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 interaction... | Bos taurus (Bovine) |
P02640 | VILI_CHICK | MVELSKKVTGKLDKTTPGIQIWRIENMEMVPVPTKSYGNFYEGDCYVLLSTRKTGSGFSYNIHYWLGKNSSQDEQGAAAIYTTQMDEYLGSVAVQHREVQGHESETFRAYFKQGLIYKQGGVASGMKHVETNTYNVQRLLHVKGKKNVVAAEVEMSWKSFNLGDVFLLDLGQLIIQWNGPESNRAERLRAMTLAKDIRDRERAGRAKVGVVEGENEAASPELMQALTHVLGEKKNIKAATPDEQVHQALNSALKLYHVSDASGNLVIQEVAIRPLTQDMLQHEDCYILDQAGLKIFVWKGKNANKEEKQQAMSRALGFIK... | 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 stimulu... | 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 tyrosi... | 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... | 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:00... | 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]; extracel... | 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]; hig... | 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 chol... | 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 pr... | 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 end... | 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 [... | 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:1983... | 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:... | 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... | 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:0... | 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 [... | 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:0... | 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 ... | 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:P026... | 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. Apolipoprot... | Rattus norvegicus (Rat) |
P02651 | APOA4_RAT | MFLKAVVLTVALVAITGTQAEVTSDQVANVMWDYFTQLSNNAKEAVEQLQKTDVTQQLNTLFQDKLGNINTYADDLQNKLVPFAVQLSGHLTKETERVREEIQKELEDLRANMMPHANKVSQMFGDNVQKLQEHLRPYATDLQAQINAQTQDMKRQLTPYIQRMQTTIQDNVENLQSSMVPFANELKEKFNQNMEGLKGQLTPRANELKATIDQNLEDLRSRLAPLAEGVQEKLNHQMEGLAFQMKKNAEELQTKVSTNIDQLQKNLAPLVEDVQSKLKGNTEGLQKSLEDLNKQLDQQVEVFRRAVEPLGDKFNMALVQ... | 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 ... | 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:0034... | 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... | 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 ... | 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:... | 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]; lipas... | 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 remodelin... | 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:003... | 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];... | 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 V... | 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 regu... | 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 partic... | 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 ... | 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 ... | 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 [... | 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:0... | 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 o... | 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 (VLDL... | 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... | 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... | 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 | MFSMRIVCLVLSVVGTAWTADSGEGDFLAEGGGVRGPRVVERHQSACKDSDWPFCSDEDWNYKCPSGCRMKGLIDEVNQDFTNRINKLKNSLFEYQKNNKDSHSLTTNIMEILRGDFSSANNRDNTYNRVSEDLRSRIEVLKRKVIEKVQHIQLLQKNVRAQLVDMKRLEVDIDIKIRSCRGSCSRALAREVDLKDYEDQQKQLEQVIAKDLLPSRDRQHLPLIKMKPVPDLVPGNFKSQLQKVPPEWKALTDMPQMRMELERPGGNEITRGGSTSYGTGSETESPRNPSSAGSWNSGSSGPGSTGNRNPGSSGTGGTAT... | 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 endot... | 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]; extracel... | 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. Beside... | 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 ... | Homo sapiens (Human) |
P02672 | FIBA_BOVIN | MFSVRDLCLVLSLVGAIKTEDGSDPPSGDFLTEGGGVRGPRLVERQQSACKETGWPFCSDEDWNTKCPSGCRMKGLIDEVDQDFTSRINKLRDSLFNYQKNSKDSNTLTKNIVELMRGDFAKANNNDNTFKQISEDLRSRIEILRRKVIEQVQRIKVLQKNVRDQLVDMKRLEVDIDIKIRSCKGSCSRALEHKVDLEDYKNQQKQLEQVIAINLLPSRDIQYLPLIKMSTITGPVPREFKSQLQEAPLEWKALLEMQQTKMVLETFGGDGHARGDSVSQGTGLAPGSPRKPGTSSIGNVNPGSYGPGSSGTWNPGRPEP... | 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:19020... | 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 epsil... | 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 ... | Bos taurus (Bovine) |
P02674 | FIBA1_PETMA | QVCIADDISLRGPRLTEQRSAGQGSCASATADLCVHGDWGRKCPNGCRMQGLMSHAEKDIGKRIGDLTERLARLGRLYTQVHTDFRAVSDTSGQTLNEHNELEVRYSEVLRELERRIIHLQRRINMQLQQLTLLQHNIKTQVSQILRVEVDIDVALRTCKGSCARYLEYRLDKEKNLQLEKAASYIANLKFERFEEVVVEETLNRRVETSSHAFQPTHGQGTPQPGHGTHSLSATSSITSAPNFVPHRQPTYVDHGRLSNPNEVAHSASSSSTHTSSSSSPSQPVSRDSAFPLPGSNTGTSEWDFNFHDESTPGNGPRDE... | 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... | 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 w... | 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 | MKRMVSWSFHKLKTMKHLLLLLLCVFLVKSQGVNDNEEGFFSARGHRPLDKKREEAPSLRPAPPPISGGGYRARPAKAAATQKKVERKAPDAGGCLHADPDLGVLCPTGCQLQEALLQQERPIRNSVDELNNNVEAVSQTSSSSFQYMYLLKDLWQKRQKQVKDNENVVNEYSSELEKHQLYIDETVNSNIPTNLRVLRSILENLRSKIQKLESDVSAQMEYCRTPCTVSCNIPVVSGKECEEIIRKGGETSEMYLIQPDSSVKPYRVYCDMNTENGGWTVIQNRQDGSVDFGRKWDPYKQGFGNVATNTDGKNYCGLPG... | 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... | 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:... | 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 epsil... | 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... | Homo sapiens (Human) |
P02676 | FIBB_BOVIN | QFPTDYDEGQDDRPKVGLGARGHRPYDKKKEEAPSLRPVPPPISGGGYRARPATATVGQKKVERKPPDADGCLHADPDLGVLCPTGCKLQDTLVRQERPIRKSIEDLRNTVDSVSRTSSSTFQYITLLKNMWKGRQNQVQDNENVVNEYSSHLEKHQLYIDETVKNNIPTKLRVLRSILENLRSKIQKLESDVSTQMEYCRTPCTVTCNIPVVSGKECEKIIRNEGETSEMYLIQPEDSSKPYRVYCDMKTEKGGWTVIQNRQDGSVDFGRKWDPYKQGFGNIATNAEGKKYCGVPGEYWLGNDRISQLTNMGPTKLLIE... | 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 epsil... | 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... | Bos taurus (Bovine) |
P02679 | FIBG_HUMAN | MSWSLHPRNLILYFYALLFLSSTCVAYVATRDNCCILDERFGSYCPTTCGIADFLSTYQTKVDKDLQSLEDILHQVENKTSEVKQLIKAIQLTYNPDESSKPNMIDAATLKSRKMLEEIMKYEASILTHDSSIRYLQEIYNSNNQKIVNLKEKVAQLEAQCQEPCKDTVQIHDITGKDCQDIANKGAKQSGLYFIKPLKANQQFLVYCEIDGSGNGWTVFQKRLDGSVDFKKNWIQYKEGFGHLSPTGTTEFWLGNEKIHLISTQSAIPYALRVELEDWNGRTSTADYAMFKVGPEADKYRLTYAYFAGGDAGDAFDGFD... | 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 ... | 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... | 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 epsil... | 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 du... | Homo sapiens (Human) |
P02680 | FIBG_RAT | MNWSLQLRSFILCWALLLLSPTGLAQYTATRDNCCILDERFGSYCPTTCGISDFLNSYQTDVDTDLQTLENILQRAENRTTEAKELIKAIQVYYNPDQPPKPGMIEGATQKSKKMVEEILKYEALLLTHESSIRYLQDIYTSNKQKITNLKQKVAQLEAQCQEPCKDSVRIHDTTGKDCQDIANKGAKESGLYFIRPLKATQQFLVYCEIDGSGNGWTVLQKRLDGSVDFKKNWIQYKEGFGHLSPTGTTEFWLGNEKIHLISMQSTIPYALRIQLKDWSGRTSTADYAMFRVGPESDKYRLTYAYFIGGDAGDAFDGYD... | 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 ... | 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 epsil... | 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 du... | 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 m... | 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 ... | 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:0000... | 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 GRI... | 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 het... | 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 an... | 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... | 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... | 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 funct... | 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 producti... | 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:00002... | 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 funct... | 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... | 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... | 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). {E... | 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 fat... | 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 [... | 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 | MNGTEGPNFYVPFSNKTGVVRSPFEAPQYYLAEPWQFSMLAAYMFLLIMLGFPINFLTLYVTVQHKKLRTPLNYILLNLAVADLFMVFGGFTTTLYTSLHGYFVFGPTGCNLEGFFATLGGEIALWSLVVLAIERYVVVCKPMSNFRFGENHAIMGVAFTWVMALACAAPPLVGWSRYIPEGMQCSCGIDYYTPHEETNNESFVIYMFVVHFIIPLIVIFFCYGQLVFTVKEAAAQQQESATTQKAEKEVTRMVIIMVIAFLICWLPYAGVAFYIFTHQGSDFGPIFMTIPAFFAKTSAVYNPVIYIMMNKQFRNCMVTT... | 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]; microtub... | 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 se... | 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 bi... | 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 conver... | 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,... | 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, ... | Bos taurus (Bovine) |
P02700 | OPSD_SHEEP | MNGTEGPNFYVPFSNKTGVVRSPFEAPQYYLAEPWQFSMLAAYMFLLIVLGFPINFLTLYVTVQHKKLRTPLNYILLNLAVADLFMVFGGFTTTLYTSLHGYFVFGPTGCNLEGFFATLGGEIALWSLVVLAIERYVVVCKPMSNFRFGENHAIMGVAFTWVMALACAAPPLVGWSRYIPQGMQCSCGALYFTLKPEINNESFVIYMFVVHFSIPLIVIFFCYGQLVFTVKEAAAQQQESATTQKAEKEVTRMVIIMVIAFLICWLPYAGVAFYIFTHQGSDFGPIFMTIPAFFAKSSSVYNPVIYIMMNKQFRNCMLTT... | 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.... | 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 segm... | 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 phosphorylatio... | 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-anch... | 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 s... | 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 transp... | Rattus norvegicus (Rat) |
P02708 | ACHA_HUMAN | MEPWPLLLLFSLCSAGLVLGSEHETRLVAKLFKDYSSVVRPVEDHRQVVEVTVGLQLIQLINVDEVNQIVTTNVRLKQQWVDYNLKWNPDDYGGVKKIHIPSEKIWRPDLVLYNNADGDFAIVKFTKVLLQYTGHITWTPPAIFKSYCEIIVTHFPFDEQNCSMKLGTWTYDGSVVAINPESDQPDLSNFMESGEWVIKESRGWKHSVTYSCCPDTPYLDITYHFVMQRLPLYFIVNVIIPCLLFSFLTGLVFYLPTDSGEKMTLSISVLLSLTVFLLVIVELIPSTSSAVPLIGKYMLFTMVFVIASIIITVIVINTHH... | 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... | 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 w... | Homo sapiens (Human) |
P02709 | ACHA_BOVIN | MEPRPLLLLLGLCSAGLVLGSEHETRLVAKLFEDYNSVVRPVEDHRQAVEVTVGLQLIQLINVDEVNQIVTTNVRLKQQWVDYNLKWNPDDYGGVKKIHIPSEKIWRPDLVLYNNADGDFAIVKFTKVLLDYTGHITWTPPAIFKSYCEIIVTHFPFDEQNCSMKLGTWTYDGSVVVINPESDQPDLSNFMESGEWVIKESRGWKHWVFYACCPSTPYLDITYHFVMQRLPLYFIVNVIIPCLLFSFLTGLVFYLPTDSGEKMTLSISVLLSLTVFLLVIVELIPSTSSAVPLIGKYMLFTMVFVIASIIITVIVINTHH... | 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];... | 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 | MENVRRMALGLVVMMALALSGVGASVMEDTLLSVLFETYNPKVRPAQTVGDKVTVRVGLTLTNLLILNEKIEEMTTNVFLNLAWTDYRLQWDPAAYEGIKDLRIPSSDVWQPDIVLMNNNDGSFEITLHVNVLVQHTGAVSWQPSAIYRSSCTIKVMYFPFDWQNCTMVFKSYTYDTSEVTLQHALDAKGEREVKEIVINKDAFTENGQWSIEHKPSRKNWRSDDPSYEDVTFYLIIQRKPLFYIVYTIIPCILISILAILVFYLPPDAGEKMSLSISALLAVTVFLLLLADKVPETSLSVPIIIRYLMFIMILVAFSVI... | 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 | MRCSDLLLLFLLALCVLPGISCRNQEEKLLQDLMTNYNRHLRPALRGDQVIDVTLKLTLTNLISLNEREETLTTNVWIEMQWSDYRLRWDPDKYDDIQQLRVPSAMVWLPDIVLENNIDGTFEITLYTNVLVYPDGSIYWLPPAIYRSSCSIHVTYFPFDWQNCTMVFQSQTYSANEINLLLTVEEGQTIEWIFIDPEAFTENGEWAIKHRPARKIINSGRFTPDDIQYQQVIFYLIIQRKPLFYIINIIVPCVLISSMAVLVYFLPAKAGGQKCTVSINVLLAQTVFLFLIAQKVPETSQAVPLIGKYLTFLMVVTVVI... | 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 | MVLTLLLIICLALEVRSENEEGRLIEKLLGDYDKRIIPAKTLDHIIDVTLKLTLTNLISLNEKEEALTTNVWIEIQWNDYRLSWNTSEYEGIDLVRIPSELLWLPDVVLENNVDGQFEVAYYANVLVYNDGSMYWLPPAIYRSTCPIAVTYFPFDWQNCSLVFRSQTYNAHEVNLQLSAEEGEAVEWIHIDPEDFTENGEWTIRHRPAKKNYNWQLTKDDTDFQEIIFFLIIQRKPLFYIINIIAPCVLISSLVVLVYFLPAQAGGQKCTLSISVLLAQTIFLFLIAQKVPETSLNVPLIGKYLIFVMFVSMLIVMNCVI... | 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 | MAGPVLTLGLLAALVVCALPGSWGLNEEQRLIQHLFNEKGYDKDLRPVARKEDKVDVALSLTLSNLISLKEVEETLTTNVWIDHAWVDSRLQWDANDFGNITVLRLPPDMVWLPEIVLENNNDGSFQISYACNVLVYDSGYVTWLPPAIFRSSCPISVTYFPFDWQNCSLKFSSLKYTAKEITLSLKQEEENNRSYPIEWIIIDPEGFTENGEWEIVHRAAKLNVDPSVPMDSTNHQDVTFYLIIRRKPLFYIINILVPCVLISFMINLVFYLPGDCGEKTSVAISVLLAQSVFLLLISKRLPATSMAIPLVGKFLLFGM... | 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 | MGNIHFVYLLISCLYYSGCSGVNEEERLINDLLIVNKYNKHVRPVKHNNEVVNIALSLTLSNLISLKETDETLTSNVWMDHAWYDHRLTWNASEYSDISILRLPPELVWIPDIVLQNNNDGQYHVAYFCNVLVRPNGYVTWLPPAIFRSSCPINVLYFPFDWQNCSLKFTALNYDANEITMDLMTDTIDGKDYPIEWIIIDPEAFTENGEWEIIHKPAKKNIYPDKFPNGTNYQDVTFYLIIRRKPLFYVINFITPCVLISFLASLAFYLPAESGEKMSTAISVLLAQAVFLLLTSQRLPETALAVPLIGKYLMFIMSLV... | 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 ... | 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:162... | 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-... | 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. Abo... | 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... | Homo sapiens (Human) |
P02730 | B3AT_HUMAN | MEELQDDYEDMMEENLEQEEYEDPDIPESQMEEPAAHDTEATATDYHTTSHPGTHKVYVELQELVMDEKNQELRWMEAARWVQLEENLGENGAWGRPHLSHLTFWSLLELRRVFTKGTVLLDLQETSLAGVANQLLDRFIFEDQIRPQDREELLRALLLKHSHAGELEALGGVKPAVLTRSGDPSQPLLPQHSSLETQLFCEQGDGGTEGHSPSGILEKIPPDSEATLVLVGRADFLEQPVLGFVRLQEAAELEAVELPVPIRFLFVLLGPEAPHIDYTQLGRAAATLMSERVFRIDAYMAQSRGELLHSLEGFLDCSLV... | 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 proc... | 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 homodimer... | 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... | 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:7506... | 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:2838730... | 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 er... | 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 o... | 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 circulati... | 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... | 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]; ... | 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... | 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:00... | 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... | 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:0... | 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... | Homo sapiens (Human) |
P02748 | CO9_HUMAN | MSACRSFAVAICILEISILTAQYTTSYDPELTESSGSASHIDCRMSPWSEWSQCDPCLRQMFRSRSIEVFGQFNGKRCTDAVGDRRQCVPTEPCEDAEDDCGNDFQCSTGRCIKMRLRCNGDNDCGDFSDEDDCESEPRPPCRDRVVEESELARTAGYGINILGMDPLSTPFDNEFYNGLCNRDRDGNTLTYYRRPWNVASLIYETKGEKNFRTEHYEEQIEAFKSIIQEKTSNFNAAISLKFTPTETNKAEQCCEETASSISLHGKGSFRFSYSKNETYQLFLSYSSKKEKMFLHVKGEIHLGRFVMRNRDVVLTTTFV... | 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 f... | 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:000... | 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:40558... | Homo sapiens (Human) |
P02749 | APOH_HUMAN | MISPVLILFSSFLCHVAIAGRTCPKPDDLPFSTVVPLKTFYEPGEEITYSCKPGYVSRGGMRKFICPLTGLWPINTLKCTPRVCPFAGILENGAVRYTTFEYPNTISFSCNTGFYLNGADSAKCTEEGKWSPELPVCAPIICPPPSIPTFATLRVYKPSAGNNSLYRDTAVFECLPQHAMFGNDTITCTTHGNWTKLPECREVKCPFPSRPDNGFVNYPAKPTLYYKDKATFGCHDGYSLDGPEEIECTKLGNWSAMPSCKASCKVPVKKATVVYQGERVKIQEKFKNGMLHGDKVSFFCKNKEKKCSYTEDAQCIDGTI... | 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... | 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 ... | 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|Pub... | 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 | MSSWSRQRPKSPGGIQPHVSRTLFLLLLLAASAWGVTLSPKDCQVFRSDHGSSISCQPPAEIPGYLPADTVHLAVEFFNLTHLPANLLQGASKLQELHLSSNGLESLSPEFLRPVPQLRVLDLTRNALTGLPPGLFQASATLDTLVLKENQLEVLEVSWLHGLKALGHLDLSGNRLRKLPPGLLANFTLLRTLDLGENQLETLPPDLLRGPLQLERLHLEGNKLQVLGKDLLLPQPDLRYLFLNGNKLARVAAGAFQGLRQLDMLDLSNNSLASVPEGLWASLGQPNWDMRDGFDISGNPWICDQNLSDLYRWLQAQKDK... | 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 invol... | 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 | MLRGPGPGLLLLAVQCLGTAVPSTGASKSKRQAQQMVQPQSPVAVSQSKPGCYDNGKHYQINQQWERTYLGNALVCTCYGGSRGFNCESKPEAEETCFDKYTGNTYRVGDTYERPKDSMIWDCTCIGAGRGRISCTIANRCHEGGQSYKIGDTWRRPHETGGYMLECVCLGNGKGEWTCKPIAEKCFDHAAGTSYVVGETWEKPYQGWMMVDCTCLGEGSGRITCTSRNRCNDQDTRTSYRIGDTWSKKDNRGNLLQCICTGNGRGEWKCERHTSVQTTSSGSGPFTDVRAAVYQPQPHPQPPPYGHCVTDSGVVYSVGM... | 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 differ... | 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 mat... | 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 bi... | 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:000... | 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, Pub... | 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... | 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:000026... | 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 | MRSLGALLLLLSACLAVSAGPVPTPPDNIQVQENFNISRIYGKWYNLAIGSTCPWLKKIMDRMTVSTLVLGEGATEAEISMTSTRWRKGVCEETSGAYEKTDTDGKFLYHKSKWNITMESYVVHTNYDEYAIFLTKKFSRHHGPTITAKLYGRAPQLRETLLQDFRVVAQGVGIPEDSIFTMADRGECVPGEQEPEPILIPRVRRAVLPQEEEGSGGGQLVTEVTKKEDSCQLGYSAGPCMGMTSRYFYNGTSMACETFQYGGCMGNGNNFVTEKECLQTCRTVAACNLPIVRGPCRAFIQLWAFDAVKGKCVLFPYGGC... | 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]... | 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 r... | 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}... | 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,... | 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... | 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 vomero... | 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... | 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 [G... | 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:1... | 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.... | 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 inflam... | 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 | MKSLVLLLCLAQLWGCHSAPHGPGLIYRQPNCDDPETEEAALVAIDYINQNLPWGYKHTLNQIDEVKVWPQQPSGELFEIEIDTLETTCHVLDPTPVARCSVRQLKEHAVEGDCDFQLLKLDGKFSVVYAKCDSSPDSAEDVRKVCQDCPLLAPLNDTRVVHAAKAALAAFNAQNNGSNFQLEEISRAQLVPLPPSTYVEFTVSGTDCVAKEATEAAKCNLLAEKQYGFCKATLSEKLGGAEVAVTCMVFQTQPVSSQPQPEGANEAVPTPVVDPDAPPSPPLGAPGLPPAGSPPDSHVLLAAPPGHQLHRAHYDLRHTF... | 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]; regul... | 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 gran... | 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). {EC... | 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... | 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 | MKWVTFISLLFLFSSAYSRGVFRRDAHKSEVAHRFKDLGEENFKALVLIAFAQYLQQCPFEDHVKLVNEVTEFAKTCVADESAENCDKSLHTLFGDKLCTVATLRETYGEMADCCAKQEPERNECFLQHKDDNPNLPRLVRPEVDVMCTAFHDNEETFLKKYLYEIARRHPYFYAPELLFFAKRYKAAFTECCQAADKAACLLPKLDELRDEGKASSAKQRLKCASLQKFGERAFKAWAVARLSQRFPKAEFAEVSKLVTDLTKVHTECCHGDLLECADDRADLAKYICENQDSISSKLKECCEKPLLEKSHCIAEVEND... | 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 lume... | 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 [G... | 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 tran... | Homo sapiens (Human) |
P02769 | ALBU_BOVIN | MKWVTFISLLLLFSSAYSRGVFRRDTHKSEIAHRFKDLGEEHFKGLVLIAFSQYLQQCPFDEHVKLVNELTEFAKTCVADESHAGCEKSLHTLFGDELCKVASLRETYGDMADCCEKQEPERNECFLSHKDDSPDLPKLKPDPNTLCDEFKADEKKFWGKYLYEIARRHPYFYAPELLYYANKYNGVFQECCQAEDKGACLLPKIETMREKVLASSARQRLRCASIQKFGERALKAWSVARLSQKFPKAEFVEVTKLVTDLTKVHKECCHGDLLECADDRADLAKYICDNQDTISSKLKECCDKPLLEKSHCIAEVEKDA... | 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... | Bos taurus (Bovine) |
P02770 | ALBU_RAT | MKWVTFLLLLFISGSAFSRGVFRREAHKSEIAHRFKDLGEQHFKGLVLIAFSQYLQKCPYEEHIKLVQEVTDFAKTCVADENAENCDKSIHTLFGDKLCAIPKLRDNYGELADCCAKQEPERNECFLQHKDDNPNLPPFQRPEAEAMCTSFQENPTSFLGHYLHEVARRHPYFYAPELLYYAEKYNEVLTQCCTESDKAACLTPKLDAVKEKALVAAVRQRMKCSSMQRFGERAFKAWAVARMSQRFPNAEFAEITKLATDVTKINKECCHGDLLECADDRAELAKYMCENQATISSKLQACCDKPVLQKSQCLAEIEHD... | 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]... | 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... | 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... | Rattus norvegicus (Rat) |
P02771 | FETA_HUMAN | MKWVESIFLIFLLNFTESRTLHRNEYGIASILDSYQCTAEISLADLATIFFAQFVQEATYKEVSKMVKDALTAIEKPTGDEQSSGCLENQLPAFLEELCHEKEILEKYGHSDCCSQSEEGRHNCFLAHKKPTPASIPLFQVPEPVTSCEAYEEDRETFMNKFIYEIARRHPFLYAPTILLWAARYDKIIPSCCKAENAVECFQTKAATVTKELRESSLLNQHACAVMKNFGTRTFQAITVTKLSQKFTKVNFTEIQKLVLDVAHVHEHCCRGDVLDCLQDGEKIMSYICSQQDTLSNKITECCKLTTLERGQCIIHAEND... | 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 | MKWITPASLILLLHFAASKALHENEFGIASTLDSSQCVTEKNVLSIATITFTQFVPEATEEEVNKMTSDVLAAMKKNSGDGCLESQLSVFLDEICHETELSNKYGLSGCCSQSGVERHQCLLARKKTAPASVPPFQFPEPAESCKAHEENRAVFMNRFIYEVSRRNPFMYAPAILSLAAQYDKVVLACCKADNKEECFQTKRASIAKELREGSMLNEHVCSVIRKFGSRNLQATTIIKLSQKLTEANFTEIQKLALDVAHIHEECCQGNSLECLQDGEKVMTYICSQQNILSSKIAECCKLPMIQLGFCIIHAENGVKPE... | 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 | MKQPATMKWSASISFLLLLNFAEPRVLHTNEFGIESTLDSSQCPTEKNMFNVATIVVAQFVQDATKAEVNKMSSDALAAMKENTGDGCLENQLSVFLDEICHETELSNKYGFSGCCNQSGVERHQCLLARKKTAPDSVPPFHFPETAESCPAYEENRAMSINTFIYDVSKRNPFLYAPTILYLAAQYDKAVPACCKADNMEECFQTKRASMAKELREGSMLNEHVCAVIRKFGSRNLQAVLIIKLSQKFPKANITEIRKLALDVAHIHEQCCHGNAMECLQDGESVMTHMCSQQEILSSKTAECCKLPTIELGYCIIHAE... | 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]; ... | 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 | MKRVLVLLLAVAFGHALERGRDYEKNKVCKEFSHLGKEDFTSLSLVLYSRKFPSGTFEQVSQLVKEVVSLTEACCAEGADPDCYDTRTSALSAKSCESNSPFPVHPGTAECCTKEGLERKLCMAALKHQPQEFPTYVEPTNDEICEAFRKDPKEYANQFMWEYSTNYGQAPLSLLVSYTKSYLSMVGSCCTSASPTVCFLKERLQLKHLSLLTTLSNRVCSQYAAYGEKKSRLSNLIKLAQKVPTADLEDVLPLAEDITNILSKCCESASEDCMAKELPEHTVKLCDNLSTKNSKFEDCCQEKTAMDVFVCTYFMPAAQL... | 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 p... | 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]; neu... | 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 ... | 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 C... | 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:0... | 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:2... | 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:0... | 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-... | 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 sig... | 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 ro... | 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 | MMDQARSAFSNLFGGEPLSYTRFSLARQVDGDNSHVEMKLAVDEEENADNNTKANVTKPKRCSGSICYGTIAVIVFFLIGFMIGYLGYCKGVEPKTECERLAGTESPVREEPGEDFPAARRLYWDDLKRKLSEKLDSTDFTGTIKLLNENSYVPREAGSQKDENLALYVENQFREFKLSKVWRDQHFVKIQVKDSAQNSVIIVDKNGRLVYLVENPGGYVAYSKAATVTGKLVHANFGTKKDFEDLYTPVNGSIVIVRAGKITFAEKVANAESLNAIGVLIYMDQTKFPIVNAELSFFGHAHLGTGDPYTPGFPSFNHTQ... | 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 proce... | 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... | 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]... | 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 ... | 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: [T... | 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 con... | Homo sapiens (Human) |
P02787 | TRFE_HUMAN | MRLAVGALLVCAVLGLCLAVPDKTVRWCAVSEHEATKCQSFRDHMKSVIPSDGPSVACVKKASYLDCIRAIAANEADAVTLDAGLVYDAYLAPNNLKPVVAEFYGSKEDPQTFYYAVAVVKKDSGFQMNQLRGKKSCHTGLGRSAGWNIPIGLLYCDLPEPRKPLEKAVANFFSGSCAPCADGTDFPQLCQLCPGCGCSTLNQYFGYSGAFKCLKDGAGDVAFVKHSTIFENLANKADRDQYELLCLDNTRKPVDEYKDCHLAQVPSHTVVARSMGGKEDLIWELLNQAQEHFGKDKSKEFQLFSSPHGKDLLFKDSAHG... | 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 re... | 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];... | 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 fur... | Homo sapiens (Human) |
P02788 | TRFL_HUMAN | MKLVFLVLLFLGALGLCLAGRRRSVQWCAVSQPEATKCFQWQRNMRKVRGPPVSCIKRDSPIQCIQAIAENRADAVTLDGGFIYEAGLAPYKLRPVAAEVYGTERQPRTHYYAVAVVKKGGSFQLNELQGLKSCHTGLRRTAGWNVPIGTLRPFLNWTGPPEPIEAAVARFFSASCVPGADKGQFPNLCRLCAGTGENKCAFSSQEPYFSYSGAFKCLRDGAGDVAFIRESTVFEDLSDEAERDEYELLCPDNTRKPVDKFKDCHLARVPSHAVVARSVNGKEDAIWNLLRQAQEKFGKDKSPKFQLFGSPSGQKDLLFK... | 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 resp... | 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]; rec... | 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 endopept... | 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-... | 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 mucosa... | Homo sapiens (Human) |
P02789 | TRFE_CHICK | MKLILCTVLSLGIAAVCFAAPPKSVIRWCTISSPEEKKCNNLRDLTQQERISLTCVQKATYLDCIKAIANNEADAISLDGGQAFEAGLAPYKLKPIAAEVYEHTEGSTTSYYAVAVVKKGTEFTVNDLQGKTSCHTGLGRSAGWNIPIGTLLHRGAIEWEGIESGSVEQAVAKFFSASCVPGATIEQKLCRQCKGDPKTKCARNAPYSGYSGAFHCLKDGKGDVAFVKHTTVNENAPDQKDEYELLCLDGSRQPVDNYKTCNWARVAAHAVVARDDNKVEDIWSFLSKAQSDFGVDTKSDFHLFGPPGKKDPVLKDLLFK... | 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... | 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... | 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, ovo... | Gallus gallus (Chicken) |
P02790 | HEMO_HUMAN | MARVLGAPVALGLWSLCWSLAIATPLPPTSAHGNVAEGETKPDPDVTERCSDGWSFDATTLDDNGTMLFFKGEFVWKSHKWDRELISERWKNFPSPVDAAFRQGHNSVFLIKGDKVWVYPPEKKEKGYPKLLQDEFPGIPSPLDAAVECHRGECQAEGVLFFQGDREWFWDLATGTMKERSWPAVGNCSSALRWLGRYYCFQGNQFLRFDPVRGEVPPRYPRDVRDYFMPCPGRGHGHRNGTGHGNSTHHGPEYMRCSPHLVLSALTSDNHGATYAFSGTHYWRLDTSRDGWHSWPIAHQWPQGPSAVDAAFSWEEKLYL... | 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];... | 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... | 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). ... | 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). Medi... | 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:... | 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:0... | 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... | 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 isom... | 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 | MLLILLSVALLALSSAQNLNEDVSQEESPSLIAGNPQGAPPQGGNKPQGPPSPPGKPQGPPPQGGNQPQGPPPPPGKPQGPPPQGGNKPQGPPPPGKPQGPPPQGDKSRSPRSPPGKPQGPPPQGGNQPQGPPPPPGKPQGPPPQGGNKPQGPPPPGKPQGPPPQGDNKSRSSRSPPGKPQGPPPQGGNQPQGPPPPPGKPQGPPPQGGNKPQGPPPPGKPQGPPPQGDNKSQSARSPPGKPQGPPPQGGNQPQGPPPPPGKPQGPPPQGGNKPQGPPPPGKPQGPPPQGGSKSRSSRSPPGKPQGPPPQGGNQPQGPPP... | 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, whe... | 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... | 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:... | 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:69678... | 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 diffe... | 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:... | 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 ... | Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey) |
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