
RET1_RAT
|
MPVDFNGYWKMLSNENFEEYLRALDVNVALRKIANLLKPDKEIVQDGDHMIIRTLSTFRNYIMDFQVGKEFEEDLTGIDDRKCMTTVSWDGDKLQCVQKGEKEGRGWTQWIEGDELHLEMRAEGVTCKQVFKKVH
| null | null |
fatty acid transport [GO:0015908]; lipid homeostasis [GO:0055088]; regulation of granulocyte differentiation [GO:0030852]; response to benzoic acid [GO:0080021]; response to retinoic acid [GO:0032526]; response to vitamin A [GO:0033189]; retinoic acid biosynthetic process [GO:0002138]; retinoic acid metabolic process [GO:0042573]; retinol metabolic process [GO:0042572]; vitamin A metabolic process [GO:0006776]
|
cell body [GO:0044297]; cytosol [GO:0005829]; lipid droplet [GO:0005811]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
all-trans-retinol binding [GO:1904768]; fatty acid binding [GO:0005504]; retinal binding [GO:0016918]; retinol binding [GO:0019841]
|
PF00061;
|
2.40.128.20;
|
Calycin superfamily, Fatty-acid binding protein (FABP) family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q00915}. Lipid droplet {ECO:0000250|UniProtKB:Q00915}.
| null | null | null | null | null |
FUNCTION: Cytoplasmic retinol-binding protein (PubMed:12850148, PubMed:7683727). Accepts retinol from the transport protein STRA6, and thereby contributes to retinol uptake, storage and retinoid homeostasis (By similarity). {ECO:0000250|UniProtKB:P09455, ECO:0000269|PubMed:12850148, ECO:0000269|PubMed:7683727}.
|
Rattus norvegicus (Rat)
|
P02698
|
GBG1_BOVIN
|
MPVINIEDLTEKDKLKMEVDQLKKEVTLERMLVSKCCEEFRDYVEERSGEDPLVKGIPEDKNPFKELKGGCVIS
| null | null |
G protein-coupled receptor signaling pathway [GO:0007186]
|
heterotrimeric G-protein complex [GO:0005834]; photoreceptor disc membrane [GO:0097381]
|
G-protein beta-subunit binding [GO:0031681]
|
PF00631;
|
4.10.260.10;
|
G protein gamma family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction.
|
Bos taurus (Bovine)
|
P02699
|
OPSD_BOVIN
|
MNGTEGPNFYVPFSNKTGVVRSPFEAPQYYLAEPWQFSMLAAYMFLLIMLGFPINFLTLYVTVQHKKLRTPLNYILLNLAVADLFMVFGGFTTTLYTSLHGYFVFGPTGCNLEGFFATLGGEIALWSLVVLAIERYVVVCKPMSNFRFGENHAIMGVAFTWVMALACAAPPLVGWSRYIPEGMQCSCGIDYYTPHEETNNESFVIYMFVVHFIIPLIVIFFCYGQLVFTVKEAAAQQQESATTQKAEKEVTRMVIIMVIAFLICWLPYAGVAFYIFTHQGSDFGPIFMTIPAFFAKTSAVYNPVIYIMMNKQFRNCMVTTLCCGKNPLGDDEASTTVSKTETSQVAPA
| null | null |
absorption of visible light [GO:0016038]; adaptation of rhodopsin mediated signaling [GO:0016062]; cellular response to light stimulus [GO:0071482]; detection of temperature stimulus involved in thermoception [GO:0050960]; G protein-coupled receptor signaling pathway [GO:0007186]; gene expression [GO:0010467]; microtubule cytoskeleton organization [GO:0000226]; photoreceptor cell maintenance [GO:0045494]; phototransduction [GO:0007602]; phototransduction, visible light [GO:0007603]; podosome assembly [GO:0071800]; response to light stimulus [GO:0009416]; rhodopsin mediated signaling pathway [GO:0016056]; rod bipolar cell differentiation [GO:1904389]; thermotaxis [GO:0043052]; visual perception [GO:0007601]
|
cell-cell junction [GO:0005911]; G protein-coupled receptor complex [GO:0097648]; Golgi membrane [GO:0000139]; membrane [GO:0016020]; outer membrane [GO:0019867]; photoreceptor disc membrane [GO:0097381]; photoreceptor inner segment membrane [GO:0060342]; photoreceptor outer segment [GO:0001750]; photoreceptor outer segment membrane [GO:0042622]; plasma membrane [GO:0005886]; rod photoreceptor outer segment [GO:0120200]; sperm head plasma membrane [GO:1990913]; sperm midpiece [GO:0097225]
|
11-cis retinal binding [GO:0005502]; arrestin family protein binding [GO:1990763]; G protein-coupled photoreceptor activity [GO:0008020]; G-protein alpha-subunit binding [GO:0001965]; guanyl-nucleotide exchange factor activity [GO:0005085]; identical protein binding [GO:0042802]; opsin binding [GO:0002046]; zinc ion binding [GO:0008270]
|
PF00001;PF10413;
|
1.20.1070.10;
|
G-protein coupled receptor 1 family, Opsin subfamily
|
PTM: Phosphorylated on some or all of the serine and threonine residues present in the C-terminal region. {ECO:0000269|PubMed:1396673, ECO:0000269|PubMed:15111114, ECO:0000269|PubMed:15351781}.; PTM: Contains one covalently linked retinal chromophore. Upon light absorption, the covalently bound 11-cis-retinal is converted to all-trans-retinal. After hydrolysis of the Schiff base and release of the covalently bound all-trans-retinal, active rhodopsin is regenerated by binding of a fresh molecule of 11-cis-retinal. {ECO:0000269|PubMed:10926528, ECO:0000269|PubMed:11425302, ECO:0000269|PubMed:11972040, ECO:0000269|PubMed:12044163, ECO:0000269|PubMed:15327956, ECO:0000269|PubMed:15491621, ECO:0000269|PubMed:16586416, ECO:0000269|PubMed:16908857, ECO:0000269|PubMed:17449675, ECO:0000269|PubMed:21389983, ECO:0000269|PubMed:22198838, ECO:0000269|PubMed:23303210, ECO:0000269|PubMed:27458239, ECO:0000269|PubMed:6870827, ECO:0000305|PubMed:6759163}.
|
SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:10926528, ECO:0000269|PubMed:22198838, ECO:0000269|PubMed:23303210, ECO:0000269|PubMed:27509380, ECO:0000269|PubMed:3350146, ECO:0000269|PubMed:9541408}; Multi-pass membrane protein {ECO:0000269|PubMed:10926528, ECO:0000269|PubMed:11425302, ECO:0000269|PubMed:11972040, ECO:0000269|PubMed:15327956, ECO:0000269|PubMed:15491621, ECO:0000269|PubMed:16586416, ECO:0000269|PubMed:16908857, ECO:0000269|PubMed:17060607, ECO:0000269|PubMed:17449675, ECO:0000269|PubMed:17825322, ECO:0000269|PubMed:18563085, ECO:0000269|PubMed:18645239, ECO:0000269|PubMed:18818650, ECO:0000269|PubMed:21389983, ECO:0000269|PubMed:22198838, ECO:0000269|PubMed:23579341, ECO:0000269|PubMed:25205354, ECO:0000269|PubMed:26526852, ECO:0000269|PubMed:27458239}. Cell projection, cilium, photoreceptor outer segment {ECO:0000269|PubMed:27509380, ECO:0000269|PubMed:28655769, ECO:0000269|PubMed:3350146, ECO:0000269|PubMed:9541408}. Note=Synthesized in the inner segment (IS) of rod photoreceptor cells before vectorial transport to disk membranes in the rod outer segment (OS) photosensory cilia. {ECO:0000250|UniProtKB:P08100}.
| null | null | null | null | null |
FUNCTION: Photoreceptor required for image-forming vision at low light intensity. Required for photoreceptor cell viability after birth (By similarity). Light-induced isomerization of 11-cis to all-trans retinal triggers a conformational change that activates signaling via G-proteins (PubMed:10926528, PubMed:11972040, PubMed:12044163, PubMed:16586416, PubMed:16908857, PubMed:17060607, PubMed:17449675, PubMed:18818650, PubMed:21389983, PubMed:22198838, PubMed:23579341, PubMed:25205354, PubMed:27458239). Subsequent receptor phosphorylation mediates displacement of the bound G-protein alpha subunit by the arrestin SAG and terminates signaling (PubMed:1396673, PubMed:15111114). {ECO:0000250|UniProtKB:P08100, ECO:0000269|PubMed:1396673, ECO:0000269|PubMed:16586416, ECO:0000269|PubMed:16908857, ECO:0000269|PubMed:17060607, ECO:0000269|PubMed:17449675, ECO:0000269|PubMed:18818650, ECO:0000269|PubMed:21389983, ECO:0000269|PubMed:22198838, ECO:0000269|PubMed:23579341, ECO:0000269|PubMed:25205354, ECO:0000269|PubMed:27458239, ECO:0000305|PubMed:10926528, ECO:0000305|PubMed:11972040, ECO:0000305|PubMed:12044163, ECO:0000305|PubMed:15111114, ECO:0000305|PubMed:26526852}.
|
Bos taurus (Bovine)
|
P02700
|
OPSD_SHEEP
|
MNGTEGPNFYVPFSNKTGVVRSPFEAPQYYLAEPWQFSMLAAYMFLLIVLGFPINFLTLYVTVQHKKLRTPLNYILLNLAVADLFMVFGGFTTTLYTSLHGYFVFGPTGCNLEGFFATLGGEIALWSLVVLAIERYVVVCKPMSNFRFGENHAIMGVAFTWVMALACAAPPLVGWSRYIPQGMQCSCGALYFTLKPEINNESFVIYMFVVHFSIPLIVIFFCYGQLVFTVKEAAAQQQESATTQKAEKEVTRMVIIMVIAFLICWLPYAGVAFYIFTHQGSDFGPIFMTIPAFFAKSSSVYNPVIYIMMNKQFRNCMLTTLCCGKNPLGDDEASTTVSKTETSQVAPA
| null | null |
absorption of visible light [GO:0016038]; rhodopsin mediated signaling pathway [GO:0016056]; visual perception [GO:0007601]
|
membrane [GO:0016020]; photoreceptor disc membrane [GO:0097381]; photoreceptor inner segment membrane [GO:0060342]; photoreceptor outer segment membrane [GO:0042622]; plasma membrane [GO:0005886]
|
11-cis retinal binding [GO:0005502]; G protein-coupled photoreceptor activity [GO:0008020]; metal ion binding [GO:0046872]
|
PF00001;PF10413;
|
1.20.1070.10;
|
G-protein coupled receptor 1 family, Opsin subfamily
|
PTM: Phosphorylated on some or all of the serine and threonine residues present in the C-terminal region. {ECO:0000269|PubMed:6466303}.; PTM: Contains one covalently linked retinal chromophore (PubMed:6370231, PubMed:7278988). Upon light absorption, the covalently bound 11-cis-retinal is converted to all-trans-retinal. After hydrolysis of the Schiff base and release of the covalently bound all-trans-retinal, active rhodopsin is regenerated by binding of a fresh molecule of 11-cis-retinal (By similarity). {ECO:0000250|UniProtKB:P02699, ECO:0000269|PubMed:6370231, ECO:0000269|PubMed:7278988}.
|
SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:6466303, ECO:0000269|PubMed:7278988}; Multi-pass membrane protein {ECO:0000269|PubMed:6466303, ECO:0000269|PubMed:7278988}. Cell projection, cilium, photoreceptor outer segment {ECO:0000269|PubMed:6466303, ECO:0000269|PubMed:7278988}. Note=Synthesized in the inner segment (IS) of rod photoreceptor cells before vectorial transport to disk membranes in the rod outer segment (OS) photosensory cilia. {ECO:0000250|UniProtKB:P08100}.
| null | null | null | null | null |
FUNCTION: Photoreceptor required for image-forming vision at low light intensity. Required for photoreceptor cell viability after birth (By similarity). Light-induced isomerization of 11-cis to all-trans retinal triggers a conformational change that activates signaling via G-proteins. Subsequent receptor phosphorylation mediates displacement of the bound G-protein alpha subunit by the arrestin SAG and terminates signaling (By similarity). {ECO:0000250|UniProtKB:P02699, ECO:0000250|UniProtKB:P08100}.
|
Ovis aries (Sheep)
|
P02701
|
AVID_CHICK
|
MVHATSPLLLLLLLSLALVAPGLSARKCSLTGKWTNDLGSNMTIGAVNSRGEFTGTYITAVTATSNEIKESPLHGTQNTINKRTQPTFGFTVNWKFSESTTVFTGQCFIDRNGKEVLKTMWLLRSSVNDIGDDWKATRVGINIFTRLRTQKE
| null | null |
antibacterial humoral response [GO:0019731]
|
extracellular region [GO:0005576]
|
biotin binding [GO:0009374]
|
PF01382;
|
2.40.128.30;
|
Avidin/streptavidin family
|
PTM: N-linked glycan at Asn-41 consists of GlcNAc(beta1-2)Man(alpha1-3)[GlcNAc(beta1-4)][Man(alpha1-?)Man(alpha1-6)] Man(beta1-4)GlcNAc(beta1-4)GlcNAc. {ECO:0000269|PubMed:5100763}.
|
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: The biological function of avidin is not known. Forms a strong non-covalent specific complex with biotin (one molecule of biotin per subunit of avidin).
|
Gallus gallus (Chicken)
|
P02702
|
FOLR1_BOVIN
|
MAWQMTQLLLLALVAAAWGAQAPRTPRARTDLLNVCMDAKHHKAEPGPEDSLHEQCSPWRKNACCSVNTSIEAHKDISYLYRFNWDHCGKMEPACKRHFIQDTCLYECSPNLGPWIREVNQRWRKERVLGVPLCKEDCQSWWEDCRTSYTCKSNWHKGWNWTSGYNQCPVKAACHRFDFYFPTPAALCNEIWSHSYKVSNYSRGSGRCIQMWFDPFQGNPNEEVARFYAENPTSGSTPQGI
| null | null |
cell adhesion [GO:0007155]; folic acid transport [GO:0015884]; fusion of sperm to egg plasma membrane involved in single fertilization [GO:0007342]; sperm-egg recognition [GO:0035036]
|
apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; clathrin-coated vesicle [GO:0030136]; endosome [GO:0005768]; external side of plasma membrane [GO:0009897]; extracellular region [GO:0005576]
|
folic acid binding [GO:0005542]; folic acid receptor activity [GO:0061714]; signaling receptor activity [GO:0038023]
|
PF03024;
| null |
Folate receptor family
|
PTM: The secreted form is derived from the membrane-bound form either by cleavage of the GPI anchor, or/and by proteolysis catalyzed by a metalloprotease. {ECO:0000250|UniProtKB:P15328}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P15328}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:P15328}. Apical cell membrane {ECO:0000250|UniProtKB:P15328}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:P15328}. Basolateral cell membrane {ECO:0000250|UniProtKB:P15328}; Lipid-anchor, GPI-like-anchor {ECO:0000250|UniProtKB:P15328}. Secreted {ECO:0000269|Ref.3}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:P15328}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250|UniProtKB:P15328}. Endosome {ECO:0000250|UniProtKB:P15328}. Note=Endocytosed into cytoplasmic vesicles and then recycled to the cell membrane. {ECO:0000250|UniProtKB:P15328}.
| null | null | null | null | null |
FUNCTION: Binds to folate and reduced folic acid derivatives and mediates delivery of 5-methyltetrahydrofolate and folate analogs into the interior of cells. Has high affinity for folate and folic acid analogs at neutral pH. Exposure to slightly acidic pH after receptor endocytosis triggers a conformation change that strongly reduces its affinity for folates and mediates their release (By similarity). Required for normal embryonic development and normal cell proliferation (By similarity). {ECO:0000250|UniProtKB:P15328, ECO:0000250|UniProtKB:P35846}.
|
Bos taurus (Bovine)
|
P02706
|
ASGR1_RAT
|
MTKDYQDFQHLDNENDHHQLQRGPPPAPRLLQRLCSGFRLFLLSLGLSILLLVVVCVITSQNSQLREDLRVLRQNFSNFTVSTEDQVKALTTQGERVGRKMKLVESQLEKHQEDLREDHSRLLLHVKQLVSDVRSLSCQMAALRGNGSERICCPINWVEYEGSCYWFSSSVKPWTEADKYCQLENAHLVVVTSWEEQRFVQQHMGPLNTWIGLTDQNGPWKWVDGTDYETGFKNWRPGQPDDWYGHGLGGGEDCAHFTTDGHWNDDVCRRPYRWVCETELGKAN
| null | null |
cellular response to extracellular stimulus [GO:0031668]; endocytosis [GO:0006897]
|
external side of plasma membrane [GO:0009897]
|
asialoglycoprotein receptor activity [GO:0004873]; fucose binding [GO:0042806]; identical protein binding [GO:0042802]; mannose binding [GO:0005537]; metal ion binding [GO:0046872]; signaling receptor activity [GO:0038023]
|
PF00059;PF03954;
|
3.10.100.10;
| null |
PTM: Phosphorylated on a cytoplasmic Ser residue. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein.
| null | null | null | null | null |
FUNCTION: Mediates the endocytosis of plasma glycoproteins to which the terminal sialic acid residue on their complex carbohydrate moieties has been removed. The receptor recognizes terminal galactose and N-acetylgalactosamine units. After ligand binding to the receptor, the resulting complex is internalized and transported to a sorting organelle, where receptor and ligand are disassociated. The receptor then returns to the cell membrane surface.
|
Rattus norvegicus (Rat)
|
P02708
|
ACHA_HUMAN
|
MEPWPLLLLFSLCSAGLVLGSEHETRLVAKLFKDYSSVVRPVEDHRQVVEVTVGLQLIQLINVDEVNQIVTTNVRLKQQWVDYNLKWNPDDYGGVKKIHIPSEKIWRPDLVLYNNADGDFAIVKFTKVLLQYTGHITWTPPAIFKSYCEIIVTHFPFDEQNCSMKLGTWTYDGSVVAINPESDQPDLSNFMESGEWVIKESRGWKHSVTYSCCPDTPYLDITYHFVMQRLPLYFIVNVIIPCLLFSFLTGLVFYLPTDSGEKMTLSISVLLSLTVFLLVIVELIPSTSSAVPLIGKYMLFTMVFVIASIIITVIVINTHHRSPSTHVMPNWVRKVFIDTIPNIMFFSTMKRPSREKQDKKIFTEDIDISDISGKPGPPPMGFHSPLIKHPEVKSAIEGIKYIAETMKSDQESNNAAAEWKYVAMVMDHILLGVFMLVCIIGTLAVFAGRLIELNQQG
| null | null |
acetylcholine receptor signaling pathway [GO:0095500]; membrane depolarization [GO:0051899]; muscle cell cellular homeostasis [GO:0046716]; musculoskeletal movement [GO:0050881]; neuromuscular junction development [GO:0007528]; neuromuscular process [GO:0050905]; neuromuscular synaptic transmission [GO:0007274]; neuron cellular homeostasis [GO:0070050]; neuronal action potential [GO:0019228]; regulation of membrane potential [GO:0042391]; response to nicotine [GO:0035094]; skeletal muscle contraction [GO:0003009]; skeletal muscle tissue growth [GO:0048630]; synaptic transmission, cholinergic [GO:0007271]
|
acetylcholine-gated channel complex [GO:0005892]; cell surface [GO:0009986]; neuromuscular junction [GO:0031594]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; postsynaptic specialization membrane [GO:0099634]; synapse [GO:0045202]
|
acetylcholine binding [GO:0042166]; acetylcholine receptor activity [GO:0015464]; acetylcholine-gated monoatomic cation-selective channel activity [GO:0022848]; transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential [GO:1904315]
|
PF02931;PF02932;
|
2.70.170.10;1.20.58.390;
|
Ligand-gated ion channel (TC 1.A.9) family, Acetylcholine receptor (TC 1.A.9.1) subfamily, Alpha-1/CHRNA1 sub-subfamily
| null |
SUBCELLULAR LOCATION: Postsynaptic cell membrane {ECO:0000305|PubMed:27375219}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:27375219}; Multi-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=K(+)(in) = K(+)(out); Xref=Rhea:RHEA:29463, ChEBI:CHEBI:29103; Evidence={ECO:0000250|UniProtKB:P02709}; CATALYTIC ACTIVITY: Reaction=Na(+)(in) = Na(+)(out); Xref=Rhea:RHEA:34963, ChEBI:CHEBI:29101; Evidence={ECO:0000250|UniProtKB:P02709};
| null | null | null | null |
FUNCTION: [Isoform 1]: Upon acetylcholine binding, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. {ECO:0000269|PubMed:27375219}.; FUNCTION: [Isoform 2]: Non functional acetylcholine receptor alpha subunit which is not integrated into functional acetylcholine-gated cation-selective channels. {ECO:0000269|PubMed:8788941}.
|
Homo sapiens (Human)
|
P02709
|
ACHA_BOVIN
|
MEPRPLLLLLGLCSAGLVLGSEHETRLVAKLFEDYNSVVRPVEDHRQAVEVTVGLQLIQLINVDEVNQIVTTNVRLKQQWVDYNLKWNPDDYGGVKKIHIPSEKIWRPDLVLYNNADGDFAIVKFTKVLLDYTGHITWTPPAIFKSYCEIIVTHFPFDEQNCSMKLGTWTYDGSVVVINPESDQPDLSNFMESGEWVIKESRGWKHWVFYACCPSTPYLDITYHFVMQRLPLYFIVNVIIPCLLFSFLTGLVFYLPTDSGEKMTLSISVLLSLTVFLLVIVELIPSTSSAVPLIGKYMLFTMVFVIASIIITVIVINTHHRSPSTHVMPEWVRKVFIDTIPNIMFFSTMKRPSREKQDKKIFTEDIDISDISGKPGPPPMGFHSPLIKHPEVKSAIEGIKYIAETMKSDQESNNAAEEWKYVAMVMDHILLAVFMLVCIIGTLAVFAGRLIELNQQG
| null | null |
acetylcholine receptor signaling pathway [GO:0095500]; membrane depolarization [GO:0051899]; muscle cell cellular homeostasis [GO:0046716]; neuromuscular junction development [GO:0007528]; neuromuscular synaptic transmission [GO:0007274]; neuron cellular homeostasis [GO:0070050]; neuronal action potential [GO:0019228]; response to nicotine [GO:0035094]; skeletal muscle contraction [GO:0003009]; skeletal muscle tissue growth [GO:0048630]; synaptic transmission, cholinergic [GO:0007271]
|
acetylcholine-gated channel complex [GO:0005892]; cell surface [GO:0009986]; neuromuscular junction [GO:0031594]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; postsynaptic specialization membrane [GO:0099634]; synapse [GO:0045202]
|
acetylcholine binding [GO:0042166]; acetylcholine receptor activity [GO:0015464]; acetylcholine-gated monoatomic cation-selective channel activity [GO:0022848]
|
PF02931;PF02932;
|
2.70.170.10;1.20.58.390;
|
Ligand-gated ion channel (TC 1.A.9) family, Acetylcholine receptor (TC 1.A.9.1) subfamily, Alpha-1/CHRNA1 sub-subfamily
| null |
SUBCELLULAR LOCATION: Postsynaptic cell membrane {ECO:0000250|UniProtKB:P02708}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:P02708}; Multi-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=K(+)(in) = K(+)(out); Xref=Rhea:RHEA:29463, ChEBI:CHEBI:29103; Evidence={ECO:0000269|PubMed:2423878}; CATALYTIC ACTIVITY: Reaction=Na(+)(in) = Na(+)(out); Xref=Rhea:RHEA:34963, ChEBI:CHEBI:29101; Evidence={ECO:0000269|PubMed:2423878};
| null | null | null | null |
FUNCTION: Upon acetylcholine binding, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. {ECO:0000269|PubMed:2423878}.
|
Bos taurus (Bovine)
|
P02712
|
ACHB_TETCF
|
MENVRRMALGLVVMMALALSGVGASVMEDTLLSVLFETYNPKVRPAQTVGDKVTVRVGLTLTNLLILNEKIEEMTTNVFLNLAWTDYRLQWDPAAYEGIKDLRIPSSDVWQPDIVLMNNNDGSFEITLHVNVLVQHTGAVSWQPSAIYRSSCTIKVMYFPFDWQNCTMVFKSYTYDTSEVTLQHALDAKGEREVKEIVINKDAFTENGQWSIEHKPSRKNWRSDDPSYEDVTFYLIIQRKPLFYIVYTIIPCILISILAILVFYLPPDAGEKMSLSISALLAVTVFLLLLADKVPETSLSVPIIIRYLMFIMILVAFSVILSVVVLNLHHRSPNTHTMPNWIRQIFIETLPPFLWIQRPVTTPSPDSKPTIISRANDEYFIRKPAGDFVCPVDNARVAVQPERLFSEMKWHLNGLTQPVTLPQDLKEAVEAIKYIAEQLESASEFDDLKKDWQYVAMVADRLFLYVFFVICSIGTFSIFLDASHNVPPDNPFA
| null | null | null |
neuron projection [GO:0043005]; postsynaptic membrane [GO:0045211]
|
acetylcholine-gated monoatomic cation-selective channel activity [GO:0022848]; transmembrane signaling receptor activity [GO:0004888]
|
PF02931;PF02932;
|
2.70.170.10;1.20.58.390;
|
Ligand-gated ion channel (TC 1.A.9) family, Acetylcholine receptor (TC 1.A.9.1) subfamily, Beta-1/CHRNB1 sub-subfamily
| null |
SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein.
|
CATALYTIC ACTIVITY: Reaction=K(+)(in) = K(+)(out); Xref=Rhea:RHEA:29463, ChEBI:CHEBI:29103; Evidence={ECO:0000250|UniProtKB:P04758}; CATALYTIC ACTIVITY: Reaction=Na(+)(in) = Na(+)(out); Xref=Rhea:RHEA:34963, ChEBI:CHEBI:29101; Evidence={ECO:0000250|UniProtKB:P04758};
| null | null | null | null |
FUNCTION: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.
|
Tetronarce californica (Pacific electric ray) (Torpedo californica)
|
P02713
|
ACHG_CHICK
|
MRCSDLLLLFLLALCVLPGISCRNQEEKLLQDLMTNYNRHLRPALRGDQVIDVTLKLTLTNLISLNEREETLTTNVWIEMQWSDYRLRWDPDKYDDIQQLRVPSAMVWLPDIVLENNIDGTFEITLYTNVLVYPDGSIYWLPPAIYRSSCSIHVTYFPFDWQNCTMVFQSQTYSANEINLLLTVEEGQTIEWIFIDPEAFTENGEWAIKHRPARKIINSGRFTPDDIQYQQVIFYLIIQRKPLFYIINIIVPCVLISSMAVLVYFLPAKAGGQKCTVSINVLLAQTVFLFLIAQKVPETSQAVPLIGKYLTFLMVVTVVIVVNAVIVLNVSLRTPNTHSMSQRVRQVWLHLLPRYLGMHMPEEAPGPPQATRRRSSLGLMVKADEYMLWKARTELLFEKQKERDGLMKTVLEKIGRGLESNCAQDFCQSLEEASPEIRACVEACNHIANATREQNDFSSENEEWILVGRVIDRVCFFIMASLFVCGTIGIFLMAHFNQAPALPFPGDPKTYLPP
| null | null |
acetylcholine receptor signaling pathway [GO:0095500]; membrane depolarization [GO:0051899]
|
acetylcholine-gated channel complex [GO:0005892]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; synapse [GO:0045202]
|
acetylcholine receptor activity [GO:0015464]; acetylcholine-gated monoatomic cation-selective channel activity [GO:0022848]; transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential [GO:1904315]
|
PF02931;PF02932;
|
2.70.170.10;1.20.58.390;
|
Ligand-gated ion channel (TC 1.A.9) family, Acetylcholine receptor (TC 1.A.9.1) subfamily, Gamma/CHRNG sub-subfamily
| null |
SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein.
|
CATALYTIC ACTIVITY: Reaction=K(+)(in) = K(+)(out); Xref=Rhea:RHEA:29463, ChEBI:CHEBI:29103; Evidence={ECO:0000250|UniProtKB:P13536}; CATALYTIC ACTIVITY: Reaction=Na(+)(in) = Na(+)(out); Xref=Rhea:RHEA:34963, ChEBI:CHEBI:29101; Evidence={ECO:0000250|UniProtKB:P13536};
| null | null | null | null |
FUNCTION: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.
|
Gallus gallus (Chicken)
|
P02714
|
ACHG_TETCF
|
MVLTLLLIICLALEVRSENEEGRLIEKLLGDYDKRIIPAKTLDHIIDVTLKLTLTNLISLNEKEEALTTNVWIEIQWNDYRLSWNTSEYEGIDLVRIPSELLWLPDVVLENNVDGQFEVAYYANVLVYNDGSMYWLPPAIYRSTCPIAVTYFPFDWQNCSLVFRSQTYNAHEVNLQLSAEEGEAVEWIHIDPEDFTENGEWTIRHRPAKKNYNWQLTKDDTDFQEIIFFLIIQRKPLFYIINIIAPCVLISSLVVLVYFLPAQAGGQKCTLSISVLLAQTIFLFLIAQKVPETSLNVPLIGKYLIFVMFVSMLIVMNCVIVLNVSLRTPNTHSLSEKIKHLFLGFLPKYLGMQLEPSEETPEKPQPRRRSSFGIMIKAEEYILKKPRSELMFEEQKDRHGLKRVNKMTSDIDIGTTVDLYKDLANFAPEIKSCVEACNFIAKSTKEQNDSGSENENWVLIGKVIDKACFWIALLLFSIGTLAIFLTGHFNQVPEFPFPGDPRKYVP
| null | null | null |
neuron projection [GO:0043005]; postsynaptic membrane [GO:0045211]
|
acetylcholine-gated monoatomic cation-selective channel activity [GO:0022848]; transmembrane signaling receptor activity [GO:0004888]; transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential [GO:1904315]
|
PF02931;PF02932;
|
2.70.170.10;1.20.58.390;
|
Ligand-gated ion channel (TC 1.A.9) family, Acetylcholine receptor (TC 1.A.9.1) subfamily, Gamma/CHRNG sub-subfamily
|
PTM: Seems not to be glycosylated on Asn-158.
|
SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein.
|
CATALYTIC ACTIVITY: Reaction=K(+)(in) = K(+)(out); Xref=Rhea:RHEA:29463, ChEBI:CHEBI:29103; Evidence={ECO:0000250|UniProtKB:P13536}; CATALYTIC ACTIVITY: Reaction=Na(+)(in) = Na(+)(out); Xref=Rhea:RHEA:34963, ChEBI:CHEBI:29101; Evidence={ECO:0000250|UniProtKB:P13536};
| null | null | null | null |
FUNCTION: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.
|
Tetronarce californica (Pacific electric ray) (Torpedo californica)
|
P02716
|
ACHD_MOUSE
|
MAGPVLTLGLLAALVVCALPGSWGLNEEQRLIQHLFNEKGYDKDLRPVARKEDKVDVALSLTLSNLISLKEVEETLTTNVWIDHAWVDSRLQWDANDFGNITVLRLPPDMVWLPEIVLENNNDGSFQISYACNVLVYDSGYVTWLPPAIFRSSCPISVTYFPFDWQNCSLKFSSLKYTAKEITLSLKQEEENNRSYPIEWIIIDPEGFTENGEWEIVHRAAKLNVDPSVPMDSTNHQDVTFYLIIRRKPLFYIINILVPCVLISFMINLVFYLPGDCGEKTSVAISVLLAQSVFLLLISKRLPATSMAIPLVGKFLLFGMVLVTMVVVICVIVLNIHFRTPSTHVLSEGVKKFFLETLPKLLHMSRPAEEDPGPRALIRRSSSLGYICKAEEYFSLKSRSDLMFEKQSERHGLARRLTTARRPPASSEQVQQELFNEMKPAVDGANFIVNHMRDQNSYNEEKDNWNQVARTVDRLCLFVVTPVMVVGTAWIFLQGVYNQPPLQPFPGDPFSYSEQDKRFI
| null | null |
acetylcholine receptor signaling pathway [GO:0095500]; membrane depolarization [GO:0051899]; monoatomic cation transport [GO:0006812]; regulation of membrane potential [GO:0042391]; skeletal muscle contraction [GO:0003009]; skeletal muscle tissue growth [GO:0048630]
|
acetylcholine-gated channel complex [GO:0005892]; neuromuscular junction [GO:0031594]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; postsynaptic specialization membrane [GO:0099634]; synapse [GO:0045202]
|
acetylcholine receptor activity [GO:0015464]; acetylcholine-gated monoatomic cation-selective channel activity [GO:0022848]; ligand-gated monoatomic ion channel activity [GO:0015276]
|
PF02931;PF02932;
|
2.70.170.10;1.20.58.390;
|
Ligand-gated ion channel (TC 1.A.9) family, Acetylcholine receptor (TC 1.A.9.1) subfamily, Delta/CHRND sub-subfamily
| null |
SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein.
|
CATALYTIC ACTIVITY: Reaction=K(+)(in) = K(+)(out); Xref=Rhea:RHEA:29463, ChEBI:CHEBI:29103; Evidence={ECO:0000250|UniProtKB:P04759}; CATALYTIC ACTIVITY: Reaction=Na(+)(in) = Na(+)(out); Xref=Rhea:RHEA:34963, ChEBI:CHEBI:29101; Evidence={ECO:0000250|UniProtKB:P04759};
| null | null | null | null |
FUNCTION: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.
|
Mus musculus (Mouse)
|
P02718
|
ACHD_TETCF
|
MGNIHFVYLLISCLYYSGCSGVNEEERLINDLLIVNKYNKHVRPVKHNNEVVNIALSLTLSNLISLKETDETLTSNVWMDHAWYDHRLTWNASEYSDISILRLPPELVWIPDIVLQNNNDGQYHVAYFCNVLVRPNGYVTWLPPAIFRSSCPINVLYFPFDWQNCSLKFTALNYDANEITMDLMTDTIDGKDYPIEWIIIDPEAFTENGEWEIIHKPAKKNIYPDKFPNGTNYQDVTFYLIIRRKPLFYVINFITPCVLISFLASLAFYLPAESGEKMSTAISVLLAQAVFLLLTSQRLPETALAVPLIGKYLMFIMSLVTGVIVNCGIVLNFHFRTPSTHVLSTRVKQIFLEKLPRILHMSRADESEQPDWQNDLKLRRSSSVGYISKAQEYFNIKSRSELMFEKQSERHGLVPRVTPRIGFGNNNENIAASDQLHDEIKSGIDSTNYIVKQIKEKNAYDEEVGNWNLVGQTIDRLSMFIITPVMVLGTIFIFVMGNFNHPPAKPFEGDPFDYSSDHPRCA
| null | null | null |
neuron projection [GO:0043005]; postsynaptic membrane [GO:0045211]
|
acetylcholine-gated monoatomic cation-selective channel activity [GO:0022848]; transmembrane signaling receptor activity [GO:0004888]
|
PF02931;PF02932;
|
2.70.170.10;1.20.58.390;
|
Ligand-gated ion channel (TC 1.A.9) family, Acetylcholine receptor (TC 1.A.9.1) subfamily
| null |
SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein.
|
CATALYTIC ACTIVITY: Reaction=K(+)(in) = K(+)(out); Xref=Rhea:RHEA:29463, ChEBI:CHEBI:29103; Evidence={ECO:0000250|UniProtKB:P04759}; CATALYTIC ACTIVITY: Reaction=Na(+)(in) = Na(+)(out); Xref=Rhea:RHEA:34963, ChEBI:CHEBI:29101; Evidence={ECO:0000250|UniProtKB:P04759};
| null | null | null | null |
FUNCTION: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.
|
Tetronarce californica (Pacific electric ray) (Torpedo californica)
|
P02722
|
ADT1_BOVIN
|
MSDQALSFLKDFLAGGVAAAISKTAVAPIERVKLLLQVQHASKQISAEKQYKGIIDCVVRIPKEQGFLSFWRGNLANVIRYFPTQALNFAFKDKYKQIFLGGVDRHKQFWRYFAGNLASGGAAGATSLCFVYPLDFARTRLAADVGKGAAQREFTGLGNCITKIFKSDGLRGLYQGFNVSVQGIIIYRAAYFGVYDTAKGMLPDPKNVHIIVSWMIAQTVTAVAGLVSYPFDTVRRRMMMQSGRKGADIMYTGTVDCWRKIAKDEGPKAFFKGAWSNVLRGMGGAFVLVLYDEIKKFV
| null | null |
adaptive thermogenesis [GO:1990845]; ADP transport [GO:0015866]; mitochondrial ADP transmembrane transport [GO:0140021]; mitochondrial ATP transmembrane transport [GO:1990544]; negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway [GO:1901029]; positive regulation of mitophagy [GO:1901526]; regulation of mitochondrial membrane permeability [GO:0046902]
|
mitochondrial inner membrane [GO:0005743]; mitochondrial membrane [GO:0031966]; mitochondrial permeability transition pore complex [GO:0005757]
|
ATP:ADP antiporter activity [GO:0005471]; oxidative phosphorylation uncoupler activity [GO:0017077]
|
PF00153;
|
1.50.40.10;
|
Mitochondrial carrier (TC 2.A.29) family
|
PTM: Under cell death induction, transglutaminated by TGM2. Transglutamination leads to formation of covalent cross-links between a glutamine and the epsilon-amino group of a lysine residue, forming polymers. {ECO:0000250|UniProtKB:P48962}.
|
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000305|PubMed:14603310, ECO:0000305|PubMed:16226253}; Multi-pass membrane protein {ECO:0000269|PubMed:14603310, ECO:0000269|PubMed:16226253}. Membrane {ECO:0000250|UniProtKB:P12235}; Multi-pass membrane protein {ECO:0000269|PubMed:14603310, ECO:0000269|PubMed:16226253}. Note=The complex formed with ARL2BP, ARL2 and SLC25A4/ANT1 is expressed in mitochondria (By similarity). May localize to non-mitochondrial membranes (By similarity). {ECO:0000250|UniProtKB:P12235, ECO:0000250|UniProtKB:P48962}.
|
CATALYTIC ACTIVITY: Reaction=ADP(in) + ATP(out) = ADP(out) + ATP(in); Xref=Rhea:RHEA:34999, ChEBI:CHEBI:30616, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P48962}; CATALYTIC ACTIVITY: Reaction=H(+)(in) = H(+)(out); Xref=Rhea:RHEA:34979, ChEBI:CHEBI:15378; Evidence={ECO:0000250|UniProtKB:P48962};
| null | null | null | null |
FUNCTION: ADP:ATP antiporter that mediates import of ADP into the mitochondrial matrix for ATP synthesis, and export of ATP out to fuel the cell (By similarity). Cycles between the cytoplasmic-open state (c-state) and the matrix-open state (m-state): operates by the alternating access mechanism with a single substrate-binding site intermittently exposed to either the cytosolic (c-state) or matrix (m-state) side of the inner mitochondrial membrane (By similarity). In addition to its ADP:ATP antiporter activity, also involved in mitochondrial uncoupling and mitochondrial permeability transition pore (mPTP) activity (By similarity). Plays a role in mitochondrial uncoupling by acting as a proton transporter: proton transport uncouples the proton flows via the electron transport chain and ATP synthase to reduce the efficiency of ATP production and cause mitochondrial thermogenesis (PubMed:7961643). Proton transporter activity is inhibited by ADP:ATP antiporter activity, suggesting that SLC25A4/ANT1 acts as a master regulator of mitochondrial energy output by maintaining a delicate balance between ATP production (ADP:ATP antiporter activity) and thermogenesis (proton transporter activity) (By similarity). Proton transporter activity requires free fatty acids as cofactor, but does not transport it (PubMed:7961643). Probably mediates mitochondrial uncoupling in tissues that do not express UCP1 (By similarity). Also plays a key role in mPTP opening, a non-specific pore that enables free passage of the mitochondrial membranes to solutes of up to 1.5 kDa, and which contributes to cell death (By similarity). It is however unclear if SLC25A4/ANT1 constitutes a pore-forming component of mPTP or regulates it (By similarity). Acts as a regulator of mitophagy independently of ADP:ATP antiporter activity: promotes mitophagy via interaction with TIMM44, leading to inhibit the presequence translocase TIMM23, thereby promoting stabilization of PINK1 (By similarity). {ECO:0000250|UniProtKB:G2QNH0, ECO:0000250|UniProtKB:P48962, ECO:0000269|PubMed:7961643}.
|
Bos taurus (Bovine)
|
P02724
|
GLPA_HUMAN
|
MYGKIIFVLLLSEIVSISASSTTGVAMHTSTSSSVTKSYISSQTNDTHKRDTYAATPRAHEVSEISVRTVYPPEEETGERVQLAHHFSEPEITLIIFGVMAGVIGTILLISYGIRRLIKKSPSDVKPLPSPDTDVPLSSVEIENPETSDQ
| null | null | null |
ankyrin-1 complex [GO:0170014]; cytosol [GO:0005829]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]
|
identical protein binding [GO:0042802]; virus receptor activity [GO:0001618]
|
PF01102;
|
1.20.5.70;
|
Glycophorin A family
|
PTM: The major O-linked glycan are NeuAc-alpha-(2-3)-Gal-beta-(1-3)-[NeuAc-alpha-(2-6)]-GalNAcOH (about 78 %) and NeuAc-alpha-(2-3)-Gal-beta-(1-3)-GalNAcOH (17 %). Minor O-glycans (5 %) include NeuAc-alpha-(2-3)-Gal-beta-(1-3)-[NeuAc-alpha-(2-6)]-GalNAcOH NeuAc-alpha-(2-8)-NeuAc-alpha-(2-3)-Gal-beta-(1-3)-GalNAcOH. About 1% of all O-linked glycans carry blood group A, B and H determinants. They derive from a type-2 precursor core structure, Gal-beta-(1,3)-GlcNAc-beta-1-R, and the antigens are synthesized by addition of fucose (H antigen-specific) and then N-acetylgalactosamine (A antigen-specific) or galactose (B antigen-specific). Specifically O-linked-glycans are NeuAc-alpha-(2-3)-Gal-beta-(1-3)-GalNAcOH-(6-1)-GlcNAc-beta-(4-1)-[Fuc-alpha-(1-2)]-Gal-beta-(3-1)-GalNAc-alpha (about 1%, B antigen-specific) and NeuAc-alpha-(2-3)-Gal-beta-(1-3)-GalNAcOH-(6-1)-GlcNAc-beta-(4-1)-[Fuc-alpha-(1-2)]-Gal-beta (1 %, O antigen-, A antigen- and B antigen-specific). {ECO:0000269|PubMed:10912628, ECO:0000269|PubMed:15313217, ECO:0000269|PubMed:3624241, ECO:0000269|PubMed:5350948, ECO:0000269|PubMed:8286855}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11402026}; Single-pass type I membrane protein {ECO:0000269|PubMed:11402026}. Note=Appears to be colocalized with SLC4A1.
| null | null | null | null | null |
FUNCTION: Component of the ankyrin-1 complex, a multiprotein complex involved in the stability and shape of the erythrocyte membrane (PubMed:35835865). Glycophorin A is the major intrinsic membrane protein of the erythrocyte. The N-terminal glycosylated segment, which lies outside the erythrocyte membrane, has MN blood group receptors. Appears to be important for the function of SLC4A1 and is required for high activity of SLC4A1. May be involved in translocation of SLC4A1 to the plasma membrane. {ECO:0000269|PubMed:10926825, ECO:0000269|PubMed:12813056, ECO:0000269|PubMed:14604989, ECO:0000269|PubMed:19438409, ECO:0000269|PubMed:35835865}.; FUNCTION: (Microbial infection) Appears to be a receptor for Hepatitis A virus (HAV). {ECO:0000269|PubMed:15331714}.; FUNCTION: (Microbial infection) Receptor for P.falciparum erythrocyte-binding antigen 175 (EBA-175); binding of EBA-175 is dependent on sialic acid residues of the O-linked glycans. {ECO:0000269|PubMed:8009226}.
|
Homo sapiens (Human)
|
P02730
|
B3AT_HUMAN
|
MEELQDDYEDMMEENLEQEEYEDPDIPESQMEEPAAHDTEATATDYHTTSHPGTHKVYVELQELVMDEKNQELRWMEAARWVQLEENLGENGAWGRPHLSHLTFWSLLELRRVFTKGTVLLDLQETSLAGVANQLLDRFIFEDQIRPQDREELLRALLLKHSHAGELEALGGVKPAVLTRSGDPSQPLLPQHSSLETQLFCEQGDGGTEGHSPSGILEKIPPDSEATLVLVGRADFLEQPVLGFVRLQEAAELEAVELPVPIRFLFVLLGPEAPHIDYTQLGRAAATLMSERVFRIDAYMAQSRGELLHSLEGFLDCSLVLPPTDAPSEQALLSLVPVQRELLRRRYQSSPAKPDSSFYKGLDLNGGPDDPLQQTGQLFGGLVRDIRRRYPYYLSDITDAFSPQVLAAVIFIYFAALSPAITFGGLLGEKTRNQMGVSELLISTAVQGILFALLGAQPLLVVGFSGPLLVFEEAFFSFCETNGLEYIVGRVWIGFWLILLVVLVVAFEGSFLVRFISRYTQEIFSFLISLIFIYETFSKLIKIFQDHPLQKTYNYNVLMVPKPQGPLPNTALLSLVLMAGTFFFAMMLRKFKNSSYFPGKLRRVIGDFGVPISILIMVLVDFFIQDTYTQKLSVPDGFKVSNSSARGWVIHPLGLRSEFPIWMMFASALPALLVFILIFLESQITTLIVSKPERKMVKGSGFHLDLLLVVGMGGVAALFGMPWLSATTVRSVTHANALTVMGKASTPGAAAQIQEVKEQRISGLLVAVLVGLSILMEPILSRIPLAVLFGIFLYMGVTSLSGIQLFDRILLLFKPPKYHPDVPYVKRVKTWRMHLFTGIQIICLAVLWVVKSTPASLALPFVLILTVPLRRVLLPLIFRNVELQCLDADDAKATFDEEEGRDEYDEVAMPV
| null | null |
bicarbonate transport [GO:0015701]; blood coagulation [GO:0007596]; chloride transmembrane transport [GO:1902476]; chloride transport [GO:0006821]; erythrocyte development [GO:0048821]; intracellular monoatomic ion homeostasis [GO:0006873]; monoatomic anion transport [GO:0006820]; negative regulation of glycolytic process through fructose-6-phosphate [GO:1904539]; negative regulation of urine volume [GO:0035811]; pH elevation [GO:0045852]; plasma membrane phospholipid scrambling [GO:0017121]; protein localization to plasma membrane [GO:0072659]; regulation of intracellular pH [GO:0051453]; transmembrane transport [GO:0055085]
|
ankyrin-1 complex [GO:0170014]; basolateral plasma membrane [GO:0016323]; blood microparticle [GO:0072562]; cortical cytoskeleton [GO:0030863]; cytoplasmic side of plasma membrane [GO:0009898]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; plasma membrane [GO:0005886]; Z disc [GO:0030018]
|
ankyrin binding [GO:0030506]; bicarbonate transmembrane transporter activity [GO:0015106]; chloride transmembrane transporter activity [GO:0015108]; chloride:bicarbonate antiporter activity [GO:0140900]; hemoglobin binding [GO:0030492]; monoatomic anion transmembrane transporter activity [GO:0008509]; protein homodimerization activity [GO:0042803]; protein-membrane adaptor activity [GO:0043495]; solute:inorganic anion antiporter activity [GO:0005452]
|
PF07565;PF00955;
|
1.10.287.570;
|
Anion exchanger (TC 2.A.31) family
|
PTM: Phosphorylated on Tyr-8 and Tyr-21 most likely by SYK. PP1-resistant phosphorylation that precedes Tyr-359 and Tyr-904 phosphorylation. {ECO:0000269|PubMed:10942405, ECO:0000269|PubMed:1998697}.; PTM: Phosphorylated on Tyr-359 and Tyr-904 most likely by LYN. PP1-inhibited phosphorylation that follows Tyr-8 and Tyr-21 phosphorylation. {ECO:0000269|PubMed:10942405, ECO:0000269|PubMed:1998697}.; PTM: N-glycosylated. {ECO:0000269|PubMed:26542571}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10926824, ECO:0000269|PubMed:24121512, ECO:0000269|PubMed:26542571, ECO:0000269|PubMed:7506871}; Multi-pass membrane protein {ECO:0000269|PubMed:26542571}. Basolateral cell membrane {ECO:0000269|PubMed:7506871}; Multi-pass membrane protein {ECO:0000269|PubMed:7506871}. Note=Detected in the erythrocyte cell membrane and on the basolateral membrane of alpha-intercalated cells in the collecting duct in the kidney. {ECO:0000269|PubMed:7506871}.
|
CATALYTIC ACTIVITY: Reaction=chloride(out) + hydrogencarbonate(in) = chloride(in) + hydrogencarbonate(out); Xref=Rhea:RHEA:72363, ChEBI:CHEBI:17544, ChEBI:CHEBI:17996; Evidence={ECO:0000269|PubMed:10926824, ECO:0000269|PubMed:14734552, ECO:0000269|PubMed:16227998, ECO:0000269|PubMed:24121512, ECO:0000269|PubMed:28387307};
| null | null | null | null |
FUNCTION: Functions both as a transporter that mediates electroneutral anion exchange across the cell membrane and as a structural protein (PubMed:10926824, PubMed:14734552, PubMed:1538405, PubMed:16227998, PubMed:20151848, PubMed:24121512, PubMed:28387307, PubMed:35835865). Component of the ankyrin-1 complex of the erythrocyte membrane; required for normal flexibility and stability of the erythrocyte membrane and for normal erythrocyte shape via the interactions of its cytoplasmic domain with cytoskeletal proteins, glycolytic enzymes, and hemoglobin (PubMed:1538405, PubMed:20151848, PubMed:35835865). Functions as a transporter that mediates the 1:1 exchange of inorganic anions across the erythrocyte membrane. Mediates chloride-bicarbonate exchange in the kidney, and is required for normal acidification of the urine (PubMed:10926824, PubMed:14734552, PubMed:16227998, PubMed:24121512, PubMed:28387307). {ECO:0000269|PubMed:10926824, ECO:0000269|PubMed:14734552, ECO:0000269|PubMed:1538405, ECO:0000269|PubMed:16227998, ECO:0000269|PubMed:20151848, ECO:0000269|PubMed:24121512, ECO:0000269|PubMed:28387307, ECO:0000269|PubMed:35835865}.; FUNCTION: (Microbial infection) Acts as a receptor for P.falciparum (isolate 3D7) MSP9 and thus, facilitates merozoite invasion of erythrocytes (PubMed:14630931). Acts as a receptor for P.falciparum (isolate 3D7) MSP1 and thus, facilitates merozoite invasion of erythrocytes (PubMed:12692305). {ECO:0000269|PubMed:12692305, ECO:0000269|PubMed:14630931}.
|
Homo sapiens (Human)
|
P02741
|
CRP_HUMAN
|
MEKLLCFLVLTSLSHAFGQTDMSRKAFVFPKESDTSYVSLKAPLTKPLKAFTVCLHFYTELSSTRGYSIFSYATKRQDNEILIFWSKDIGYSFTVGGSEILFEVPEVTVAPVHICTSWESASGIVEFWVDGKPRVRKSLKKGYTVGAEASIILGQEQDSFGGNFEGSQSLVGDIGNVNMWDFVLSPDEINTIYLGGPFSPNVLNWRALKYEVQGEVFTKPQLWP
| null |
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Note=Binds 2 calcium ions per subunit.;
|
acute-phase response [GO:0006953]; defense response to Gram-positive bacterium [GO:0050830]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; negative regulation of lipid storage [GO:0010888]; negative regulation of macrophage derived foam cell differentiation [GO:0010745]; negative regulation of mononuclear cell proliferation [GO:0032945]; opsonization [GO:0008228]; positive regulation of gene expression [GO:0010628]; positive regulation of superoxide anion generation [GO:0032930]; regulation of interleukin-8 production [GO:0032677]; vasoconstriction [GO:0042310]
|
extracellular region [GO:0005576]; extracellular space [GO:0005615]
|
calcium ion binding [GO:0005509]; choline binding [GO:0033265]; complement component C1q complex binding [GO:0001849]; identical protein binding [GO:0042802]; low-density lipoprotein particle binding [GO:0030169]; low-density lipoprotein particle receptor binding [GO:0050750]
|
PF00354;
|
2.60.120.200;
|
Pentraxin family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Displays several functions associated with host defense: it promotes agglutination, bacterial capsular swelling, phagocytosis and complement fixation through its calcium-dependent binding to phosphorylcholine. Can interact with DNA and histones and may scavenge nuclear material released from damaged circulating cells.
|
Homo sapiens (Human)
|
P02743
|
SAMP_HUMAN
|
MNKPLLWISVLTSLLEAFAHTDLSGKVFVFPRESVTDHVNLITPLEKPLQNFTLCFRAYSDLSRAYSLFSYNTQGRDNELLVYKERVGEYSLYIGRHKVTSKVIEKFPAPVHICVSWESSSGIAEFWINGTPLVKKGLRQGYFVEAQPKIVLGQEQDSYGGKFDRSQSFVGEIGDLYMWDSVLPPENILSAYQGTPLPANILDWQALNYEIRGYVIIKPLVWV
| null |
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Note=Binds 2 calcium ions per subunit.;
|
acute-phase response [GO:0006953]; chaperone-mediated protein complex assembly [GO:0051131]; innate immune response [GO:0045087]; negative regulation by host of viral exo-alpha-sialidase activity [GO:0044869]; negative regulation by host of viral glycoprotein metabolic process [GO:0044871]; negative regulation of acute inflammatory response [GO:0002674]; negative regulation of exo-alpha-sialidase activity [GO:1903016]; negative regulation of glycoprotein metabolic process [GO:1903019]; negative regulation of monocyte differentiation [GO:0045656]; negative regulation of viral entry into host cell [GO:0046597]; negative regulation of viral process [GO:0048525]; negative regulation of wound healing [GO:0061045]; protein folding [GO:0006457]
|
blood microparticle [GO:0072562]; collagen-containing extracellular matrix [GO:0062023]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; nucleus [GO:0005634]
|
calcium ion binding [GO:0005509]; carbohydrate binding [GO:0030246]; complement component C1q complex binding [GO:0001849]; identical protein binding [GO:0042802]; unfolded protein binding [GO:0051082]; virion binding [GO:0046790]
|
PF00354;
|
2.60.120.200;
|
Pentraxin family
|
PTM: N-glycosylated with a complex biantennary oligosaccharide chain with a sialic acid at the end (disialo-SAP). Monosialo-SAP as well as asioalo-SAP are also detected (PubMed:15174148). {ECO:0000269|PubMed:15174148, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218}.
|
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Can interact with DNA and histones and may scavenge nuclear material released from damaged circulating cells. May also function as a calcium-dependent lectin.
|
Homo sapiens (Human)
|
P02745
|
C1QA_HUMAN
|
MEGPRGWLVLCVLAISLASMVTEDLCRAPDGKKGEAGRPGRRGRPGLKGEQGEPGAPGIRTGIQGLKGDQGEPGPSGNPGKVGYPGPSGPLGARGIPGIKGTKGSPGNIKDQPRPAFSAIRRNPPMGGNVVIFDTVITNQEEPYQNHSGRFVCTVPGYYYFTFQVLSQWEICLSIVSSSRGQVRRSLGFCDTTNKGLFQVVSGGMVLQLQQGDQVWVEKDPKKGHIYQGSEADSVFSGFLIFPSA
| null | null |
astrocyte activation [GO:0048143]; cell-cell signaling [GO:0007267]; complement activation [GO:0006956]; complement activation, classical pathway [GO:0006958]; complement-mediated synapse pruning [GO:0150062]; innate immune response [GO:0045087]; microglial cell activation [GO:0001774]; neuron remodeling [GO:0016322]; synapse organization [GO:0050808]; synapse pruning [GO:0098883]; vertebrate eye-specific patterning [GO:0150064]
|
collagen trimer [GO:0005581]; collagen-containing extracellular matrix [GO:0062023]; complement component C1 complex [GO:0005602]; complement component C1q complex [GO:0062167]; extracellular region [GO:0005576]; postsynapse [GO:0098794]; synapse [GO:0045202]
|
amyloid-beta binding [GO:0001540]
|
PF00386;PF01391;
|
2.60.120.40;
| null |
PTM: O-linked glycans are assumed to be the Glc-Gal disaccharides typically found as secondary modifications of hydroxylated lysines in collagen-like domains. {ECO:0000269|PubMed:486087}.
|
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: C1q associates with the proenzymes C1r and C1s to yield C1, the first component of the serum complement system. The collagen-like regions of C1q interact with the Ca(2+)-dependent C1r(2)C1s(2) proenzyme complex, and efficient activation of C1 takes place on interaction of the globular heads of C1q with the Fc regions of IgG or IgM antibody present in immune complexes.
|
Homo sapiens (Human)
|
P02746
|
C1QB_HUMAN
|
MMMKIPWGSIPVLMLLLLLGLIDISQAQLSCTGPPAIPGIPGIPGTPGPDGQPGTPGIKGEKGLPGLAGDHGEFGEKGDPGIPGNPGKVGPKGPMGPKGGPGAPGAPGPKGESGDYKATQKIAFSATRTINVPLRRDQTIRFDHVITNMNNNYEPRSGKFTCKVPGLYYFTYHASSRGNLCVNLMRGRERAQKVVTFCDYAYNTFQVTTGGMVLKLEQGENVFLQATDKNSLLGMEGANSIFSGFLLFPDMEA
| null | null |
complement activation [GO:0006956]; complement activation, classical pathway [GO:0006958]; innate immune response [GO:0045087]; synapse pruning [GO:0098883]
|
blood microparticle [GO:0072562]; collagen trimer [GO:0005581]; collagen-containing extracellular matrix [GO:0062023]; complement component C1 complex [GO:0005602]; complement component C1q complex [GO:0062167]; extracellular region [GO:0005576]; postsynapse [GO:0098794]; synapse [GO:0045202]
| null |
PF00386;PF01391;
|
2.60.120.40;
| null |
PTM: Hydroxylated on lysine and proline residues. Hydroxylated lysine residues can be glycosylated. Human C1Q contains up to 68.3 hydroxylysine-galactosylglucose residues and up to 2.5 hydroxylysine-galactose per molecule. Total percentage hydroxylysine residues glycosylated is 86.4%. {ECO:0000269|PubMed:486087, ECO:0000269|PubMed:6286235, ECO:0000269|PubMed:708376}.
|
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: C1q associates with the proenzymes C1r and C1s to yield C1, the first component of the serum complement system. The collagen-like regions of C1q interact with the Ca(2+)-dependent C1r(2)C1s(2) proenzyme complex, and efficient activation of C1 takes place on interaction of the globular heads of C1q with the Fc regions of IgG or IgM antibody present in immune complexes.
|
Homo sapiens (Human)
|
P02747
|
C1QC_HUMAN
|
MDVGPSSLPHLGLKLLLLLLLLPLRGQANTGCYGIPGMPGLPGAPGKDGYDGLPGPKGEPGIPAIPGIRGPKGQKGEPGLPGHPGKNGPMGPPGMPGVPGPMGIPGEPGEEGRYKQKFQSVFTVTRQTHQPPAPNSLIRFNAVLTNPQGDYDTSTGKFTCKVPGLYYFVYHASHTANLCVLLYRSGVKVVTFCGHTSKTNQVNSGGVLLRLQVGEEVWLAVNDYYDMVGIQGSDSVFSGFLLFPD
| null | null |
complement activation, classical pathway [GO:0006958]; immune response [GO:0006955]; innate immune response [GO:0045087]; negative regulation of granulocyte differentiation [GO:0030853]; negative regulation of macrophage differentiation [GO:0045650]; synapse pruning [GO:0098883]
|
blood microparticle [GO:0072562]; collagen trimer [GO:0005581]; collagen-containing extracellular matrix [GO:0062023]; complement component C1 complex [GO:0005602]; complement component C1q complex [GO:0062167]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; postsynapse [GO:0098794]; synapse [GO:0045202]
| null |
PF00386;PF01391;
|
2.60.120.40;
| null |
PTM: O-linked glycans consist of Glc-Gal disaccharides bound to the oxygen atom of post-translationally added hydroxyl groups.
|
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: C1q associates with the proenzymes C1r and C1s to yield C1, the first component of the serum complement system. The collagen-like regions of C1q interact with the Ca(2+)-dependent C1r(2)C1s(2) proenzyme complex, and efficient activation of C1 takes place on interaction of the globular heads of C1q with the Fc regions of IgG or IgM antibody present in immune complexes.
|
Homo sapiens (Human)
|
P02748
|
CO9_HUMAN
|
MSACRSFAVAICILEISILTAQYTTSYDPELTESSGSASHIDCRMSPWSEWSQCDPCLRQMFRSRSIEVFGQFNGKRCTDAVGDRRQCVPTEPCEDAEDDCGNDFQCSTGRCIKMRLRCNGDNDCGDFSDEDDCESEPRPPCRDRVVEESELARTAGYGINILGMDPLSTPFDNEFYNGLCNRDRDGNTLTYYRRPWNVASLIYETKGEKNFRTEHYEEQIEAFKSIIQEKTSNFNAAISLKFTPTETNKAEQCCEETASSISLHGKGSFRFSYSKNETYQLFLSYSSKKEKMFLHVKGEIHLGRFVMRNRDVVLTTTFVDDIKALPTTYEKGEYFAFLETYGTHYSSSGSLGGLYELIYVLDKASMKRKGVELKDIKRCLGYHLDVSLAFSEISVGAEFNKDDCVKRGEGRAVNITSENLIDDVVSLIRGGTRKYAFELKEKLLRGTVIDVTDFVNWASSINDAPVLISQKLSPIYNLVPVKMKNAHLKKQNLERAIEDYINEFSVRKCHTCQNGGTVILMDGKCLCACPFKFEGIACEISKQKISEGLPALEFPNEK
| null | null |
cell killing [GO:0001906]; complement activation [GO:0006956]; complement activation, alternative pathway [GO:0006957]; complement activation, classical pathway [GO:0006958]; killing of cells of another organism [GO:0031640]; positive regulation of immune response [GO:0050778]; protein homooligomerization [GO:0051260]
|
blood microparticle [GO:0072562]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; membrane attack complex [GO:0005579]; other organism cell membrane [GO:0044218]; plasma membrane [GO:0005886]
| null |
PF00057;PF01823;PF00090;
|
2.10.25.10;4.10.400.10;2.20.100.10;
|
Complement C6/C7/C8/C9 family
|
PTM: Thrombin cleaves factor C9 to produce C9a and C9b. {ECO:0000269|PubMed:4055801}.; PTM: Phosphorylation sites are present in the extracellular medium.; PTM: Initially, positions and connectivity of disulfide bonds were based on peptide sequencing done for the human protein (PubMed:8603752). The crystal structures for the human and mouse proteins corrected the positions and connectivities of the disulfide bonds (PubMed:30111885). The distance between Cys-57 and Cys-94 in the monomeric mouse protein precludes formation of a disulfide bond, contrary to what is seen in the structure of the human polymeric form of the protein (Probable). {ECO:0000269|PubMed:30111885, ECO:0000269|PubMed:8603752, ECO:0000305|PubMed:30111885}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22832194, ECO:0000269|PubMed:26841934, ECO:0000269|PubMed:8603752, ECO:0000269|PubMed:9212048, ECO:0000269|PubMed:9634479}. Target cell membrane {ECO:0000269|PubMed:26841934, ECO:0000269|PubMed:30111885, ECO:0000269|PubMed:9212048}; Multi-pass membrane protein {ECO:0000269|PubMed:26841934}. Note=Secreted as soluble monomer. Oligomerizes at target membranes, forming a pre-pore. A conformation change then leads to the formation of a 100 Angstrom diameter pore. {ECO:0000269|PubMed:26841934, ECO:0000269|PubMed:30111885, ECO:0000269|PubMed:4055801, ECO:0000269|PubMed:9634479}.
| null | null | null | null | null |
FUNCTION: Constituent of the membrane attack complex (MAC) that plays a key role in the innate and adaptive immune response by forming pores in the plasma membrane of target cells (PubMed:26841934, PubMed:9212048, PubMed:9634479). C9 is the pore-forming subunit of the MAC (PubMed:26841934, PubMed:30111885, PubMed:4055801). {ECO:0000269|PubMed:26841934, ECO:0000269|PubMed:30111885, ECO:0000269|PubMed:4055801, ECO:0000269|PubMed:9212048, ECO:0000269|PubMed:9634479}.
|
Homo sapiens (Human)
|
P02749
|
APOH_HUMAN
|
MISPVLILFSSFLCHVAIAGRTCPKPDDLPFSTVVPLKTFYEPGEEITYSCKPGYVSRGGMRKFICPLTGLWPINTLKCTPRVCPFAGILENGAVRYTTFEYPNTISFSCNTGFYLNGADSAKCTEEGKWSPELPVCAPIICPPPSIPTFATLRVYKPSAGNNSLYRDTAVFECLPQHAMFGNDTITCTTHGNWTKLPECREVKCPFPSRPDNGFVNYPAKPTLYYKDKATFGCHDGYSLDGPEEIECTKLGNWSAMPSCKASCKVPVKKATVVYQGERVKIQEKFKNGMLHGDKVSFFCKNKEKKCSYTEDAQCIDGTIEVPKCFKEHSSLAFWKTDASDVKPC
| null | null |
blood coagulation, intrinsic pathway [GO:0007597]; negative regulation of angiogenesis [GO:0016525]; negative regulation of blood coagulation [GO:0030195]; negative regulation of complement activation, classical pathway [GO:0045959]; negative regulation of endothelial cell migration [GO:0010596]; negative regulation of endothelial cell proliferation [GO:0001937]; negative regulation of fibrinolysis [GO:0051918]; negative regulation of myeloid cell apoptotic process [GO:0033033]; negative regulation of smooth muscle cell apoptotic process [GO:0034392]; plasminogen activation [GO:0031639]; positive regulation of blood coagulation [GO:0030194]; positive regulation of lipoprotein lipase activity [GO:0051006]; regulation of fibrinolysis [GO:0051917]; T cell mediated immunity [GO:0002456]; triglyceride metabolic process [GO:0006641]; triglyceride transport [GO:0034197]
|
cell surface [GO:0009986]; chylomicron [GO:0042627]; collagen-containing extracellular matrix [GO:0062023]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; high-density lipoprotein particle [GO:0034364]; plasma membrane [GO:0005886]; platelet dense granule lumen [GO:0031089]; very-low-density lipoprotein particle [GO:0034361]
|
heparin binding [GO:0008201]; identical protein binding [GO:0042802]; lipid binding [GO:0008289]; lipoprotein lipase activator activity [GO:0060230]; phospholipid binding [GO:0005543]
|
PF00084;PF09014;
|
2.10.70.10;
| null |
PTM: N- and O-glycosylated. PubMed:6587378 also reports glycosylation on 'Asn-188' for their allele. {ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:16740002, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:6587378}.
|
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Binds to various kinds of negatively charged substances such as heparin, phospholipids, and dextran sulfate. May prevent activation of the intrinsic blood coagulation cascade by binding to phospholipids on the surface of damaged cells.
|
Homo sapiens (Human)
|
P02750
|
A2GL_HUMAN
|
MSSWSRQRPKSPGGIQPHVSRTLFLLLLLAASAWGVTLSPKDCQVFRSDHGSSISCQPPAEIPGYLPADTVHLAVEFFNLTHLPANLLQGASKLQELHLSSNGLESLSPEFLRPVPQLRVLDLTRNALTGLPPGLFQASATLDTLVLKENQLEVLEVSWLHGLKALGHLDLSGNRLRKLPPGLLANFTLLRTLDLGENQLETLPPDLLRGPLQLERLHLEGNKLQVLGKDLLLPQPDLRYLFLNGNKLARVAAGAFQGLRQLDMLDLSNNSLASVPEGLWASLGQPNWDMRDGFDISGNPWICDQNLSDLYRWLQAQKDKMFSQNDTRCAGPEAVKGQTLLAVAKSQ
| null | null |
brown fat cell differentiation [GO:0050873]; keratinocyte migration [GO:0051546]; leukocyte adhesion to vascular endothelial cell [GO:0061756]; positive regulation of angiogenesis [GO:0045766]; positive regulation of endothelial cell proliferation [GO:0001938]; positive regulation of epithelial cell proliferation involved in wound healing [GO:0060054]; positive regulation of epithelial to mesenchymal transition [GO:0010718]; positive regulation of keratinocyte proliferation [GO:0010838]; positive regulation of transforming growth factor beta receptor signaling pathway [GO:0030511]; response to bacterium [GO:0009617]; wound healing, spreading of epidermal cells [GO:0035313]
|
extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; ficolin-1-rich granule lumen [GO:1904813]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; specific granule lumen [GO:0035580]; tertiary granule lumen [GO:1904724]
|
type I transforming growth factor beta receptor binding [GO:0034713]; type II transforming growth factor beta receptor binding [GO:0005114]
|
PF00560;PF13855;
|
3.80.10.10;
| null | null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null | null |
Homo sapiens (Human)
|
P02751
|
FINC_HUMAN
|
MLRGPGPGLLLLAVQCLGTAVPSTGASKSKRQAQQMVQPQSPVAVSQSKPGCYDNGKHYQINQQWERTYLGNALVCTCYGGSRGFNCESKPEAEETCFDKYTGNTYRVGDTYERPKDSMIWDCTCIGAGRGRISCTIANRCHEGGQSYKIGDTWRRPHETGGYMLECVCLGNGKGEWTCKPIAEKCFDHAAGTSYVVGETWEKPYQGWMMVDCTCLGEGSGRITCTSRNRCNDQDTRTSYRIGDTWSKKDNRGNLLQCICTGNGRGEWKCERHTSVQTTSSGSGPFTDVRAAVYQPQPHPQPPPYGHCVTDSGVVYSVGMQWLKTQGNKQMLCTCLGNGVSCQETAVTQTYGGNSNGEPCVLPFTYNGRTFYSCTTEGRQDGHLWCSTTSNYEQDQKYSFCTDHTVLVQTRGGNSNGALCHFPFLYNNHNYTDCTSEGRRDNMKWCGTTQNYDADQKFGFCPMAAHEEICTTNEGVMYRIGDQWDKQHDMGHMMRCTCVGNGRGEWTCIAYSQLRDQCIVDDITYNVNDTFHKRHEEGHMLNCTCFGQGRGRWKCDPVDQCQDSETGTFYQIGDSWEKYVHGVRYQCYCYGRGIGEWHCQPLQTYPSSSGPVEVFITETPSQPNSHPIQWNAPQPSHISKYILRWRPKNSVGRWKEATIPGHLNSYTIKGLKPGVVYEGQLISIQQYGHQEVTRFDFTTTSTSTPVTSNTVTGETTPFSPLVATSESVTEITASSFVVSWVSASDTVSGFRVEYELSEEGDEPQYLDLPSTATSVNIPDLLPGRKYIVNVYQISEDGEQSLILSTSQTTAPDAPPDTTVDQVDDTSIVVRWSRPQAPITGYRIVYSPSVEGSSTELNLPETANSVTLSDLQPGVQYNITIYAVEENQESTPVVIQQETTGTPRSDTVPSPRDLQFVEVTDVKVTIMWTPPESAVTGYRVDVIPVNLPGEHGQRLPISRNTFAEVTGLSPGVTYYFKVFAVSHGRESKPLTAQQTTKLDAPTNLQFVNETDSTVLVRWTPPRAQITGYRLTVGLTRRGQPRQYNVGPSVSKYPLRNLQPASEYTVSLVAIKGNQESPKATGVFTTLQPGSSIPPYNTEVTETTIVITWTPAPRIGFKLGVRPSQGGEAPREVTSDSGSIVVSGLTPGVEYVYTIQVLRDGQERDAPIVNKVVTPLSPPTNLHLEANPDTGVLTVSWERSTTPDITGYRITTTPTNGQQGNSLEEVVHADQSSCTFDNLSPGLEYNVSVYTVKDDKESVPISDTIIPEVPQLTDLSFVDITDSSIGLRWTPLNSSTIIGYRITVVAAGEGIPIFEDFVDSSVGYYTVTGLEPGIDYDISVITLINGGESAPTTLTQQTAVPPPTDLRFTNIGPDTMRVTWAPPPSIDLTNFLVRYSPVKNEEDVAELSISPSDNAVVLTNLLPGTEYVVSVSSVYEQHESTPLRGRQKTGLDSPTGIDFSDITANSFTVHWIAPRATITGYRIRHHPEHFSGRPREDRVPHSRNSITLTNLTPGTEYVVSIVALNGREESPLLIGQQSTVSDVPRDLEVVAATPTSLLISWDAPAVTVRYYRITYGETGGNSPVQEFTVPGSKSTATISGLKPGVDYTITVYAVTGRGDSPASSKPISINYRTEIDKPSQMQVTDVQDNSISVKWLPSSSPVTGYRVTTTPKNGPGPTKTKTAGPDQTEMTIEGLQPTVEYVVSVYAQNPSGESQPLVQTAVTNIDRPKGLAFTDVDVDSIKIAWESPQGQVSRYRVTYSSPEDGIHELFPAPDGEEDTAELQGLRPGSEYTVSVVALHDDMESQPLIGTQSTAIPAPTDLKFTQVTPTSLSAQWTPPNVQLTGYRVRVTPKEKTGPMKEINLAPDSSSVVVSGLMVATKYEVSVYALKDTLTSRPAQGVVTTLENVSPPRRARVTDATETTITISWRTKTETITGFQVDAVPANGQTPIQRTIKPDVRSYTITGLQPGTDYKIYLYTLNDNARSSPVVIDASTAIDAPSNLRFLATTPNSLLVSWQPPRARITGYIIKYEKPGSPPREVVPRPRPGVTEATITGLEPGTEYTIYVIALKNNQKSEPLIGRKKTDELPQLVTLPHPNLHGPEILDVPSTVQKTPFVTHPGYDTGNGIQLPGTSGQQPSVGQQMIFEEHGFRRTTPPTTATPIRHRPRPYPPNVGEEIQIGHIPREDVDYHLYPHGPGLNPNASTGQEALSQTTISWAPFQDTSEYIISCHPVGTDEEPLQFRVPGTSTSATLTGLTRGATYNVIVEALKDQQRHKVREEVVTVGNSVNEGLNQPTDDSCFDPYTVSHYAVGDEWERMSESGFKLLCQCLGFGSGHFRCDSSRWCHDNGVNYKIGEKWDRQGENGQMMSCTCLGNGKGEFKCDPHEATCYDDGKTYHVGEQWQKEYLGAICSCTCFGGQRGWRCDNCRRPGGEPSPEGTTGQSYNQYSQRYHQRTNTNVNCPIECFMPLDVQADREDSRE
| null | null |
acute-phase response [GO:0006953]; angiogenesis [GO:0001525]; biological process involved in interaction with symbiont [GO:0051702]; calcium-independent cell-matrix adhesion [GO:0007161]; cell adhesion [GO:0007155]; cell-matrix adhesion [GO:0007160]; cell-substrate junction assembly [GO:0007044]; endodermal cell differentiation [GO:0035987]; heart development [GO:0007507]; integrin activation [GO:0033622]; integrin-mediated signaling pathway [GO:0007229]; negative regulation of monocyte activation [GO:0150102]; negative regulation of transforming growth factor beta production [GO:0071635]; nervous system development [GO:0007399]; neural crest cell migration involved in autonomic nervous system development [GO:1901166]; peptide cross-linking [GO:0018149]; positive regulation of axon extension [GO:0045773]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of fibroblast proliferation [GO:0048146]; positive regulation of gene expression [GO:0010628]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of substrate-dependent cell migration, cell attachment to substrate [GO:1904237]; regulation of cell shape [GO:0008360]; regulation of ERK1 and ERK2 cascade [GO:0070372]; regulation of protein phosphorylation [GO:0001932]; response to wounding [GO:0009611]; substrate adhesion-dependent cell spreading [GO:0034446]; wound healing [GO:0042060]
|
apical plasma membrane [GO:0016324]; basement membrane [GO:0005604]; blood microparticle [GO:0072562]; collagen-containing extracellular matrix [GO:0062023]; endoplasmic reticulum lumen [GO:0005788]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; extracellular exosome [GO:0070062]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; fibrinogen complex [GO:0005577]; plasma membrane [GO:0005886]; platelet alpha granule lumen [GO:0031093]
|
collagen binding [GO:0005518]; extracellular matrix structural constituent [GO:0005201]; heparin binding [GO:0008201]; identical protein binding [GO:0042802]; integrin binding [GO:0005178]; peptidase activator activity [GO:0016504]; protease binding [GO:0002020]; proteoglycan binding [GO:0043394]; signaling receptor binding [GO:0005102]
|
PF00039;PF00040;PF00041;
|
2.10.70.10;2.10.10.10;2.60.40.10;
| null |
PTM: Sulfated. {ECO:0000269|PubMed:2414772}.; PTM: It is not known whether both or only one of Thr-2155 and Thr-2156 are/is glycosylated. {ECO:0000269|PubMed:11285216, ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16037490, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:17614963, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:2012601, ECO:0000269|PubMed:3584091}.; PTM: Forms covalent cross-links mediated by a transglutaminase, such as F13A or TGM2, between a glutamine and the epsilon-amino group of a lysine residue, forming homopolymers and heteropolymers (e.g. fibrinogen-fibronectin, collagen-fibronectin heteropolymers). {ECO:0000250|UniProtKB:P11276}.; PTM: Phosphorylated by FAM20C in the extracellular medium. {ECO:0000269|PubMed:26091039}.; PTM: Proteolytic processing produces the C-terminal NC1 peptide, anastellin. {ECO:0000305|PubMed:8114919}.; PTM: Some lysine residues are oxidized to allysine by LOXL3, promoting fibronectin activation and matrix formation. {ECO:0000250|UniProtKB:P11276}.; PTM: Serotonylated on Gln residues by TGM2 in response to hypoxia. {ECO:0000250|UniProtKB:P07589}.
|
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000305|PubMed:29100092}. Secreted {ECO:0000250|UniProtKB:P11276}.
| null | null | null | null | null |
FUNCTION: Fibronectins bind cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin (PubMed:3024962, PubMed:3593230, PubMed:3900070, PubMed:7989369). Fibronectins are involved in cell adhesion, cell motility, opsonization, wound healing, and maintenance of cell shape (PubMed:3024962, PubMed:3593230, PubMed:3900070, PubMed:7989369). Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process, essential for osteoblast mineralization (By similarity). Participates in the regulation of type I collagen deposition by osteoblasts (By similarity). Acts as a ligand for the LILRB4 receptor, inhibiting FCGR1A/CD64-mediated monocyte activation (PubMed:34089617). {ECO:0000250|UniProtKB:P11276, ECO:0000269|PubMed:3024962, ECO:0000269|PubMed:34089617, ECO:0000269|PubMed:3593230, ECO:0000269|PubMed:3900070, ECO:0000269|PubMed:7989369}.; FUNCTION: [Anastellin]: Binds fibronectin and induces fibril formation. This fibronectin polymer, named superfibronectin, exhibits enhanced adhesive properties. Both anastellin and superfibronectin inhibit tumor growth, angiogenesis and metastasis. Anastellin activates p38 MAPK and inhibits lysophospholipid signaling. {ECO:0000269|PubMed:11209058, ECO:0000269|PubMed:15665290, ECO:0000269|PubMed:19379667, ECO:0000269|PubMed:8114919}.; FUNCTION: Secreted by contracting muscle, induces liver autophagy, a degradative pathway for nutrient mobilization and damage removal, and systemic insulin sensitization via hepatic ITGA5:ITGB1 integrin receptor signaling. {ECO:0000250|UniProtKB:P11276}.
|
Homo sapiens (Human)
|
P02752
|
RBP_CHICK
|
MLRFAITLFAVITSSTCQQYGCLEGDTHKANPSPEPNMHECTLYSESSCCYANFTEQLAHSPIIKVSNSYWNRCGQLSKSCEDFTKKIECFYRCSPHAARWIDPRYTAAIQSVPLCQSFCDDWYEACKDDSICAHNWLTDWERDESGENHCKSKCVPYSEMYANGTDMCQSMWGESFKVSESSCLCLQMNKKDMVAIKHLLSESSEESSSMSSSEEHACQKKLLKFEALQQEEGEERR
| null | null |
negative regulation of sensory perception of bitter taste [GO:1904661]; negative regulation of sensory perception of sweet taste [GO:1904657]; riboflavin transport [GO:0032218]
|
external side of plasma membrane [GO:0009897]
|
riboflavin binding [GO:1902444]; riboflavin transmembrane transporter activity [GO:0032217]; signaling receptor activity [GO:0038023]
|
PF03024;
| null |
Folate receptor family
|
PTM: Plasma and yolk RBPS have the same carbohydrate components, whereas egg-white RBP has a different, ovomucoid-type carbohydrate chain.; PTM: Plasma RBP has the same C-terminal sequence as the egg-white RBP, which suggests that the C-terminal residues are cleaved off upon incorporation into the oocyte.
| null | null | null | null | null | null |
FUNCTION: Required for the transport of riboflavin to the developing oocyte.
|
Gallus gallus (Chicken)
|
P02753
|
RET4_HUMAN
|
MKWVWALLLLAALGSGRAERDCRVSSFRVKENFDKARFSGTWYAMAKKDPEGLFLQDNIVAEFSVDETGQMSATAKGRVRLLNNWDVCADMVGTFTDTEDPAKFKMKYWGVASFLQKGNDDHWIVDTDYDTYAVQYSCRLLNLDGTCADSYSFVFSRDPNGLPPEAQKIVRQRQEELCLARQYRLIVHNGYCDGRSERNLL
| null | null |
cardiac muscle tissue development [GO:0048738]; embryonic organ morphogenesis [GO:0048562]; embryonic retina morphogenesis in camera-type eye [GO:0060059]; embryonic skeletal system development [GO:0048706]; eye development [GO:0001654]; female genitalia morphogenesis [GO:0048807]; gluconeogenesis [GO:0006094]; glucose homeostasis [GO:0042593]; heart development [GO:0007507]; heart trabecula formation [GO:0060347]; lung development [GO:0030324]; maintenance of gastrointestinal epithelium [GO:0030277]; negative regulation of cardiac muscle cell proliferation [GO:0060044]; positive regulation of immunoglobulin production [GO:0002639]; positive regulation of insulin secretion [GO:0032024]; response to retinoic acid [GO:0032526]; retinol metabolic process [GO:0042572]; retinol transport [GO:0034633]; urinary bladder development [GO:0060157]; uterus development [GO:0060065]; vagina development [GO:0060068]; visual perception [GO:0007601]
|
extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]
|
retinal binding [GO:0016918]; retinol binding [GO:0019841]; retinol transmembrane transporter activity [GO:0034632]
|
PF00061;
|
2.40.128.20;
|
Calycin superfamily, Lipocalin family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12237133, ECO:0000269|PubMed:2444024, ECO:0000269|PubMed:5541771}.
| null | null | null | null | null |
FUNCTION: Retinol-binding protein that mediates retinol transport in blood plasma (PubMed:5541771). Delivers retinol from the liver stores to the peripheral tissues (Probable). Transfers the bound all-trans retinol to STRA6, that then facilitates retinol transport across the cell membrane (PubMed:22665496). {ECO:0000269|PubMed:22665496, ECO:0000305, ECO:0000305|PubMed:5541771}.
|
Homo sapiens (Human)
|
P02754
|
LACB_BOVIN
|
MKCLLLALALTCGAQALIVTQTMKGLDIQKVAGTWYSLAMAASDISLLDAQSAPLRVYVEELKPTPEGDLEILLQKWENGECAQKKIIAEKTKIPAVFKIDALNENKVLVLDTDYKKYLLFCMENSAEPEQSLACQCLVRTPEVDDEALEKFDKALKALPMHIRLSFNPTQLEEQCHI
| null | null | null |
extracellular space [GO:0005615]
|
identical protein binding [GO:0042802]; long-chain fatty acid binding [GO:0036041]; retinol binding [GO:0019841]
|
PF00061;
|
2.40.128.20;
|
Calycin superfamily, Lipocalin family
|
PTM: Alternate disulfide bonds occur in equal amounts in all variants examined.
|
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Primary component of whey, it binds retinol and is probably involved in the transport of that molecule.
|
Bos taurus (Bovine)
|
P02760
|
AMBP_HUMAN
|
MRSLGALLLLLSACLAVSAGPVPTPPDNIQVQENFNISRIYGKWYNLAIGSTCPWLKKIMDRMTVSTLVLGEGATEAEISMTSTRWRKGVCEETSGAYEKTDTDGKFLYHKSKWNITMESYVVHTNYDEYAIFLTKKFSRHHGPTITAKLYGRAPQLRETLLQDFRVVAQGVGIPEDSIFTMADRGECVPGEQEPEPILIPRVRRAVLPQEEEGSGGGQLVTEVTKKEDSCQLGYSAGPCMGMTSRYFYNGTSMACETFQYGGCMGNGNNFVTEKECLQTCRTVAACNLPIVRGPCRAFIQLWAFDAVKGKCVLFPYGGCQGNGNKFYSEKECREYCGVPGDGDEELLRFSN
|
1.6.2.-
| null |
cell adhesion [GO:0007155]; female pregnancy [GO:0007565]; heme catabolic process [GO:0042167]; negative regulation of immune response [GO:0050777]; negative regulation of JNK cascade [GO:0046329]
|
blood microparticle [GO:0072562]; cell surface [GO:0009986]; collagen-containing extracellular matrix [GO:0062023]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; mitochondrial inner membrane [GO:0005743]; nuclear membrane [GO:0031965]; plasma membrane [GO:0005886]
|
calcium channel inhibitor activity [GO:0019855]; calcium oxalate binding [GO:0046904]; carbohydrate binding [GO:0030246]; heme binding [GO:0020037]; IgA binding [GO:0019862]; oxidoreductase activity [GO:0016491]; protein homodimerization activity [GO:0042803]; serine-type endopeptidase inhibitor activity [GO:0004867]
|
PF00014;PF00061;
|
2.40.128.20;4.10.410.10;
|
Calycin superfamily, Lipocalin family
|
PTM: The precursor is proteolytically processed into separately functioning proteins. {ECO:0000305}.; PTM: [Alpha-1-microglobulin]: Proteolytically cleaved in the presence of oxyhemoglobin or MPO (PubMed:11877257, PubMed:25698971). The cleaved form t-alpha-1-microglobulin lacks the C-terminal tetrapeptide LIPR and is released from IgA-alpha-1-microglobulin complex as well as from free alpha-1-microglobulin when exposed to oxyhemoglobin or erythrocyte membranes. The cleavage of IgA-alpha-1-microglobulin complex is associated with the reduction of the covalent bond between IgA and alpha-1-microglobulin, yielding an intact IgA molecule (PubMed:11877257). The cleavage by MPO is associated with the transfer of heme group from MPO to t-alpha-1-microglobulin (PubMed:25698971). t-alpha-1-microglobulin has higher reductase activity when compared with full length protein (PubMed:15683711). {ECO:0000269|PubMed:11877257, ECO:0000269|PubMed:15683711, ECO:0000269|PubMed:25698971}.; PTM: [Alpha-1-microglobulin]: 3-hydroxykynurenine, an oxidized tryptophan metabolite that is common in biological fluids, reacts with Cys-53, Lys-111, Lys-137, and Lys-149 to form heterogeneous polycyclic chromophores including hydroxanthommatin. The reaction by alpha-1-microglobulin is autocatalytic; the human protein forms chromophore even when expressed in insect and bacterial cells. The chromophore can react with accessible cysteines forming non-reducible thioether cross-links with other molecules of alpha-1-microglobulin or with other proteins such as Ig alpha-1 chain C region 'Cys-352'. {ECO:0000269|PubMed:10631976, ECO:0000269|PubMed:1714898, ECO:0000269|PubMed:7535251}.; PTM: [Inter-alpha-trypsin inhibitor light chain]: Heavy chains are interlinked with bikunin via a chondroitin 4-sulfate bridge to the C-terminal aspartate. {ECO:0000269|PubMed:1898736, ECO:0000269|PubMed:6171497, ECO:0000269|PubMed:7682553}.; PTM: [Inter-alpha-trypsin inhibitor light chain]: Proteolytically cleaved by PRSS3 at Kunitz domain 2. {ECO:0000269|PubMed:25301953}.; PTM: N-glycosylated. N-glycan heterogeneity at Asn-115: Hex5HexNAc4 (major), Hex6HexNAc5 (minor) and dHex1Hex6HexNAc5 (minor). N-glycan at Asn-250: Hex5HexNAc4. {ECO:0000269|PubMed:1694784, ECO:0000269|PubMed:22171320, ECO:0000269|PubMed:6171497}.; PTM: O-glycosylated. O-linkage of the glycosaminoglycan, chondroitin sulfate, at Ser-215 allows cross-linking between the three polypeptide chains. {ECO:0000269|PubMed:1694784, ECO:0000269|PubMed:1898736, ECO:0000269|PubMed:22171320, ECO:0000269|PubMed:6171497, ECO:0000269|PubMed:7682553}.
|
SUBCELLULAR LOCATION: [Alpha-1-microglobulin]: Secreted {ECO:0000269|PubMed:11877257, ECO:0000269|PubMed:32092412, ECO:0000269|PubMed:37453717}. Endoplasmic reticulum {ECO:0000269|PubMed:22096585}. Cytoplasm, cytosol {ECO:0000269|PubMed:32092412}. Cell membrane {ECO:0000269|PubMed:22096585, ECO:0000269|PubMed:32092412}; Peripheral membrane protein {ECO:0000305|PubMed:22096585, ECO:0000305|PubMed:32092412}. Nucleus membrane {ECO:0000269|PubMed:22096585}; Peripheral membrane protein {ECO:0000305|PubMed:22096585}. Mitochondrion inner membrane {ECO:0000305|PubMed:23157686}; Peripheral membrane protein {ECO:0000305|PubMed:23157686}. Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:22096585}. Note=The cellular uptake occurs via a non-endocytotic pathway and allows for localization to various membrane structures. A specific binding to plasma membrane suggests the presence of a cell receptor, yet to be identified. Directly binds collagen fibers type I. {ECO:0000269|PubMed:22096585}.; SUBCELLULAR LOCATION: [Inter-alpha-trypsin inhibitor light chain]: Secreted {ECO:0000269|PubMed:25326458, ECO:0000269|PubMed:36213313}.
| null | null | null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: The reductase activity toward cytochrome c increases at alkaline pH 8-9 when compared to pH 6-7. {ECO:0000269|PubMed:15683711};
| null |
FUNCTION: [Alpha-1-microglobulin]: Antioxidant and tissue repair protein with reductase, heme-binding and radical-scavenging activities. Removes and protects against harmful oxidants and repairs macromolecules in intravascular and extravascular spaces and in intracellular compartments (PubMed:11877257, PubMed:15683711, PubMed:22096585, PubMed:23157686, PubMed:23642167, PubMed:25698971, PubMed:32092412, PubMed:32823731). Intravascularly, plays a regulatory role in red cell homeostasis by preventing heme- and reactive oxygen species-induced cell damage. Binds and degrades free heme to protect fetal and adult red blood cells from hemolysis (PubMed:11877257, PubMed:32092412). Reduces extracellular methemoglobin, a Fe3+ (ferric) form of hemoglobin that cannot bind oxygen, back to the Fe2+ (ferrous) form deoxyhemoglobin, which has oxygen-carrying potential (PubMed:15683711). Upon acute inflammation, inhibits oxidation of low-density lipoprotein particles by MPO and limits vascular damage (PubMed:25698971). Extravascularly, protects from oxidation products formed on extracellular matrix structures and cell membranes. Catalyzes the reduction of carbonyl groups on oxidized collagen fibers and preserves cellular and extracellular matrix ultrastructures (PubMed:22096585, PubMed:23642167). Importantly, counteracts the oxidative damage at blood-placenta interface, preventing leakage of free fetal hemoglobin into the maternal circulation (PubMed:21356557). Intracellularly, has a role in maintaining mitochondrial redox homeostasis. Bound to complex I of the respiratory chain of mitochondria, may scavenge free radicals and preserve mitochondrial ATP synthesis. Protects renal tubule epithelial cells from heme-induced oxidative damage to mitochondria (PubMed:23157686, PubMed:32823731). Reduces cytochrome c from Fe3+ (ferric) to the Fe2+ (ferrous) state through formation of superoxide anion radicals in the presence of ascorbate or NADH/NADPH electron donor cofactors, ascorbate being the preferred cofactor (PubMed:15683711). Has a chaperone role in facilitating the correct folding of bikunin in the endoplasmic reticulum compartment (By similarity). {ECO:0000250|UniProtKB:Q07456, ECO:0000269|PubMed:11877257, ECO:0000269|PubMed:15683711, ECO:0000269|PubMed:21356557, ECO:0000269|PubMed:22096585, ECO:0000269|PubMed:23157686, ECO:0000269|PubMed:23642167, ECO:0000269|PubMed:25698971, ECO:0000269|PubMed:32092412, ECO:0000269|PubMed:32823731}.; FUNCTION: [Inter-alpha-trypsin inhibitor light chain]: Kunitz-type serine protease inhibitor and structural component of extracellular matrix with a role in extracellular space remodeling and cell adhesion (PubMed:20463016, PubMed:25301953). Among others, has antiprotease activity toward kallikrein, a protease involved in airway inflammation; inhibits GZMK/granzyme, a granule-stored serine protease involved in NK and T cell cytotoxic responses; and inhibits PLG/plasmin, a protease required for activation of matrix metalloproteinases (PubMed:10480954, PubMed:15917224, PubMed:16873769). As part of I-alpha-I complex, provides for the heavy chains to be transferred from I-alpha-I complex to hyaluronan in the presence of TNFAIP6, in a dynamic process that releases free bikunin and remodels extracellular matrix proteoglycan structures. Free bikunin, but not its heavy chain-bound form, acts as potent protease inhibitor in airway secretions (PubMed:16873769). Part of hyaluronan-rich extracellular matrix that surrounds oocyte during cumulus oophorus expansion, an indispensable process for proper ovulation (By similarity). Also inhibits calcium oxalate crystallization (PubMed:7676539). {ECO:0000250|UniProtKB:Q07456, ECO:0000269|PubMed:10480954, ECO:0000269|PubMed:15917224, ECO:0000269|PubMed:16873769, ECO:0000269|PubMed:20463016, ECO:0000269|PubMed:25301953, ECO:0000269|PubMed:7676539}.; FUNCTION: [Trypstatin]: Kunitz-type serine protease inhibitor. Has high catalytic efficiency for F10/blood coagulation factor Xa and may act as an anticoagulant by inhibiting prothrombin activation. Inhibits trypsin and mast cell CMA1/chymase and tryptase proteases. {ECO:0000250|UniProtKB:Q64240}.
|
Homo sapiens (Human)
|
P02761
|
MUP_RAT
|
MKLLLLLLCLGLTLVCGHAEEASSTRGNLDVAKLNGDWFSIVVASNKREKIEENGSMRVFMQHIDVLENSLGFKFRIKENGECRELYLVAYKTPEDGEYFVEYDGGNTFTILKTDYDRYVMFHLINFKNGETFQLMVLYGRTKDLSSDIKEKFAKLCEAHGITRDNIIDLTKTDRCLQARG
| null | null |
aerobic respiration [GO:0009060]; cellular response to lipid [GO:0071396]; energy reserve metabolic process [GO:0006112]; glucose homeostasis [GO:0042593]; heat generation [GO:0031649]; locomotor rhythm [GO:0045475]; mitochondrion organization [GO:0007005]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of gluconeogenesis [GO:0045721]; negative regulation of insulin secretion involved in cellular response to glucose stimulus [GO:0061179]; negative regulation of lipid biosynthetic process [GO:0051055]; negative regulation of lipid storage [GO:0010888]; positive regulation of gene expression [GO:0010628]; positive regulation of glucose metabolic process [GO:0010907]; positive regulation of lipid metabolic process [GO:0045834]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]
|
cytosol [GO:0005829]; extracellular space [GO:0005615]; nucleus [GO:0005634]
|
insulin receptor activity [GO:0005009]; odorant binding [GO:0005549]; pheromone binding [GO:0005550]; small molecule binding [GO:0036094]
|
PF00061;
|
2.40.128.20;
|
Calycin superfamily, Lipocalin family
| null |
SUBCELLULAR LOCATION: [15.5 kDa fatty acid-binding protein]: Cytoplasm, cytosol. Note=It is probably taken up from the urinary lumen by endocytosis.; SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Major urinary proteins (Mups) bind and release pheromones. They may also protect pheromones from oxidation. In this context, they play a role in the regulation of social behaviors, such as aggression, mating, pup-suckling, territory establishment and dominance. Acts as a kairomone, detected by the prey vomeronasal organ and inducing fear reactions in mice.
|
Rattus norvegicus (Rat)
|
P02762
|
MUP6_MOUSE
|
MKMLLLLCLGLTLVCVHAEEASSTGRNFNVEKINGEWHTIILASDKREKIEDNGNFRLFLEQIHVLENSLVLKFHTVRDEECSELSMVADKTEKAGEYSVTYDGFNTFTIPKTDYDNFLMAHLINEKDGETFQLMGLYGREPDLSSDIKERFAQLCEEHGILRENIIDLSNANRCLQARE
| null | null |
aerobic respiration [GO:0009060]; cellular response to lipid [GO:0071396]; energy reserve metabolic process [GO:0006112]; glucose homeostasis [GO:0042593]; heat generation [GO:0031649]; locomotor rhythm [GO:0045475]; mitochondrion organization [GO:0007005]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of gluconeogenesis [GO:0045721]; negative regulation of insulin secretion involved in cellular response to glucose stimulus [GO:0061179]; negative regulation of lipid biosynthetic process [GO:0051055]; negative regulation of lipid storage [GO:0010888]; positive regulation of gene expression [GO:0010628]; positive regulation of glucose metabolic process [GO:0010907]; positive regulation of lipid metabolic process [GO:0045834]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]
|
cytosol [GO:0005829]; extracellular space [GO:0005615]; nucleus [GO:0005634]
|
insulin receptor activity [GO:0005009]; odorant binding [GO:0005549]; pheromone binding [GO:0005550]; small molecule binding [GO:0036094]
|
PF00061;
|
2.40.128.20;
|
Calycin superfamily, Lipocalin family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Binds pheromones that are released from drying urine of males. These pheromones affect the sexual behavior of females.
|
Mus musculus (Mouse)
|
P02763
|
A1AG1_HUMAN
|
MALSWVLTVLSLLPLLEAQIPLCANLVPVPITNATLDRITGKWFYIASAFRNEEYNKSVQEIQATFFYFTPNKTEDTIFLREYQTRQDQCIYNTTYLNVQRENGTISRYVGGQEHFAHLLILRDTKTYMLAFDVNDEKNWGLSVYADKPETTKEQLGEFYEALDCLRIPKSDVVYTDWKKDKCEPLEKQHEKERKQEEGES
| null | null |
acute-phase response [GO:0006953]; inflammatory response [GO:0006954]; negative regulation of interleukin-6 production [GO:0032715]; negative regulation of tumor necrosis factor production [GO:0032720]; positive regulation of interleukin-1 beta production [GO:0032731]; positive regulation of interleukin-1 production [GO:0032732]; positive regulation of tumor necrosis factor production [GO:0032760]; regulation of immune system process [GO:0002682]
|
blood microparticle [GO:0072562]; collagen-containing extracellular matrix [GO:0062023]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; platelet alpha granule lumen [GO:0031093]; specific granule lumen [GO:0035580]; tertiary granule lumen [GO:1904724]
| null |
PF00061;
|
2.40.128.20;
|
Calycin superfamily, Lipocalin family
|
PTM: N-glycosylated. N-glycan heterogeneity at Asn-33: Hex5HexNAc4 (minor), Hex6HexNAc5 (major) and dHex1Hex6HexNAc5 (minor). {ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:15253437, ECO:0000269|PubMed:1567356, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:16740002, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:22171320}.
|
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Functions as a transport protein in the blood stream. Binds various ligands in the interior of its beta-barrel domain. Also binds synthetic drugs and influences their distribution and availability in the body. Appears to function in modulating the activity of the immune system during the acute-phase reaction. {ECO:0000269|PubMed:17008009, ECO:0000269|PubMed:17321687}.
|
Homo sapiens (Human)
|
P02764
|
A1AG_RAT
|
MALHMVLVVLSLLPLLEAQNPEPANITLGIPITNETLKWLSDKWFYMGAAFRDPVFKQAVQTIQTEYFYLTPNLINDTIELREFQTTDDQCVYNFTHLGVQRENGTLSKCAGAVKIFAHLIVLKKHGTFMLAFNLTDENRGLSFYAKKPDLSPELRKIFQQAVKDVGMDESEIVFVDWTKDKCSEQQKQQLELEKETKKETKKDP
| null | null |
acute inflammatory response to antigenic stimulus [GO:0002438]; acute-phase response [GO:0006953]; animal organ regeneration [GO:0031100]; cellular response to glucocorticoid stimulus [GO:0071385]; cellular response to growth hormone stimulus [GO:0071378]; cellular response to retinoic acid [GO:0071300]; chronic inflammatory response to antigenic stimulus [GO:0002439]; negative regulation of interleukin-6 production [GO:0032715]; negative regulation of tumor necrosis factor production [GO:0032720]; positive regulation of interleukin-1 beta production [GO:0032731]; positive regulation of interleukin-1 production [GO:0032732]; positive regulation of tumor necrosis factor production [GO:0032760]; regulation of immune system process [GO:0002682]; response to lipopolysaccharide [GO:0032496]; response to organic cyclic compound [GO:0014070]; response to vitamin E [GO:0033197]; response to xenobiotic stimulus [GO:0009410]
|
extracellular space [GO:0005615]
|
small molecule binding [GO:0036094]
|
PF00061;
|
2.40.128.20;
|
Calycin superfamily, Lipocalin family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Functions as a transport protein in the blood stream. Binds various ligands in the interior of its beta-barrel domain (By similarity). Appears to function in modulating the activity of the immune system during the acute-phase reaction. {ECO:0000250}.
|
Rattus norvegicus (Rat)
|
P02765
|
FETUA_HUMAN
|
MKSLVLLLCLAQLWGCHSAPHGPGLIYRQPNCDDPETEEAALVAIDYINQNLPWGYKHTLNQIDEVKVWPQQPSGELFEIEIDTLETTCHVLDPTPVARCSVRQLKEHAVEGDCDFQLLKLDGKFSVVYAKCDSSPDSAEDVRKVCQDCPLLAPLNDTRVVHAAKAALAAFNAQNNGSNFQLEEISRAQLVPLPPSTYVEFTVSGTDCVAKEATEAAKCNLLAEKQYGFCKATLSEKLGGAEVAVTCMVFQTQPVSSQPQPEGANEAVPTPVVDPDAPPSPPLGAPGLPPAGSPPDSHVLLAAPPGHQLHRAHYDLRHTFMGVVSLGSPSGEVSHPRKTRTVVQPSVGAAAGPVVPPCPGRIRHFKV
| null | null |
acute-phase response [GO:0006953]; negative regulation of bone mineralization [GO:0030502]; negative regulation of insulin receptor signaling pathway [GO:0046627]; ossification [GO:0001503]; pinocytosis [GO:0006907]; positive regulation of phagocytosis [GO:0050766]; regulation of bone mineralization [GO:0030500]; regulation of inflammatory response [GO:0050727]; skeletal system development [GO:0001501]
|
blood microparticle [GO:0072562]; collagen-containing extracellular matrix [GO:0062023]; endoplasmic reticulum lumen [GO:0005788]; extracellular exosome [GO:0070062]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; platelet alpha granule lumen [GO:0031093]; secretory granule lumen [GO:0034774]
|
cysteine-type endopeptidase inhibitor activity [GO:0004869]; endopeptidase inhibitor activity [GO:0004866]; kinase inhibitor activity [GO:0019210]
|
PF00031;
|
3.10.450.10;
|
Fetuin family
|
PTM: Phosphorylated by FAM20C in the extracellular medium. {ECO:0000269|PubMed:11439093, ECO:0000269|PubMed:26091039}.; PTM: O- and N-glycosylated. O-glycosylated with core 1 or possibly core 8 glycans. N-glycan at Asn-156: Hex5HexNAc4; N-glycan heterogeneity at Asn-176: Hex5HexNAc4 (major) and Hex6HexNAc5 (minor). {ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:16740002, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:22171320}.
|
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Promotes endocytosis, possesses opsonic properties and influences the mineral phase of bone. Shows affinity for calcium and barium ions.
|
Homo sapiens (Human)
|
P02766
|
TTHY_HUMAN
|
MASHRLLLLCLAGLVFVSEAGPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE
| null | null |
purine nucleobase metabolic process [GO:0006144]
|
azurophil granule lumen [GO:0035578]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]
|
hormone activity [GO:0005179]; identical protein binding [GO:0042802]; thyroid hormone binding [GO:0070324]
|
PF00576;
|
2.60.40.180;
|
Transthyretin family
|
PTM: Not glycosylated under normal conditions. Following unfolding, caused for example by variant AMYL-TTR 'Gly-38', the cryptic Asn-118 site is exposed and glycosylated by STT3B-containing OST complex, leading to its degradation by the ER-associated degradation (ERAD) pathway. {ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19167329}.; PTM: Sulfonation of the reactive cysteine Cys-30 enhances the stability of the native conformation of TTR, avoiding misassembly of the protein leading to amyloid formation. {ECO:0000305|PubMed:17175208}.
|
SUBCELLULAR LOCATION: Secreted. Cytoplasm.
| null | null | null | null | null |
FUNCTION: Thyroid hormone-binding protein. Probably transports thyroxine from the bloodstream to the brain. {ECO:0000269|PubMed:3714052}.
|
Homo sapiens (Human)
|
P02767
|
TTHY_RAT
|
MASLRLFLLCLAGLIFASEAGPGGAGESKCPLMVKVLDAVRGSPAVDVAVKVFKKTADGSWEPFASGKTAESGELHGLTTDEKFTEGVYRVELDTKSYWKALGISPFHEYAEVVFTANDSGHRHYTIAALLSPYSYSTTAVVSNPQN
| null | null |
purine nucleobase metabolic process [GO:0006144]; thyroid hormone metabolic process [GO:0042403]
|
extracellular space [GO:0005615]; protein-containing complex [GO:0032991]
|
hormone activity [GO:0005179]; hormone binding [GO:0042562]; identical protein binding [GO:0042802]; protein-containing complex binding [GO:0044877]; thyroid hormone binding [GO:0070324]
|
PF00576;
|
2.60.40.180;
|
Transthyretin family
|
PTM: Sulfonation of the reactive cysteine Cys-30 enhances the stability of the native conformation of TTR, avoiding misassembly of the protein leading to amyloid formation. {ECO:0000250|UniProtKB:P02766}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2309926, ECO:0000269|PubMed:873934}.
| null | null | null | null | null |
FUNCTION: Thyroid hormone-binding protein. Probably transports thyroxine from the bloodstream to the brain. {ECO:0000269|PubMed:2309926}.
|
Rattus norvegicus (Rat)
|
P02768
|
ALBU_HUMAN
|
MKWVTFISLLFLFSSAYSRGVFRRDAHKSEVAHRFKDLGEENFKALVLIAFAQYLQQCPFEDHVKLVNEVTEFAKTCVADESAENCDKSLHTLFGDKLCTVATLRETYGEMADCCAKQEPERNECFLQHKDDNPNLPRLVRPEVDVMCTAFHDNEETFLKKYLYEIARRHPYFYAPELLFFAKRYKAAFTECCQAADKAACLLPKLDELRDEGKASSAKQRLKCASLQKFGERAFKAWAVARLSQRFPKAEFAEVSKLVTDLTKVHTECCHGDLLECADDRADLAKYICENQDSISSKLKECCEKPLLEKSHCIAEVENDEMPADLPSLAADFVESKDVCKNYAEAKDVFLGMFLYEYARRHPDYSVVLLLRLAKTYETTLEKCCAAADPHECYAKVFDEFKPLVEEPQNLIKQNCELFEQLGEYKFQNALLVRYTKKVPQVSTPTLVEVSRNLGKVGSKCCKHPEAKRMPCAEDYLSVVLNQLCVLHEKTPVSDRVTKCCTESLVNRRPCFSALEVDETYVPKEFNAETFTFHADICTLSEKERQIKKQTALVELVKHKPKATKEQLKAVMDDFAAFVEKCCKADDKETCFAEEGKKLVAASQAALGL
| null | null |
cellular response to calcium ion starvation [GO:0072732]; cellular response to starvation [GO:0009267]; negative regulation of mitochondrial depolarization [GO:0051902]
|
blood microparticle [GO:0072562]; cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum lumen [GO:0005788]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; nucleus [GO:0005634]; platelet alpha granule lumen [GO:0031093]; protein-containing complex [GO:0032991]
|
antioxidant activity [GO:0016209]; copper ion binding [GO:0005507]; DNA binding [GO:0003677]; enterobactin binding [GO:1903981]; exogenous protein binding [GO:0140272]; fatty acid binding [GO:0005504]; identical protein binding [GO:0042802]; protein-folding chaperone binding [GO:0051087]; pyridoxal phosphate binding [GO:0030170]; small molecule binding [GO:0036094]; toxic substance binding [GO:0015643]
|
PF00273;
|
1.10.246.10;
|
ALB/AFP/VDB family
|
PTM: Kenitra variant is partially O-glycosylated at Thr-620. It has two new disulfide bonds Cys-600 to Cys-602 and Cys-601 to Cys-606.; PTM: Glycated in diabetic patients.; PTM: Phosphorylated by FAM20C in the extracellular medium. {ECO:0000269|PubMed:26091039}.; PTM: Acetylated on Lys-223 by acetylsalicylic acid.
|
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Binds water, Ca(2+), Na(+), K(+), fatty acids, hormones, bilirubin and drugs (Probable). Its main function is the regulation of the colloidal osmotic pressure of blood (Probable). Major zinc transporter in plasma, typically binds about 80% of all plasma zinc (PubMed:19021548). Major calcium and magnesium transporter in plasma, binds approximately 45% of circulating calcium and magnesium in plasma (By similarity). Potentially has more than two calcium-binding sites and might additionally bind calcium in a non-specific manner (By similarity). The shared binding site between zinc and calcium at residue Asp-273 suggests a crosstalk between zinc and calcium transport in the blood (By similarity). The rank order of affinity is zinc > calcium > magnesium (By similarity). Binds to the bacterial siderophore enterobactin and inhibits enterobactin-mediated iron uptake of E.coli from ferric transferrin, and may thereby limit the utilization of iron and growth of enteric bacteria such as E.coli (PubMed:6234017). Does not prevent iron uptake by the bacterial siderophore aerobactin (PubMed:6234017). {ECO:0000250|UniProtKB:P02769, ECO:0000269|PubMed:19021548, ECO:0000269|PubMed:6234017, ECO:0000305|PubMed:1630489}.
|
Homo sapiens (Human)
|
P02769
|
ALBU_BOVIN
|
MKWVTFISLLLLFSSAYSRGVFRRDTHKSEIAHRFKDLGEEHFKGLVLIAFSQYLQQCPFDEHVKLVNELTEFAKTCVADESHAGCEKSLHTLFGDELCKVASLRETYGDMADCCEKQEPERNECFLSHKDDSPDLPKLKPDPNTLCDEFKADEKKFWGKYLYEIARRHPYFYAPELLYYANKYNGVFQECCQAEDKGACLLPKIETMREKVLASSARQRLRCASIQKFGERALKAWSVARLSQKFPKAEFVEVTKLVTDLTKVHKECCHGDLLECADDRADLAKYICDNQDTISSKLKECCDKPLLEKSHCIAEVEKDAIPENLPPLTADFAEDKDVCKNYQEAKDAFLGSFLYEYSRRHPEYAVSVLLRLAKEYEATLEECCAKDDPHACYSTVFDKLKHLVDEPQNLIKQNCDQFEKLGEYGFQNALIVRYTRKVPQVSTPTLVEVSRSLGKVGTRCCTKPESERMPCTEDYLSLILNRLCVLHEKTPVSEKVTKCCTESLVNRRPCFSALTPDETYVPKAFDEKLFTFHADICTLPDTEKQIKKQTALVELLKHKPKATEEQLKTVMENFVAFVDKCCAADDKEACFAVEGPKLVVSTQTALA
| null | null |
cellular response to calcium ion starvation [GO:0072732]; cellular response to starvation [GO:0009267]; negative regulation of mitochondrial depolarization [GO:0051902]
|
blood microparticle [GO:0072562]; cytoplasm [GO:0005737]; extracellular region [GO:0005576]; protein-containing complex [GO:0032991]
|
DNA binding [GO:0003677]; enterobactin binding [GO:1903981]; fatty acid binding [GO:0005504]; metal ion binding [GO:0046872]; pyridoxal phosphate binding [GO:0030170]; small molecule binding [GO:0036094]; toxic substance binding [GO:0015643]
|
PF00273;
|
1.10.246.10;
|
ALB/AFP/VDB family
|
PTM: Phosphorylated by FAM20C in the extracellular medium. {ECO:0000250|UniProtKB:P02768}.
|
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Binds water, Ca(2+), Na(+), K(+), fatty acids, hormones, bilirubin and drugs. Its main function is the regulation of the colloidal osmotic pressure of blood. Major zinc transporter in plasma, typically binds about 80% of all plasma zinc (By similarity). Major calcium and magnesium transporter in plasma, binds approximately 45% of circulating calcium and magnesium in plasma (Probable). Potentially has more than two calcium-binding sites and might additionally bind calcium in a non-specific manner (PubMed:22677715). The shared binding site between zinc and calcium at residue Asp-272 suggests a crosstalk between zinc and calcium transport in the blood (Probable). The rank order of affinity is zinc > calcium > magnesium (Probable). Binds to the bacterial siderophore enterobactin and inhibits enterobactin-mediated iron uptake of E.coli, and may thereby limit the utilization of iron and growth of enteric bacteria such as E.coli (PubMed:6234017). Does not prevent iron uptake by the bacterial siderophore aerobactin (PubMed:6234017). {ECO:0000250|UniProtKB:P02768, ECO:0000269|PubMed:22677715, ECO:0000269|PubMed:6234017, ECO:0000305|PubMed:22677715}.
|
Bos taurus (Bovine)
|
P02770
|
ALBU_RAT
|
MKWVTFLLLLFISGSAFSRGVFRREAHKSEIAHRFKDLGEQHFKGLVLIAFSQYLQKCPYEEHIKLVQEVTDFAKTCVADENAENCDKSIHTLFGDKLCAIPKLRDNYGELADCCAKQEPERNECFLQHKDDNPNLPPFQRPEAEAMCTSFQENPTSFLGHYLHEVARRHPYFYAPELLYYAEKYNEVLTQCCTESDKAACLTPKLDAVKEKALVAAVRQRMKCSSMQRFGERAFKAWAVARMSQRFPNAEFAEITKLATDVTKINKECCHGDLLECADDRAELAKYMCENQATISSKLQACCDKPVLQKSQCLAEIEHDNIPADLPSIAADFVEDKEVCKNYAEAKDVFLGTFLYEYSRRHPDYSVSLLLRLAKKYEATLEKCCAEGDPPACYGTVLAEFQPLVEEPKNLVKTNCELYEKLGEYGFQNAVLVRYTQKAPQVSTPTLVEAARNLGRVGTKCCTLPEAQRLPCVEDYLSAILNRLCVLHEKTPVSEKVTKCCSGSLVERRPCFSALTVDETYVPKEFKAETFTFHSDICTLPDKEKQIKKQTALAELVKHKPKATEDQLKTVMGDFAQFVDKCCKAADKDNCFATEGPNLVARSKEALA
| null | null |
cellular response to calcium ion starvation [GO:0072732]; cellular response to starvation [GO:0009267]; negative regulation of mitochondrial depolarization [GO:0051902]; positive regulation of circadian sleep/wake cycle, non-REM sleep [GO:0046010]; response to mercury ion [GO:0046689]; response to nutrient [GO:0007584]; response to organic substance [GO:0010033]; response to platinum ion [GO:0070541]; vasodilation [GO:0042311]
|
basement membrane [GO:0005604]; blood microparticle [GO:0072562]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; protein-containing complex [GO:0032991]
|
DNA binding [GO:0003677]; enterobactin binding [GO:1903981]; enzyme binding [GO:0019899]; exogenous protein binding [GO:0140272]; fatty acid binding [GO:0005504]; identical protein binding [GO:0042802]; modified amino acid binding [GO:0072341]; protein-folding chaperone binding [GO:0051087]; pyridoxal phosphate binding [GO:0030170]; small molecule binding [GO:0036094]; toxic substance binding [GO:0015643]; zinc ion binding [GO:0008270]
|
PF00273;
|
1.10.246.10;
|
ALB/AFP/VDB family
|
PTM: Phosphorylated by FAM20C in the extracellular medium. {ECO:0000250|UniProtKB:P02768}.
|
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Binds water, Ca(2+), Na(+), K(+), fatty acids, hormones, bilirubin and drugs. Its main function is the regulation of the colloidal osmotic pressure of blood. Major zinc transporter in plasma, typically binds about 80% of all plasma zinc (By similarity). Major calcium and magnesium transporter in plasma, binds approximately 45% of circulating calcium and magnesium in plasma (By similarity). Potentially has more than two calcium-binding sites and might additionally bind calcium in a non-specific manner (By similarity). The shared binding site between zinc and calcium at residue Asp-273 suggests a crosstalk between zinc and calcium transport in the blood (By similarity). The rank order of affinity is zinc > calcium > magnesium (By similarity). Binds to the bacterial siderophore enterobactin and inhibits enterobactin-mediated iron uptake of E.coli from ferric transferrin, and may thereby limit the utilization of iron and growth of enteric bacteria such as E.coli (By similarity). Does not prevent iron uptake by the bacterial siderophore aerobactin (By similarity). {ECO:0000250|UniProtKB:P02768, ECO:0000250|UniProtKB:P02769}.
|
Rattus norvegicus (Rat)
|
P02771
|
FETA_HUMAN
|
MKWVESIFLIFLLNFTESRTLHRNEYGIASILDSYQCTAEISLADLATIFFAQFVQEATYKEVSKMVKDALTAIEKPTGDEQSSGCLENQLPAFLEELCHEKEILEKYGHSDCCSQSEEGRHNCFLAHKKPTPASIPLFQVPEPVTSCEAYEEDRETFMNKFIYEIARRHPFLYAPTILLWAARYDKIIPSCCKAENAVECFQTKAATVTKELRESSLLNQHACAVMKNFGTRTFQAITVTKLSQKFTKVNFTEIQKLVLDVAHVHEHCCRGDVLDCLQDGEKIMSYICSQQDTLSNKITECCKLTTLERGQCIIHAENDEKPEGLSPNLNRFLGDRDFNQFSSGEKNIFLASFVHEYSRRHPQLAVSVILRVAKGYQELLEKCFQTENPLECQDKGEEELQKYIQESQALAKRSCGLFQKLGEYYLQNAFLVAYTKKAPQLTSSELMAITRKMAATAATCCQLSEDKLLACGEGAADIIIGHLCIRHEMTPVNPGVGQCCTSSYANRRPCFSSLVVDETYVPPAFSDDKFIFHKDLCQAQGVALQTMKQEFLINLVKQKPQITEEQLEAVIADFSGLLEKCCQGQEQEVCFAEEGQKLISKTRAALGV
| null | null |
ovulation from ovarian follicle [GO:0001542]; progesterone metabolic process [GO:0042448]
|
blood microparticle [GO:0072562]; cytoplasm [GO:0005737]; endoplasmic reticulum lumen [GO:0005788]
|
metal ion binding [GO:0046872]; small molecule binding [GO:0036094]
|
PF00273;
|
1.10.246.10;
|
ALB/AFP/VDB family
|
PTM: Independent studies suggest heterogeneity of the N-terminal sequence of the mature protein and of the cleavage site of the signal sequence.; PTM: Sulfated. {ECO:0000269|PubMed:2414772}.
|
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Binds copper, nickel, and fatty acids as well as, and bilirubin less well than, serum albumin. Only a small percentage (less than 2%) of the human AFP shows estrogen-binding properties.
|
Homo sapiens (Human)
|
P02772
|
FETA_MOUSE
|
MKWITPASLILLLHFAASKALHENEFGIASTLDSSQCVTEKNVLSIATITFTQFVPEATEEEVNKMTSDVLAAMKKNSGDGCLESQLSVFLDEICHETELSNKYGLSGCCSQSGVERHQCLLARKKTAPASVPPFQFPEPAESCKAHEENRAVFMNRFIYEVSRRNPFMYAPAILSLAAQYDKVVLACCKADNKEECFQTKRASIAKELREGSMLNEHVCSVIRKFGSRNLQATTIIKLSQKLTEANFTEIQKLALDVAHIHEECCQGNSLECLQDGEKVMTYICSQQNILSSKIAECCKLPMIQLGFCIIHAENGVKPEGLSLNPSQFLGDRNFAQFSSEEKIMFMASFLHEYSRTHPNLPVSVILRIAKTYQEILEKCSQSGNLPGCQDNLEEELQKHIEESQALSKQSCALYQTLGDYKLQNLFLIGYTRKAPQLTSAELIDLTGKMVSIASTCCQLSEEKWSGCGEGMADIFIGHLCIRNEASPVNSGISHCCNSSYSNRRLCITSFLRDETYAPPPFSEDKFIFHKDLCQAQGKALQTMKQELLINLVKQKPELTEEQLAAVTADFSGLLEKCCKAQDQEVCFTEEGPKLISKTRDALGV
| null | null |
ovulation from ovarian follicle [GO:0001542]; progesterone metabolic process [GO:0042448]; sexual reproduction [GO:0019953]
|
blood microparticle [GO:0072562]; cytoplasm [GO:0005737]; extracellular space [GO:0005615]
|
metal ion binding [GO:0046872]; small molecule binding [GO:0036094]
|
PF00273;
|
1.10.246.10;
|
ALB/AFP/VDB family
|
PTM: Glycosylated; contains two glycans.; PTM: Sulfated. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Binds estrogens, fatty acids and metals.
|
Mus musculus (Mouse)
|
P02773
|
FETA_RAT
|
MKQPATMKWSASISFLLLLNFAEPRVLHTNEFGIESTLDSSQCPTEKNMFNVATIVVAQFVQDATKAEVNKMSSDALAAMKENTGDGCLENQLSVFLDEICHETELSNKYGFSGCCNQSGVERHQCLLARKKTAPDSVPPFHFPETAESCPAYEENRAMSINTFIYDVSKRNPFLYAPTILYLAAQYDKAVPACCKADNMEECFQTKRASMAKELREGSMLNEHVCAVIRKFGSRNLQAVLIIKLSQKFPKANITEIRKLALDVAHIHEQCCHGNAMECLQDGESVMTHMCSQQEILSSKTAECCKLPTIELGYCIIHAENGDKPEGLTLNPSEFLGDRNFAQFSSEEKLLFMASFLHEYSRNHPNLPVSVILKTAKSYQEILEKCSQSETPSKCQDNMEEELQKHIQESQALAKQSCNLYQKLGPYYLQNLFLIGYTRKAPQLTSAELIDLTGKMVSIASTCCQLSEEKRSACGEGLADIYIGHLCLRHEANPVNSGINHCCSSSYSNRRLCITSFLRDETYVPPPFSEDKFIFHKDLCQAQGRALQTMKQELLINLVKQKPEMTEEQHAAVTADFSGLLEKCCKDQDQEACFAKEGPKLISKTREALGV
| null | null |
animal organ regeneration [GO:0031100]; cellular response to retinoic acid [GO:0071300]; liver development [GO:0001889]; liver regeneration [GO:0097421]; ovulation from ovarian follicle [GO:0001542]; pancreas development [GO:0031016]; progesterone metabolic process [GO:0042448]; response to dexamethasone [GO:0071548]; response to organic substance [GO:0010033]; sexual reproduction [GO:0019953]
|
blood microparticle [GO:0072562]; cytoplasm [GO:0005737]; extracellular space [GO:0005615]
|
metal ion binding [GO:0046872]; small molecule binding [GO:0036094]
|
PF00273;
|
1.10.246.10;
|
ALB/AFP/VDB family
|
PTM: Sulfated. {ECO:0000250}.
|
SUBCELLULAR LOCATION: [Isoform 1]: Secreted.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm.
| null | null | null | null | null |
FUNCTION: Binds estrogens, fatty acids and metals.
|
Rattus norvegicus (Rat)
|
P02774
|
VTDB_HUMAN
|
MKRVLVLLLAVAFGHALERGRDYEKNKVCKEFSHLGKEDFTSLSLVLYSRKFPSGTFEQVSQLVKEVVSLTEACCAEGADPDCYDTRTSALSAKSCESNSPFPVHPGTAECCTKEGLERKLCMAALKHQPQEFPTYVEPTNDEICEAFRKDPKEYANQFMWEYSTNYGQAPLSLLVSYTKSYLSMVGSCCTSASPTVCFLKERLQLKHLSLLTTLSNRVCSQYAAYGEKKSRLSNLIKLAQKVPTADLEDVLPLAEDITNILSKCCESASEDCMAKELPEHTVKLCDNLSTKNSKFEDCCQEKTAMDVFVCTYFMPAAQLPELPDVELPTNKDVCDPGNTKVMDKYTFELSRRTHLPEVFLSKVLEPTLKSLGECCDVEDSTTCFNAKGPLLKKELSSFIDKGQELCADYSENTFTEYKKKLAERLKAKLPDATPTELAKLVNKHSDFASNCCSINSPPLYCDSEIDAELKNIL
| null | null |
vitamin D metabolic process [GO:0042359]; vitamin transport [GO:0051180]
|
blood microparticle [GO:0072562]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; lysosomal lumen [GO:0043202]
|
actin binding [GO:0003779]; calcidiol binding [GO:1902118]; vitamin D binding [GO:0005499]; vitamin transmembrane transporter activity [GO:0090482]
|
PF00273;PF09164;
|
1.10.246.10;
|
ALB/AFP/VDB family
|
PTM: Allele GC*1S is O-glycosylated at Thr-436 (PubMed:20079467). The trisaccharide sugar moiety can be modified by the successive removal of neuraminic acid and galactose leaving an O-mceeN-acetyl-galactosamine. This conversion is thought to produce a macrophage-activating factor (Gc-MAF). Only a minor proportion of plasma GC is O-glycosylated (PubMed:17360250). The potential N-glycosylation site predicted at Asn-288 is thought to be nonglycosylated. {ECO:0000269|PubMed:17360250, ECO:0000269|PubMed:20079467, ECO:0000305|PubMed:16302727}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2423133}.
| null | null | null | null | null |
FUNCTION: Involved in vitamin D transport and storage, scavenging of extracellular G-actin, enhancement of the chemotactic activity of C5 alpha for neutrophils in inflammation and macrophage activation. {ECO:0000305|PubMed:16302727}.
|
Homo sapiens (Human)
|
P02775
|
CXCL7_HUMAN
|
MSLRLDTTPSCNSARPLHALQVLLLLSLLLTALASSTKGQTKRNLAKGKEESLDSDLYAELRCMCIKTTSGIHPKNIQSLEVIGKGTHCNQVEVIATLKDGRKICLDPDAPRIKKIVQKKLAGDESAD
| null | null |
antimicrobial humoral immune response mediated by antimicrobial peptide [GO:0061844]; cellular response to lipopolysaccharide [GO:0071222]; chemokine-mediated signaling pathway [GO:0070098]; defense response to bacterium [GO:0042742]; glucose transmembrane transport [GO:1904659]; inflammatory response [GO:0006954]; neutrophil chemotaxis [GO:0030593]; positive regulation of cell division [GO:0051781]
|
extracellular region [GO:0005576]; extracellular space [GO:0005615]; platelet alpha granule lumen [GO:0031093]; tertiary granule lumen [GO:1904724]
|
chemokine activity [GO:0008009]; CXCR chemokine receptor binding [GO:0045236]; glucose transmembrane transporter activity [GO:0005355]; growth factor activity [GO:0008083]
|
PF00048;
|
2.40.50.40;
|
Intercrine alpha (chemokine CxC) family
|
PTM: Proteolytic removal of residues 1-9 produces the active peptide connective tissue-activating peptide III (CTAP-III) (low-affinity platelet factor IV (LA-PF4)).; PTM: Proteolytic removal of residues 1-13 produces the active peptide beta-thromboglobulin, which is released from platelets along with platelet factor 4 and platelet-derived growth factor.; PTM: NAP-2(1-66) is produced by proteolytical processing, probably after secretion by leukocytes other than neutrophils. {ECO:0000269|PubMed:9794434}.; PTM: NAP-2(73) and NAP-2(74) seem not be produced by proteolytical processing of secreted precursors but are released in an active form from platelets. {ECO:0000269|PubMed:9794434}.
|
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: LA-PF4 stimulates DNA synthesis, mitosis, glycolysis, intracellular cAMP accumulation, prostaglandin E2 secretion, and synthesis of hyaluronic acid and sulfated glycosaminoglycan. It also stimulates the formation and secretion of plasminogen activator by human synovial cells. NAP-2 is a ligand for CXCR1 and CXCR2, and NAP-2, NAP-2(73), NAP-2(74), NAP-2(1-66), and most potent NAP-2(1-63) are chemoattractants and activators for neutrophils. TC-1 and TC-2 are antibacterial proteins, in vitro released from activated platelet alpha-granules. CTAP-III(1-81) is more potent than CTAP-III desensitize chemokine-induced neutrophil activation. {ECO:0000269|PubMed:10877842, ECO:0000269|PubMed:7890771, ECO:0000269|PubMed:8950790, ECO:0000269|PubMed:9794434}.
|
Homo sapiens (Human)
|
P02776
|
PLF4_HUMAN
|
MSSAAGFCASRPGLLFLGLLLLPLVVAFASAEAEEDGDLQCLCVKTTSQVRPRHITSLEVIKAGPHCPTAQLIATLKNGRKICLDLQAPLYKKIIKKLLES
| null | null |
adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; antimicrobial humoral immune response mediated by antimicrobial peptide [GO:0061844]; cellular response to lipopolysaccharide [GO:0071222]; chemokine-mediated signaling pathway [GO:0070098]; cytokine-mediated signaling pathway [GO:0019221]; defense response to protozoan [GO:0042832]; inflammatory response [GO:0006954]; killing by host of symbiont cells [GO:0051873]; leukocyte chemotaxis [GO:0030595]; negative regulation of angiogenesis [GO:0016525]; negative regulation of extrinsic apoptotic signaling pathway in absence of ligand [GO:2001240]; negative regulation of megakaryocyte differentiation [GO:0045653]; negative regulation of MHC class II biosynthetic process [GO:0045347]; neutrophil chemotaxis [GO:0030593]; platelet activation [GO:0030168]; positive regulation of gene expression [GO:0010628]; positive regulation of macrophage derived foam cell differentiation [GO:0010744]; positive regulation of macrophage differentiation [GO:0045651]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of tumor necrosis factor production [GO:0032760]; regulation of cell population proliferation [GO:0042127]
|
collagen-containing extracellular matrix [GO:0062023]; cytoplasm [GO:0005737]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; platelet alpha granule lumen [GO:0031093]
|
chemokine activity [GO:0008009]; CXCR chemokine receptor binding [GO:0045236]; CXCR3 chemokine receptor binding [GO:0048248]; heparin binding [GO:0008201]
|
PF00048;
|
2.40.50.40;
|
Intercrine alpha (chemokine CxC) family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:7644496}.
| null | null | null | null | null |
FUNCTION: Chemokine released during platelet aggregation that plays a role in different biological processes including hematopoiesis, cell proliferation, differentiation, and activation (PubMed:9531587, PubMed:29930254). Acts via different functional receptors including CCR1, CXCR3A or CXCR3B (PubMed:18174362, PubMed:29930254). Upon interaction with CXCR3A receptor, induces activated T-lymphocytes migration mediated via downstream Ras/extracellular signal-regulated kinase (ERK) signaling (PubMed:18174362, PubMed:24469069). Neutralizes the anticoagulant effect of heparin by binding more strongly to heparin than to the chondroitin-4-sulfate chains of the carrier molecule. Plays a role in the inhibition of hematopoiesis and in the maintenance of hematopoietic stem cell (HSC) quiescence (PubMed:9531587). Chemotactic for neutrophils and monocytes via CCR1 (PubMed:29930254). Inhibits endothelial cell proliferation. In cooperation with toll-like receptor 8/TLR8, induces chromatin remodeling and activates inflammatory gene expression via the TBK1-IRF5 axis (PubMed:35701499). In addition, induces myofibroblast differentiation and collagen synthesis in different precursor cells, including endothelial cells, by stimulating endothelial-to-mesenchymal transition (PubMed:34986347). {ECO:0000269|PubMed:18174362, ECO:0000269|PubMed:24469069, ECO:0000269|PubMed:29930254, ECO:0000269|PubMed:34986347, ECO:0000269|PubMed:35701499, ECO:0000269|PubMed:7644496, ECO:0000269|PubMed:9531587}.
|
Homo sapiens (Human)
|
P02777
|
PLF4_BOVIN
|
ESSFPATFVPLPADSEGGEDEDLQCVCLKTTSGINPRHISSLEVIGAGTHCPSPQLLATKKTGRKICLDQQRPLYKKILKKLLDGDES
| null | null |
adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; antimicrobial humoral immune response mediated by antimicrobial peptide [GO:0061844]; cellular response to lipopolysaccharide [GO:0071222]; chemokine-mediated signaling pathway [GO:0070098]; cytokine-mediated signaling pathway [GO:0019221]; inflammatory response [GO:0006954]; leukocyte chemotaxis [GO:0030595]; negative regulation of angiogenesis [GO:0016525]; negative regulation of megakaryocyte differentiation [GO:0045653]; neutrophil chemotaxis [GO:0030593]; platelet activation [GO:0030168]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of cell population proliferation [GO:0042127]
|
extracellular space [GO:0005615]
|
chemokine activity [GO:0008009]; CXCR chemokine receptor binding [GO:0045236]; CXCR3 chemokine receptor binding [GO:0048248]; heparin binding [GO:0008201]
|
PF00048;
|
2.40.50.40;
|
Intercrine alpha (chemokine CxC) family
|
PTM: O-linked glycan consists of Gal-GalNAc disaccharide which is modified with sialic acid residues (microheterogeneity). {ECO:0000269|PubMed:2914894}.
|
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Chemokine released during platelet aggregation that plays a role in different biological processes including hematopoiesis, cell proliferation, differentiation, and activation. Acts via different functional receptors including CCR1, CXCR3A or CXCR3B. Upon interaction with CXCR3A receptor, induces activated T-lymphocytes migration mediated via downstream Ras/extracellular signal-regulated kinase (ERK) signaling. Neutralizes the anticoagulant effect of heparin by binding more strongly to heparin than to the chondroitin-4-sulfate chains of the carrier molecule. Plays a role in the inhibition of hematopoiesis and in the maintenance of hematopoietic stem cell (HSC) quiescence. Chemotactic for neutrophils and monocytes via CCR1. Inhibits endothelial cell proliferation. In cooperation with toll-like receptor 8/TLR8, induces chromatin remodeling and activates inflammatory gene expression via the TBK1-IRF5 axis. In addition, induces myofibroblast differentiation and collagen synthesis in different precursor cells, including endothelial cells, by stimulating endothelial-to-mesenchymal transition. {ECO:0000250|UniProtKB:P02776}.
|
Bos taurus (Bovine)
|
P02778
|
CXL10_HUMAN
|
MNQTAILICCLIFLTLSGIQGVPLSRTVRCTCISISNQPVNPRSLEKLEIIPASQFCPRVEIIATMKKKGEKRCLNPESKAIKNLLKAVSKERSKRSP
| null | null |
adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; antimicrobial humoral immune response mediated by antimicrobial peptide [GO:0061844]; antiviral innate immune response [GO:0140374]; blood circulation [GO:0008015]; cell surface receptor signaling pathway [GO:0007166]; cell-cell signaling [GO:0007267]; cellular response to heat [GO:0034605]; cellular response to interleukin-17 [GO:0097398]; cellular response to lipopolysaccharide [GO:0071222]; cellular response to virus [GO:0098586]; chemokine-mediated signaling pathway [GO:0070098]; chemotaxis [GO:0006935]; endothelial cell activation [GO:0042118]; G protein-coupled receptor signaling pathway [GO:0007186]; inflammatory response [GO:0006954]; muscle organ development [GO:0007517]; negative regulation of angiogenesis [GO:0016525]; negative regulation of myoblast differentiation [GO:0045662]; negative regulation of myoblast fusion [GO:1901740]; neutrophil chemotaxis [GO:0030593]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of monocyte chemotaxis [GO:0090026]; positive regulation of release of sequestered calcium ion into cytosol [GO:0051281]; positive regulation of T cell migration [GO:2000406]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of apoptotic process [GO:0042981]; regulation of cell population proliferation [GO:0042127]; regulation of endothelial tube morphogenesis [GO:1901509]; regulation of T cell chemotaxis [GO:0010819]; response to auditory stimulus [GO:0010996]; response to gamma radiation [GO:0010332]; response to vitamin D [GO:0033280]; signal transduction [GO:0007165]; T cell chemotaxis [GO:0010818]
|
external side of plasma membrane [GO:0009897]; extracellular region [GO:0005576]; extracellular space [GO:0005615]
|
cAMP-dependent protein kinase regulator activity [GO:0008603]; chemoattractant activity [GO:0042056]; chemokine activity [GO:0008009]; CXCR chemokine receptor binding [GO:0045236]; CXCR3 chemokine receptor binding [GO:0048248]; heparin binding [GO:0008201]; signaling receptor binding [GO:0005102]
|
PF00048;
|
2.40.50.40;
|
Intercrine alpha (chemokine CxC) family
|
PTM: Several proteases can mediate post-secretion cleavages. DPP4 cleaves CXCL10 on its N-terminal 2 amino acids leading to an antagonist form of CXCL10. This dominant negative form is capable of binding CXCR3 but does not induce signaling. MMP9 cleaves 9 amino acids instead. {ECO:0000269|PubMed:21183794}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21183794}.
| null | null | null | null | null |
FUNCTION: Pro-inflammatory cytokine that is involved in a wide variety of processes such as chemotaxis, differentiation, and activation of peripheral immune cells, regulation of cell growth, apoptosis and modulation of angiostatic effects (PubMed:11157474, PubMed:22652417, PubMed:7540647). Plays thereby an important role during viral infections by stimulating the activation and migration of immune cells to the infected sites (By similarity). Mechanistically, binding of CXCL10 to the CXCR3 receptor activates G protein-mediated signaling and results in downstream activation of phospholipase C-dependent pathway, an increase in intracellular calcium production and actin reorganization (PubMed:12750173, PubMed:19151743). In turn, recruitment of activated Th1 lymphocytes occurs at sites of inflammation (PubMed:12663757, PubMed:12750173). Activation of the CXCL10/CXCR3 axis also plays an important role in neurons in response to brain injury for activating microglia, the resident macrophage population of the central nervous system, and directing them to the lesion site. This recruitment is an essential element for neuronal reorganization (By similarity). {ECO:0000250|UniProtKB:P17515, ECO:0000269|PubMed:11157474, ECO:0000269|PubMed:12663757, ECO:0000269|PubMed:12750173, ECO:0000269|PubMed:19151743, ECO:0000269|PubMed:22652417, ECO:0000269|PubMed:7540647}.
|
Homo sapiens (Human)
|
P02784
|
SFP1_BOVIN
|
MALQLGLFLIWAGVSVFLQLDPVNGDQDEGVSTEPTQDGPAELPEDEECVFPFVYRNRKHFDCTVHGSLFPWCSLDADYVGRWKYCAQRDYAKCVFPFIYGGKKYETCTKIGSMWMSWCSLSPNYDKDRAWKYC
| null | null |
phospholipid efflux [GO:0033700]; positive regulation of sperm capacitation [GO:1902492]; single fertilization [GO:0007338]; sperm capacitation [GO:0048240]
|
cell surface [GO:0009986]; extracellular space [GO:0005615]
|
heparin binding [GO:0008201]
|
PF00040;
|
2.10.10.10;
|
Seminal plasma protein family
|
PTM: O-linked glycan consists of Gal-GalNAc disaccharide which is modified with a sialic acid residue (macro- and/or microheterogeneity account for differences between BSP-A1 and BSP-A2). {ECO:0000269|PubMed:8070564}.
|
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Could enhance the fertilizing capacity of bull spermatozoa upon interaction with heparin-like glycosaminoglycans present in the female genital tract. Exhibits both simulatory and inhibitory actions on the release of pituitary gonadotropins.
|
Bos taurus (Bovine)
|
P02786
|
TFR1_HUMAN
|
MMDQARSAFSNLFGGEPLSYTRFSLARQVDGDNSHVEMKLAVDEEENADNNTKANVTKPKRCSGSICYGTIAVIVFFLIGFMIGYLGYCKGVEPKTECERLAGTESPVREEPGEDFPAARRLYWDDLKRKLSEKLDSTDFTGTIKLLNENSYVPREAGSQKDENLALYVENQFREFKLSKVWRDQHFVKIQVKDSAQNSVIIVDKNGRLVYLVENPGGYVAYSKAATVTGKLVHANFGTKKDFEDLYTPVNGSIVIVRAGKITFAEKVANAESLNAIGVLIYMDQTKFPIVNAELSFFGHAHLGTGDPYTPGFPSFNHTQFPPSRSSGLPNIPVQTISRAAAEKLFGNMEGDCPSDWKTDSTCRMVTSESKNVKLTVSNVLKEIKILNIFGVIKGFVEPDHYVVVGAQRDAWGPGAAKSGVGTALLLKLAQMFSDMVLKDGFQPSRSIIFASWSAGDFGSVGATEWLEGYLSSLHLKAFTYINLDKAVLGTSNFKVSASPLLYTLIEKTMQNVKHPVTGQFLYQDSNWASKVEKLTLDNAAFPFLAYSGIPAVSFCFCEDTDYPYLGTTMDTYKELIERIPELNKVARAAAEVAGQFVIKLTHDVELNLDYERYNSQLLSFVRDLNQYRADIKEMGLSLQWLYSARGDFFRATSRLTTDFGNAEKTDRFVMKKLNDRVMRVEYHFLSPYVSPKESPFRHVFWGSGSHTLPALLENLKLRKQNNGAFNETLFRNQLALATWTIQGAANALSGDVWDIDNEF
| null | null |
acute-phase response [GO:0006953]; cellular response to leukemia inhibitory factor [GO:1990830]; cellular response to xenobiotic stimulus [GO:0071466]; intracellular iron ion homeostasis [GO:0006879]; intracellular signal transduction [GO:0035556]; iron ion transport [GO:0006826]; negative regulation of apoptotic process [GO:0043066]; negative regulation of mitochondrial fusion [GO:0010637]; osteoclast differentiation [GO:0030316]; positive regulation of B cell proliferation [GO:0030890]; positive regulation of bone resorption [GO:0045780]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of gene expression [GO:0010628]; positive regulation of isotype switching [GO:0045830]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; positive regulation of protein localization to nucleus [GO:1900182]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of protein-containing complex assembly [GO:0031334]; positive regulation of T cell proliferation [GO:0042102]; receptor internalization [GO:0031623]; response to copper ion [GO:0046688]; response to hypoxia [GO:0001666]; response to iron ion [GO:0010039]; response to manganese ion [GO:0010042]; response to nutrient [GO:0007584]; response to retinoic acid [GO:0032526]; transferrin transport [GO:0033572]; transport across blood-brain barrier [GO:0150104]
|
basolateral plasma membrane [GO:0016323]; blood microparticle [GO:0072562]; cell surface [GO:0009986]; clathrin-coated endocytic vesicle membrane [GO:0030669]; clathrin-coated pit [GO:0005905]; cytoplasmic vesicle [GO:0031410]; early endosome [GO:0005769]; endosome [GO:0005768]; endosome membrane [GO:0010008]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; extracellular vesicle [GO:1903561]; HFE-transferrin receptor complex [GO:1990712]; intracellular membrane-bounded organelle [GO:0043231]; melanosome [GO:0042470]; membrane [GO:0016020]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; recycling endosome [GO:0055037]; recycling endosome membrane [GO:0055038]
|
double-stranded RNA binding [GO:0003725]; Hsp70 protein binding [GO:0030544]; identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803]; protein kinase binding [GO:0019901]; protein-containing complex binding [GO:0044877]; RNA binding [GO:0003723]; transferrin receptor activity [GO:0004998]; virus receptor activity [GO:0001618]
|
PF02225;PF04389;PF04253;
|
3.50.30.30;1.20.930.40;3.40.630.10;
|
Peptidase M28 family, M28B subfamily
|
PTM: Stearoylated by ZDHHC6 which inhibits TFRC-mediated activation of the JNK pathway and promotes mitochondrial fragmentation (PubMed:26214738). Stearoylation does not affect iron uptake (PubMed:26214738). {ECO:0000269|PubMed:26214738}.; PTM: N- and O-glycosylated, phosphorylated and palmitoylated. The serum form is only glycosylated. {ECO:0000269|PubMed:1421756, ECO:0000269|PubMed:1421757, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19349973, ECO:0000269|PubMed:3582362}.; PTM: Proteolytically cleaved on Arg-100 to produce the soluble serum form (sTfR).; PTM: Palmitoylated on both Cys-62 and Cys-67. Cys-62 seems to be the major site of palmitoylation. {ECO:0000269|PubMed:3582362}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17081065}; Single-pass type II membrane protein {ECO:0000269|PubMed:17081065}. Melanosome {ECO:0000269|PubMed:17081065}. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV. {ECO:0000269|PubMed:17081065}.; SUBCELLULAR LOCATION: [Transferrin receptor protein 1, serum form]: Secreted {ECO:0000269|PubMed:17081065}.
| null | null | null | null | null |
FUNCTION: Cellular uptake of iron occurs via receptor-mediated endocytosis of ligand-occupied transferrin receptor into specialized endosomes (PubMed:26214738). Endosomal acidification leads to iron release. The apotransferrin-receptor complex is then recycled to the cell surface with a return to neutral pH and the concomitant loss of affinity of apotransferrin for its receptor. Transferrin receptor is necessary for development of erythrocytes and the nervous system (By similarity). A second ligand, the hereditary hemochromatosis protein HFE, competes for binding with transferrin for an overlapping C-terminal binding site. Positively regulates T and B cell proliferation through iron uptake (PubMed:26642240). Acts as a lipid sensor that regulates mitochondrial fusion by regulating activation of the JNK pathway (PubMed:26214738). When dietary levels of stearate (C18:0) are low, promotes activation of the JNK pathway, resulting in HUWE1-mediated ubiquitination and subsequent degradation of the mitofusin MFN2 and inhibition of mitochondrial fusion (PubMed:26214738). When dietary levels of stearate (C18:0) are high, TFRC stearoylation inhibits activation of the JNK pathway and thus degradation of the mitofusin MFN2 (PubMed:26214738). {ECO:0000250, ECO:0000269|PubMed:26214738, ECO:0000269|PubMed:26642240, ECO:0000269|PubMed:3568132}.; FUNCTION: (Microbial infection) Acts as a receptor for new-world arenaviruses: Guanarito, Junin and Machupo virus. {ECO:0000269|PubMed:17287727, ECO:0000269|PubMed:18268337}.
|
Homo sapiens (Human)
|
P02787
|
TRFE_HUMAN
|
MRLAVGALLVCAVLGLCLAVPDKTVRWCAVSEHEATKCQSFRDHMKSVIPSDGPSVACVKKASYLDCIRAIAANEADAVTLDAGLVYDAYLAPNNLKPVVAEFYGSKEDPQTFYYAVAVVKKDSGFQMNQLRGKKSCHTGLGRSAGWNIPIGLLYCDLPEPRKPLEKAVANFFSGSCAPCADGTDFPQLCQLCPGCGCSTLNQYFGYSGAFKCLKDGAGDVAFVKHSTIFENLANKADRDQYELLCLDNTRKPVDEYKDCHLAQVPSHTVVARSMGGKEDLIWELLNQAQEHFGKDKSKEFQLFSSPHGKDLLFKDSAHGFLKVPPRMDAKMYLGYEYVTAIRNLREGTCPEAPTDECKPVKWCALSHHERLKCDEWSVNSVGKIECVSAETTEDCIAKIMNGEADAMSLDGGFVYIAGKCGLVPVLAENYNKSDNCEDTPEAGYFAVAVVKKSASDLTWDNLKGKKSCHTAVGRTAGWNIPMGLLYNKINHCRFDEFFSEGCAPGSKKDSSLCKLCMGSGLNLCEPNNKEGYYGYTGAFRCLVEKGDVAFVKHQTVPQNTGGKNPDPWAKNLNEKDYELLCLDGTRKPVEEYANCHLARAPNHAVVTRKDKEACVHKILRQQQHLFGSNVTDCSGNFCLFRSETKDLLFRDDTVCLAKLHDRNTYEKYLGEEYVKAVGNLRKCSTSSLLEACTFRRP
| null | null |
actin filament organization [GO:0007015]; antibacterial humoral response [GO:0019731]; cellular response to iron ion [GO:0071281]; ERK1 and ERK2 cascade [GO:0070371]; intracellular iron ion homeostasis [GO:0006879]; iron ion transport [GO:0006826]; osteoclast differentiation [GO:0030316]; positive regulation of bone resorption [GO:0045780]; positive regulation of cell motility [GO:2000147]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of phosphorylation [GO:0042327]; positive regulation of receptor-mediated endocytosis [GO:0048260]; regulation of iron ion transport [GO:0034756]; regulation of protein stability [GO:0031647]
|
apical plasma membrane [GO:0016324]; basal part of cell [GO:0045178]; basal plasma membrane [GO:0009925]; blood microparticle [GO:0072562]; cell surface [GO:0009986]; clathrin-coated endocytic vesicle membrane [GO:0030669]; clathrin-coated pit [GO:0005905]; cytoplasmic vesicle [GO:0031410]; early endosome [GO:0005769]; endocytic vesicle [GO:0030139]; endoplasmic reticulum lumen [GO:0005788]; endosome membrane [GO:0010008]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; HFE-transferrin receptor complex [GO:1990712]; late endosome [GO:0005770]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; recycling endosome [GO:0055037]; secretory granule lumen [GO:0034774]; vesicle [GO:0031982]
|
ferric iron binding [GO:0008199]; ferrous iron binding [GO:0008198]; iron chaperone activity [GO:0034986]; transferrin receptor binding [GO:1990459]
|
PF00405;
|
3.40.190.10;
|
Transferrin family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. It is responsible for the transport of iron from sites of absorption and heme degradation to those of storage and utilization. Serum transferrin may also have a further role in stimulating cell proliferation.; FUNCTION: (Microbial infection) Serves as an iron source for Neisseria species, which capture the protein and extract its iron for their own use. {ECO:0000269|PubMed:22327295, ECO:0000269|PubMed:22343719}.; FUNCTION: (Microbial infection) Serves as an iron source for parasite T.brucei (strain 427), which capture TF via its own transferrin receptor ESAG6:ESAG7 and extract its iron for its own use. {ECO:0000269|PubMed:31636418}.
|
Homo sapiens (Human)
|
P02788
|
TRFL_HUMAN
|
MKLVFLVLLFLGALGLCLAGRRRSVQWCAVSQPEATKCFQWQRNMRKVRGPPVSCIKRDSPIQCIQAIAENRADAVTLDGGFIYEAGLAPYKLRPVAAEVYGTERQPRTHYYAVAVVKKGGSFQLNELQGLKSCHTGLRRTAGWNVPIGTLRPFLNWTGPPEPIEAAVARFFSASCVPGADKGQFPNLCRLCAGTGENKCAFSSQEPYFSYSGAFKCLRDGAGDVAFIRESTVFEDLSDEAERDEYELLCPDNTRKPVDKFKDCHLARVPSHAVVARSVNGKEDAIWNLLRQAQEKFGKDKSPKFQLFGSPSGQKDLLFKDSAIGFSRVPPRIDSGLYLGSGYFTAIQNLRKSEEEVAARRARVVWCAVGEQELRKCNQWSGLSEGSVTCSSASTTEDCIALVLKGEADAMSLDGGYVYTAGKCGLVPVLAENYKSQQSSDPDPNCVDRPVEGYLAVAVVRRSDTSLTWNSVKGKKSCHTAVDRTAGWNIPMGLLFNQTGSCKFDEYFSQSCAPGSDPRSNLCALCIGDEQGENKCVPNSNERYYGYTGAFRCLAENAGDVAFVKDVTVLQNTDGNNNEAWAKDLKLADFALLCLDGKRKPVTEARSCHLAMAPNHAVVSRMDKVERLKQVLLHQQAKFGRNGSDCPDKFCLFQSETKNLLFNDNTECLARLHGKTTYEKYLGPQYVAGITNLKKCSTSPLLEACEFLRK
|
3.4.21.-
| null |
antibacterial humoral response [GO:0019731]; antifungal humoral response [GO:0019732]; antimicrobial humoral immune response mediated by antimicrobial peptide [GO:0061844]; bone morphogenesis [GO:0060349]; defense response to Gram-negative bacterium [GO:0050829]; humoral immune response [GO:0006959]; innate immune response in mucosa [GO:0002227]; iron ion transport [GO:0006826]; killing of cells of another organism [GO:0031640]; negative regulation by host of viral process [GO:0044793]; negative regulation of apoptotic process [GO:0043066]; negative regulation of ATP-dependent activity [GO:0032780]; negative regulation of cysteine-type endopeptidase activity [GO:2000117]; negative regulation of lipopolysaccharide-mediated signaling pathway [GO:0031665]; negative regulation of osteoclast development [GO:2001205]; negative regulation of single-species biofilm formation in or on host organism [GO:1900229]; negative regulation of tumor necrosis factor (ligand) superfamily member 11 production [GO:2000308]; negative regulation of viral genome replication [GO:0045071]; negative regulation of viral process [GO:0048525]; ossification [GO:0001503]; positive regulation of bone mineralization involved in bone maturation [GO:1900159]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of chondrocyte proliferation [GO:1902732]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of osteoblast differentiation [GO:0045669]; positive regulation of osteoblast proliferation [GO:0033690]; positive regulation of protein serine/threonine kinase activity [GO:0071902]; positive regulation of toll-like receptor 4 signaling pathway [GO:0034145]; proteolysis [GO:0006508]; regulation of cytokine production [GO:0001817]; regulation of tumor necrosis factor production [GO:0032680]
|
cell surface [GO:0009986]; cytoplasm [GO:0005737]; early endosome [GO:0005769]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; nucleus [GO:0005634]; phagocytic vesicle lumen [GO:0097013]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]; recycling endosome [GO:0055037]; secretory granule [GO:0030141]; specific granule [GO:0042581]; specific granule lumen [GO:0035580]; tertiary granule lumen [GO:1904724]
|
cysteine-type endopeptidase inhibitor activity [GO:0004869]; DNA binding [GO:0003677]; heparin binding [GO:0008201]; iron ion binding [GO:0005506]; lipopolysaccharide binding [GO:0001530]; membrane destabilizing activity [GO:0140912]; protein serine/threonine kinase activator activity [GO:0043539]; serine-type endopeptidase activity [GO:0004252]
|
PF00405;
|
3.40.190.10;
|
Transferrin family
|
PTM: [Isoform DeltaLf]: Phosphorylation at Ser-10 activates the transcriptional activity (PubMed:20404350). Phosphorylation at Ser-10 also promotes proteasomal degradation (PubMed:20404350). Alternatively can undergo O-GlcNAcylation at Ser-10 (PubMed:20404350). {ECO:0000269|PubMed:20404350}.; PTM: [Isoform DeltaLf]: O-GlcNAcylation at Ser-10 inhibits DNA binding and negatively regulates the transcriptional activity (PubMed:20404350). Alternatively can undergo phosphorylation at Ser-10 (PubMed:20404350). {ECO:0000269|PubMed:20404350}.; PTM: Poly-N-acetyllactosaminic carbohydrate moiety seems to be needed for TLR4 activation.
|
SUBCELLULAR LOCATION: [Isoform 1]: Secreted. Cytoplasmic granule. Note=Secreted into most exocrine fluids by various endothelial cells. Stored in the secondary granules of neutrophils.; SUBCELLULAR LOCATION: [Isoform DeltaLf]: Cytoplasm. Nucleus. Note=Mainly localized in the cytoplasm.
| null | null | null | null | null |
FUNCTION: Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. {ECO:0000269|PubMed:22900286}.; FUNCTION: [Lactotransferrin]: Major iron-binding and multifunctional protein found in exocrine fluids such as breast milk and mucosal secretions (PubMed:11179314, PubMed:12693969, PubMed:14573629, PubMed:1599934, PubMed:3169987, PubMed:6802759). Has antimicrobial activity, which depends on the extracellular cation concentration (PubMed:6802759). Antimicrobial properties include bacteriostasis, which is related to its ability to sequester free iron and thus inhibit microbial growth, as well as direct bactericidal properties leading to the release of lipopolysaccharides from the bacterial outer membrane (PubMed:11179314, PubMed:12693969, PubMed:14573629, PubMed:1599934, PubMed:3169987, PubMed:6802759). Can also prevent bacterial biofilm development in P.aeruginosa infection (PubMed:12037568). Has weak antifungal activity against C.albicans (PubMed:11083624). Has anabolic, differentiating and anti-apoptotic effects on osteoblasts and can also inhibit osteoclastogenesis, possibly playing a role in the regulation of bone growth (PubMed:15166119). Promotes binding of species C adenoviruses to epithelial cells, promoting adenovirus infection (PubMed:17079302). Can inhibit papillomavirus infections (PubMed:17481742). Stimulates the TLR4 signaling pathway leading to NF-kappa-B activation and subsequent pro-inflammatory cytokine production while also interfering with the lipopolysaccharide (LPS)-stimulated TLR4 signaling (PubMed:20345905). Inhibits neutrophil granulocyte migration to sites of apoptosis, when secreted by apoptotic cells (PubMed:19033648). Stimulates VEGFA-mediated endothelial cell migration and proliferation (PubMed:16842782). Binds heparin, chondroitin sulfate and possibly other glycosaminoglycans (GAGs) (PubMed:9359845). Also binds specifically to pneumococcal surface protein A (PspA), the lipid A portion of bacterial lipopolysaccharide (LPS), lysozyme and DNA (PubMed:9359845). {ECO:0000269|PubMed:11083624, ECO:0000269|PubMed:11179314, ECO:0000269|PubMed:12037568, ECO:0000269|PubMed:12693969, ECO:0000269|PubMed:14573629, ECO:0000269|PubMed:15166119, ECO:0000269|PubMed:1599934, ECO:0000269|PubMed:16842782, ECO:0000269|PubMed:17079302, ECO:0000269|PubMed:17481742, ECO:0000269|PubMed:19033648, ECO:0000269|PubMed:20345905, ECO:0000269|PubMed:3169987, ECO:0000269|PubMed:6802759, ECO:0000269|PubMed:9359845}.; FUNCTION: Lactoferricin binds to the bacterial surface and is crucial for the bactericidal functions. Has some antiviral activity against papillomavirus infection (PubMed:17481742). N-terminal region shows strong antifungal activity against C.albicans (PubMed:11083624). Contains two BBXB heparin-binding consensus sequences that appear to form the predominate functional GAG-binding site. {ECO:0000269|PubMed:11083624, ECO:0000269|PubMed:17481742}.; FUNCTION: [Kaliocin-1]: Has antimicrobial activity and is able to permeabilize different ions through liposomal membranes. {ECO:0000269|PubMed:12693969}.; FUNCTION: [Lactoferroxin-A]: Has opioid antagonist activity (PubMed:1369293). Shows preference for mu-receptor (PubMed:1369293). {ECO:0000269|PubMed:1369293}.; FUNCTION: [Lactoferroxin-B]: Has opioid antagonist activity (PubMed:1369293). Shows higher degrees of preference for kappa-receptors than for mu-receptors (PubMed:1369293). {ECO:0000269|PubMed:1369293}.; FUNCTION: [Lactoferroxin-C]: Has opioid antagonist activity (PubMed:1369293). Shows higher degrees of preference for kappa-receptors than for mu-receptors (PubMed:1369293). {ECO:0000269|PubMed:1369293}.; FUNCTION: The lactotransferrin transferrin-like domain 1 functions as a serine protease of the peptidase S60 family that cuts arginine rich regions (PubMed:12535064). This function contributes to the antimicrobial activity (PubMed:12535064). Shows a preferential cleavage at -Arg-Ser-Arg-Arg-|- and -Arg-Arg-Ser-Arg-|-, and of Z-Phe-Arg-|-aminomethylcoumarin sites (PubMed:12535064). {ECO:0000269|PubMed:12535064}.; FUNCTION: [Isoform DeltaLf]: Transcription factor with antiproliferative properties and ability to induce cell cycle arrest (PubMed:15222485). Binds to the DeltaLf response element found in the SKP1, BAX, DCPS, and SELENOH promoters (PubMed:22320386). {ECO:0000269|PubMed:15222485, ECO:0000269|PubMed:22320386}.
|
Homo sapiens (Human)
|
P02789
|
TRFE_CHICK
|
MKLILCTVLSLGIAAVCFAAPPKSVIRWCTISSPEEKKCNNLRDLTQQERISLTCVQKATYLDCIKAIANNEADAISLDGGQAFEAGLAPYKLKPIAAEVYEHTEGSTTSYYAVAVVKKGTEFTVNDLQGKTSCHTGLGRSAGWNIPIGTLLHRGAIEWEGIESGSVEQAVAKFFSASCVPGATIEQKLCRQCKGDPKTKCARNAPYSGYSGAFHCLKDGKGDVAFVKHTTVNENAPDQKDEYELLCLDGSRQPVDNYKTCNWARVAAHAVVARDDNKVEDIWSFLSKAQSDFGVDTKSDFHLFGPPGKKDPVLKDLLFKDSAIMLKRVPSLMDSQLYLGFEYYSAIQSMRKDQLTPSPRENRIQWCAVGKDEKSKCDRWSVVSNGDVECTVVDETKDCIIKIMKGEADAVALDGGLVYTAGVCGLVPVMAERYDDESQCSKTDERPASYFAVAVARKDSNVNWNNLKGKKSCHTAVGRTAGWVIPMGLIHNRTGTCNFDEYFSEGCAPGSPPNSRLCQLCQGSGGIPPEKCVASSHEKYFGYTGALRCLVEKGDVAFIQHSTVEENTGGKNKADWAKNLQMDDFELLCTDGRRANVMDYRECNLAEVPTHAVVVRPEKANKIRDLLERQEKRFGVNGSEKSKFMMFESQNKDLLFKDLTKCLFKVREGTTYKEFLGDKFYTVISSLKTCNPSDILQMCSFLEGK
| null | null |
acute-phase response [GO:0006953]; antibacterial humoral response [GO:0019731]; antimicrobial humoral response [GO:0019730]; extracellular sequestering of iron ion [GO:0006881]; intracellular sequestering of iron ion [GO:0006880]; iron ion transport [GO:0006826]; response to lipopolysaccharide [GO:0032496]; response to xenobiotic stimulus [GO:0009410]
|
early endosome [GO:0005769]; extracellular space [GO:0005615]; organomineral extracellular matrix [GO:1990377]; plasma membrane [GO:0005886]; recycling endosome [GO:0055037]
|
ferric iron binding [GO:0008199]; iron ion binding [GO:0005506]
|
PF00405;
|
3.40.190.10;
|
Transferrin family
|
PTM: Different forms of hen transferrin are distinguished by their carbohydrate composition. Ovotransferrin and embryo serum transferrin but not adult serum transferrin, have bisecting N-acetylglucosamine. Transferrin secreted by embryo hepatocytes in primary culture is marked by the presence of (alpha1-6) fucosylation of the core N-acetylglucosamine. Serum transferrins also differ in the number of attached neuraminic acid residues. In both embryo forms, sialylation occurs on the Man (alpha 1-3)-linked antennae.
|
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. Responsible for the transport of iron from sites of absorption and heme degradation to those of storage and utilization. There are two forms of hen transferrin, ovotransferrin, found in the ovoducts and, serum transferrin, secreted by the liver. Serum transferrin may also have a role in stimulating cell proliferation and is regulated by iron levels. Ovotransferrin has a bacteriostatic function and, is not controlled by iron levels.
|
Gallus gallus (Chicken)
|
P02790
|
HEMO_HUMAN
|
MARVLGAPVALGLWSLCWSLAIATPLPPTSAHGNVAEGETKPDPDVTERCSDGWSFDATTLDDNGTMLFFKGEFVWKSHKWDRELISERWKNFPSPVDAAFRQGHNSVFLIKGDKVWVYPPEKKEKGYPKLLQDEFPGIPSPLDAAVECHRGECQAEGVLFFQGDREWFWDLATGTMKERSWPAVGNCSSALRWLGRYYCFQGNQFLRFDPVRGEVPPRYPRDVRDYFMPCPGRGHGHRNGTGHGNSTHHGPEYMRCSPHLVLSALTSDNHGATYAFSGTHYWRLDTSRDGWHSWPIAHQWPQGPSAVDAAFSWEEKLYLVQGTQVYVFLTKGGYTLVSGYPKRLEKEVGTPHGIILDSVDAAFICPGSSRLHIMAGRRLWWLDLKSGAQATWTELPWPHEKVDGALCMEKSLGPNSCSANGPGLYLIHGPNLYCYSDVEKLNAAKALPQPQNVTSLLGCTH
| null | null |
heme metabolic process [GO:0042168]; heme transport [GO:0015886]; hemoglobin metabolic process [GO:0020027]; intracellular iron ion homeostasis [GO:0006879]; positive regulation of humoral immune response mediated by circulating immunoglobulin [GO:0002925]; positive regulation of immunoglobulin production [GO:0002639]; positive regulation of type II interferon-mediated signaling pathway [GO:0060335]; positive regulation of tyrosine phosphorylation of STAT protein [GO:0042531]; type II interferon-mediated signaling pathway [GO:0060333]
|
blood microparticle [GO:0072562]; collagen-containing extracellular matrix [GO:0062023]; endocytic vesicle lumen [GO:0071682]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]
|
heme transmembrane transporter activity [GO:0015232]; metal ion binding [GO:0046872]
|
PF00045;
|
2.110.10.10;
|
Hemopexin family
|
PTM: N- and O-glycosylated. O-glycosylated with core 1 or possibly core 8 glycans. O-glycosylation in the 30-40 region is minor compared to glycosylation at Thr-24 and Thr-29. {ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:16740002, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:23234360, ECO:0000269|PubMed:6371807}.
|
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Binds heme and transports it to the liver for breakdown and iron recovery, after which the free hemopexin returns to the circulation.
|
Homo sapiens (Human)
|
P02792
|
FRIL_HUMAN
|
MSSQIRQNYSTDVEAAVNSLVNLYLQASYTYLSLGFYFDRDDVALEGVSHFFRELAEEKREGYERLLKMQNQRGGRALFQDIKKPAEDEWGKTPDAMKAAMALEKKLNQALLDLHALGSARTDPHLCDFLETHFLDEEVKLIKKMGDHLTNLHRLGGPEAGLGEYLFERLTLKHD
| null | null |
intracellular iron ion homeostasis [GO:0006879]; intracellular sequestering of iron ion [GO:0006880]; iron ion transport [GO:0006826]
|
autolysosome [GO:0044754]; azurophil granule lumen [GO:0035578]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; intracellular ferritin complex [GO:0008043]; membrane [GO:0016020]
|
ferric iron binding [GO:0008199]; ferrous iron binding [GO:0008198]; identical protein binding [GO:0042802]; iron ion binding [GO:0005506]
|
PF00210;
|
1.20.1260.10;
|
Ferritin family
| null | null | null | null | null | null | null |
FUNCTION: Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation. Also plays a role in delivery of iron to cells. Mediates iron uptake in capsule cells of the developing kidney (By similarity). {ECO:0000250, ECO:0000269|PubMed:19923220, ECO:0000269|PubMed:20159981}.
|
Homo sapiens (Human)
|
P02794
|
FRIH_HUMAN
|
MTTASTSQVRQNYHQDSEAAINRQINLELYASYVYLSMSYYFDRDDVALKNFAKYFLHQSHEEREHAEKLMKLQNQRGGRIFLQDIKKPDCDDWESGLNAMECALHLEKNVNQSLLELHKLATDKNDPHLCDFIETHYLNEQVKAIKELGDHVTNLRKMGAPESGLAEYLFDKHTLGDSDNES
|
1.16.3.1
| null |
immune response [GO:0006955]; intracellular iron ion homeostasis [GO:0006879]; intracellular sequestering of iron ion [GO:0006880]; iron ion transport [GO:0006826]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of fibroblast proliferation [GO:0048147]
|
autolysosome [GO:0044754]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; ficolin-1-rich granule lumen [GO:1904813]; intracellular ferritin complex [GO:0008043]; membrane [GO:0016020]; nucleus [GO:0005634]; tertiary granule lumen [GO:1904724]
|
ferric iron binding [GO:0008199]; ferrous iron binding [GO:0008198]; ferroxidase activity [GO:0004322]; identical protein binding [GO:0042802]; iron ion binding [GO:0005506]; iron ion sequestering activity [GO:0140315]
|
PF00210;
|
1.20.1260.10;
|
Ferritin family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P19130}.
|
CATALYTIC ACTIVITY: Reaction=4 Fe(2+) + 4 H(+) + O2 = 4 Fe(3+) + 2 H2O; Xref=Rhea:RHEA:11148, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.16.3.1; Evidence={ECO:0000269|PubMed:9003196};
| null | null | null | null |
FUNCTION: Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Has ferroxidase activity (PubMed:9003196). Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation (PubMed:9003196). Also plays a role in delivery of iron to cells (By similarity). Mediates iron uptake in capsule cells of the developing kidney (By similarity). {ECO:0000250|UniProtKB:P09528, ECO:0000269|PubMed:9003196}.
|
Homo sapiens (Human)
|
P02795
|
MT2_HUMAN
|
MDPNCSCAAGDSCTCAGSCKCKECKCTSCKKSCCSCCPVGCAKCAQGCICKGASDKCSCCA
| null | null |
cellular response to cadmium ion [GO:0071276]; cellular response to copper ion [GO:0071280]; cellular response to erythropoietin [GO:0036018]; cellular response to interleukin-3 [GO:0036016]; cellular response to zinc ion [GO:0071294]; detoxification of copper ion [GO:0010273]; intracellular copper ion homeostasis [GO:0006878]; intracellular zinc ion homeostasis [GO:0006882]; negative regulation of growth [GO:0045926]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]
|
metal ion binding [GO:0046872]; zinc ion binding [GO:0008270]
|
PF00131;
|
4.10.10.10;
|
Metallothionein superfamily, Type 1 family
| null | null | null | null | null | null | null |
FUNCTION: Metallothioneins have a high content of cysteine residues that bind various heavy metals; these proteins are transcriptionally regulated by both heavy metals and glucocorticoids.
|
Homo sapiens (Human)
|
P02798
|
MT2_MOUSE
|
MDPNCSCASDGSCSCAGACKCKQCKCTSCKKSCCSCCPVGCAKCSQGCICKEASDKCSCCA
| null | null |
cellular response to cadmium ion [GO:0071276]; cellular response to copper ion [GO:0071280]; cellular response to zinc ion [GO:0071294]; detoxification of copper ion [GO:0010273]; intracellular zinc ion homeostasis [GO:0006882]; negative regulation of growth [GO:0045926]; nitric oxide mediated signal transduction [GO:0007263]; response to bacterium [GO:0009617]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]
|
cadmium ion binding [GO:0046870]; metal ion binding [GO:0046872]; zinc ion binding [GO:0008270]
|
PF00131;
|
4.10.10.10;
|
Metallothionein superfamily, Type 1 family
| null | null | null | null | null | null | null |
FUNCTION: Metallothioneins have a high content of cysteine residues that bind various heavy metals; these proteins are transcriptionally regulated by both heavy metals and glucocorticoids.
|
Mus musculus (Mouse)
|
P02802
|
MT1_MOUSE
|
MDPNCSCSTGGSCTCTSSCACKNCKCTSCKKSCCSCCPVGCSKCAQGCVCKGAADKCTCCA
| null | null |
cellular response to cadmium ion [GO:0071276]; cellular response to chromate [GO:0071247]; cellular response to copper ion [GO:0071280]; cellular response to zinc ion [GO:0071294]; detoxification of copper ion [GO:0010273]; intracellular monoatomic cation homeostasis [GO:0030003]; intracellular zinc ion homeostasis [GO:0006882]; negative regulation of growth [GO:0045926]; negative regulation of neuron apoptotic process [GO:0043524]; nitric oxide mediated signal transduction [GO:0007263]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; lysosome [GO:0005764]; nucleus [GO:0005634]
|
copper ion binding [GO:0005507]; metal ion binding [GO:0046872]; zinc ion binding [GO:0008270]
|
PF00131;
|
4.10.10.10;
|
Metallothionein superfamily, Type 1 family
| null | null | null | null | null | null | null |
FUNCTION: Metallothioneins have a high content of cysteine residues that bind various heavy metals; these proteins are transcriptionally regulated by both heavy metals and glucocorticoids.
|
Mus musculus (Mouse)
|
P02808
|
STAT_HUMAN
|
MKFLVFAFILALMVSMIGADSSEEKFLRRIGRFGYGYGPYQPVPEQPLYPQPYQPQYQQYTF
| null | null |
biomineral tissue development [GO:0031214]; defense response to bacterium [GO:0042742]; negative regulation of bone mineralization [GO:0030502]; ossification [GO:0001503]; saliva secretion [GO:0046541]
|
extracellular region [GO:0005576]
|
extracellular matrix constituent, lubricant activity [GO:0030197]; hydroxyapatite binding [GO:0046848]; structural constituent of tooth enamel [GO:0030345]
|
PF03875;
| null |
Histatin/statherin family
|
PTM: Substrate for transglutaminase-2. More than 95% of the cyclized peptide is cyclo-statherin Q-37, and less than 5% is cyclo-statherin Q-39. Cyclized forms account for about 1% of total statherin in saliva. {ECO:0000269|PubMed:17313100}.; PTM: Sulfated on tyrosine residues. {ECO:0000269|PubMed:17389930}.
|
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Salivary protein that stabilizes saliva supersaturated with calcium salts by inhibiting the precipitation of calcium phosphate salts. It also modulates hydroxyapatite crystal formation on the tooth surface.
|
Homo sapiens (Human)
|
P02810
|
PRPC_HUMAN
|
MLLILLSVALLAFSSAQDLDEDVSQEDVPLVISDGGDSEQFIDEERQGPPLGGQQSQPSAGDGNQNDGPQQGPPQQGGQQQQGPPPPQGKPQGPPQQGGHPPPPQGRPQGPPQQGGHPRPPRGRPQGPPQQGGHQQGPPPPPPGKPQGPPPQGGRPQGPPQGQSPQ
| null | null | null |
extracellular space [GO:0005615]
| null |
PF15240;
| null | null |
PTM: Proteolytically cleaved; PRP-2, PRP-1, PIF-S and Db-S yield PRP-4, PRP-3 (protein A), PIF-F and Db-F, respectively. {ECO:0000269|PubMed:18463091}.; PTM: An hexuronic acid was shown to be linked to Ser-33 in about 40% of the polypeptides. Neither the structure of the carbohydrate (whether glucuronic acid or an isomer of), nor the linkage (whether a glycoside or an ester) has been definitely established. {ECO:0000269|PubMed:10858503}.
|
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: PRP's act as highly potent inhibitors of crystal growth of calcium phosphates. They provide a protective and reparative environment for dental enamel which is important for the integrity of the teeth.
|
Homo sapiens (Human)
|
P02812
|
PRB2_HUMAN
|
MLLILLSVALLALSSAQNLNEDVSQEESPSLIAGNPQGAPPQGGNKPQGPPSPPGKPQGPPPQGGNQPQGPPPPPGKPQGPPPQGGNKPQGPPPPGKPQGPPPQGDKSRSPRSPPGKPQGPPPQGGNQPQGPPPPPGKPQGPPPQGGNKPQGPPPPGKPQGPPPQGDNKSRSSRSPPGKPQGPPPQGGNQPQGPPPPPGKPQGPPPQGGNKPQGPPPPGKPQGPPPQGDNKSQSARSPPGKPQGPPPQGGNQPQGPPPPPGKPQGPPPQGGNKPQGPPPPGKPQGPPPQGGSKSRSSRSPPGKPQGPPPQGGNQPQGPPPPPGKPQGPPPQGGNKPQGPPPPGKPQGPPPQGGSKSRSARSPPGKPQGPPQQEGNNPQGPPPPAGGNPQQPQAPPAGQPQGPPRPPQGGRPSRPPQ
| null | null | null |
extracellular space [GO:0005615]
| null |
PF15240;
| null | null |
PTM: N- and O-glycosylated. In head and neck cancer patients, O-glycosylated with glucosylgalactosyl carbohydrate moiety. This modification would require prior hydroxylation on the lysine residue. {ECO:0000269|PubMed:20879038, ECO:0000269|PubMed:8554050}.; PTM: Proteolytically cleaved at the tripeptide Xaa-Pro-Gln, where Xaa in the P(3) position is mostly lysine. The endoprotease may be of microbial origin. {ECO:0000269|PubMed:18463091}.; PTM: Pyroglutamate formation occurs on terminal Gln residues of cleaved peptides. Pyroglutamate formation found on at least Gln-398 and Gln-400. {ECO:0000269|PubMed:18463091}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
| null | null | null | null | null | null |
Homo sapiens (Human)
|
P02814
|
SMR3B_HUMAN
|
MKSLTWILGLWALAACFTPGESQRGPRGPYPPGPLAPPQPFGPGFVPPPPPPPYGPGRIPPPPPAPYGPGIFPPPPPQP
| null | null |
regulation of sensory perception of pain [GO:0051930]
|
extracellular exosome [GO:0070062]; extracellular space [GO:0005615]
|
endopeptidase inhibitor activity [GO:0004866]
|
PF15621;
| null |
PROL1/PROL3 family
|
PTM: P-A and D1A are probably degradation products of P-B.
|
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null | null |
Homo sapiens (Human)
|
P02817
|
AMELX_BOVIN
|
MGTWILFACLLGAAFSMPLPPHPGHPGYINFSYEVLTPLKWYQSMIRHPYPSYGYEPMGGWLHHQIIPVVSQQTPQNHALQPHHHIPMVPAQQPVVPQQPMMPVPGQHSMTPTQHHQPNLPLPAQQPFQPQSIQPQPHQPLQPHQPLQPMQPMQPLQPLQPLQPQPPVHPIQPLPPQPPLPPIFPMQPLPPMLPDLPLEAWPATDKTKREEVD
| null | null |
chondrocyte differentiation [GO:0002062]; enamel mineralization [GO:0070166]; epithelial to mesenchymal transition [GO:0001837]; osteoblast differentiation [GO:0001649]; positive regulation of collagen biosynthetic process [GO:0032967]
|
collagen-containing extracellular matrix [GO:0062023]; extracellular region [GO:0005576]
|
structural constituent of tooth enamel [GO:0030345]
|
PF02948;
| null |
Amelogenin family
|
PTM: Phosphorylated by FAM20C in vitro. {ECO:0000250|UniProtKB:Q99217}.
|
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:Q99217}.
| null | null | null | null | null |
FUNCTION: Plays a role in the biomineralization of teeth. Seems to regulate the formation of crystallites during the secretory stage of tooth enamel development. Thought to play a major role in the structural organization and mineralization of developing enamel.
|
Bos taurus (Bovine)
|
P02818
|
OSTCN_HUMAN
|
MRALTLLALLALAALCIAGQAGAKPSGAESSKGAAFVSKQEGSEVVKRPRRYLYQWLGAPVPYPDPLEPRREVCELNPDCDELADHIGFQEAYRRFYGPV
| null | null |
bone development [GO:0060348]; bone mineralization [GO:0030282]; brain development [GO:0007420]; cell adhesion [GO:0007155]; cellular response to growth factor stimulus [GO:0071363]; cellular response to insulin stimulus [GO:0032869]; cellular response to vitamin D [GO:0071305]; cellular response to zinc ion starvation [GO:0034224]; cognition [GO:0050890]; dephosphorylation [GO:0016311]; glucose homeostasis [GO:0042593]; learning or memory [GO:0007611]; negative regulation of bone development [GO:1903011]; osteoblast development [GO:0002076]; osteoblast differentiation [GO:0001649]; positive regulation of neurotransmitter secretion [GO:0001956]; regulation of bone mineralization [GO:0030500]; regulation of bone resorption [GO:0045124]; regulation of cellular response to insulin stimulus [GO:1900076]; regulation of osteoclast differentiation [GO:0045670]; regulation of testosterone biosynthetic process [GO:2000224]; response to activity [GO:0014823]; response to estrogen [GO:0043627]; response to ethanol [GO:0045471]; response to glucocorticoid [GO:0051384]; response to gravity [GO:0009629]; response to hydroxyisoflavone [GO:0033594]; response to macrophage colony-stimulating factor [GO:0036005]; response to mechanical stimulus [GO:0009612]; response to testosterone [GO:0033574]; response to vitamin D [GO:0033280]; response to vitamin K [GO:0032571]; response to xenobiotic stimulus [GO:0009410]; response to zinc ion [GO:0010043]; skeletal system development [GO:0001501]; stem cell differentiation [GO:0048863]; type B pancreatic cell proliferation [GO:0044342]
|
cytoplasm [GO:0005737]; dendrite [GO:0030425]; endoplasmic reticulum lumen [GO:0005788]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; Golgi lumen [GO:0005796]; perikaryon [GO:0043204]; vesicle [GO:0031982]
|
calcium ion binding [GO:0005509]; hormone activity [GO:0005179]; hydroxyapatite binding [GO:0046848]; structural constituent of bone [GO:0008147]; structural molecule activity [GO:0005198]
| null | null |
Osteocalcin/matrix Gla protein family
|
PTM: Gamma-carboxyglutamate residues are formed by vitamin K dependent carboxylation by GGCX. These residues are essential for the binding of calcium (By similarity) (PubMed:6967872). Decarboxylation promotes the hormone activity (By similarity). {ECO:0000250|UniProtKB:P86546, ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:6967872}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:6967872}.
| null | null | null | null | null |
FUNCTION: Bone protein that constitutes 1-2% of the total bone protein, and which acts as a negative regulator of bone formation (PubMed:3019668, PubMed:6967872). Functions to limit bone formation without impairing bone resorption or mineralization (By similarity). It binds strongly to apatite and calcium (PubMed:6967872). {ECO:0000250|UniProtKB:P86546, ECO:0000269|PubMed:3019668, ECO:0000269|PubMed:6967872}.; FUNCTION: The uncarboxylated form acts as a hormone secreted by osteoblasts, which regulates different cellular processes, such as energy metabolism, male fertility and brain development. Regulates of energy metabolism by acting as a hormone favoring pancreatic beta-cell proliferation, insulin secretion and sensitivity and energy expenditure. Uncarboxylated osteocalcin hormone also promotes testosterone production in the testes: acts as a ligand for G protein-coupled receptor GPRC6A at the surface of Leydig cells, initiating a signaling response that promotes the expression of enzymes required for testosterone synthesis in a CREB-dependent manner. Also acts as a regulator of brain development: osteocalcin hormone crosses the blood-brain barrier and acts as a ligand for GPR158 on neurons, initiating a signaling response that prevents neuronal apoptosis in the hippocampus, favors the synthesis of all monoamine neurotransmitters and inhibits that of gamma-aminobutyric acid (GABA). Osteocalcin also crosses the placenta during pregnancy and maternal osteocalcin is required for fetal brain development. {ECO:0000250|UniProtKB:P86546}.
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Homo sapiens (Human)
|
P02819
|
OSTCN_MACFA
|
YLYQWLGAPAPYPDPLEPKREVCELNPDCDELADHIGFQEAYRRFYGPV
| null | null |
biomineral tissue development [GO:0031214]; bone development [GO:0060348]; brain development [GO:0007420]; cellular response to insulin stimulus [GO:0032869]; cognition [GO:0050890]; glucose homeostasis [GO:0042593]; learning or memory [GO:0007611]; negative regulation of bone development [GO:1903011]; osteoblast differentiation [GO:0001649]; positive regulation of neurotransmitter secretion [GO:0001956]; regulation of bone mineralization [GO:0030500]; regulation of cellular response to insulin stimulus [GO:1900076]; regulation of testosterone biosynthetic process [GO:2000224]; response to vitamin K [GO:0032571]; type B pancreatic cell proliferation [GO:0044342]
|
cytoplasm [GO:0005737]; extracellular region [GO:0005576]
|
calcium ion binding [GO:0005509]; hormone activity [GO:0005179]; hydroxyapatite binding [GO:0046848]; structural constituent of bone [GO:0008147]
| null | null |
Osteocalcin/matrix Gla protein family
|
PTM: Gamma-carboxyglutamate residues are formed by vitamin K dependent carboxylation by GGCX. These residues are essential for the binding of calcium (By similarity) (PubMed:6978733). Decarboxylation promotes the hormone activity (By similarity). {ECO:0000250|UniProtKB:P86546, ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:6978733}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:6978733}.
| null | null | null | null | null |
FUNCTION: The carboxylated form is one of the main organic components of the bone matrix, which constitutes 1-2% of the total bone protein: it acts as a negative regulator of bone formation and is required to limit bone formation without impairing bone resorption or mineralization. The carboxylated form binds strongly to apatite and calcium. {ECO:0000250|UniProtKB:P86546}.; FUNCTION: The uncarboxylated form acts as a hormone secreted by osteoblasts, which regulates different cellular processes, such as energy metabolism, male fertility and brain development. Regulates of energy metabolism by acting as a hormone favoring pancreatic beta-cell proliferation, insulin secretion and sensitivity and energy expenditure. Uncarboxylated osteocalcin hormone also promotes testosterone production in the testes: acts as a ligand for G protein-coupled receptor GPRC6A at the surface of Leydig cells, initiating a signaling response that promotes the expression of enzymes required for testosterone synthesis in a CREB-dependent manner. Also acts as a regulator of brain development: osteocalcin hormone crosses the blood-brain barrier and acts as a ligand for GPR158 on neurons, initiating a signaling response that prevents neuronal apoptosis in the hippocampus, favors the synthesis of all monoamine neurotransmitters and inhibits that of gamma-aminobutyric acid (GABA). Osteocalcin also crosses the placenta during pregnancy and maternal osteocalcin is required for fetal brain development. {ECO:0000250|UniProtKB:P86546}.
|
Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
|
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