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
|
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
P01216
|
GLHA_MOUSE
|
MDYYRKYAAVILVMLSMFLHILHSLPDGDFIIQGCPECKLKENKYFSKLGAPIYQCMGCCFSRAYPTPARSKKTMLVPKNITSEATCCVAKAFTKATVMGNARVENHTECHCSTCYYHKS
| null | null |
cellular response to hormone stimulus [GO:0032870]; developmental growth [GO:0048589]; follicle-stimulating hormone secretion [GO:0046884]; G protein-coupled receptor signaling pathway [GO:0007186]; gonad development [GO:0008406]; luteinizing hormone secretion [GO:0032275]; negative regulation of organ growth [GO:0046621]; organ growth [GO:0035265]; positive regulation of steroid biosynthetic process [GO:0010893]; regulation of signaling receptor activity [GO:0010469]; thyroid gland development [GO:0030878]; thyroid hormone generation [GO:0006590]
|
extracellular space [GO:0005615]; follicle-stimulating hormone complex [GO:0016914]
|
follicle-stimulating hormone activity [GO:0016913]
|
PF00236;
|
2.10.90.10;
|
Glycoprotein hormones subunit alpha family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P01215}.
| null | null | null | null | null |
FUNCTION: Shared alpha chain of the active heterodimeric glycoprotein hormones thyrotropin/thyroid stimulating hormone/TSH, lutropin/luteinizing hormone/LH and follitropin/follicle stimulating hormone/FSH. These hormones bind specific receptors on target cells that in turn activate downstream signaling pathways. {ECO:0000250|UniProtKB:P01215}.
|
Mus musculus (Mouse)
|
P01218
|
GLHA_SHEEP
|
MDYYRKYAAAILAILSLFLQILHSFPDGEFTMQGCPECKLKENKYFSKPDAPIYQCMGCCFSRAYPTPARSKKTMLVPKNITSEATCCVAKAFTKATVMGNVRVENHTECHCSTCYYHKS
| null | null |
G protein-coupled receptor signaling pathway [GO:0007186]; positive regulation of steroid biosynthetic process [GO:0010893]; regulation of signaling receptor activity [GO:0010469]; thyroid hormone generation [GO:0006590]
|
extracellular space [GO:0005615]; follicle-stimulating hormone complex [GO:0016914]
|
follicle-stimulating hormone activity [GO:0016913]
|
PF00236;
|
2.10.90.10;
|
Glycoprotein hormones subunit alpha family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P01215}.
| null | null | null | null | null |
FUNCTION: Shared alpha chain of the active heterodimeric glycoprotein hormones thyrotropin/thyroid stimulating hormone/TSH, lutropin/luteinizing hormone/LH and follitropin/follicle stimulating hormone/FSH. These hormones bind specific receptors on target cells that in turn activate downstream signaling pathways. {ECO:0000250|UniProtKB:P01215}.
|
Ovis aries (Sheep)
|
P01222
|
TSHB_HUMAN
|
MTALFLMSMLFGLTCGQAMSFCIPTEYTMHIERRECAYCLTINTTICAGYCMTRDINGKLFLPKYALSQDVCTYRDFIYRTVEIPGCPLHVAPYFSYPVALSCKCGKCNTDYSDCIHEAIKTNYCTKPQKSYLVGFSV
| null | null |
anatomical structure morphogenesis [GO:0009653]; cell-cell signaling [GO:0007267]; G protein-coupled receptor signaling pathway [GO:0007186]; response to calcium ion [GO:0051592]; response to estrogen [GO:0043627]; response to vitamin A [GO:0033189]
|
cytoplasm [GO:0005737]; extracellular region [GO:0005576]; extracellular space [GO:0005615]
|
hormone activity [GO:0005179]
|
PF00007;
|
2.10.90.10;
|
Glycoprotein hormones subunit beta family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Indispensable for the control of thyroid structure and metabolism.
|
Homo sapiens (Human)
|
P01223
|
TSHB_BOVIN
|
MTATFLMSMIFGLACGQAMSFCIPTEYMMHVERKECAYCLTINTTVCAGYCMTRDVNGKLFLPKYALSQDVCTYRDFMYKTAEIPGCPRHVTPYFSYPVAISCKCGKCNTDYSDCIHEAIKTNYCTKPQKSYMVGFSI
| null | null |
G protein-coupled receptor signaling pathway [GO:0007186]
|
cytoplasm [GO:0005737]; extracellular space [GO:0005615]
|
hormone activity [GO:0005179]
|
PF00007;
|
2.10.90.10;
|
Glycoprotein hormones subunit beta family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Indispensable for the control of thyroid structure and metabolism.
|
Bos taurus (Bovine)
|
P01225
|
FSHB_HUMAN
|
MKTLQFFFLFCCWKAICCNSCELTNITIAIEKEECRFCISINTTWCAGYCYTRDLVYKDPARPKIQKTCTFKELVYETVRVPGCAHHADSLYTYPVATQCHCGKCDSDSTDCTVRGLGPSYCSFGEMKE
| null | null |
female gamete generation [GO:0007292]; female pregnancy [GO:0007565]; follicle-stimulating hormone signaling pathway [GO:0042699]; G protein-coupled receptor signaling pathway [GO:0007186]; positive regulation of bone resorption [GO:0045780]; positive regulation of cell migration [GO:0030335]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of gene expression [GO:0010628]; positive regulation of steroid biosynthetic process [GO:0010893]; positive regulation of transcription by RNA polymerase II [GO:0045944]; progesterone biosynthetic process [GO:0006701]; regulation of osteoclast differentiation [GO:0045670]; regulation of signaling receptor activity [GO:0010469]; Sertoli cell proliferation [GO:0060011]; spermatogenesis [GO:0007283]; transforming growth factor beta receptor signaling pathway [GO:0007179]
|
cytoplasm [GO:0005737]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; follicle-stimulating hormone complex [GO:0016914]
|
follicle-stimulating hormone activity [GO:0016913]
|
PF00007;
|
2.10.90.10;
|
Glycoprotein hormones subunit beta family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2494176}. Note=Efficient secretion requires dimerization with CGA. {ECO:0000269|PubMed:2494176}.
| null | null | null | null | null |
FUNCTION: Together with the alpha chain CGA constitutes follitropin, the follicle-stimulating hormone, and provides its biological specificity to the hormone heterodimer. Binds FSHR, a G protein-coupled receptor, on target cells to activate downstream signaling pathways (PubMed:24692546, PubMed:2494176). Follitropin is involved in follicle development and spermatogenesis in reproductive organs (PubMed:407105, PubMed:8220432). {ECO:0000269|PubMed:24692546, ECO:0000269|PubMed:2494176, ECO:0000269|PubMed:407105, ECO:0000269|PubMed:8220432}.
|
Homo sapiens (Human)
|
P01229
|
LSHB_HUMAN
|
MEMLQGLLLLLLLSMGGAWASREPLRPWCHPINAILAVEKEGCPVCITVNTTICAGYCPTMMRVLQAVLPPLPQVVCTYRDVRFESIRLPGCPRGVDPVVSFPVALSCRCGPCRRSTSDCGGPKDHPLTCDHPQLSGLLFL
| null | null |
cell-cell signaling [GO:0007267]; G protein-coupled receptor signaling pathway [GO:0007186]; hormone-mediated signaling pathway [GO:0009755]; male gonad development [GO:0008584]; ovulation [GO:0030728]; progesterone biosynthetic process [GO:0006701]; signal transduction [GO:0007165]
|
cytoplasm [GO:0005737]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; Golgi lumen [GO:0005796]; pituitary gonadotropin complex [GO:0061696]
|
hormone activity [GO:0005179]; signaling receptor binding [GO:0005102]
|
PF00007;
|
2.10.90.10;
|
Glycoprotein hormones subunit beta family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Promotes spermatogenesis and ovulation by stimulating the testes and ovaries to synthesize steroids.
|
Homo sapiens (Human)
|
P01231
|
LSHB_SHEEP
|
MEMLQGLLLWLLLGVAGVWASRGPLRPLCQPINATLAAEKEACPVCITFTTSICAGYCLSMKRVLPVILPPMPQRVCTYHELRFASVRLPGCPPGVDPMVSFPVALSCHCGPCRLSSTDCGGPRTQPLACDHPPLPDILFL
| null | null |
estradiol secretion [GO:0035938]; G protein-coupled receptor signaling pathway [GO:0007186]; ovulation [GO:0030728]
|
cytoplasm [GO:0005737]; extracellular space [GO:0005615]
|
hormone activity [GO:0005179]
|
PF00007;
|
2.10.90.10;
|
Glycoprotein hormones subunit beta family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Promotes spermatogenesis and ovulation by stimulating the testes and ovaries to synthesize steroids. The LH alpha 3/LH beta 3 heterodimer was shown to have potent renotropic and weak gonadotropic activity. {ECO:0000269|PubMed:2456202}.
|
Ovis aries (Sheep)
|
P01232
|
LSHB_PIG
|
MEMLQGLLLWLLLSVAGVWASRGPLRPLCRPINATLAAENEACPVCITFTTSICAGYCPSMVRVLPAALPPVPQPVCTYRELSFASIRLPGCPPGVDPTVSFPVALSCHCGPCRLSSSDCGGPRAQPLACDRPLLPGLLFL
| null | null |
G protein-coupled receptor signaling pathway [GO:0007186]; ovulation [GO:0030728]
|
cytoplasm [GO:0005737]; extracellular space [GO:0005615]
|
hormone activity [GO:0005179]
|
PF00007;
|
2.10.90.10;
|
Glycoprotein hormones subunit beta family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Promotes spermatogenesis and ovulation by stimulating the testes and ovaries to synthesize steroids.
|
Sus scrofa (Pig)
|
P01235
|
GTHB2_CYPCA
|
MGTPVKILVVRNHILFSVVVLLAVAQSSYLPPCEPVNETVAVEKEGCPKCLVLQTTICSGHCLTKEPVYKSPFSTVYQHVCTYRDVRYETVRLPDCPPGVDPHITYPVALSCDCSLCTMDTSDCTIESLQPDFCMSQREDFLVY
| null | null |
G protein-coupled receptor signaling pathway [GO:0007186]; ovulation [GO:0030728]; positive regulation of androgen secretion [GO:2000836]; positive regulation of estradiol secretion [GO:2000866]; positive regulation of gene expression [GO:0010628]
|
cytoplasm [GO:0005737]; extracellular space [GO:0005615]
|
follicle-stimulating hormone receptor binding [GO:0031762]; hormone activity [GO:0005179]; lutropin-choriogonadotropic hormone receptor binding [GO:0031775]; protein heterodimerization activity [GO:0046982]
|
PF00007;
|
2.10.90.10;
|
Glycoprotein hormones subunit beta family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Involved in gametogenesis and steroidogenesis.
|
Cyprinus carpio (Common carp)
|
P01236
|
PRL_HUMAN
|
MNIKGSPWKGSLLLLLVSNLLLCQSVAPLPICPGGAARCQVTLRDLFDRAVVLSHYIHNLSSEMFSEFDKRYTHGRGFITKAINSCHTSSLATPEDKEQAQQMNQKDFLSLIVSILRSWNEPLYHLVTEVRGMQEAPEAILSKAVEIEEQTKRLLEGMELIVSQVHPETKENEIYPVWSGLPSLQMADEESRLSAYYNLLHCLRRDSHKIDNYLKLLKCRIIHNNNC
| null | null |
cell surface receptor signaling pathway [GO:0007166]; female pregnancy [GO:0007565]; lactation [GO:0007595]; mammary gland development [GO:0030879]; negative regulation of angiogenesis [GO:0016525]; negative regulation of endothelial cell proliferation [GO:0001937]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of lactation [GO:1903489]; positive regulation of miRNA transcription [GO:1902895]; positive regulation of receptor signaling pathway via JAK-STAT [GO:0046427]; prolactin signaling pathway [GO:0038161]; response to nutrient levels [GO:0031667]
|
endosome lumen [GO:0031904]; extracellular region [GO:0005576]; extracellular space [GO:0005615]
|
hormone activity [GO:0005179]; prolactin receptor binding [GO:0005148]
|
PF00103;
|
1.20.1250.10;
|
Somatotropin/prolactin family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Prolactin acts primarily on the mammary gland by promoting lactation.
|
Homo sapiens (Human)
|
P01237
|
PRL_RAT
|
MNSQVSARKAGTLLLLMMSNLLFCQNVQTLPVCSGGDCQTPLPELFDRVVMLSHYIHTLYTDMFIEFDKQYVQDREFIAKAINDCPTSSLATPEDKEQAQKVPPEVLLNLILSLVHSWNDPLFQLITGLGGIHEAPDAIISRAKEIEEQNKRLLEGIEKIISQAYPEAKGNEIYLVWSQLPSLQGVDEESKDLAFYNNIRCLRRDSHKVDNYLKFLRCQIVHKNNC
| null | null |
cell population proliferation [GO:0008283]; cellular response to hormone stimulus [GO:0032870]; circadian rhythm [GO:0007623]; epithelial cell proliferation [GO:0050673]; female pregnancy [GO:0007565]; lactation [GO:0007595]; mammary gland development [GO:0030879]; maternal behavior [GO:0042711]; multicellular organismal response to stress [GO:0033555]; negative regulation of endothelial cell proliferation [GO:0001937]; ovulation cycle [GO:0042698]; parturition [GO:0007567]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of epithelial cell proliferation [GO:0050679]; positive regulation of lactation [GO:1903489]; positive regulation of miRNA transcription [GO:1902895]; positive regulation of receptor signaling pathway via JAK-STAT [GO:0046427]; prolactin signaling pathway [GO:0038161]; regulation of ossification [GO:0030278]; regulation of receptor signaling pathway via JAK-STAT [GO:0046425]; response to estradiol [GO:0032355]; response to ethanol [GO:0045471]; response to lipopolysaccharide [GO:0032496]; response to macrophage colony-stimulating factor [GO:0036005]; response to nutrient [GO:0007584]; response to nutrient levels [GO:0031667]; response to organic cyclic compound [GO:0014070]; response to xenobiotic stimulus [GO:0009410]
|
extracellular region [GO:0005576]; extracellular space [GO:0005615]; secretory granule [GO:0030141]
|
hormone activity [GO:0005179]; prolactin receptor binding [GO:0005148]
|
PF00103;
|
1.20.1250.10;
|
Somatotropin/prolactin family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Prolactin acts primarily on the mammary gland by promoting lactation.
|
Rattus norvegicus (Rat)
|
P01238
|
PRL_PIG
|
MDNRGSSQKGSLLLLLLLVSNLFLCKSVASLPICPSGAVNCQVSLRDLFDRAVILSHYIHNLSSEMFNEFDKRYAQGRGFITKAINSCHTSSLSTPEDKEQAQQIHHEVLLNLILRVLRSWNDPLYHLVTEVRGMQEAPDAILSRAIEIEEQNKRLLEGMEKIVGQVHPGIKENEVYSVWSGLPSLQMADEDTRLFAFYNLLHCLRRDSHKIDNYLKLLKCRIIYDSNC
| null | null |
cellular response to hypoxia [GO:0071456]; female pregnancy [GO:0007565]; lactation [GO:0007595]; mammary gland development [GO:0030879]; negative regulation of estrogen biosynthetic process [GO:1904077]; negative regulation of hydrogen peroxide biosynthetic process [GO:0010730]; negative regulation of nitric oxide biosynthetic process [GO:0045019]; negative regulation of progesterone biosynthetic process [GO:2000183]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of endothelial cell proliferation [GO:0001938]; positive regulation of lactation [GO:1903489]; positive regulation of receptor signaling pathway via JAK-STAT [GO:0046427]; positive regulation of vascular endothelial growth factor production [GO:0010575]; response to nutrient levels [GO:0031667]
|
extracellular space [GO:0005615]
|
hormone activity [GO:0005179]; prolactin receptor binding [GO:0005148]
|
PF00103;
|
1.20.1250.10;
|
Somatotropin/prolactin family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Prolactin acts primarily on the mammary gland by promoting lactation.
|
Sus scrofa (Pig)
|
P01239
|
PRL_BOVIN
|
MDSKGSSQKGSRLLLLLVVSNLLLCQGVVSTPVCPNGPGNCQVSLRDLFDRAVMVSHYIHDLSSEMFNEFDKRYAQGKGFITMALNSCHTSSLPTPEDKEQAQQTHHEVLMSLILGLLRSWNDPLYHLVTEVRGMKGAPDAILSRAIEIEEENKRLLEGMEMIFGQVIPGAKETEPYPVWSGLPSLQTKDEDARYSAFYNLLHCLRRDSSKIDTYLKLLNCRIIYNNNC
| null | null |
biosynthetic process [GO:0009058]; blastocyst formation [GO:0001825]; cell surface receptor signaling pathway [GO:0007166]; female pregnancy [GO:0007565]; inflammatory response [GO:0006954]; lactation [GO:0007595]; long-day photoperiodism [GO:0048571]; mammary gland development [GO:0030879]; negative regulation of apoptotic process [GO:0043066]; negative regulation of gene expression [GO:0010629]; peptide hormone secretion [GO:0030072]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of endocytosis [GO:0045807]; positive regulation of fatty acid biosynthetic process [GO:0045723]; positive regulation of gene expression [GO:0010628]; positive regulation of lactation [GO:1903489]; positive regulation of nitric oxide biosynthetic process [GO:0045429]; positive regulation of non-canonical NF-kappaB signal transduction [GO:1901224]; positive regulation of phagocytosis [GO:0050766]; positive regulation of receptor signaling pathway via JAK-STAT [GO:0046427]; regulation of meiotic cell cycle process involved in oocyte maturation [GO:1903538]; response to external biotic stimulus [GO:0043207]; response to food [GO:0032094]; response to L-arginine [GO:1903576]; response to mechanical stimulus [GO:0009612]; response to nutrient levels [GO:0031667]
|
cytosol [GO:0005829]; endoplasmic reticulum lumen [GO:0005788]; endoplasmic reticulum membrane [GO:0005789]; extracellular space [GO:0005615]
|
hormone activity [GO:0005179]; prolactin receptor binding [GO:0005148]
|
PF00103;
|
1.20.1250.10;
|
Somatotropin/prolactin family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Prolactin acts primarily on the mammary gland by promoting lactation.
|
Bos taurus (Bovine)
|
P01240
|
PRL_SHEEP
|
MDSKGSAQKGSRLLLLLVVSNLLLCQGVVSTPVCPNGPGNCQVSLRDLFDRAVMVSHYIHNLSSEMFNEFDKRYAQGKGFITMALNSCHTSSLPTPEDKEQAQQTHHEVLMSLILGLLRSWNDPLYHLVTEVRGMKGVPDAILSRAIEIEEENKRLLEGMEMIFGQVIPGAKETEPYPVWSGLPSLQTKDEDARHSAFYNLLHCLRRDSSKIDTYLKLLNCRIIYNNNC
| null | null |
biosynthetic process [GO:0009058]; blastocyst formation [GO:0001825]; cell surface receptor signaling pathway [GO:0007166]; female pregnancy [GO:0007565]; lactation [GO:0007595]; negative regulation of apoptotic process [GO:0043066]; negative regulation of luteinizing hormone secretion [GO:0033685]; negative regulation of peptide hormone secretion [GO:0090278]; peptide hormone secretion [GO:0030072]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of fatty acid biosynthetic process [GO:0045723]; positive regulation of gene expression [GO:0010628]; positive regulation of lactation [GO:1903489]; positive regulation of receptor signaling pathway via JAK-STAT [GO:0046427]; response to nutrient levels [GO:0031667]
|
extracellular space [GO:0005615]
|
hormone activity [GO:0005179]; prolactin receptor binding [GO:0005148]
|
PF00103;
|
1.20.1250.10;
|
Somatotropin/prolactin family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Prolactin acts primarily on the mammary gland by promoting lactation, mammogenesis, mitogenesis and osmoregulation.
|
Ovis aries (Sheep)
|
P01241
|
SOMA_HUMAN
|
MATGSRTSLLLAFGLLCLPWLQEGSAFPTIPLSRLFDNAMLRAHRLHQLAFDTYQEFEEAYIPKEQKYSFLQNPQTSLCFSESIPTPSNREETQQKSNLELLRISLLLIQSWLEPVQFLRSVFANSLVYGASDSNVYDLLKDLEEGIQTLMGRLEDGSPRTGQIFKQTYSKFDTNSHNDDALLKNYGLLYCFRKDMDKVETFLRIVQCRSVEGSCGF
| null | null |
animal organ development [GO:0048513]; bone maturation [GO:0070977]; cytokine-mediated signaling pathway [GO:0019221]; growth hormone receptor signaling pathway [GO:0060396]; positive regulation of activation of Janus kinase activity [GO:0010536]; positive regulation of glucose transmembrane transport [GO:0010828]; positive regulation of growth [GO:0045927]; positive regulation of insulin-like growth factor receptor signaling pathway [GO:0043568]; positive regulation of MAP kinase activity [GO:0043406]; positive regulation of multicellular organism growth [GO:0040018]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of receptor signaling pathway via JAK-STAT [GO:0046427]; positive regulation of tyrosine phosphorylation of STAT protein [GO:0042531]; receptor signaling pathway via JAK-STAT [GO:0007259]; response to estradiol [GO:0032355]; response to nutrient levels [GO:0031667]
|
endosome lumen [GO:0031904]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; growth hormone receptor complex [GO:0070195]
|
cytokine activity [GO:0005125]; growth factor activity [GO:0008083]; growth hormone activity [GO:0070186]; growth hormone receptor binding [GO:0005131]; hormone activity [GO:0005179]; metal ion binding [GO:0046872]; prolactin receptor binding [GO:0005148]
|
PF00103;
|
1.20.1250.10;
|
Somatotropin/prolactin family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Plays an important role in growth control. Its major role in stimulating body growth is to stimulate the liver and other tissues to secrete IGF-1. It stimulates both the differentiation and proliferation of myoblasts. It also stimulates amino acid uptake and protein synthesis in muscle and other tissues.
|
Homo sapiens (Human)
|
P01242
|
SOM2_HUMAN
|
MAAGSRTSLLLAFGLLCLSWLQEGSAFPTIPLSRLFDNAMLRARRLYQLAYDTYQEFEEAYILKEQKYSFLQNPQTSLCFSESIPTPSNRVKTQQKSNLELLRISLLLIQSWLEPVQLLRSVFANSLVYGASDSNVYRHLKDLEEGIQTLMWRLEDGSPRTGQIFNQSYSKFDTKSHNDDALLKNYGLLYCFRKDMDKVETFLRIVQCRSVEGSCGF
| null | null |
animal organ development [GO:0048513]; growth hormone receptor signaling pathway [GO:0060396]; positive regulation of growth [GO:0045927]; positive regulation of receptor signaling pathway via JAK-STAT [GO:0046427]; positive regulation of tyrosine phosphorylation of STAT protein [GO:0042531]; response to nutrient levels [GO:0031667]
|
endosome lumen [GO:0031904]; extracellular region [GO:0005576]; extracellular space [GO:0005615]
|
growth factor activity [GO:0008083]; growth hormone receptor binding [GO:0005131]; hormone activity [GO:0005179]
|
PF00103;
|
1.20.1250.10;
|
Somatotropin/prolactin family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Plays an important role in growth control. Its major role in stimulating body growth is to stimulate the liver and other tissues to secrete IGF-1. It stimulates both the differentiation and proliferation of myoblasts. It also stimulates amino acid uptake and protein synthesis in muscle and other tissues.
|
Homo sapiens (Human)
|
P01244
|
SOMA_RAT
|
MAADSQTPWLLTFSLLCLLWPQEAGAFPAMPLSSLFANAVLRAQHLHQLAADTYKEFERAYIPEGQRYSIQNAQAAFCFSETIPAPTGKEEAQQRTDMELLRFSLLLIQSWLGPVQFLSRIFTNSLMFGTSDRVYEKLKDLEEGIQALMQELEDGSPRIGQILKQTYDKFDANMRSDDALLKNYGLLSCFKKDLHKAETYLRVMKCRRFAESSCAF
| null | null |
animal organ development [GO:0048513]; bone maturation [GO:0070977]; cellular response to alkaline pH [GO:0071469]; cellular response to insulin stimulus [GO:0032869]; cellular response to thyroid hormone stimulus [GO:0097067]; cytokine-mediated signaling pathway [GO:0019221]; female pregnancy [GO:0007565]; growth hormone receptor signaling pathway [GO:0060396]; lung alveolus development [GO:0048286]; neuroblast proliferation [GO:0007405]; positive regulation of glucose transmembrane transport [GO:0010828]; positive regulation of growth [GO:0045927]; positive regulation of insulin-like growth factor receptor signaling pathway [GO:0043568]; positive regulation of multicellular organism growth [GO:0040018]; positive regulation of neurogenesis [GO:0050769]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of receptor signaling pathway via JAK-STAT [GO:0046427]; positive regulation of steroid hormone biosynthetic process [GO:0090031]; positive regulation of tyrosine phosphorylation of STAT protein [GO:0042531]; receptor signaling pathway via JAK-STAT [GO:0007259]; regulation of response to nutrient levels [GO:0032107]; response to cytokine [GO:0034097]; response to estradiol [GO:0032355]; response to food [GO:0032094]; response to light stimulus [GO:0009416]; response to nutrient levels [GO:0031667]; response to peptide hormone [GO:0043434]
|
collagen-containing extracellular matrix [GO:0062023]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; growth hormone receptor complex [GO:0070195]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; secretory granule [GO:0030141]; trans-Golgi network [GO:0005802]
|
cytokine activity [GO:0005125]; growth factor activity [GO:0008083]; growth hormone activity [GO:0070186]; growth hormone receptor binding [GO:0005131]; hormone activity [GO:0005179]; metal ion binding [GO:0046872]; prolactin receptor binding [GO:0005148]
|
PF00103;
|
1.20.1250.10;
|
Somatotropin/prolactin family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Plays an important role in growth control. Its major role in stimulating body growth is to stimulate the liver and other tissues to secrete IGF-1. It stimulates both the differentiation and proliferation of myoblasts. It also stimulates amino acid uptake and protein synthesis in muscle and other tissues.
|
Rattus norvegicus (Rat)
|
P01246
|
SOMA_BOVIN
|
MMAAGPRTSLLLAFALLCLPWTQVVGAFPAMSLSGLFANAVLRAQHLHQLAADTFKEFERTYIPEGQRYSIQNTQVAFCFSETIPAPTGKNEAQQKSDLELLRISLLLIQSWLGPLQFLSRVFTNSLVFGTSDRVYEKLKDLEEGILALMRELEDGTPRAGQILKQTYDKFDTNMRSDDALLKNYGLLSCFRKDLHKTETYLRVMKCRRFGEASCAF
| null | null |
animal organ development [GO:0048513]; cell population proliferation [GO:0008283]; growth hormone receptor signaling pathway [GO:0060396]; insulin secretion [GO:0030073]; negative regulation of apoptotic process [GO:0043066]; negative regulation of fatty acid biosynthetic process [GO:0045717]; negative regulation of gene expression [GO:0010629]; negative regulation of plasminogen activation [GO:0010757]; negative regulation of protein acetylation [GO:1901984]; negative regulation of testosterone secretion [GO:2000844]; negative regulation of urine volume [GO:0035811]; positive regulation of aldosterone secretion [GO:2000860]; positive regulation of cholesterol biosynthetic process [GO:0045542]; positive regulation of cytoplasmic translation [GO:2000767]; positive regulation of diacylglycerol biosynthetic process [GO:1900482]; positive regulation of fatty acid biosynthetic process [GO:0045723]; positive regulation of feeding behavior [GO:2000253]; positive regulation of gene expression [GO:0010628]; positive regulation of growth [GO:0045927]; positive regulation of lactation [GO:1903489]; positive regulation of lipid catabolic process [GO:0050996]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of peptidyl-threonine phosphorylation [GO:0010800]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; positive regulation of phospholipid biosynthetic process [GO:0071073]; positive regulation of receptor signaling pathway via JAK-STAT [GO:0046427]; positive regulation of steroid hormone secretion [GO:2000833]; positive regulation of TOR signaling [GO:0032008]; positive regulation of triglyceride biosynthetic process [GO:0010867]; positive regulation of tyrosine phosphorylation of STAT protein [GO:0042531]; protein secretion [GO:0009306]; regulation of intracellular steroid hormone receptor signaling pathway [GO:0033143]; renal sodium ion absorption [GO:0070294]; response to food [GO:0032094]; response to L-arginine [GO:1903576]; response to nutrient levels [GO:0031667]
|
extracellular space [GO:0005615]
|
growth factor activity [GO:0008083]; growth hormone activity [GO:0070186]; growth hormone receptor binding [GO:0005131]; hormone activity [GO:0005179]; metal ion binding [GO:0046872]
|
PF00103;
|
1.20.1250.10;
|
Somatotropin/prolactin family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Plays an important role in growth control. Its major role in stimulating body growth is to stimulate the liver and other tissues to secrete IGF-1. It stimulates both the differentiation and proliferation of myoblasts. It also stimulates amino acid uptake and protein synthesis in muscle and other tissues.
|
Bos taurus (Bovine)
|
P01248
|
SOMA_PIG
|
MAAGPRTSALLAFALLCLPWTREVGAFPAMPLSSLFANAVLRAQHLHQLAADTYKEFERAYIPEGQRYSIQNAQAAFCFSETIPAPTGKDEAQQRSDVELLRFSLLLIQSWLGPVQFLSRVFTNSLVFGTSDRVYEKLKDLEEGIQALMRELEDGSPRAGQILKQTYDKFDTNLRSDDALLKNYGLLSCFKKDLHKAETYLRVMKCRRFVESSCAF
| null | null |
animal organ development [GO:0048513]; growth hormone receptor signaling pathway [GO:0060396]; positive regulation of growth [GO:0045927]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of receptor signaling pathway via JAK-STAT [GO:0046427]; positive regulation of tyrosine phosphorylation of STAT protein [GO:0042531]; response to nutrient levels [GO:0031667]
|
extracellular space [GO:0005615]
|
growth factor activity [GO:0008083]; growth hormone activity [GO:0070186]; growth hormone receptor binding [GO:0005131]; hormone activity [GO:0005179]; metal ion binding [GO:0046872]
|
PF00103;
|
1.20.1250.10;
|
Somatotropin/prolactin family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Plays an important role in growth control. Its major role in stimulating body growth is to stimulate the liver and other tissues to secrete IGF-1. It stimulates both the differentiation and proliferation of myoblasts. It also stimulates amino acid uptake and protein synthesis in muscle and other tissues.
|
Sus scrofa (Pig)
|
P01256
|
CALCA_RAT
|
MGFLKFSPFLVVSILLLYQACGLQAVPLRSTLESSPGMAATLSEEEARLLLAALVQNYMQMKVRELEQEQEAEGSSVTAQKRSCNTATCVTHRLAGLLSRSGGVVKDNFVPTNVGSEAFGRRRRDLQA
| null | null |
adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; artery vasodilation involved in baroreceptor response to increased systemic arterial blood pressure [GO:0001984]; calcitonin gene-related peptide receptor signaling pathway [GO:1990408]; cell adhesion [GO:0007155]; cellular response to nerve growth factor stimulus [GO:1990090]; cellular response to tumor necrosis factor [GO:0071356]; detection of temperature stimulus involved in sensory perception of pain [GO:0050965]; embryo implantation [GO:0007566]; endothelial cell migration [GO:0043542]; endothelial cell proliferation [GO:0001935]; feeding behavior [GO:0007631]; G protein-coupled receptor internalization [GO:0002031]; inflammatory response [GO:0006954]; intracellular calcium ion homeostasis [GO:0006874]; leukocyte cell-cell adhesion [GO:0007159]; monocyte chemotaxis [GO:0002548]; negative regulation of blood pressure [GO:0045776]; negative regulation of bone resorption [GO:0045779]; negative regulation of calcium ion transport into cytosol [GO:0010523]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of ossification [GO:0030279]; negative regulation of osteoclast differentiation [GO:0045671]; negative regulation of smooth muscle contraction [GO:0045986]; neuropeptide signaling pathway [GO:0007218]; ossification [GO:0001503]; phospholipase C-activating G protein-coupled receptor signaling pathway [GO:0007200]; positive regulation of cell adhesion [GO:0045785]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; positive regulation of interleukin-1 alpha production [GO:0032730]; positive regulation of interleukin-8 production [GO:0032757]; positive regulation of macrophage differentiation [GO:0045651]; receptor internalization [GO:0031623]; regulation of cytosolic calcium ion concentration [GO:0051480]; response to heat [GO:0009408]; response to pain [GO:0048265]; smooth muscle contraction [GO:0006939]; vasculature development [GO:0001944]; vasodilation [GO:0042311]
|
axon [GO:0030424]; cytoplasm [GO:0005737]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; hippocampal mossy fiber to CA3 synapse [GO:0098686]; neuron projection [GO:0043005]; neuronal cell body [GO:0043025]; neuronal dense core vesicle [GO:0098992]; terminal bouton [GO:0043195]
|
calcitonin receptor binding [GO:0031716]; identical protein binding [GO:0042802]; neuropeptide hormone activity [GO:0005184]; protein-containing complex binding [GO:0044877]; signaling receptor binding [GO:0005102]
|
PF00214;
|
6.10.250.2190;
|
Calcitonin family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: CGRP induces vasodilation. It dilates a variety of vessels including the coronary, cerebral and systemic vasculature. Its abundance in the CNS also points toward a neurotransmitter or neuromodulator role.
|
Rattus norvegicus (Rat)
|
P01257
|
CALC_RAT
|
MGFLKFSPFLVVSILLLYQACGLQAVPLRSTLESSPGMATLSEEEARLLAALVQNYMQMKVRELEQEEEQEAEGSSLDSPRSKRCGNLSTCMLGTYTQDLNKFHTFPQTSIGVGAPGKKRDMAKDLETNHHPYFGN
| null | null |
adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; artery vasodilation involved in baroreceptor response to increased systemic arterial blood pressure [GO:0001984]; calcitonin gene-related peptide receptor signaling pathway [GO:1990408]; cell adhesion [GO:0007155]; cellular response to nerve growth factor stimulus [GO:1990090]; cellular response to tumor necrosis factor [GO:0071356]; detection of temperature stimulus involved in sensory perception of pain [GO:0050965]; embryo implantation [GO:0007566]; endothelial cell migration [GO:0043542]; endothelial cell proliferation [GO:0001935]; feeding behavior [GO:0007631]; G protein-coupled receptor internalization [GO:0002031]; inflammatory response [GO:0006954]; intracellular calcium ion homeostasis [GO:0006874]; leukocyte cell-cell adhesion [GO:0007159]; monocyte chemotaxis [GO:0002548]; negative regulation of blood pressure [GO:0045776]; negative regulation of bone resorption [GO:0045779]; negative regulation of calcium ion transport into cytosol [GO:0010523]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of ossification [GO:0030279]; negative regulation of osteoclast differentiation [GO:0045671]; negative regulation of smooth muscle contraction [GO:0045986]; neuropeptide signaling pathway [GO:0007218]; ossification [GO:0001503]; phospholipase C-activating G protein-coupled receptor signaling pathway [GO:0007200]; positive regulation of cell adhesion [GO:0045785]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; positive regulation of interleukin-1 alpha production [GO:0032730]; positive regulation of interleukin-8 production [GO:0032757]; positive regulation of macrophage differentiation [GO:0045651]; receptor internalization [GO:0031623]; regulation of cytosolic calcium ion concentration [GO:0051480]; response to heat [GO:0009408]; response to pain [GO:0048265]; smooth muscle contraction [GO:0006939]; vasculature development [GO:0001944]; vasodilation [GO:0042311]
|
axon [GO:0030424]; cytoplasm [GO:0005737]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; hippocampal mossy fiber to CA3 synapse [GO:0098686]; neuron projection [GO:0043005]; neuronal cell body [GO:0043025]; neuronal dense core vesicle [GO:0098992]; terminal bouton [GO:0043195]
|
calcitonin receptor binding [GO:0031716]; identical protein binding [GO:0042802]; neuropeptide hormone activity [GO:0005184]; protein-containing complex binding [GO:0044877]; signaling receptor binding [GO:0005102]
|
PF00214;
| null |
Calcitonin family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Causes a rapid but short-lived drop in the level of calcium and phosphate in blood by promoting the incorporation of those ions in the bones.
|
Rattus norvegicus (Rat)
|
P01258
|
CALC_HUMAN
|
MGFQKFSPFLALSILVLLQAGSLHAAPFRSALESSPADPATLSEDEARLLLAALVQDYVQMKASELEQEQEREGSSLDSPRSKRCGNLSTCMLGTYTQDFNKFHTFPQTAIGVGAPGKKRDMSSDLERDHRPHVSMPQNAN
| null | null |
activation of protein kinase activity [GO:0032147]; adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; artery vasodilation involved in baroreceptor response to increased systemic arterial blood pressure [GO:0001984]; cellular response to nerve growth factor stimulus [GO:1990090]; cellular response to tumor necrosis factor [GO:0071356]; detection of temperature stimulus involved in sensory perception of pain [GO:0050965]; embryo implantation [GO:0007566]; feeding behavior [GO:0007631]; inflammatory response [GO:0006954]; monocyte chemotaxis [GO:0002548]; negative regulation of bone resorption [GO:0045779]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of ossification [GO:0030279]; negative regulation of smooth muscle contraction [GO:0045986]; neuropeptide signaling pathway [GO:0007218]; ossification [GO:0001503]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; regulation of cytosolic calcium ion concentration [GO:0051480]; response to heat [GO:0009408]; response to pain [GO:0048265]; smooth muscle contraction [GO:0006939]
|
extracellular region [GO:0005576]; extracellular space [GO:0005615]; hippocampal mossy fiber to CA3 synapse [GO:0098686]; neuronal cell body [GO:0043025]; neuronal dense core vesicle [GO:0098992]; terminal bouton [GO:0043195]
|
calcitonin receptor binding [GO:0031716]; hormone activity [GO:0005179]; identical protein binding [GO:0042802]
|
PF00214;
| null |
Calcitonin family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Calcitonin causes a rapid but short-lived drop in the level of calcium and phosphate in blood by promoting the incorporation of those ions in the bones.; FUNCTION: Katacalcin is a potent plasma calcium-lowering peptide.
|
Homo sapiens (Human)
|
P01266
|
THYG_HUMAN
|
MALVLEIFTLLASICWVSANIFEYQVDAQPLRPCELQRETAFLKQADYVPQCAEDGSFQTVQCQNDGRSCWCVGANGSEVLGSRQPGRPVACLSFCQLQKQQILLSGYINSTDTSYLPQCQDSGDYAPVQCDVQQVQCWCVDAEGMEVYGTRQLGRPKRCPRSCEIRNRRLLHGVGDKSPPQCSAEGEFMPVQCKFVNTTDMMIFDLVHSYNRFPDAFVTFSSFQRRFPEVSGYCHCADSQGRELAETGLELLLDEIYDTIFAGLDLPSTFTETTLYRILQRRFLAVQSVISGRFRCPTKCEVERFTATSFGHPYVPSCRRNGDYQAVQCQTEGPCWCVDAQGKEMHGTRQQGEPPSCAEGQSCASERQQALSRLYFGTSGYFSQHDLFSSPEKRWASPRVARFATSCPPTIKELFVDSGLLRPMVEGQSQQFSVSENLLKEAIRAIFPSRGLARLALQFTTNPKRLQQNLFGGKFLVNVGQFNLSGALGTRGTFNFSQFFQQLGLASFLNGGRQEDLAKPLSVGLDSNSSTGTPEAAKKDGTMNKPTVGSFGFEINLQENQNALKFLASLLELPEFLLFLQHAISVPEDVARDLGDVMETVLSSQTCEQTPERLFVPSCTTEGSYEDVQCFSGECWCVNSWGKELPGSRVRGGQPRCPTDCEKQRARMQSLMGSQPAGSTLFVPACTSEGHFLPVQCFNSECYCVDAEGQAIPGTRSAIGKPKKCPTPCQLQSEQAFLRTVQALLSNSSMLPTLSDTYIPQCSTDGQWRQVQCNGPPEQVFELYQRWEAQNKGQDLTPAKLLVKIMSYREAASGNFSLFIQSLYEAGQQDVFPVLSQYPSLQDVPLAALEGKRPQPRENILLEPYLFWQILNGQLSQYPGSYSDFSTPLAHFDLRNCWCVDEAGQELEGMRSEPSKLPTCPGSCEEAKLRVLQFIRETEEIVSASNSSRFPLGESFLVAKGIRLRNEDLGLPPLFPPREAFAEQFLRGSDYAIRLAAQSTLSFYQRRRFSPDDSAGASALLRSGPYMPQCDAFGSWEPVQCHAGTGHCWCVDEKGGFIPGSLTARSLQIPQCPTTCEKSRTSGLLSSWKQARSQENPSPKDLFVPACLETGEYARLQASGAGTWCVDPASGEELRPGSSSSAQCPSLCNVLKSGVLSRRVSPGYVPACRAEDGGFSPVQCDQAQGSCWCVMDSGEEVPGTRVTGGQPACESPRCPLPFNASEVVGGTILCETISGPTGSAMQQCQLLCRQGSWSVFPPGPLICSLESGRWESQLPQPRACQRPQLWQTIQTQGHFQLQLPPGKMCSADYADLLQTFQVFILDELTARGFCQIQVKTFGTLVSIPVCNNSSVQVGCLTRERLGVNVTWKSRLEDIPVASLPDLHDIERALVGKDLLGRFTDLIQSGSFQLHLDSKTFPAETIRFLQGDHFGTSPRTWFGCSEGFYQVLTSEASQDGLGCVKCPEGSYSQDEECIPCPVGFYQEQAGSLACVPCPVGRTTISAGAFSQTHCVTDCQRNEAGLQCDQNGQYRASQKDRGSGKAFCVDGEGRRLPWWETEAPLEDSQCLMMQKFEKVPESKVIFDANAPVAVRSKVPDSEFPVMQCLTDCTEDEACSFFTVSTTEPEISCDFYAWTSDNVACMTSDQKRDALGNSKATSFGSLRCQVKVRSHGQDSPAVYLKKGQGSTTTLQKRFEPTGFQNMLSGLYNPIVFSASGANLTDAHLFCLLACDRDLCCDGFVLTQVQGGAIICGLLSSPSVLLCNVKDWMDPSEAWANATCPGVTYDQESHQVILRLGDQEFIKSLTPLEGTQDTFTNFQQVYLWKDSDMGSRPESMGCRKDTVPRPASPTEAGLTTELFSPVDLNQVIVNGNQSLSSQKHWLFKHLFSAQQANLWCLSRCVQEHSFCQLAEITESASLYFTCTLYPEAQVCDDIMESNAQGCRLILPQMPKALFRKKVILEDKVKNFYTRLPFQKLMGISIRNKVPMSEKSISNGFFECERRCDADPCCTGFGFLNVSQLKGGEVTCLTLNSLGIQMCSEENGGAWRILDCGSPDIEVHTYPFGWYQKPIAQNNAPSFCPLVVLPSLTEKVSLDSWQSLALSSVVVDPSIRHFDVAHVSTAATSNFSAVRDLCLSECSQHEACLITTLQTQPGAVRCMFYADTQSCTHSLQGQNCRLLLREEATHIYRKPGISLLSYEASVPSVPISTHGRLLGRSQAIQVGTSWKQVDQFLGVPYAAPPLAERRFQAPEPLNWTGSWDASKPRASCWQPGTRTSTSPGVSEDCLYLNVFIPQNVAPNASVLVFFHNTMDREESEGWPAIDGSFLAAVGNLIVVTASYRVGVFGFLSSGSGEVSGNWGLLDQVAALTWVQTHIRGFGGDPRRVSLAADRGGADVASIHLLTARATNSQLFRRAVLMGGSALSPAAVISHERAQQQAIALAKEVSCPMSSSQEVVSCLRQKPANVLNDAQTKLLAVSGPFHYWGPVIDGHFLREPPARALKRSLWVEVDLLIGSSQDDGLINRAKAVKQFEESRGRTSSKTAFYQALQNSLGGEDSDARVEAAATWYYSLEHSTDDYASFSRALENATRDYFIICPIIDMASAWAKRARGNVFMYHAPENYGHGSLELLADVQFALGLPFYPAYEGQFSLEEKSLSLKIMQYFSHFIRSGNPNYPYEFSRKVPTFATPWPDFVPRAGGENYKEFSELLPNRQGLKKADCSFWSKYISSLKTSADGAKGGQSAESEEEELTAGSGLREDLLSLQEPGSKTYSK
| null | null |
hormone biosynthetic process [GO:0042446]; iodide transport [GO:0015705]; regulation of myelination [GO:0031641]; signal transduction [GO:0007165]; thyroid gland development [GO:0030878]; thyroid hormone generation [GO:0006590]
|
extracellular region [GO:0005576]; extracellular space [GO:0005615]
|
hormone activity [GO:0005179]; identical protein binding [GO:0042802]
|
PF00135;PF07699;PF00086;
|
3.40.50.1820;4.10.800.10;2.10.50.10;
|
Type-B carboxylesterase/lipase family
|
PTM: Iodinated on tyrosine residues by TPO (PubMed:2760035, PubMed:32025030). There are 4 pairs of iodinated tyrosines used for coupling: acceptor Tyr-24 is coupled to donor Tyr-149 or Tyr-234, acceptor Tyr-2573 is coupled to donor Tyr-2540, acceptor Tyr-2766 in monomer 1 is coupled to donor Tyr-2766 in monomer 2 and acceptor Tyr-1310 in monomer 1 is coupled to donor Tyr-108 in monomer 2 (PubMed:32025030). {ECO:0000269|PubMed:2760035, ECO:0000269|PubMed:32025030}.; PTM: Sulfated tyrosines are desulfated during iodination. {ECO:0000269|PubMed:10448091}.; PTM: Undergoes sequential proteolysis by cathepsins to release thyroxine (T4) and triiodothyronine (T3) hormones. In the thyroid follicle lumen, cross-linked TG (storage form) is solubilized by limited proteolysis mediated by cathepsins CTSB and/or CTSL. Partially cleaved TG is further processed by CTSK/cathepsin K and/or CTSL resulting in the release of T4. Following endocytosis, further processing occurs leading to the release of T3 and more T4 hormones. {ECO:0000250|UniProtKB:O08710}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11082042, ECO:0000269|PubMed:19509106, ECO:0000269|PubMed:8626858}. Note=Secreted into the thyroid follicle lumen (PubMed:19509106). Localizes to colloid globules, a structure formed in the thyroid follicle lumen consisting of cross-linked TG arranged in concentric layers (PubMed:11082042, PubMed:8626858). {ECO:0000269|PubMed:11082042, ECO:0000269|PubMed:19509106, ECO:0000269|PubMed:8626858}.
| null | null | null | null | null |
FUNCTION: Acts as a substrate for the production of iodinated thyroid hormones thyroxine (T4) and triiodothyronine (T3) (PubMed:17532758, PubMed:32025030). The synthesis of T3 and T4 involves iodination of selected tyrosine residues of TG/thyroglobulin followed by their oxidative coupling in the thyroid follicle lumen (PubMed:32025030). Following TG re-internalization and lysosomal-mediated proteolysis, T3 and T4 are released from the polypeptide backbone leading to their secretion into the bloodstream (PubMed:32025030). One dimer produces 7 thyroid hormone molecules (PubMed:32025030). {ECO:0000269|PubMed:17532758, ECO:0000269|PubMed:32025030}.
|
Homo sapiens (Human)
|
P01267
|
THYG_BOVIN
|
MALALWVFGLLDLICLASANIFEYQVDAQPLRPCELQRERAFLKREDYVPQCAEDGSFQTVQCGKDGASCWCVDADGREVPGSRQPGRPAACLSFCQLQKQQILLSSYINSTATSYLPQCQDSGDYSPVQCDLRRRQCWCVDAEGMEVYGTRQQGRPARCPRSCEIRNRRLLHGVGDRSPPQCSPDGAFRPVQCKLVNTTDMMIFDLVHSYSRFPDAFVTFSSFRSRFPEVSGYCYCADSQGRELAETGLELLLDEIYDTIFAGLDLASTFAETTLYRILQRRFLAVQLVISGRFRCPTKCEVERFAATSFRHPYVPSCHPDGEYQAAQCQQGGPCWCVDSRGQEIPGTRQRGEPPSCAEDQSCPSERRRAFSRLRFGPSGYFSRRSLLLAPEEGPVSQRFARFTASCPPSIKELFLDSGIFQPMLQGRDTRFVAPESLKEAIRGLFPSRELARLALQFTTNAKRLQQNLFGGRFLVKVGQFNLSGALGTRGTFNFSHFFQQLGLPGFQDGRALADLAKPLSVGLNSNPASEAPKASKIDVALRKPVVGSFGFEVNLQENQNALQFLSSFLELPEFLLFLQHAISVPEDIARDLGDVMEMVFSSQGCGQAPGSLFVPACTAEGSYEEVQCFAGDCWCVDAQGRELAGSRVRGGRPRCPTECEKQRARMQSLLGSQPAGSSLFVPACTSKGNFLPVQCFNSECYCVDTEGQPIPGTRSALGEPKKCPSPCQLQAERAFLGTVRTLVSNPSTLPALSSIYIPQCSASGQWSPVQCDGPPEQAFEWYERWEAQNSAGQALTPAELLMKIMSYREAASRNFRLFIQNLYEAGQQGIFPGLARYSSFQDVPVSVLEGNQTQPGGNVFLEPYLFWQILNGQLDRYPGPYSDFSAPLAHFDLRSCWCVDEAGQKLEGTRNEPNKVPACPGSCEEVKLRVLQFIREAEEIVTYSNSSRFPLGESFLAAKGIRLTDEELAFPPLSPSRETFLEKFLSGSDYAIRLAAQSTFDFYQRRLVTLAESPRAPSPVWSSAYLPQCDAFGGWEPVQCHAATGHCWCVDGKGEYVPTSLTARSRQIPQCPTSCERLRASGLLSSWKQAGVQAEPSPKDLFIPTCLETGEFARLQASEAGTWCVDPASGEGVPPGTNSSAQCPSLCEVLQSGVPSRRTSPGYSPACRAEDGGFSPVQCDPAQGSCWCVLGSGEEVPGTRVAGSQPACESPQCPLPFSVADVAGGAILCERASGLGAAAGQRCQLRCSQGYRSAFPPEPLLCSVQRRRWESRPPQPRACQRPQFWQTLQTQAQFQLLLPLGKVCSADYSGLLLAFQVFLLDELTARGFCQIQVKTAGTPVSIPVCDDSSVKVECLSRERLGVNITWKLQLVDAPPASLPDLQDVEEALAGKYLAGRFADLIQSGTFQLHLDSKTFSADTSIRFLQGDRFGTSPRTQFGCLEGFGRVVAASDASQDALGCVKCPEGSYFQDEQCIPCPAGFYQEQAGSLACVPCPEGRTTVYAGAFSQTHCVTDCQKNEVGLQCDQDSQYRASQRDRTSGKAFCVDGEGRRLPWTEAEAPLVDAQCLVMRKFEKLPESKVIFSADVAVMVRSEVPGSESSLMQCLADCALDEACGFLTVSTAGSEVSCDFYAWASDSIACTTSGRSEDALGTSQATSFGSLQCQVKVRSREGDPLAVYLKKGQEFTITGQKRFEQTGFQSALSGMYSPVTFSASGASLAEVHLFCLLACDHDSCCDGFILVQVQGGPLLCGLLSSPDVLLCHVRDWRDPAEAQANASCPGVTYDQDSRQVTLRLGGQEIRGLTPLEGTQDTLTSFQQVYLWKDSDMGSRSESMGCRRDTEPRPASPSETDLTTGLFSPVDLIQVIVDGNVSLPSQQHWLFKHLFSLQQANLWCLSRCAGEPSFCQLAEVTDSEPLYFTCTLYPEAQVCDDILESSPKGCRLILPRRPSALYRKKVVLQDRVKNFYNRLPFQKLTGISIRNKVPMSDKSISSGFFECERLCDMDPCCTGFGFLNVSQLKGGEVTCLTLNSLGLQTCSEEYGGVWRILDCGSPDTEVRTYPFGWYQKPVSPSDAPSFCPSVALPALTENVALDSWQSLALSSVIVDPSIRNFDVAHISTAAVGNFSAARDRCLWECSRHQDCLVTTLQTQPGAVRCMFYADTQSCTHSLQAQNCRLLLHEEATYIYRKPNIPLPGFGTSSPSVPIATHGQLLGRSQAIQVGTSWKPVDQFLGVPYAAPPLGEKRFRAPEHLNWTGSWEATKPRARCWQPGIRTPTPPGVSEDCLYLNVFVPQNMAPNASVLVFFHNAAEGKGSGDRPAVDGSFLAAVGNLIVVTASYRTGIFGFLSSGSSELSGNWGLLDQVVALTWVQTHIQAFGGDPRRVTLAADRGGADIASIHLVTTRAANSRLFRRAVLMGGSALSPAAVIRPERARQQAAALAKEVGCPSSSVQEMVSCLRQEPARILNDAQTKLLAVSGPFHYWGPVVDGQYLRETPARVLQRAPRVKVDLLIGSSQDDGLINRAKAVKQFEESQGRTSSKTAFYQALQNSLGGEAADAGVQAAATWYYSLEHDSDDYASFSRALEQATRDYFIICPVIDMASHWARTVRGNVFMYHAPESYSHSSLELLTDVLYAFGLPFYPAYEGQFTLEEKSLSLKIMQYFSNFIRSGNPNYPHEFSRRAPEFAAPWPDFVPRDGAESYKELSVLLPNRQGLKKADCSFWSKYIQSLKASADETKDGPSADSEEEDQPAGSGLTEDLLGLPELASKTYSK
| null | null |
hormone biosynthetic process [GO:0042446]; thyroid hormone generation [GO:0006590]
|
extracellular space [GO:0005615]
|
histone binding [GO:0042393]; hormone activity [GO:0005179]
|
PF00135;PF07699;PF00086;
|
3.40.50.1820;4.10.800.10;2.10.50.10;
|
Type-B carboxylesterase/lipase family
|
PTM: Iodinated on tyrosine residues by TPO (By similarity). There are 4 pairs of iodinated tyrosines used for coupling: acceptor Tyr-24 is coupled to donor Tyr-149 or Tyr-234, acceptor Tyr-2574 is coupled to donor Tyr-2541, acceptor Tyr-2767 in monomer 1 is coupled to donor Tyr-2767 in monomer 2 and acceptor Tyr-1310 in monomer 1 is coupled to donor Tyr-108 in monomer 2 (By similarity). {ECO:0000250|UniProtKB:F1RRV3, ECO:0000250|UniProtKB:P01266}.; PTM: Sulfated tyrosines are desulfated during iodination. {ECO:0000250|UniProtKB:P01266}.; PTM: Undergoes sequential proteolysis by cathepsins to release thyroxine (T4) and triiodothyronine (T3) hormones. In the thyroid follicle lumen, cross-linked TG (storage form) is solubilized by limited proteolysis mediated by cathepsins CTSB and/or CTSL. Partially cleaved TG is further processed by CTSK/cathepsin K and/or CTSL resulting in the release of T4. Following endocytosis, further processing occurs leading to the release of T3 and more T4 hormones. {ECO:0000250|UniProtKB:O08710}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:O08710}. Note=Secreted into the thyroid follicle lumen. Localizes to colloid globules, a structure formed in the thyroid follicle lumen consisting of cross-linked TG arranged in concentric layers. {ECO:0000250|UniProtKB:O08710}.
| null | null | null | null | null |
FUNCTION: Acts as a substrate for the production of iodinated thyroid hormones thyroxine (T4) and triiodothyronine (T3) (By similarity). The synthesis of T3 and T4 involves iodination of selected tyrosine residues of TG/thyroglobulin followed by their oxidative coupling (By similarity). Following TG re-internalization and lysosomal-mediated proteolysis, T3 and T4 are released from the polypeptide backbone leading to their secretion into the bloodstream (By similarity). One dimer produces 7 thyroid hormone molecules (By similarity). {ECO:0000250|UniProtKB:F1RRV3, ECO:0000250|UniProtKB:O08710, ECO:0000250|UniProtKB:P01266}.
|
Bos taurus (Bovine)
|
P01268
|
PTHY_BOVIN
|
MMSAKDMVKVMIVMLAICFLARSDGKSVKKRAVSEIQFMHNLGKHLSSMERVEWLRKKLQDVHNFVALGASIAYRDGSSQRPRKKEDNVLVESHQKSLGEADKADVDVLIKAKPQ
| null | null |
adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; bone mineralization [GO:0030282]; cell-cell signaling [GO:0007267]; homeostasis of number of cells within a tissue [GO:0048873]; intracellular calcium ion homeostasis [GO:0006874]; magnesium ion homeostasis [GO:0010960]; negative regulation of apoptotic process in bone marrow cell [GO:0071866]; negative regulation of gene expression [GO:0010629]; phosphate ion homeostasis [GO:0055062]; positive regulation of bone mineralization [GO:0030501]; positive regulation of cell proliferation in bone marrow [GO:0071864]; positive regulation of glucose import [GO:0046326]; positive regulation of glycogen biosynthetic process [GO:0045725]; positive regulation of inositol phosphate biosynthetic process [GO:0060732]; positive regulation of osteoclast proliferation [GO:0090290]; positive regulation of signal transduction [GO:0009967]; positive regulation of transcription by RNA polymerase II [GO:0045944]; transcription by RNA polymerase II [GO:0006366]
|
extracellular space [GO:0005615]
|
hormone activity [GO:0005179]; parathyroid hormone receptor binding [GO:0031856]; peptide hormone receptor binding [GO:0051428]; type 1 parathyroid hormone receptor binding [GO:0031857]
|
PF01279;
| null |
Parathyroid hormone family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: PTH elevates calcium level by dissolving the salts in bone and preventing their renal excretion. Stimulates [1-14C]-2-deoxy-D-glucose (2DG) transport and glycogen synthesis in osteoblastic cells (By similarity). {ECO:0000250}.
|
Bos taurus (Bovine)
|
P01269
|
PTHY_PIG
|
MMSAKDTVKVMVVMLAICFLARSDGKPIKKRSVSEIQLMHNLGKHLSSLERVEWLRKKLQDVHNFVALGASIVHRDGGSQRPRKKEDNVLVESHQKSLGEADKAAVDVLIKAKPQ
| null | null |
adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; bone mineralization [GO:0030282]; cell-cell signaling [GO:0007267]; homeostasis of number of cells within a tissue [GO:0048873]; intracellular calcium ion homeostasis [GO:0006874]; magnesium ion homeostasis [GO:0010960]; negative regulation of apoptotic process in bone marrow cell [GO:0071866]; negative regulation of gene expression [GO:0010629]; phosphate ion homeostasis [GO:0055062]; positive regulation of bone mineralization [GO:0030501]; positive regulation of cell proliferation in bone marrow [GO:0071864]; positive regulation of glucose import [GO:0046326]; positive regulation of glycogen biosynthetic process [GO:0045725]; positive regulation of inositol phosphate biosynthetic process [GO:0060732]; positive regulation of osteoclast proliferation [GO:0090290]; positive regulation of signal transduction [GO:0009967]; positive regulation of transcription by RNA polymerase II [GO:0045944]; transcription by RNA polymerase II [GO:0006366]
|
extracellular space [GO:0005615]
|
hormone activity [GO:0005179]; parathyroid hormone receptor binding [GO:0031856]; peptide hormone receptor binding [GO:0051428]; type 1 parathyroid hormone receptor binding [GO:0031857]
|
PF01279;
| null |
Parathyroid hormone family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: PTH elevates calcium level by dissolving the salts in bone and preventing their renal excretion. Stimulates [1-14C]-2-deoxy-D-glucose (2DG) transport and glycogen synthesis in osteoblastic cells (By similarity). {ECO:0000250}.
|
Sus scrofa (Pig)
|
P01270
|
PTHY_HUMAN
|
MIPAKDMAKVMIVMLAICFLTKSDGKSVKKRSVSEIQLMHNLGKHLNSMERVEWLRKKLQDVHNFVALGAPLAPRDAGSQRPRKKEDNVLVESHEKSLGEADKADVNVLTKAKSQ
| null | null |
activation of phospholipase C activity [GO:0007202]; adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; bone mineralization [GO:0030282]; bone resorption [GO:0045453]; cAMP metabolic process [GO:0046058]; cell-cell signaling [GO:0007267]; G protein-coupled receptor signaling pathway [GO:0007186]; homeostasis of number of cells within a tissue [GO:0048873]; hormone-mediated apoptotic signaling pathway [GO:0008628]; intracellular calcium ion homeostasis [GO:0006874]; macromolecule biosynthetic process [GO:0009059]; magnesium ion homeostasis [GO:0010960]; negative regulation of apoptotic process in bone marrow cell [GO:0071866]; negative regulation of bone mineralization involved in bone maturation [GO:1900158]; negative regulation of chondrocyte differentiation [GO:0032331]; negative regulation of gene expression [GO:0010629]; phosphate ion homeostasis [GO:0055062]; positive regulation of bone mineralization [GO:0030501]; positive regulation of cell proliferation in bone marrow [GO:0071864]; positive regulation of gene expression [GO:0010628]; positive regulation of glucose import [GO:0046326]; positive regulation of glycogen biosynthetic process [GO:0045725]; positive regulation of inositol phosphate biosynthetic process [GO:0060732]; positive regulation of osteoclast proliferation [GO:0090290]; positive regulation of signal transduction [GO:0009967]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of gene expression [GO:0010468]; response to cadmium ion [GO:0046686]; response to ethanol [GO:0045471]; response to fibroblast growth factor [GO:0071774]; response to lead ion [GO:0010288]; response to parathyroid hormone [GO:0071107]; response to vitamin D [GO:0033280]; response to xenobiotic stimulus [GO:0009410]; Rho protein signal transduction [GO:0007266]; skeletal system development [GO:0001501]; transcription by RNA polymerase II [GO:0006366]
|
extracellular region [GO:0005576]; extracellular space [GO:0005615]
|
hormone activity [GO:0005179]; parathyroid hormone receptor binding [GO:0031856]; peptide hormone receptor binding [GO:0051428]; receptor ligand activity [GO:0048018]; type 1 parathyroid hormone receptor binding [GO:0031857]
|
PF01279;
| null |
Parathyroid hormone family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: PTH elevates calcium level by dissolving the salts in bone and preventing their renal excretion. Stimulates [1-14C]-2-deoxy-D-glucose (2DG) transport and glycogen synthesis in osteoblastic cells. {ECO:0000269|PubMed:21076856}.
|
Homo sapiens (Human)
|
P01272
|
GLUC_BOVIN
|
MKSLYFVAGLFVMLVQGSWQRSLQNTEEKSSSFPAPQTDPLGDPDQINEDKRHSQGTFTSDYSKYLDSRRAQDFVQWLMNTKRNKNNIAKRHDEFERHAEGTFTSDVSSYLEGQAAKEFIAWLVKGRGRRDFPEEVNIVEELRRRHADGSFSDEMNTVLDSLATRDFINWLLQTKITDRK
| null | null |
adenylate cyclase-modulating G protein-coupled receptor signaling pathway [GO:0007188]; glucose homeostasis [GO:0042593]; lactate biosynthetic process [GO:0019249]; lipid biosynthetic process [GO:0008610]; negative regulation of apoptotic process [GO:0043066]; positive regulation of gluconeogenesis [GO:0045722]; positive regulation of insulin secretion involved in cellular response to glucose stimulus [GO:0035774]; protein kinase A signaling [GO:0010737]; regulation of insulin secretion [GO:0050796]; response to activity [GO:0014823]; response to starvation [GO:0042594]
|
extracellular space [GO:0005615]
|
glucagon receptor binding [GO:0031769]; hormone activity [GO:0005179]
|
PF00123;
|
6.10.250.590;
|
Glucagon family
|
PTM: Proglucagon is post-translationally processed in a tissue-specific manner in pancreatic A cells and intestinal L cells. In pancreatic A cells, the major bioactive hormone is glucagon cleaved by PCSK2/PC2. In the intestinal L cells PCSK1/PC1 liberates GLP-1, GLP-2, glicentin and oxyntomodulin. GLP-1 is further N-terminally truncated by post-translational processing in the intestinal L cells resulting in GLP-1(7-37) GLP-1-(7-36)amide. The C-terminal amidation is neither important for the metabolism of GLP-1 nor for its effects on the endocrine pancreas (By similarity). {ECO:0000250}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P01275}.; SUBCELLULAR LOCATION: [Glucagon-like peptide 1]: Secreted {ECO:0000250|UniProtKB:P01275}.
| null | null | null | null | null |
FUNCTION: [Glucagon]: Plays a key role in glucose metabolism and homeostasis. Regulates blood glucose by increasing gluconeogenesis and decreasing glycolysis. A counterregulatory hormone of insulin, raises plasma glucose levels in response to insulin-induced hypoglycemia. Plays an important role in initiating and maintaining hyperglycemic conditions in diabetes. {ECO:0000250|UniProtKB:P55095}.; FUNCTION: [Glucagon-like peptide 1]: Potent stimulator of glucose-dependent insulin release. Also stimulates insulin release in response to IL6. Plays important roles on gastric motility and the suppression of plasma glucagon levels. May be involved in the suppression of satiety and stimulation of glucose disposal in peripheral tissues, independent of the actions of insulin. Has growth-promoting activities on intestinal epithelium. May also regulate the hypothalamic pituitary axis (HPA) via effects on LH, TSH, CRH, oxytocin, and vasopressin secretion. Increases islet mass through stimulation of islet neogenesis and pancreatic beta cell proliferation. Inhibits beta cell apoptosis. {ECO:0000250|UniProtKB:P55095}.; FUNCTION: [Glucagon-like peptide 2]: Stimulates intestinal growth and up-regulates villus height in the small intestine, concomitant with increased crypt cell proliferation and decreased enterocyte apoptosis. The gastrointestinal tract, from the stomach to the colon is the principal target for GLP-2 action. Plays a key role in nutrient homeostasis, enhancing nutrient assimilation through enhanced gastrointestinal function, as well as increasing nutrient disposal. Stimulates intestinal glucose transport and decreases mucosal permeability. {ECO:0000250|UniProtKB:P55095}.; FUNCTION: [Oxyntomodulin]: Significantly reduces food intake. Inhibits gastric emptying in humans. Suppression of gastric emptying may lead to increased gastric distension, which may contribute to satiety by causing a sensation of fullness. {ECO:0000250|UniProtKB:P55095}.; FUNCTION: [Glicentin]: May modulate gastric acid secretion and the gastro-pyloro-duodenal activity. May play an important role in intestinal mucosal growth in the early period of life. {ECO:0000250|UniProtKB:P55095}.
|
Bos taurus (Bovine)
|
P01274
|
GLUC_PIG
|
MKTIYFVAGLFVMLVQGSWQRSLQNTEEKSRSFPAPQTDPLDDPDQMTEDKRHSQGTFTSDYSKYLDSRRAQDFVQWLMNTKRNKNNIAKRHDEFERHAEGTFTSDVSSYLEGQAAKEFIAWLVKGRGRRDFPEEVTIVEELRRRHADGSFSDEMNTVLDNLATRDFINWLLHTKITDSL
| null | null |
adenylate cyclase-modulating G protein-coupled receptor signaling pathway [GO:0007188]; glucose homeostasis [GO:0042593]; negative regulation of apoptotic process [GO:0043066]; positive regulation of insulin secretion involved in cellular response to glucose stimulus [GO:0035774]; protein kinase A signaling [GO:0010737]; regulation of insulin secretion [GO:0050796]; response to activity [GO:0014823]; response to starvation [GO:0042594]
|
extracellular space [GO:0005615]
|
glucagon receptor binding [GO:0031769]; hormone activity [GO:0005179]
|
PF00123;
|
6.10.250.590;
|
Glucagon family
|
PTM: Proglucagon is post-translationally processed in a tissue-specific manner in pancreatic A cells and intestinal L cells. In pancreatic A cells, the major bioactive hormone is glucagon cleaved by PCSK2/PC2. In the intestinal L cells PCSK1/PC1 liberates GLP-1, GLP-2, glicentin and oxyntomodulin. GLP-1 is further N-terminally truncated by post-translational processing in the intestinal L cells resulting in GLP-1(7-37) GLP-1-(7-36)amide. The C-terminal amidation is neither important for the metabolism of GLP-1 nor for its effects on the endocrine pancreas (By similarity). {ECO:0000250}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P01275}.; SUBCELLULAR LOCATION: [Glucagon-like peptide 1]: Secreted {ECO:0000250|UniProtKB:P01275}.
| null | null | null | null | null |
FUNCTION: [Glucagon]: Plays a key role in glucose metabolism and homeostasis. Regulates blood glucose by increasing gluconeogenesis and decreasing glycolysis. A counterregulatory hormone of insulin, raises plasma glucose levels in response to insulin-induced hypoglycemia. Plays an important role in initiating and maintaining hyperglycemic conditions in diabetes. {ECO:0000250|UniProtKB:P55095}.; FUNCTION: [Glucagon-like peptide 1]: Potent stimulator of glucose-dependent insulin release. Also stimulates insulin release in response to IL6. Plays important roles on gastric motility and the suppression of plasma glucagon levels. May be involved in the suppression of satiety and stimulation of glucose disposal in peripheral tissues, independent of the actions of insulin. Has growth-promoting activities on intestinal epithelium. May also regulate the hypothalamic pituitary axis (HPA) via effects on LH, TSH, CRH, oxytocin, and vasopressin secretion. Increases islet mass through stimulation of islet neogenesis and pancreatic beta cell proliferation. Inhibits beta cell apoptosis. {ECO:0000250|UniProtKB:P55095}.; FUNCTION: [Glucagon-like peptide 2]: Stimulates intestinal growth and up-regulates villus height in the small intestine, concomitant with increased crypt cell proliferation and decreased enterocyte apoptosis. The gastrointestinal tract, from the stomach to the colon is the principal target for GLP-2 action. Plays a key role in nutrient homeostasis, enhancing nutrient assimilation through enhanced gastrointestinal function, as well as increasing nutrient disposal. Stimulates intestinal glucose transport and decreases mucosal permeability. {ECO:0000250|UniProtKB:P55095}.; FUNCTION: [Oxyntomodulin]: Significantly reduces food intake. Inhibits gastric emptying in humans. Suppression of gastric emptying may lead to increased gastric distension, which may contribute to satiety by causing a sensation of fullness. {ECO:0000250|UniProtKB:P55095}.; FUNCTION: [Glicentin]: May modulate gastric acid secretion and the gastro-pyloro-duodenal activity. May play an important role in intestinal mucosal growth in the early period of life. {ECO:0000250|UniProtKB:P55095}.
|
Sus scrofa (Pig)
|
P01275
|
GLUC_HUMAN
|
MKSIYFVAGLFVMLVQGSWQRSLQDTEEKSRSFSASQADPLSDPDQMNEDKRHSQGTFTSDYSKYLDSRRAQDFVQWLMNTKRNRNNIAKRHDEFERHAEGTFTSDVSSYLEGQAAKEFIAWLVKGRGRRDFPEEVAIVEELGRRHADGSFSDEMNTILDNLAARDFINWLIQTKITDRK
| null | null |
adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; adenylate cyclase-modulating G protein-coupled receptor signaling pathway [GO:0007188]; cellular response to glucagon stimulus [GO:0071377]; feeding behavior [GO:0007631]; G protein-coupled receptor signaling pathway [GO:0007186]; gluconeogenesis [GO:0006094]; glucose homeostasis [GO:0042593]; negative regulation of apoptotic process [GO:0043066]; negative regulation of execution phase of apoptosis [GO:1900118]; positive regulation of calcium ion import [GO:0090280]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of gluconeogenesis [GO:0045722]; positive regulation of insulin secretion involved in cellular response to glucose stimulus [GO:0035774]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; positive regulation of peptidyl-threonine phosphorylation [GO:0010800]; protein kinase A signaling [GO:0010737]; regulation of insulin secretion [GO:0050796]; response to activity [GO:0014823]; response to starvation [GO:0042594]
|
endoplasmic reticulum lumen [GO:0005788]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]; secretory granule lumen [GO:0034774]
|
glucagon receptor binding [GO:0031769]; hormone activity [GO:0005179]; identical protein binding [GO:0042802]; signaling receptor binding [GO:0005102]
|
PF00123;
|
6.10.250.590;
|
Glucagon family
|
PTM: Proglucagon is post-translationally processed in a tissue-specific manner in pancreatic A cells and intestinal L cells. In pancreatic A cells, the major bioactive hormone is glucagon cleaved by PCSK2/PC2. In the intestinal L cells PCSK1/PC1 liberates GLP-1, GLP-2, glicentin and oxyntomodulin. GLP-1 is further N-terminally truncated by post-translational processing in the intestinal L cells resulting in GLP-1(7-37) GLP-1-(7-36)amide. The C-terminal amidation is neither important for the metabolism of GLP-1 nor for its effects on the endocrine pancreas. {ECO:0000269|PubMed:12651102, ECO:0000269|PubMed:2753890, ECO:0000269|PubMed:9287128}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000305}.; SUBCELLULAR LOCATION: [Glucagon-like peptide 1]: Secreted {ECO:0000269|PubMed:22037645}.
| null | null | null | null | null |
FUNCTION: [Glucagon]: Plays a key role in glucose metabolism and homeostasis. Regulates blood glucose by increasing gluconeogenesis and decreasing glycolysis. A counterregulatory hormone of insulin, raises plasma glucose levels in response to insulin-induced hypoglycemia. Plays an important role in initiating and maintaining hyperglycemic conditions in diabetes. {ECO:0000305|PubMed:10605628, ECO:0000305|PubMed:12626323}.; FUNCTION: [Glucagon-like peptide 1]: Potent stimulator of glucose-dependent insulin release. Also stimulates insulin release in response to IL6 (PubMed:22037645). Plays important roles on gastric motility and the suppression of plasma glucagon levels. May be involved in the suppression of satiety and stimulation of glucose disposal in peripheral tissues, independent of the actions of insulin. Has growth-promoting activities on intestinal epithelium. May also regulate the hypothalamic pituitary axis (HPA) via effects on LH, TSH, CRH, oxytocin, and vasopressin secretion. Increases islet mass through stimulation of islet neogenesis and pancreatic beta cell proliferation. Inhibits beta cell apoptosis (Probable). {ECO:0000269|PubMed:22037645, ECO:0000305|PubMed:10605628, ECO:0000305|PubMed:12554744, ECO:0000305|PubMed:14719035}.; FUNCTION: [Glucagon-like peptide 2]: Stimulates intestinal growth and up-regulates villus height in the small intestine, concomitant with increased crypt cell proliferation and decreased enterocyte apoptosis. The gastrointestinal tract, from the stomach to the colon is the principal target for GLP-2 action. Plays a key role in nutrient homeostasis, enhancing nutrient assimilation through enhanced gastrointestinal function, as well as increasing nutrient disposal. Stimulates intestinal glucose transport and decreases mucosal permeability. {ECO:0000305|PubMed:10322410, ECO:0000305|PubMed:10605628, ECO:0000305|PubMed:12554744, ECO:0000305|PubMed:14719035}.; FUNCTION: [Oxyntomodulin]: Significantly reduces food intake. Inhibits gastric emptying in humans. Suppression of gastric emptying may lead to increased gastric distension, which may contribute to satiety by causing a sensation of fullness. {ECO:0000305|PubMed:10605628, ECO:0000305|PubMed:12554744}.; FUNCTION: [Glicentin]: May modulate gastric acid secretion and the gastro-pyloro-duodenal activity. May play an important role in intestinal mucosal growth in the early period of life. {ECO:0000305|PubMed:10605628, ECO:0000305|PubMed:12554744}.
|
Homo sapiens (Human)
|
P01282
|
VIP_HUMAN
|
MDTRNKAQLLVLLTLLSVLFSQTSAWPLYRAPSALRLGDRIPFEGANEPDQVSLKEDIDMLQNALAENDTPYYDVSRNARHADGVFTSDFSKLLGQLSAKKYLESLMGKRVSSNISEDPVPVKRHSDAVFTDNYTRLRKQMAVKKYLNSILNGKRSSEGESPDFPEELEK
| null | null |
adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; body fluid secretion [GO:0007589]; epinephrine secretion [GO:0048242]; G protein-coupled receptor signaling pathway [GO:0007186]; learning or memory [GO:0007611]; mRNA stabilization [GO:0048255]; negative regulation of apoptotic process [GO:0043066]; negative regulation of potassium ion transport [GO:0043267]; negative regulation of smooth muscle cell proliferation [GO:0048662]; phospholipase C-activating G protein-coupled receptor signaling pathway [GO:0007200]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of endothelial cell proliferation [GO:0001938]; positive regulation of epinephrine secretion [GO:0032812]; positive regulation of penile erection [GO:0060406]; positive regulation of protein catabolic process [GO:0045732]; prolactin secretion [GO:0070459]; regulation of protein localization [GO:0032880]
|
extracellular region [GO:0005576]; neuron projection [GO:0043005]
|
hormone activity [GO:0005179]; neuropeptide hormone activity [GO:0005184]; peptide hormone receptor binding [GO:0051428]
|
PF00123;
|
6.10.250.590;
|
Glucagon family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: VIP causes vasodilation, lowers arterial blood pressure, stimulates myocardial contractility, increases glycogenolysis and relaxes the smooth muscle of trachea, stomach and gall bladder. {ECO:0000269|PubMed:15013843}.; FUNCTION: PHM and PHV also cause vasodilation. PHM-27 is a potent agonist of the calcitonin receptor CALCR, with similar efficacy as calcitonin. {ECO:0000269|PubMed:15013843}.
|
Homo sapiens (Human)
|
P01283
|
VIP_RAT
|
MESRSKPQFLAILTLFSVLFSQSLAWPLYGPPSSVRLDDRLQFEGAGDPDQVSLKADSDILQNALAENDTPYYDVSRNARHADGVFTSDYSRLLGQISAKKYLESLIGKRISSSISEDPVPVKRHSDAVFTDNYTRLRKQMAVKKYLNSILNGKRSSEGDSPDFLEELEK
| null | null |
adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; epinephrine secretion [GO:0048242]; learning or memory [GO:0007611]; mRNA stabilization [GO:0048255]; negative regulation of apoptotic process [GO:0043066]; negative regulation of potassium ion transport [GO:0043267]; negative regulation of smooth muscle cell proliferation [GO:0048662]; phospholipase C-activating G protein-coupled receptor signaling pathway [GO:0007200]; positive regulation of endothelial cell proliferation [GO:0001938]; positive regulation of epinephrine secretion [GO:0032812]; positive regulation of penile erection [GO:0060406]; positive regulation of protein catabolic process [GO:0045732]; prolactin secretion [GO:0070459]; regulation of protein localization [GO:0032880]; regulation of signal transduction [GO:0009966]
|
extracellular region [GO:0005576]; neuron projection [GO:0043005]; neuronal cell body [GO:0043025]
|
hormone activity [GO:0005179]; neuropeptide hormone activity [GO:0005184]; peptide hormone receptor binding [GO:0051428]; signaling receptor binding [GO:0005102]
|
PF00123;
|
6.10.250.590;
|
Glucagon family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: VIP causes vasodilation, lowers arterial blood pressure, stimulates myocardial contractility, increases glycogenolysis and relaxes the smooth muscle of trachea, stomach and gall bladder.; FUNCTION: PHM-27 is a potent agonist of the calcitonin receptor CALCR, with similar efficacy as calcitonin (By similarity). PHI also causes vasodilation. {ECO:0000250}.
|
Rattus norvegicus (Rat)
|
P01284
|
VIP_PIG
|
HADGVFTSDFSRLLGQLSAKKYLESLIXXXXXXXXXXXXXXXXXHSDAVFTDNYTRLRKQMAVKKYLNSILNGKR
| null | null |
adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; epinephrine secretion [GO:0048242]; learning or memory [GO:0007611]; mRNA stabilization [GO:0048255]; negative regulation of apoptotic process [GO:0043066]; negative regulation of potassium ion transport [GO:0043267]; negative regulation of smooth muscle cell proliferation [GO:0048662]; phospholipase C-activating G protein-coupled receptor signaling pathway [GO:0007200]; positive regulation of endothelial cell proliferation [GO:0001938]; positive regulation of epinephrine secretion [GO:0032812]; positive regulation of penile erection [GO:0060406]; positive regulation of protein catabolic process [GO:0045732]; prolactin secretion [GO:0070459]; regulation of protein localization [GO:0032880]
|
extracellular region [GO:0005576]; neuron projection [GO:0043005]
|
hormone activity [GO:0005179]; neuropeptide hormone activity [GO:0005184]; peptide hormone receptor binding [GO:0051428]
|
PF00123;
|
6.10.250.590;
|
Glucagon family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: VIP causes vasodilation, lowers arterial blood pressure, stimulates myocardial contractility, increases glycogenolysis and relaxes the smooth muscle of trachea, stomach and gall bladder.; FUNCTION: PHM-27 is a potent agonist of the calcitonin receptor CALCR, with similar efficacy as calcitonin (By similarity). PHI also causes vasodilation. {ECO:0000250}.
|
Sus scrofa (Pig)
|
P01286
|
SLIB_HUMAN
|
MPLWVFFFVILTLSNSSHCSPPPPLTLRMRRYADAIFTNSYRKVLGQLSARKLLQDIMSRQQGESNQERGARARLGRQVDSMWAEQKQMELESILVALLQKHSRNSQG
| null | null |
adenohypophysis development [GO:0021984]; adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; cell-cell signaling [GO:0007267]; growth hormone secretion [GO:0030252]; multicellular organism growth [GO:0035264]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of circadian sleep/wake cycle, REM sleep [GO:0046005]; positive regulation of growth hormone secretion [GO:0060124]; positive regulation of insulin-like growth factor receptor signaling pathway [GO:0043568]; positive regulation of multicellular organism growth [GO:0040018]; response to food [GO:0032094]
|
extracellular region [GO:0005576]; extracellular space [GO:0005615]; perikaryon [GO:0043204]; terminal bouton [GO:0043195]
|
growth hormone-releasing hormone activity [GO:0016608]; growth hormone-releasing hormone receptor binding [GO:0031770]; neuropeptide hormone activity [GO:0005184]; peptide hormone receptor binding [GO:0051428]
|
PF00123;
| null |
Glucagon family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: GRF is released by the hypothalamus and acts on the adenohypophyse to stimulate the secretion of growth hormone.
|
Homo sapiens (Human)
|
P01289
|
TKN1_BOVIN
|
MKILVAVAVIFFISTQLSAEEIGANDDFNYWSDWSDSDQIKEEMPEPFEHLLQRIARRPKPQQFFGLMGKRDADSSIEKQVALLKALYGHGQLSHKRHKTDSFVGLMGKRALNSVAYERSVMQDYERRRK
| null | null |
chemical synaptic transmission [GO:0007268]; inflammatory response [GO:0006954]; neuropeptide signaling pathway [GO:0007218]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; response to pain [GO:0048265]; sensory perception of pain [GO:0019233]; tachykinin receptor signaling pathway [GO:0007217]
|
axon [GO:0030424]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; neuronal cell body [GO:0043025]; synapse [GO:0045202]
|
substance P receptor binding [GO:0031835]
|
PF02202;
| null |
Tachykinin family
|
PTM: [Substance P]: The substance P form is cleaved at Pro-59 by the prolyl endopeptidase FAP (seprase) activity (in vitro). Substance P is also cleaved and degraded by Angiotensin-converting enzyme (ACE) and neprilysin (MME). {ECO:0000250|UniProtKB:P20366}.
|
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Tachykinins are active peptides which excite neurons, evoke behavioral responses, are potent vasodilators and secretagogues, and contract (directly or indirectly) many smooth muscles.
|
Bos taurus (Bovine)
|
P01297
|
NMB_PIG
|
MTLRARGARLLGGLLFFTLLAAGAAPLSWDLPEPRSRAGKIRVHPRGNLWATGHFMGKKSLEPPNPSLLGTTHHISLRDQRLQLSHDLLRILLQKKALGLSLSGPASHTPYRRLLVQTLEK
| null | null |
antiviral innate immune response [GO:0140374]; Leydig cell proliferation [GO:0160024]; negative regulation of interleukin-6 production [GO:0032715]; neuropeptide signaling pathway [GO:0007218]; positive regulation of interferon-alpha production [GO:0032727]; positive regulation of osteoclast proliferation [GO:0090290]; positive regulation of respiratory gaseous exchange [GO:1903942]; positive regulation of testosterone secretion [GO:2000845]; sensory perception of itch [GO:0160025]; sneeze reflex [GO:0160023]
|
extracellular space [GO:0005615]; neuron projection [GO:0043005]
|
neuromedin B receptor binding [GO:0031710]; neuropeptide hormone activity [GO:0005184]
|
PF02044;
| null |
Bombesin/neuromedin-B/ranatensin family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q9CR53}. Cell projection, neuron projection {ECO:0000250|UniProtKB:Q9CR53}. Note=In neurons of the retrotrapezoid nucleus//parafacial respiratory group, expressed on neuron projections which project into the pre-Botzinger complex. {ECO:0000250|UniProtKB:Q9CR53}.
| null | null | null | null | null |
FUNCTION: Stimulates smooth muscle contraction (PubMed:6882442). Induces sighing by acting directly on the pre-Botzinger complex, a cluster of several thousand neurons in the ventrolateral medulla responsible for inspiration during respiratory activity (By similarity). Contributes to the induction of sneezing following exposure to chemical irritants or allergens which causes release of NMB by nasal sensory neurons and activation of NMBR-expressing neurons in the sneeze-evoking region of the brainstem (By similarity). These in turn activate neurons of the caudal ventral respiratory group, giving rise to the sneezing response (By similarity). Contributes to induction of acute itch, possibly through activation of the NMBR receptor on dorsal root ganglion neurons (By similarity). Increases expression of NMBR and steroidogenic mediators STAR, CYP11A1 and HSD3B1 in Leydig cells, induces secretion of testosterone by Leydig cells and also promotes Leydig cell proliferation (PubMed:29632025). Plays a role in the innate immune response to influenza A virus infection by enhancing interferon alpha expression and reducing expression of IL6 (By similarity). Plays a role in CSF1-induced proliferation of osteoclast precursors by contributing to positive regulation of the expression of the CSF1 receptor CSF1R (By similarity). {ECO:0000250|UniProtKB:Q9CR53, ECO:0000269|PubMed:29632025, ECO:0000269|PubMed:6882442}.
|
Sus scrofa (Pig)
|
P01298
|
PAHO_HUMAN
|
MAAARLCLSLLLLSTCVALLLQPLLGAQGAPLEPVYPGDNATPEQMAQYAADLRRYINMLTRPRYGKRHKEDTLAFSEWGSPHAAVPRELSPLDL
| null | null |
feeding behavior [GO:0007631]; neuropeptide signaling pathway [GO:0007218]; protein secretion [GO:0009306]
|
cytoplasm [GO:0005737]; extracellular region [GO:0005576]; extracellular space [GO:0005615]
|
G protein-coupled receptor binding [GO:0001664]; hormone activity [GO:0005179]; neuropeptide hormone activity [GO:0005184]; neuropeptide Y receptor binding [GO:0031841]
|
PF00159;
|
6.10.250.900;
|
NPY family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:7493937, ECO:0000269|PubMed:7592911, ECO:0000269|PubMed:828120}.
| null | null | null | null | null |
FUNCTION: [Pancreatic polypeptide]: Hormone secreted by pancreatic cells that acts as a regulator of pancreatic and gastrointestinal functions probably by signaling through the G protein-coupled receptor NPY4R2. {ECO:0000269|PubMed:7493937, ECO:0000269|PubMed:7592911}.
|
Homo sapiens (Human)
|
P01303
|
NPY_HUMAN
|
MLGNKRLGLSGLTLALSLLVCLGALAEAYPSKPDNPGEDAPAEDMARYYSALRHYINLITRQRYGKRSSPETLISDLLMRESTENVPRTRLEDPAMW
| null | null |
adult feeding behavior [GO:0008343]; central nervous system neuron development [GO:0021954]; cerebral cortex development [GO:0021987]; chemical synaptic transmission [GO:0007268]; feeding behavior [GO:0007631]; G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger [GO:0007187]; intestinal epithelial cell differentiation [GO:0060575]; neuron projection development [GO:0031175]; neuropeptide signaling pathway [GO:0007218]; positive regulation of appetite [GO:0032100]; regulation of blood pressure [GO:0008217]; synaptic signaling via neuropeptide [GO:0099538]
|
extracellular region [GO:0005576]; extracellular space [GO:0005615]; GABA-ergic synapse [GO:0098982]; Golgi apparatus [GO:0005794]; neuronal dense core vesicle [GO:0098992]
|
calcium channel regulator activity [GO:0005246]; G protein-coupled receptor activity [GO:0004930]; neuropeptide hormone activity [GO:0005184]; neuropeptide Y receptor binding [GO:0031841]; signaling receptor binding [GO:0005102]
|
PF00159;
|
6.10.250.900;
|
NPY family
|
PTM: The neuropeptide Y form is cleaved at Pro-30 by the prolyl endopeptidase FAP (seprase) activity (in vitro). {ECO:0000269|PubMed:21314817}.
|
SUBCELLULAR LOCATION: Secreted. Cytoplasmic vesicle, secretory vesicle, neuronal dense core vesicle {ECO:0000250|UniProtKB:P07808}.
| null | null | null | null | null |
FUNCTION: NPY is implicated in the control of feeding and in secretion of gonadotrophin-release hormone.
|
Homo sapiens (Human)
|
P01308
|
INS_HUMAN
|
MALWMRLLPLLALLALWGPDPAAAFVNQHLCGSHLVEALYLVCGERGFFYTPKTRREAEDLQVGQVELGGGPGAGSLQPLALEGSLQKRGIVEQCCTSICSLYQLENYCN
| null | null |
activation of protein kinase B activity [GO:0032148]; acute-phase response [GO:0006953]; alpha-beta T cell activation [GO:0046631]; cell-cell signaling [GO:0007267]; cognition [GO:0050890]; fatty acid homeostasis [GO:0055089]; G protein-coupled receptor signaling pathway [GO:0007186]; glucose homeostasis [GO:0042593]; glucose metabolic process [GO:0006006]; insulin receptor signaling pathway [GO:0008286]; negative regulation of acute inflammatory response [GO:0002674]; negative regulation of fatty acid metabolic process [GO:0045922]; negative regulation of feeding behavior [GO:2000252]; negative regulation of gene expression [GO:0010629]; negative regulation of gluconeogenesis [GO:0045721]; negative regulation of glycogen catabolic process [GO:0045818]; negative regulation of lipid catabolic process [GO:0050995]; negative regulation of NAD(P)H oxidase activity [GO:0033861]; negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway [GO:1902176]; negative regulation of protein catabolic process [GO:0042177]; negative regulation of protein secretion [GO:0050709]; negative regulation of proteolysis [GO:0045861]; negative regulation of reactive oxygen species biosynthetic process [GO:1903427]; negative regulation of respiratory burst involved in inflammatory response [GO:0060266]; neuron projection maintenance [GO:1990535]; nitric oxide-cGMP-mediated signaling pathway [GO:0038060]; positive regulation of brown fat cell differentiation [GO:0090336]; positive regulation of cell differentiation [GO:0045597]; positive regulation of cell growth [GO:0030307]; positive regulation of cell migration [GO:0030335]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of cytokine production [GO:0001819]; positive regulation of dendritic spine maintenance [GO:1902952]; positive regulation of gene expression [GO:0010628]; positive regulation of glucose import [GO:0046326]; positive regulation of glycogen biosynthetic process [GO:0045725]; positive regulation of glycolytic process [GO:0045821]; positive regulation of insulin receptor signaling pathway [GO:0046628]; positive regulation of lipid biosynthetic process [GO:0046889]; positive regulation of long-term synaptic potentiation [GO:1900273]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of mitotic nuclear division [GO:0045840]; positive regulation of neuron projection development [GO:0010976]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of nitric oxide mediated signal transduction [GO:0010750]; positive regulation of nitric-oxide synthase activity [GO:0051000]; positive regulation of peptide hormone secretion [GO:0090277]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of protein autophosphorylation [GO:0031954]; positive regulation of protein localization to nucleus [GO:1900182]; positive regulation of protein metabolic process [GO:0051247]; positive regulation of protein secretion [GO:0050714]; positive regulation of respiratory burst [GO:0060267]; regulation of cellular amino acid metabolic process [GO:0006521]; regulation of DNA-templated transcription [GO:0006355]; regulation of protein localization [GO:0032880]; regulation of protein localization to plasma membrane [GO:1903076]; regulation of protein secretion [GO:0050708]; regulation of synaptic plasticity [GO:0048167]; regulation of transmembrane transporter activity [GO:0022898]; vasodilation [GO:0042311]; wound healing [GO:0042060]
|
endoplasmic reticulum lumen [GO:0005788]; endoplasmic reticulum-Golgi intermediate compartment membrane [GO:0033116]; endosome lumen [GO:0031904]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; Golgi lumen [GO:0005796]; Golgi membrane [GO:0000139]; secretory granule lumen [GO:0034774]; transport vesicle [GO:0030133]
|
hormone activity [GO:0005179]; identical protein binding [GO:0042802]; insulin receptor binding [GO:0005158]; insulin-like growth factor receptor binding [GO:0005159]; protease binding [GO:0002020]
|
PF00049;
|
1.10.100.10;
|
Insulin family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Insulin decreases blood glucose concentration. It increases cell permeability to monosaccharides, amino acids and fatty acids. It accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver.
|
Homo sapiens (Human)
|
P01315
|
INS_PIG
|
MALWTRLLPLLALLALWAPAPAQAFVNQHLCGSHLVEALYLVCGERGFFYTPKARREAENPQAGAVELGGGLGGLQALALEGPPQKRGIVEQCCTSICSLYQLENYCN
| null | null |
glucose homeostasis [GO:0042593]; glucose metabolic process [GO:0006006]; glycoprotein biosynthetic process [GO:0009101]; insulin receptor signaling pathway [GO:0008286]; lactate biosynthetic process [GO:0019249]; lipid biosynthetic process [GO:0008610]; lipoprotein biosynthetic process [GO:0042158]; negative regulation of gluconeogenesis [GO:0045721]; positive regulation of cell migration [GO:0030335]; positive regulation of DNA replication [GO:0045740]; positive regulation of fatty acid biosynthetic process [GO:0045723]; positive regulation of glucose metabolic process [GO:0010907]; positive regulation of insulin receptor signaling pathway [GO:0046628]; positive regulation of lipoprotein lipase activity [GO:0051006]; positive regulation of protein autophosphorylation [GO:0031954]; positive regulation of protein secretion [GO:0050714]; response to L-arginine [GO:1903576]
|
extracellular space [GO:0005615]
|
hormone activity [GO:0005179]; identical protein binding [GO:0042802]; insulin receptor binding [GO:0005158]; insulin-like growth factor receptor binding [GO:0005159]
|
PF00049;
|
1.10.100.10;
|
Insulin family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Insulin decreases blood glucose concentration. It increases cell permeability to monosaccharides, amino acids and fatty acids. It accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver.
|
Sus scrofa (Pig)
|
P01317
|
INS_BOVIN
|
MALWTRLRPLLALLALWPPPPARAFVNQHLCGSHLVEALYLVCGERGFFYTPKARREVEGPQVGALELAGGPGAGGLEGPPQKRGIVEQCCASVCSLYQLENYCN
| null | null |
estradiol secretion [GO:0035938]; feeding behavior [GO:0007631]; glucose homeostasis [GO:0042593]; glucose import in response to insulin stimulus [GO:0044381]; glucose metabolic process [GO:0006006]; negative regulation of apoptotic process [GO:0043066]; negative regulation of appetite [GO:0032099]; negative regulation of lactation [GO:1903488]; negative regulation of lipid catabolic process [GO:0050995]; positive regulation of blood circulation [GO:1903524]; positive regulation of cell maturation [GO:1903431]; positive regulation of gene expression [GO:0010628]; positive regulation of insulin secretion [GO:0032024]; positive regulation of lactation [GO:1903489]; positive regulation of mammary gland epithelial cell proliferation [GO:0033601]; positive regulation of peptide hormone secretion [GO:0090277]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of protein secretion [GO:0050714]; positive regulation of Rho protein signal transduction [GO:0035025]; protein secretion [GO:0009306]; response to butyrate [GO:1903544]; response to food [GO:0032094]; response to glucose [GO:0009749]; response to growth hormone [GO:0060416]; response to heat [GO:0009408]; response to L-arginine [GO:1903576]; response to nutrient levels [GO:0031667]
|
extracellular space [GO:0005615]
|
hormone activity [GO:0005179]; identical protein binding [GO:0042802]; insulin receptor binding [GO:0005158]
|
PF00049;
|
1.10.100.10;
|
Insulin family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Insulin decreases blood glucose concentration. It increases cell permeability to monosaccharides, amino acids and fatty acids. It accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver.
|
Bos taurus (Bovine)
|
P01322
|
INS1_RAT
|
MALWMRFLPLLALLVLWEPKPAQAFVKQHLCGPHLVEALYLVCGERGFFYTPKSRREVEDPQVPQLELGGGPEAGDLQTLALEVARQKRGIVDQCCTSICSLYQLENYCN
| null | null |
cellular response to glucose stimulus [GO:0071333]; cellular response to oxygen-containing compound [GO:1901701]; glucose homeostasis [GO:0042593]; glucose metabolic process [GO:0006006]; insulin receptor signaling pathway [GO:0008286]; positive regulation of protein secretion [GO:0050714]; receptor internalization [GO:0031623]; response to cAMP [GO:0051591]; response to cytokine [GO:0034097]; response to organic substance [GO:0010033]; response to peptide hormone [GO:0043434]
|
cytosol [GO:0005829]; extracellular space [GO:0005615]
|
hormone activity [GO:0005179]; insulin receptor binding [GO:0005158]
|
PF00049;
|
1.10.100.10;
|
Insulin family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Insulin decreases blood glucose concentration. It increases cell permeability to monosaccharides, amino acids and fatty acids. It accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver.
|
Rattus norvegicus (Rat)
|
P01323
|
INS2_RAT
|
MALWIRFLPLLALLILWEPRPAQAFVKQHLCGSHLVEALYLVCGERGFFYTPMSRREVEDPQVAQLELGGGPGAGDLQTLALEVARQKRGIVDQCCTSICSLYQLENYCN
| null | null |
acute-phase response [GO:0006953]; alpha-beta T cell activation [GO:0046631]; ER overload response [GO:0006983]; fatty acid homeostasis [GO:0055089]; G protein-coupled receptor signaling pathway [GO:0007186]; glucose homeostasis [GO:0042593]; glucose metabolic process [GO:0006006]; insulin processing [GO:0030070]; insulin receptor signaling pathway [GO:0008286]; intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress [GO:0070059]; lipid catabolic process [GO:0016042]; myoblast fusion [GO:0007520]; myotube differentiation [GO:0014902]; negative regulation of acute inflammatory response [GO:0002674]; negative regulation of fatty acid metabolic process [GO:0045922]; negative regulation of feeding behavior [GO:2000252]; negative regulation of gene expression [GO:0010629]; negative regulation of glycogen catabolic process [GO:0045818]; negative regulation of lipid catabolic process [GO:0050995]; negative regulation of protein catabolic process [GO:0042177]; negative regulation of protein secretion [GO:0050709]; negative regulation of proteolysis [GO:0045861]; negative regulation of reactive oxygen species biosynthetic process [GO:1903427]; negative regulation of respiratory burst involved in inflammatory response [GO:0060266]; negative regulation of transcription by RNA polymerase II [GO:0000122]; neuron projection maintenance [GO:1990535]; nitric oxide-cGMP-mediated signaling pathway [GO:0038060]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of cytokine production [GO:0001819]; positive regulation of dendritic spine maintenance [GO:1902952]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of gene expression [GO:0010628]; positive regulation of glucose import [GO:0046326]; positive regulation of glycogen biosynthetic process [GO:0045725]; positive regulation of glycolytic process [GO:0045821]; positive regulation of insulin receptor signaling pathway [GO:0046628]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of mitotic nuclear division [GO:0045840]; positive regulation of nitric oxide mediated signal transduction [GO:0010750]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of protein localization to nucleus [GO:1900182]; positive regulation of protein metabolic process [GO:0051247]; positive regulation of protein secretion [GO:0050714]; positive regulation of respiratory burst [GO:0060267]; receptor internalization [GO:0031623]; regulation of cellular amino acid metabolic process [GO:0006521]; regulation of gene expression [GO:0010468]; regulation of phosphorylation [GO:0042325]; regulation of protein localization [GO:0032880]; regulation of protein localization to plasma membrane [GO:1903076]; regulation of protein secretion [GO:0050708]; vasodilation [GO:0042311]; wound healing [GO:0042060]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular space [GO:0005615]; nucleus [GO:0005634]; secretory granule [GO:0030141]; sno(s)RNA-containing ribonucleoprotein complex [GO:0005732]
|
hormone activity [GO:0005179]; identical protein binding [GO:0042802]; insulin receptor binding [GO:0005158]; insulin-like growth factor receptor binding [GO:0005159]; protease binding [GO:0002020]; zinc ion binding [GO:0008270]
|
PF00049;
|
1.10.100.10;
|
Insulin family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Insulin decreases blood glucose concentration. It increases cell permeability to monosaccharides, amino acids and fatty acids. It accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver.
|
Rattus norvegicus (Rat)
|
P01325
|
INS1_MOUSE
|
MALLVHFLPLLALLALWEPKPTQAFVKQHLCGPHLVEALYLVCGERGFFYTPKSRREVEDPQVEQLELGGSPGDLQTLALEVARQKRGIVDQCCTSICSLYQLENYCN
| null | null |
cellular response to glucose stimulus [GO:0071333]; glucose homeostasis [GO:0042593]; glucose metabolic process [GO:0006006]; glucose transmembrane transport [GO:1904659]; insulin receptor signaling pathway [GO:0008286]; positive regulation of protein secretion [GO:0050714]; receptor internalization [GO:0031623]; response to cAMP [GO:0051591]; response to cytokine [GO:0034097]
|
collagen-containing extracellular matrix [GO:0062023]; cytosol [GO:0005829]; endoplasmic reticulum lumen [GO:0005788]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; secretory granule lumen [GO:0034774]
|
hormone activity [GO:0005179]; insulin receptor binding [GO:0005158]; receptor ligand activity [GO:0048018]; transmembrane receptor protein tyrosine kinase activator activity [GO:0030297]
|
PF00049;
|
1.10.100.10;
|
Insulin family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Insulin decreases blood glucose concentration. It increases cell permeability to monosaccharides, amino acids and fatty acids. It accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver.
|
Mus musculus (Mouse)
|
P01326
|
INS2_MOUSE
|
MALWMRFLPLLALLFLWESHPTQAFVKQHLCGSHLVEALYLVCGERGFFYTPMSRREVEDPQVAQLELGGGPGAGDLQTLALEVAQQKRGIVDQCCTSICSLYQLENYCN
| null | null |
ER overload response [GO:0006983]; glucose homeostasis [GO:0042593]; glucose metabolic process [GO:0006006]; glucose transmembrane transport [GO:1904659]; insulin processing [GO:0030070]; insulin receptor signaling pathway [GO:0008286]; intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress [GO:0070059]; lipid catabolic process [GO:0016042]; myoblast fusion [GO:0007520]; myotube differentiation [GO:0014902]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of protein secretion [GO:0050714]; receptor internalization [GO:0031623]; regulation of gene expression [GO:0010468]; regulation of phosphorylation [GO:0042325]
|
collagen-containing extracellular matrix [GO:0062023]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum lumen [GO:0005788]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; nucleus [GO:0005634]; secretory granule [GO:0030141]; secretory granule lumen [GO:0034774]; sno(s)RNA-containing ribonucleoprotein complex [GO:0005732]
|
hormone activity [GO:0005179]; insulin receptor binding [GO:0005158]; receptor ligand activity [GO:0048018]; transmembrane receptor protein tyrosine kinase activator activity [GO:0030297]; zinc ion binding [GO:0008270]
|
PF00049;
|
1.10.100.10;
|
Insulin family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Insulin decreases blood glucose concentration. It increases cell permeability to monosaccharides, amino acids and fatty acids. It accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver.
|
Mus musculus (Mouse)
|
P01329
|
INS_CAVPO
|
MALWMHLLTVLALLALWGPNTGQAFVSRHLCGSNLVETLYSVCQDDGFFYIPKDRRELEDPQVEQTELGMGLGAGGLQPLALEMALQKRGIVDQCCTGTCTRHQLQSYCN
| null | null |
acute-phase response [GO:0006953]; alpha-beta T cell activation [GO:0046631]; fatty acid homeostasis [GO:0055089]; G protein-coupled receptor signaling pathway [GO:0007186]; glucose homeostasis [GO:0042593]; glucose metabolic process [GO:0006006]; insulin receptor signaling pathway [GO:0008286]; negative regulation of acute inflammatory response [GO:0002674]; negative regulation of fatty acid metabolic process [GO:0045922]; negative regulation of feeding behavior [GO:2000252]; negative regulation of gene expression [GO:0010629]; negative regulation of glycogen catabolic process [GO:0045818]; negative regulation of lipid catabolic process [GO:0050995]; negative regulation of protein catabolic process [GO:0042177]; negative regulation of protein secretion [GO:0050709]; negative regulation of proteolysis [GO:0045861]; negative regulation of reactive oxygen species biosynthetic process [GO:1903427]; negative regulation of respiratory burst involved in inflammatory response [GO:0060266]; neuron projection maintenance [GO:1990535]; nitric oxide-cGMP-mediated signaling pathway [GO:0038060]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of cytokine production [GO:0001819]; positive regulation of dendritic spine maintenance [GO:1902952]; positive regulation of glucose import [GO:0046326]; positive regulation of glycogen biosynthetic process [GO:0045725]; positive regulation of glycolytic process [GO:0045821]; positive regulation of insulin receptor signaling pathway [GO:0046628]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of mitotic nuclear division [GO:0045840]; positive regulation of nitric oxide mediated signal transduction [GO:0010750]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of protein localization to nucleus [GO:1900182]; positive regulation of protein metabolic process [GO:0051247]; positive regulation of protein secretion [GO:0050714]; positive regulation of respiratory burst [GO:0060267]; regulation of cellular amino acid metabolic process [GO:0006521]; regulation of protein localization to plasma membrane [GO:1903076]; vasodilation [GO:0042311]; wound healing [GO:0042060]
|
extracellular space [GO:0005615]
|
hormone activity [GO:0005179]; identical protein binding [GO:0042802]; insulin receptor binding [GO:0005158]; insulin-like growth factor receptor binding [GO:0005159]; protease binding [GO:0002020]
|
PF00049;
|
1.10.100.10;
|
Insulin family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Insulin decreases blood glucose concentration. It increases cell permeability to monosaccharides, amino acids and fatty acids. It accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver.
|
Cavia porcellus (Guinea pig)
|
P01344
|
IGF2_HUMAN
|
MGIPMGKSMLVLLTFLAFASCCIAAYRPSETLCGGELVDTLQFVCGDRGFYFSRPASRVSRRSRGIVEECCFRSCDLALLETYCATPAKSERDVSTPPTVLPDNFPRYPVGKFFQYDTWKQSTQRLRRGLPALLRARRGHVLAKELEAFREAKRHRPLIALPTQDPAHGGAPPEMASNRK
| null | null |
animal organ morphogenesis [GO:0009887]; embryonic placenta development [GO:0001892]; embryonic placenta morphogenesis [GO:0060669]; exocrine pancreas development [GO:0031017]; genomic imprinting [GO:0071514]; glucose metabolic process [GO:0006006]; in utero embryonic development [GO:0001701]; insulin receptor signaling pathway [GO:0008286]; insulin-like growth factor receptor signaling pathway [GO:0048009]; negative regulation of muscle cell differentiation [GO:0051148]; negative regulation of transcription by RNA polymerase II [GO:0000122]; osteoblast differentiation [GO:0001649]; positive regulation of activated T cell proliferation [GO:0042104]; positive regulation of cell division [GO:0051781]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of glycogen biosynthetic process [GO:0045725]; positive regulation of insulin receptor signaling pathway [GO:0046628]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of mitotic nuclear division [GO:0045840]; positive regulation of multicellular organism growth [GO:0040018]; positive regulation of organ growth [GO:0046622]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of skeletal muscle tissue growth [GO:0048633]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of vascular endothelial cell proliferation [GO:1905564]; regulation of DNA-templated transcription [GO:0006355]; regulation of muscle cell differentiation [GO:0051147]; spongiotrophoblast cell proliferation [GO:0060720]; striated muscle cell differentiation [GO:0051146]
|
extracellular region [GO:0005576]; extracellular space [GO:0005615]; platelet alpha granule lumen [GO:0031093]
|
growth factor activity [GO:0008083]; hormone activity [GO:0005179]; insulin receptor binding [GO:0005158]; insulin-like growth factor receptor binding [GO:0005159]; integrin binding [GO:0005178]; protein serine/threonine kinase activator activity [GO:0043539]; receptor ligand activity [GO:0048018]; transmembrane receptor protein tyrosine kinase activator activity [GO:0030297]
|
PF08365;PF00049;
|
1.10.100.10;
|
Insulin family
|
PTM: O-glycosylated with core 1 or possibly core 8 glycans. Thr-96 is a minor glycosylation site compared to Thr-99. {ECO:0000269|PubMed:1569071, ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:22171320, ECO:0000269|PubMed:23234360}.; PTM: Proteolytically processed by PCSK4, proIGF2 is cleaved at Arg-128 and Arg-92 to generate big-IGF2 and mature IGF2. {ECO:0000269|PubMed:16040806}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16040806}.
| null | null | null | null | null |
FUNCTION: The insulin-like growth factors possess growth-promoting activity (By similarity). Major fetal growth hormone in mammals. Plays a key role in regulating fetoplacental development. IGF2 is influenced by placental lactogen. Also involved in tissue differentiation. In adults, involved in glucose metabolism in adipose tissue, skeletal muscle and liver (Probable). Acts as a ligand for integrin which is required for IGF2 signaling (PubMed:28873464). Positively regulates myogenic transcription factor MYOD1 function by facilitating the recruitment of transcriptional coactivators, thereby controlling muscle terminal differentiation (By similarity). Inhibits myoblast differentiation and modulates metabolism via increasing the mitochondrial respiration rate (By similarity). {ECO:0000250|UniProtKB:P09535, ECO:0000269|PubMed:28873464, ECO:0000305|PubMed:24593700}.; FUNCTION: Preptin undergoes glucose-mediated co-secretion with insulin, and acts as a physiological amplifier of glucose-mediated insulin secretion. Exhibits osteogenic properties by increasing osteoblast mitogenic activity through phosphoactivation of MAPK1 and MAPK3. {ECO:0000269|PubMed:16912056}.
|
Homo sapiens (Human)
|
P01346
|
IGF2_RAT
|
MGIPVGKSMLVLLISLAFALCCIAAYRPSETLCGGELVDTLQFVCSDRGFYFSRPSSRANRRSRGIVEECCFRSCDLALLETYCATPAKSERDVSTSQAVLPDDFPRYPVGKFFKFDTWRQSAGRLRRGLPALLRARRGRMLAKELEAFREAKRHRPLIVLPPKDPAHGGASSEMSSNHQ
| null | null |
animal organ morphogenesis [GO:0009887]; cellular response to mechanical stimulus [GO:0071260]; embryonic placenta development [GO:0001892]; embryonic placenta morphogenesis [GO:0060669]; exocrine pancreas development [GO:0031017]; female pregnancy [GO:0007565]; glucose metabolic process [GO:0006006]; in utero embryonic development [GO:0001701]; insulin receptor signaling pathway [GO:0008286]; insulin-like growth factor receptor signaling pathway [GO:0048009]; memory [GO:0007613]; negative regulation of muscle cell differentiation [GO:0051148]; negative regulation of natural killer cell mediated cytotoxicity [GO:0045953]; negative regulation of transcription by RNA polymerase II [GO:0000122]; osteoblast differentiation [GO:0001649]; positive regulation of activated T cell proliferation [GO:0042104]; positive regulation of angiogenesis [GO:0045766]; positive regulation of blood vessel endothelial cell migration [GO:0043536]; positive regulation of cell division [GO:0051781]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of glycogen biosynthetic process [GO:0045725]; positive regulation of insulin receptor signaling pathway [GO:0046628]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of mitotic nuclear division [GO:0045840]; positive regulation of multicellular organism growth [GO:0040018]; positive regulation of organ growth [GO:0046622]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of skeletal muscle tissue growth [GO:0048633]; positive regulation of steroid hormone biosynthetic process [GO:0090031]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of vascular endothelial cell proliferation [GO:1905564]; regulation of muscle cell differentiation [GO:0051147]; response to estradiol [GO:0032355]; response to ethanol [GO:0045471]; response to nicotine [GO:0035094]; response to nutrient levels [GO:0031667]; response to organic cyclic compound [GO:0014070]; response to xenobiotic stimulus [GO:0009410]; spongiotrophoblast cell proliferation [GO:0060720]; striated muscle cell differentiation [GO:0051146]
|
extracellular space [GO:0005615]
|
growth factor activity [GO:0008083]; hormone activity [GO:0005179]; insulin receptor binding [GO:0005158]; insulin-like growth factor receptor binding [GO:0005159]; integrin binding [GO:0005178]; protein serine/threonine kinase activator activity [GO:0043539]; receptor ligand activity [GO:0048018]; transmembrane receptor protein tyrosine kinase activator activity [GO:0030297]
|
PF08365;PF00049;
|
1.10.100.10;
|
Insulin family
|
PTM: Proteolytically processed by PCSK4, proIGF2 is cleaved at Arg-128 and Arg-92 to generate big-IGF2 and mature IGF2. {ECO:0000250|UniProtKB:P01344}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P01344, ECO:0000250|UniProtKB:P09535}.
| null | null | null | null | null |
FUNCTION: The insulin-like growth factors possess growth-promoting activity (By similarity). Major fetal growth hormone in mammals. Plays a key role in regulating fetoplacental development. IGF2 is influenced by placental lactogen. Also involved in tissue differentiation. In adults, involved in glucose metabolism in adipose tissue, skeletal muscle and liver. Acts as a ligand for integrin which is required for IGF2 signaling. Positively regulates myogenic transcription factor MYOD1 function by facilitating the recruitment of transcriptional coactivators, thereby controlling muscle terminal differentiation (By similarity). Inhibits myoblast differentiation and modulates metabolism via increasing the mitochondrial respiration rate (By similarity). {ECO:0000250|UniProtKB:P01344, ECO:0000250|UniProtKB:P09535}.; FUNCTION: Preptin undergoes glucose-mediated co-secretion with insulin, and acts as a physiological amplifier of glucose-mediated insulin secretion. Exhibits osteogenic properties by increasing osteoblast mitogenic activity through phosphoactivation of MAPK1 and MAPK3. {ECO:0000250|UniProtKB:P01344, ECO:0000250|UniProtKB:P09535}.
|
Rattus norvegicus (Rat)
|
P01347
|
REL1_RAT
|
MSSRLLLQLLGFWLFLSQPCRARVSEEWMDQVIQVCGRGYARAWIEVCGASVGRLALSQEEPAPLARQATAEVVPSFINKDAEPFDMTLKCLPNLSEERKAALSEGRAPFPELQQHAPALSDSVVSLEGFKKTFHNQLGEAEDGGPPELKYLGSDAQSRKKRQSGALLSEQCCHIGCTRRSIAKLC
| null | null |
adenylate cyclase-modulating G protein-coupled receptor signaling pathway [GO:0007188]; developmental growth [GO:0048589]; mammary gland morphogenesis [GO:0060443]; negative regulation of apoptotic process [GO:0043066]; nipple development [GO:0060618]; prostate gland growth [GO:0060736]; regulation of apoptotic process [GO:0042981]; regulation of body fluid levels [GO:0050878]; regulation of cell population proliferation [GO:0042127]; regulation of nitric oxide mediated signal transduction [GO:0010749]; spermatogenesis [GO:0007283]
|
extracellular region [GO:0005576]
|
hormone activity [GO:0005179]; signaling receptor binding [GO:0005102]
|
PF00049;
| null |
Insulin family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Relaxin is an ovarian hormone that acts with estrogen to produce dilatation of the birth canal in many mammals.
|
Rattus norvegicus (Rat)
|
P01348
|
RELX_PIG
|
MPRLFSYLLGVWLLLSQLPREIPGQSTNDFIKACGRELVRLWVEICGSVSWGRTALSLEEPQLETGPPAETMPSSITKDAEILKMMLEFVPNLPQELKATLSERQPSLRELQQSASKDSNLNFEEFKKIILNRQNEAEDKSLLELKNLGLDKHSRKKRLFRMTLSEKCCQVGCIRKDIARLC
| null | null |
blastocyst growth [GO:0001832]; flagellated sperm motility [GO:0030317]; oocyte maturation [GO:0001556]; positive regulation of acrosome reaction [GO:2000344]; positive regulation of epithelial cell proliferation [GO:0050679]; positive regulation of glucose import [GO:0046326]
|
extracellular region [GO:0005576]
|
hormone activity [GO:0005179]
|
PF00049;
| null |
Insulin family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Relaxin is an ovarian hormone that acts with estrogen to produce dilatation of the birth canal in many mammals.
|
Sus scrofa (Pig)
|
P01350
|
GAST_HUMAN
|
MQRLCVYVLIFALALAAFSEASWKPRSQQPDAPLGTGANRDLELPWLEQQGPASHHRRQLGPQGPPHLVADPSKKQGPWLEEEEEAYGWMDFGRRSAEDEN
| null | null |
G protein-coupled receptor signaling pathway [GO:0007186]; response to food [GO:0032094]; signal transduction [GO:0007165]
|
extracellular region [GO:0005576]; extracellular space [GO:0005615]
|
hormone activity [GO:0005179]
|
PF00918;
| null |
Gastrin/cholecystokinin family
|
PTM: Two different processing pathways probably exist in antral G-cells. In the dominant pathway progastrin is cleaved at three sites resulting in two major bioactive gastrins, gastrin-34 and gastrin-17. In the putative alternative pathway, progastrin may be processed only at the most C-terminal dibasic site resulting in the synthesis of gastrin-71.; PTM: Sulfation enhances proteolytic processing, and blocks peptide degradation. Levels of sulfation differ between proteolytically-cleaved gastrins. Thus, gastrin-6 is almost 73% sulfated, whereas the larger gastrins are less than 50% sulfated. Sulfation levels are also tissue-specific. {ECO:0000269|PubMed:11052986, ECO:0000269|PubMed:7530658, ECO:0000269|PubMed:7621822}.
|
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Gastrin stimulates the stomach mucosa to produce and secrete hydrochloric acid and the pancreas to secrete its digestive enzymes. It also stimulates smooth muscle contraction and increases blood circulation and water secretion in the stomach and intestine.
|
Homo sapiens (Human)
|
P01355
|
CCKN_RAT
|
MKCGVCLCVVMAVLAAGALAQPVVPVEAVDPMEQRAEEAPRRQLRAVLRPDSEPRARLGALLARYIQQVRKAPSGRMSVLKNLQGLDPSHRISDRDYMGWMDFGRRSAEDYEYPS
| null | null |
axonogenesis [GO:0007409]; cholecystokinin signaling pathway [GO:0038188]; digestion [GO:0007586]; eating behavior [GO:0042755]; memory [GO:0007613]; negative regulation of appetite [GO:0032099]; negative regulation of behavioral fear response [GO:2000986]; negative regulation of eating behavior [GO:1903999]; neuron migration [GO:0001764]; positive regulation of apoptotic process [GO:0043065]; positive regulation of behavioral fear response [GO:2000987]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of glutamate secretion [GO:0014049]; positive regulation of mitochondrial depolarization [GO:0051901]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; positive regulation of protein-containing complex assembly [GO:0031334]; protein kinase C-activating G protein-coupled receptor signaling pathway [GO:0007205]; release of cytochrome c from mitochondria [GO:0001836]; synaptic signaling via neuropeptide [GO:0099538]; visual learning [GO:0008542]
|
axon [GO:0030424]; axon hillock [GO:0043203]; axon initial segment [GO:0043194]; dendrite [GO:0030425]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; GABA-ergic synapse [GO:0098982]; neuronal cell body [GO:0043025]; perikaryon [GO:0043204]; terminal bouton [GO:0043195]
|
hormone activity [GO:0005179]; neuropeptide hormone activity [GO:0005184]; peptide hormone receptor binding [GO:0051428]; receptor ligand activity [GO:0048018]
|
PF00918;
| null |
Gastrin/cholecystokinin family
|
PTM: The precursor is cleaved by proteases to produce a number of active cholecystokinins.; PTM: Sulfation of Tyr-97 is essential for receptor activation. {ECO:0000269|PubMed:8208365, ECO:0000269|Ref.5}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P09240}.
| null | null | null | null | null |
FUNCTION: This peptide hormone induces gall bladder contraction and the release of pancreatic enzymes in the gut. Its function in the brain is not clear. Binding to CCK-A receptors stimulates amylase release from the pancreas, binding to CCK-B receptors stimulates gastric acid secretion. {ECO:0000303|PubMed:12479974}.
|
Rattus norvegicus (Rat)
|
P01362
|
ELH1_APLCA
|
MKRPNNRPTNTMSLILCLTLSSLCVSSQSASVHGKNFATNRAVKSSSPFVVLSPDDNVVSMSGENGYRSALREAFDKSSRDYDDNGEDVFSNEKRRLRFHKRRLRFDRRDQDEGNFRRFPTNAVSMSADENSPFDLSNEDGAVYQRDLRAPRLRFYSLRKRAAGGMEQSEGQNPETESHSRRKRSVLTPSLSSLGESLESGISKRISINQDLKAITDMLLTEQIRERQRYLADLRQRLLEKGKRSSGVSLLTSNKDEEQRELLKAISNLLD
| null | null |
neuropeptide signaling pathway [GO:0007218]
|
extracellular region [GO:0005576]
|
hormone activity [GO:0005179]
|
PF02323;
| null |
Molluscan ELH family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: ELH acts as a neurotransmitter locally, upon neurons of the abdominal ganglion and as a hormone by diffusing into the circulating hemolymph and modulating the activity of other organs. It specifically causes contraction of smooth muscle in the ovotestis and expulsion of the egg string.; FUNCTION: Alpha-BCP decreases the activity of a cluster of neurons in the left upper quadrant of the abdominal ganglion.; FUNCTION: Beta-BCP specifically excites 2 neurons, L1 and R1, in the abdominal ganglion.
|
Aplysia californica (California sea hare)
|
P01374
|
TNFB_HUMAN
|
MTPPERLFLPRVCGTTLHLLLLGLLLVLLPGAQGLPGVGLTPSAAQTARQHPKMHLAHSTLKPAAHLIGDPSKQNSLLWRANTDRAFLQDGFSLSNNSLLVPTSGIYFVYSQVVFSGKAYSPKATSSPLYLAHEVQLFSSQYPFHVPLLSSQKMVYPGLQEPWLHSMYHGAAFQLTQGDQLSTHTDGIPHLVLSPSTVFFGAFAL
| null | null |
apoptotic process [GO:0006915]; cell-cell signaling [GO:0007267]; defense response to Gram-positive bacterium [GO:0050830]; humoral immune response [GO:0006959]; lymph node development [GO:0048535]; negative regulation of fibroblast proliferation [GO:0048147]; positive regulation of apoptotic process [GO:0043065]; positive regulation of chronic inflammatory response to antigenic stimulus [GO:0002876]; positive regulation of glial cell proliferation [GO:0060252]; positive regulation of humoral immune response mediated by circulating immunoglobulin [GO:0002925]; positive regulation of type II interferon production [GO:0032729]; response to hypoxia [GO:0001666]; response to lipopolysaccharide [GO:0032496]; response to nutrient [GO:0007584]; response to xenobiotic stimulus [GO:0009410]; signal transduction [GO:0007165]
|
extracellular space [GO:0005615]; plasma membrane [GO:0005886]
|
cytokine activity [GO:0005125]; signaling receptor binding [GO:0005102]; tumor necrosis factor receptor binding [GO:0005164]
|
PF00229;
|
2.60.120.40;
|
Tumor necrosis factor family
| null |
SUBCELLULAR LOCATION: Secreted. Membrane. Note=The homotrimer is secreted. The heterotrimer is membrane-associated.
| null | null | null | null | null |
FUNCTION: Cytokine that in its homotrimeric form binds to TNFRSF1A/TNFR1, TNFRSF1B/TNFBR and TNFRSF14/HVEM (PubMed:9462508). In its heterotrimeric form with LTB binds to TNFRSF3/LTBR. Lymphotoxin is produced by lymphocytes and is cytotoxic for a wide range of tumor cells in vitro and in vivo. {ECO:0000269|PubMed:9462508}.
|
Homo sapiens (Human)
|
P01375
|
TNFA_HUMAN
|
MSTESMIRDVELAEEALPKKTGGPQGSRRCLFLSLFSFLIVAGATTLFCLLHFGVIGPQREEFPRDLSLISPLAQAVRSSSRTPSDKPVAHVVANPQAEGQLQWLNRRANALLANGVELRDNQLVVPSEGLYLIYSQVLFKGQGCPSTHVLLTHTISRIAVSYQTKVNLLSAIKSPCQRETPEGAEAKPWYEPIYLGGVFQLEKGDRLSAEINRPDYLDFAESGQVYFGIIAL
| null | null |
activation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0006919]; antiviral innate immune response [GO:0140374]; astrocyte activation [GO:0048143]; calcium-mediated signaling [GO:0019722]; cellular response to amino acid stimulus [GO:0071230]; cellular response to amyloid-beta [GO:1904646]; cellular response to lipopolysaccharide [GO:0071222]; cellular response to nicotine [GO:0071316]; cellular response to retinoic acid [GO:0071300]; cellular response to toxic substance [GO:0097237]; cellular response to type II interferon [GO:0071346]; chronic inflammatory response to antigenic stimulus [GO:0002439]; circadian rhythm [GO:0007623]; cognition [GO:0050890]; cortical actin cytoskeleton organization [GO:0030866]; defense response to Gram-positive bacterium [GO:0050830]; detection of mechanical stimulus involved in sensory perception of pain [GO:0050966]; embryonic digestive tract development [GO:0048566]; endothelial cell apoptotic process [GO:0072577]; epithelial cell proliferation involved in salivary gland morphogenesis [GO:0060664]; extracellular matrix organization [GO:0030198]; extrinsic apoptotic signaling pathway [GO:0097191]; extrinsic apoptotic signaling pathway via death domain receptors [GO:0008625]; glucose metabolic process [GO:0006006]; humoral immune response [GO:0006959]; inflammatory response [GO:0006954]; inflammatory response to wounding [GO:0090594]; intrinsic apoptotic signaling pathway in response to DNA damage [GO:0008630]; JNK cascade [GO:0007254]; leukocyte migration involved in inflammatory response [GO:0002523]; leukocyte tethering or rolling [GO:0050901]; liver regeneration [GO:0097421]; macrophage activation involved in immune response [GO:0002281]; microglial cell activation [GO:0001774]; necroptotic signaling pathway [GO:0097527]; negative regulation of amyloid-beta clearance [GO:1900222]; negative regulation of apoptotic signaling pathway [GO:2001234]; negative regulation of bicellular tight junction assembly [GO:1903347]; negative regulation of bile acid secretion [GO:0120190]; negative regulation of blood vessel endothelial cell migration [GO:0043537]; negative regulation of branching involved in lung morphogenesis [GO:0061048]; negative regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043154]; negative regulation of cytokine production involved in immune response [GO:0002719]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of endothelial cell proliferation [GO:0001937]; negative regulation of extrinsic apoptotic signaling pathway in absence of ligand [GO:2001240]; negative regulation of fat cell differentiation [GO:0045599]; negative regulation of gene expression [GO:0010629]; negative regulation of glucose import [GO:0046325]; negative regulation of heart rate [GO:0010459]; negative regulation of interleukin-6 production [GO:0032715]; negative regulation of L-glutamate import across plasma membrane [GO:0002037]; negative regulation of lipid catabolic process [GO:0050995]; negative regulation of lipid storage [GO:0010888]; negative regulation of miRNA transcription [GO:1902894]; negative regulation of mitotic cell cycle [GO:0045930]; negative regulation of myelination [GO:0031642]; negative regulation of myoblast differentiation [GO:0045662]; negative regulation of myosin-light-chain-phosphatase activity [GO:0035509]; negative regulation of neurogenesis [GO:0050768]; negative regulation of osteoblast differentiation [GO:0045668]; negative regulation of oxidative phosphorylation [GO:0090324]; negative regulation of protein-containing complex disassembly [GO:0043242]; negative regulation of signaling receptor activity [GO:2000272]; negative regulation of systemic arterial blood pressure [GO:0003085]; negative regulation of transcription by RNA polymerase II [GO:0000122]; negative regulation of vascular wound healing [GO:0061044]; negative regulation of viral genome replication [GO:0045071]; osteoclast differentiation [GO:0030316]; phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0043491]; positive regulation of action potential [GO:0045760]; positive regulation of amyloid-beta formation [GO:1902004]; positive regulation of apoptotic process [GO:0043065]; positive regulation of blood microparticle formation [GO:2000334]; positive regulation of calcidiol 1-monooxygenase activity [GO:0060559]; positive regulation of calcineurin-NFAT signaling cascade [GO:0070886]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of cell adhesion [GO:0045785]; positive regulation of chemokine (C-X-C motif) ligand 2 production [GO:2000343]; positive regulation of chemokine production [GO:0032722]; positive regulation of chronic inflammatory response to antigenic stimulus [GO:0002876]; positive regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043280]; positive regulation of cytokine production [GO:0001819]; positive regulation of cytokine production involved in inflammatory response [GO:1900017]; positive regulation of DNA biosynthetic process [GO:2000573]; positive regulation of DNA-binding transcription factor activity [GO:0051091]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of extrinsic apoptotic signaling pathway [GO:2001238]; positive regulation of fever generation [GO:0031622]; positive regulation of fractalkine production [GO:0032724]; positive regulation of gene expression [GO:0010628]; positive regulation of glial cell proliferation [GO:0060252]; positive regulation of hair follicle development [GO:0051798]; positive regulation of hepatocyte proliferation [GO:2000347]; positive regulation of heterotypic cell-cell adhesion [GO:0034116]; positive regulation of humoral immune response mediated by circulating immunoglobulin [GO:0002925]; positive regulation of I-kappaB phosphorylation [GO:1903721]; positive regulation of inflammatory response [GO:0050729]; positive regulation of interleukin-1 beta production [GO:0032731]; positive regulation of interleukin-18 production [GO:0032741]; positive regulation of interleukin-33 production [GO:0150129]; positive regulation of interleukin-6 production [GO:0032755]; positive regulation of interleukin-8 production [GO:0032757]; positive regulation of JNK cascade [GO:0046330]; positive regulation of JUN kinase activity [GO:0043507]; positive regulation of leukocyte adhesion to arterial endothelial cell [GO:1904999]; positive regulation of leukocyte adhesion to vascular endothelial cell [GO:1904996]; positive regulation of MAP kinase activity [GO:0043406]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of membrane protein ectodomain proteolysis [GO:0051044]; positive regulation of miRNA transcription [GO:1902895]; positive regulation of mitotic nuclear division [GO:0045840]; positive regulation of mononuclear cell migration [GO:0071677]; positive regulation of neuroinflammatory response [GO:0150078]; positive regulation of neuron apoptotic process [GO:0043525]; positive regulation of neutrophil activation [GO:1902565]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of nitric oxide biosynthetic process [GO:0045429]; positive regulation of nitrogen compound metabolic process [GO:0051173]; positive regulation of non-canonical NF-kappaB signal transduction [GO:1901224]; positive regulation of osteoclast differentiation [GO:0045672]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of podosome assembly [GO:0071803]; positive regulation of programmed cell death [GO:0043068]; positive regulation of protein catabolic process [GO:0045732]; positive regulation of protein localization to cell surface [GO:2000010]; positive regulation of protein localization to plasma membrane [GO:1903078]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of protein transport [GO:0051222]; positive regulation of protein-containing complex assembly [GO:0031334]; positive regulation of protein-containing complex disassembly [GO:0043243]; positive regulation of receptor signaling pathway via JAK-STAT [GO:0046427]; positive regulation of smooth muscle cell proliferation [GO:0048661]; positive regulation of superoxide dismutase activity [GO:1901671]; positive regulation of synaptic transmission [GO:0050806]; positive regulation of synoviocyte proliferation [GO:1901647]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of translational initiation by iron [GO:0045994]; positive regulation of type II interferon production [GO:0032729]; positive regulation of tyrosine phosphorylation of STAT protein [GO:0042531]; positive regulation of vascular associated smooth muscle cell proliferation [GO:1904707]; positive regulation of vitamin D biosynthetic process [GO:0060557]; protein localization to plasma membrane [GO:0072659]; regulation of branching involved in salivary gland morphogenesis [GO:0060693]; regulation of canonical NF-kappaB signal transduction [GO:0043122]; regulation of endothelial cell apoptotic process [GO:2000351]; regulation of establishment of endothelial barrier [GO:1903140]; regulation of fat cell differentiation [GO:0045598]; regulation of immunoglobulin production [GO:0002637]; regulation of insulin secretion [GO:0050796]; regulation of membrane lipid metabolic process [GO:1905038]; regulation of reactive oxygen species metabolic process [GO:2000377]; regulation of synapse organization [GO:0050807]; regulation of synaptic transmission, glutamatergic [GO:0051966]; response to 3,3',5-triiodo-L-thyronine [GO:1905242]; response to activity [GO:0014823]; response to ethanol [GO:0045471]; response to fructose [GO:0009750]; response to glucocorticoid [GO:0051384]; response to gold nanoparticle [GO:1990268]; response to Gram-negative bacterium [GO:0140460]; response to hypoxia [GO:0001666]; response to isolation stress [GO:0035900]; response to L-glutamate [GO:1902065]; response to macrophage colony-stimulating factor [GO:0036005]; response to nutrient levels [GO:0031667]; response to salt stress [GO:0009651]; response to virus [GO:0009615]; response to xenobiotic stimulus [GO:0009410]; sequestering of triglyceride [GO:0030730]; skeletal muscle contraction [GO:0003009]; toll-like receptor 3 signaling pathway [GO:0034138]; tumor necrosis factor-mediated signaling pathway [GO:0033209]; vascular endothelial growth factor production [GO:0010573]; vasodilation [GO:0042311]
|
cell surface [GO:0009986]; external side of plasma membrane [GO:0009897]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; membrane raft [GO:0045121]; neuronal cell body [GO:0043025]; phagocytic cup [GO:0001891]; plasma membrane [GO:0005886]; recycling endosome [GO:0055037]
|
cytokine activity [GO:0005125]; death receptor agonist activity [GO:0038177]; identical protein binding [GO:0042802]; protease binding [GO:0002020]; transcription cis-regulatory region binding [GO:0000976]; tumor necrosis factor receptor binding [GO:0005164]
|
PF00229;
|
2.60.120.40;
|
Tumor necrosis factor family
|
PTM: The soluble form derives from the membrane form by proteolytic processing. The membrane-bound form is further proteolytically processed by SPPL2A or SPPL2B through regulated intramembrane proteolysis producing TNF intracellular domains (ICD1 and ICD2) released in the cytosol and TNF C-domain 1 and C-domain 2 secreted into the extracellular space. {ECO:0000269|PubMed:16829951, ECO:0000269|PubMed:16829952, ECO:0000269|PubMed:9034191}.; PTM: The membrane form, but not the soluble form, is phosphorylated on serine residues. Dephosphorylation of the membrane form occurs by binding to soluble TNFRSF1A/TNFR1. {ECO:0000269|PubMed:10205166, ECO:0000269|PubMed:8597870}.; PTM: O-glycosylated; glycans contain galactose, N-acetylgalactosamine and N-acetylneuraminic acid. {ECO:0000269|PubMed:8631363}.; PTM: [Tumor necrosis factor, soluble form]: The soluble form is demyristoylated at Lys-19 and Lys-20 by SIRT6, promoting its secretion. {ECO:0000269|PubMed:23552949}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16829952}; Single-pass type II membrane protein {ECO:0000269|PubMed:16829952}.; SUBCELLULAR LOCATION: [Tumor necrosis factor, membrane form]: Membrane; Single-pass type II membrane protein.; SUBCELLULAR LOCATION: [Tumor necrosis factor, soluble form]: Secreted {ECO:0000269|PubMed:23552949}.; SUBCELLULAR LOCATION: [C-domain 1]: Secreted.; SUBCELLULAR LOCATION: [C-domain 2]: Secreted.
| null | null | null | null | null |
FUNCTION: Cytokine that binds to TNFRSF1A/TNFR1 and TNFRSF1B/TNFBR. It is mainly secreted by macrophages and can induce cell death of certain tumor cell lines. It is potent pyrogen causing fever by direct action or by stimulation of interleukin-1 secretion and is implicated in the induction of cachexia, Under certain conditions it can stimulate cell proliferation and induce cell differentiation. Impairs regulatory T-cells (Treg) function in individuals with rheumatoid arthritis via FOXP3 dephosphorylation. Up-regulates the expression of protein phosphatase 1 (PP1), which dephosphorylates the key 'Ser-418' residue of FOXP3, thereby inactivating FOXP3 and rendering Treg cells functionally defective (PubMed:23396208). Key mediator of cell death in the anticancer action of BCG-stimulated neutrophils in combination with DIABLO/SMAC mimetic in the RT4v6 bladder cancer cell line (PubMed:16829952, PubMed:22517918, PubMed:23396208). Induces insulin resistance in adipocytes via inhibition of insulin-induced IRS1 tyrosine phosphorylation and insulin-induced glucose uptake. Induces GKAP42 protein degradation in adipocytes which is partially responsible for TNF-induced insulin resistance (By similarity). Plays a role in angiogenesis by inducing VEGF production synergistically with IL1B and IL6 (PubMed:12794819). Promotes osteoclastogenesis and therefore mediates bone resorption (By similarity). {ECO:0000250|UniProtKB:P06804, ECO:0000269|PubMed:12794819, ECO:0000269|PubMed:16829952, ECO:0000269|PubMed:22517918, ECO:0000269|PubMed:23396208}.; FUNCTION: The TNF intracellular domain (ICD) form induces IL12 production in dendritic cells. {ECO:0000269|PubMed:16829952}.
|
Homo sapiens (Human)
|
P01391
|
3L21_NAJKA
|
IRCFITPDITSKDCPNGHVCYTKTWCDAFCSIRGKRVDLGCAATCPTVKTGVDIQCCSTDNCNPFPTRKRP
| null | null | null |
extracellular region [GO:0005576]
|
acetylcholine receptor inhibitor activity [GO:0030550]; ion channel regulator activity [GO:0099106]; toxin activity [GO:0090729]
| null |
2.10.60.10;
|
Snake three-finger toxin family, Long-chain subfamily, Type II alpha-neurotoxin sub-subfamily
|
PTM: In homodimer alpha-cobratoxin, selective reduction of Cys(26)-Cys(30) in one subunit does not affect the activity against the alpha-7/CHRNA7 nAChR, whereas its reduction in both subunits almost prevents alpha-7/CHRNA7 nAChR recognition. On the contrary, reduction of one or both Cys(26)-Cys(30) disulfide bonds in the homodimer considerably potentiates inhibition of the alpha-3-beta-2/CHRNA3-CHRNB2 nAChR by the toxin. {ECO:0000269|PubMed:22223648}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.1}.
| null | null | null | null | null |
FUNCTION: Monomer: binds with high affinity to muscular (alpha-1-beta-1-gamma-delta/CHRNA1-CHRNB1-CHRNG-CHRND) nAChR (tested on Torpedo californica, Kd=0.2-4.5 nM) and neuronal alpha-7/CHRNA7 nicotinic acetylcholine receptors (Kd=13-105 nM) (PubMed:18381281, PubMed:22223648, PubMed:9305882). Also inhibits GABA(A) channels (PubMed:26221036). Heteropentamer targets studied are composed of alpha-1-beta-3-gamma-2 (GABRA1-GABRB3-GABRG2) subunits (IC(50)=236 nM), alpha-1-beta-2-gamma-2 (GABRA1-GABRB2-GABRG2) subunits (IC(50)=469 nM), alpha-2-beta-2-gamma-2 (GABRA2-GABRB2-GABRG2) subunits (IC(50)=485 nM), alpha-5-beta-3-gamma-2 (GABRA5-GABRB3-GABRG2) subunits (IC(50)=635 nM), and alpha-2-beta-3-gamma-2 (GABRA2-GABRB3-GABRG2) subunits (IC(50)=1099 nM) (activated by 10 uM GABA) (PubMed:26221036). {ECO:0000269|PubMed:18381281, ECO:0000269|PubMed:22223648, ECO:0000269|PubMed:26221036, ECO:0000269|PubMed:30025921}.; FUNCTION: Homodimer: binds with high affinity (but lower than the monomeric form) to muscular (IC(50)=9.7 nM) and with low affinity to neuronal alpha-7/CHRNA7 nAChRs (IC(50)=1370 nM) (PubMed:22223648). However, it acquires (compared to the monomeric form) the capacity to block alpha-3/beta-2 (CHRNA3/CHRNB2) nAChRs (PubMed:18381281). {ECO:0000269|PubMed:18381281, ECO:0000269|PubMed:22223648}.; FUNCTION: Heterodimer with cytotoxin 3 (AC P01446): is slightly more active than the homodimer in inhibiting alpha-7/CHRNA7 nAChR and is considerably more active in blocking the alpha-3-beta-2/CHRNA3-CHRNB2 nAChR. {ECO:0000269|PubMed:22223648}.
|
Naja kaouthia (Monocled cobra) (Naja siamensis)
|
P01398
|
3LKB_BUNMU
|
MKTLLLTLVVVTIVCLDLGYTRTCLISPSSTPQTCPNGQDICFLKAQCDKFCSIRGPVIEQGCVATCPQFRSNYRSLLCCTTDNCNH
| null | null | null |
extracellular region [GO:0005576]
|
acetylcholine receptor inhibitor activity [GO:0030550]; ion channel regulator activity [GO:0099106]; toxin activity [GO:0090729]
| null |
2.10.60.10;
|
Snake three-finger toxin family, Long-chain subfamily, Kappa-neurotoxin sub-subfamily
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:3986193}.
| null | null | null | null | null |
FUNCTION: Postsynaptic neurotoxin that binds and inhibits neuronal nicotinic acetylcholine receptors (nAChR) with high affinity (IC(50)<100 nM). Is a selective, and slowly reversible antagonist of alpha-3/CHRNA3-containing and some alpha-4/CHRNA4-containing AChRs. {ECO:0000269|PubMed:3986193, ECO:0000303|PubMed:9027980}.
|
Bungarus multicinctus (Many-banded krait)
|
P01445
|
3SA7A_NAJKA
|
LKCNKLIPLAYKTCPAGKNLCYKMFMVSNKTVPVKRGCIDVCPKNSLLVKYVCCNTDRCN
| null | null |
killing of cells of another organism [GO:0031640]
|
extracellular region [GO:0005576]; membrane [GO:0016020]; other organism cell membrane [GO:0044218]
|
toxin activity [GO:0090729]
| null |
2.10.60.10;
|
Snake three-finger toxin family, Short-chain subfamily, Type IA cytotoxin sub-subfamily
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:33915327, ECO:0000269|PubMed:7210030}. Target cell membrane {ECO:0000250|UniProtKB:P60301}.
| null | null | null | null | null |
FUNCTION: Monomer: shows cytolytic activity. {ECO:0000269|PubMed:18381281}.; FUNCTION: Heterodimer: has no cytolytic activity, but retains most of the alpha-cobratoxin capacity to compete with alpha-bungarotoxin for binding to Torpedo and alpha-7/CHRNA7 nicotinic acetylcholine receptors (nAChRs) as well as to Lymnea stagnalis acetylcholine-binding protein. {ECO:0000269|PubMed:18381281}.
|
Naja kaouthia (Monocled cobra) (Naja siamensis)
|
P01446
|
3SA3_NAJKA
|
LKCNKLIPLAYKTCPAGKNLCYKMFMVSNKTVPVKRGCIDACPKNSLLVKYVCCNTDRCN
| null | null |
killing of cells of another organism [GO:0031640]; modulation of process of another organism [GO:0035821]
|
extracellular region [GO:0005576]; membrane [GO:0016020]; other organism cell membrane [GO:0044218]
|
toxin activity [GO:0090729]
| null |
2.10.60.10;
|
Snake three-finger toxin family, Short-chain subfamily, Type IA cytotoxin sub-subfamily
|
PTM: May be regulated by glycosylation. {ECO:0000269|PubMed:15128311}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:33263003, ECO:0000269|PubMed:33915327, ECO:0000269|PubMed:7210030}. Target cell membrane {ECO:0000250|UniProtKB:P60301}.
| null | null | null | null | null |
FUNCTION: Heterodimer: has no cytolytic activity, but retains most of the alpha-cobratoxin capacity to compete with alpha-bungarotoxin for binding to Torpedo and alpha-7/CHRNA7 nicotinic acetylcholine receptors (nAChRs) as well as to Lymnea stagnalis acetylcholine-binding protein. {ECO:0000269|PubMed:18381281}.; FUNCTION: Monomer: shows cytolytic activity (PubMed:18381281). Exhibits concentration-dependent growth inhibitory effects in the lung cell lines A549 (IC(50)=1.22 ug/ml) and NL20 (IC(50)=2.76 ug/ml), in the prostate cell lines PC-3 (IC(50)=4.46 ug/ml) and RWPE-1 (IC(50)=0.65 ug/ml), and in the breast cell lines MCF-7 (IC(50)=12.23 ug/ml) and 184B5 (IC(50)=2.83 ug/ml), with high selectivity for the lung cancer cell line A549 (selectivity index=2.26) (PubMed:33263003). Induces primarily necrosis in the A549 cell line, and mainly late apoptosis in the MCF-7 and PC-3 cell lines (PubMed:33263003). {ECO:0000269|PubMed:18381281, ECO:0000269|PubMed:33263003}.
|
Naja kaouthia (Monocled cobra) (Naja siamensis)
|
P01484
|
SCX2_ANDAU
|
MNYLVMISLALLFVTGVESVKDGYIVDDVNCTYFCGRNAYCNEECTKLKGESGYCQWASPYGNACYCYKLPDHVRTKGPGRCHGR
| null | null |
defense response [GO:0006952]
|
extracellular region [GO:0005576]
|
sodium channel inhibitor activity [GO:0019871]; toxin activity [GO:0090729]
|
PF00537;
|
3.30.30.10;
|
Long (4 C-C) scorpion toxin superfamily, Sodium channel inhibitor family, Alpha subfamily
|
PTM: The amidation of His-83 is not necessary for toxicity. {ECO:0000269|PubMed:15725394}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:4342910}.
| null | null | null | null | null |
FUNCTION: Alpha toxins bind voltage-independently at site-3 of sodium channels (Nav) and inhibit the inactivation of the activated channels, thereby blocking neuronal transmission. The toxin principally slows the inactivation process of TTX-sensitive sodium channels (PubMed:23685008). It is active on rat brain Nav1.2/SCN2A sodium channel (EC(50)=2.6 nM) and on rat skeletal muscle Nav1.4/SCN4A sodium channel (EC(50)=2.2 nM) (PubMed:12911331), as well as on human neuronal Nav1.7/SCN9A (EC(50)=6.8 nM) (PubMed:23685008). This toxin is active against mammals. In vivo, intraplantar injection into mice induces spontaneous pain responses (PubMed:23685008). {ECO:0000269|PubMed:12911331, ECO:0000269|PubMed:23685008}.
|
Androctonus australis (Sahara scorpion)
|
P01485
|
SCX3_BUTOC
|
LVMAGVESVKDGYIVDDRNCTYFCGRNAYCNEECTKLKGESGYCQWASPYGNACYCYKVPDHVRTKGPGRCN
| null | null |
defense response [GO:0006952]
|
extracellular region [GO:0005576]
|
sodium channel inhibitor activity [GO:0019871]; toxin activity [GO:0090729]
|
PF00537;
|
3.30.30.10;
|
Long (4 C-C) scorpion toxin superfamily, Sodium channel inhibitor family, Alpha subfamily
|
PTM: When the toxin is not amidated, there are 75% loss of toxicity to mice, and total incapacity to bind rat brain synaptosomes. {ECO:0000269|PubMed:15062995}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.2}.
| null | null | null | null | null |
FUNCTION: Alpha toxins bind voltage-independently at site-3 of sodium channels (Nav) and inhibit the inactivation of the activated channels, thereby blocking neuronal transmission. Is active against mammals and binds with high affinity to rat brain synaptosomes. {ECO:0000269|PubMed:15062995}.
|
Buthus occitanus tunetanus (Common European scorpion) (Buthus tunetanus)
|
P01489
|
SCX4_LEIQU
|
GVRDAYIADDKNCVYTCGSNSYCNTECTKNGAESGYCQWLGKYGNACWCIKLPDKVPIRIPGKCR
| null | null |
defense response [GO:0006952]
|
extracellular region [GO:0005576]
|
sodium channel inhibitor activity [GO:0019871]; toxin activity [GO:0090729]
|
PF00537;
|
3.30.30.10;
|
Long (4 C-C) scorpion toxin superfamily, Sodium channel inhibitor family, Alpha subfamily
|
PTM: The recombinant toxin which is used for activity tests is not amidated (PubMed:37501371). However, C-terminal amidation does not appear to play an important role in activity, since the non-amidated recombinant toxin and the native toxin (which is amidated) show similar activities on all sodium channels tested. {ECO:0000269|PubMed:37501371}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:37501371, ECO:0000269|Ref.1}.
| null | null | null | null | null |
FUNCTION: Alpha toxins bind voltage-independently at site-3 of sodium channels (Nav) and inhibit the inactivation of the activated channels, thereby blocking neuronal transmission. Both native and recombinant (non-amidated) toxins inhibit inactivation of Nav1.2/SCN2A (EC(50)=31.2-36.6 nM), Nav1.6/SCN8A (EC(50)=6.9-8.9 nM), and Nav1.7/SCN9A (EC(50)=182.0-260.1 nM). {ECO:0000269|PubMed:37501371}.
|
Leiurus quinquestriatus quinquestriatus (Egyptian scorpion) (Deathstalker scorpion)
|
P01492
|
SCX1_CENSC
|
MNSLLIITACFALVGTVWAKEGYLVKKSDGCKYDCFWLGKNEHCDTECKAKNQGGSYGYCYAFACWCEGLPESTPTYPLPNKSCGKK
| null | null |
defense response [GO:0006952]
|
extracellular region [GO:0005576]
|
sodium channel inhibitor activity [GO:0019871]; toxin activity [GO:0090729]
|
PF00537;
|
3.30.30.10;
|
Long (4 C-C) scorpion toxin superfamily, Sodium channel inhibitor family, Beta subfamily
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:4460885}.
| null | null | null | null | null |
FUNCTION: Beta toxins bind voltage-independently at site-4 of sodium channels (Nav) and shift the voltage of activation toward more negative potentials thereby affecting sodium channel activation and promoting spontaneous and repetitive firing (By similarity). Induces immediate paralysis in crickets after injection, with a total paralysis occurring within 15-30 minutes and lasting for 1-2 hours. Is also lethal to vertebrate (chicks) when injected in very high dosages (more than 100 mg/kg). {ECO:0000250, ECO:0000269|PubMed:4460885}.
|
Centruroides sculpturatus (Arizona bark scorpion)
|
P01500
|
APAM_APIME
|
MISMLRCIYLFLSVILITSYFVTPVMPCNCKAPETALCARRCQQHG
| null | null |
modulation of process of another organism [GO:0035821]; negative regulation of inward rectifier potassium channel activity [GO:1903609]; negative regulation of potassium ion transmembrane transport [GO:1901380]; negative regulation of potassium ion transmembrane transporter activity [GO:1901017]
|
extracellular region [GO:0005576]
|
inward rectifier potassium channel inhibitor activity [GO:0070320]; potassium channel inhibitor activity [GO:0019870]; toxin activity [GO:0090729]
|
PF17454;
| null | null | null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:5601655, ECO:0000269|Ref.4}.
| null | null | null | null | null |
FUNCTION: Toxin with unique selectivity to KCa2 channels (PubMed:10696100, PubMed:11212219, PubMed:11533126, PubMed:17142458, PubMed:20562108, PubMed:32560481, PubMed:36188602, PubMed:6122211, PubMed:9287325, PubMed:9459560). Potently blocks human, rat and mouse KCa2.2/KCNN2/SK2 channels (IC(50)=27-140 pM), and moderately blocks human and rat KCa2.3/KCNN3/SK3 channels (IC(50)=0.6-4 nM), and human (IC(50)=0.7-12 nM) and mouse (IC(50)=28 nM) KCa2.1/KCNN1/SK1 channels (PubMed:10696100, PubMed:11212219, PubMed:11533126, PubMed:17142458, PubMed:20562108, PubMed:36188602, PubMed:9287325, PubMed:9459560). Does not show any antimicrobial activity (PubMed:36188602). In vivo, intracerebroventricular injection into rats of a dose of 1 ng results in neurodegeneration specifically in the Purkinje cells of the cerebellum, and induces seizures characterized by hypersensitivity to noise, loss of postural control, paroxystic jerking, and alternating periods of great agitation with tonic-clonic convulsions and periods of total prostration (PubMed:9459560). When administered at high doses, exerts anti-inflammatory, anti-oxidative, anti-fibrotic and anti-apoptotic properties in several models of inflammatory disease, including gouty arthritis, atherosclerosis, atopic dermatitis and acute kidney injury (PubMed:28958612, PubMed:32289477, PubMed:32560481, PubMed:33287398). Down-regulates pro-inflammatory signaling pathways, such as the NF-kappaB and STAT3 pathways, probably by blocking SK channels such as KCa2.2/KCNN2/SK2 and/or KCa2.3/KCNN3/SK3 which are thought to be involved in promoting some inflammatory responses (PubMed:28958612, PubMed:32289477, PubMed:32560481, PubMed:33287398). For example in mouse and rat microglia cells, inhibits LPS-activated KCa2.2/KCNN2/SK2 channels and TLR4 expression leading to the down-regulation of the NF-kappaB, STAT, and MAPK/ERK signaling pathways and, as a consequence, decreases secretion of pro-inflammatory cytokines (PubMed:32560481). {ECO:0000269|PubMed:10696100, ECO:0000269|PubMed:11212219, ECO:0000269|PubMed:11533126, ECO:0000269|PubMed:17142458, ECO:0000269|PubMed:19818752, ECO:0000269|PubMed:20562108, ECO:0000269|PubMed:28108814, ECO:0000269|PubMed:28958612, ECO:0000269|PubMed:32289477, ECO:0000269|PubMed:32560481, ECO:0000269|PubMed:33287398, ECO:0000269|PubMed:36188602, ECO:0000269|PubMed:6122211, ECO:0000269|PubMed:9287325, ECO:0000269|PubMed:9459560}.
|
Apis mellifera (Honeybee)
|
P01501
|
MEL_APIME
|
MKFLVNVALVFMVVYISYIYAAPEPEPAPEPEAEADAEADPEAGIGAVLKVLTTGLPALISWIKRKRQQG
| null | null |
killing of cells of another organism [GO:0031640]; localization [GO:0051179]; monoatomic ion transport [GO:0006811]
|
extracellular region [GO:0005576]; other organism cell membrane [GO:0044218]; pore complex [GO:0046930]
|
lipid binding [GO:0008289]; molecular function inhibitor activity [GO:0140678]; porin activity [GO:0015288]; protein kinase inhibitor activity [GO:0004860]; toxin activity [GO:0090729]
|
PF01372;
| null |
Melittin family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20403370, ECO:0000269|PubMed:20472009, ECO:0000269|PubMed:5592400}. Target cell membrane {ECO:0000269|PubMed:11509361, ECO:0000269|PubMed:456586, ECO:0000269|PubMed:6269667}. Note=Alpha-helical peptides form toroidal pores in the prey. {ECO:0000269|PubMed:11509361, ECO:0000269|PubMed:20403370, ECO:0000269|PubMed:20472009, ECO:0000269|PubMed:456586, ECO:0000269|PubMed:5592400, ECO:0000269|PubMed:6269667}.
| null | null | null | null | null |
FUNCTION: Melittin: Main toxin of bee venom with strong antimicrobial activity and hemolytic activity (PubMed:24512991, PubMed:4057243, PubMed:5139482, PubMed:5794226). It has enhancing effects on bee venom phospholipase A2 activity (PubMed:4371280). This amphipathic toxin binds to negatively charged membrane surface and forms pore by inserting into lipid bilayers inducing the leakage of ions and molecules and the enhancement of permeability that ultimately leads to cell lysis (PubMed:3666135, PubMed:4057243, PubMed:6830776). It acts as a voltage-gated pore with higher selectivity for anions over cations (PubMed:6269667). The ion conductance has been shown to be voltage-dependent (PubMed:7061434). Self-association of melittin in membranes is promoted by high ionic strength, but not by the presence of negatively charged lipids (PubMed:3443079). In vivo, intradermal injection into healthy human volunteers produce sharp pain sensation and an inflammatory response (PubMed:26983715). It produces pain by activating primary nociceptor cells directly and indirectly due to its ability to activate plasma membrane phospholipase A2 and its pore-forming activity (PubMed:26983715). In the context of inflammation and cancer tests, is highly cytotoxic to normal cells, highly induces calcium signaling and almost completely prevents cAMP production (PubMed:36548715). In addition, prevents LPS-induced nitric oxid (NO) synthesis but does not affect the IP3 signaling and pro-inflammatory activation of endothelial cells (PubMed:36548715). Also shows significant antiproliferative activity on the breast cancer cell line MDA-MB-231 (PubMed:36548715). {ECO:0000269|PubMed:24512991, ECO:0000269|PubMed:26983715, ECO:0000269|PubMed:3443079, ECO:0000269|PubMed:36548715, ECO:0000269|PubMed:3666135, ECO:0000269|PubMed:4057243, ECO:0000269|PubMed:4371280, ECO:0000269|PubMed:5139482, ECO:0000269|PubMed:5794226, ECO:0000269|PubMed:6269667, ECO:0000269|PubMed:6830776, ECO:0000269|PubMed:7061434}.; FUNCTION: Melittin-S: 1.4-fold less hemolytic and adopts a less organized secondary structure than melittin. {ECO:0000269|PubMed:20472009}.; FUNCTION: Melittin-2: Has strong hemolytic activity (PubMed:5139482). {ECO:0000305|PubMed:5139482}.
|
Apis mellifera (Honeybee)
|
P01521
|
CA1_CONMA
|
GRCCHPACGKNYSC
| null | null | null |
extracellular region [GO:0005576]; host cell postsynaptic membrane [GO:0035792]
|
acetylcholine receptor inhibitor activity [GO:0030550]; ion channel regulator activity [GO:0099106]; toxin activity [GO:0090729]
| null | null |
Conotoxin A superfamily
|
PTM: Amidated; synthetic peptide with a C-terminus free is 6-fold less active than the amidated peptide. {ECO:0000269|PubMed:10529206}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:7149738}.
| null | null | null | null | null |
FUNCTION: Alpha-conotoxins act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them (PubMed:10529206). Specifically blocks mammalian nAChR at the alpha-1/delta binding site (PubMed:10529206). Shows very low potency in blocking the alpha-1/gamma binding site (PubMed:10529206). {ECO:0000269|PubMed:10529206}.
|
Conus magus (Magical cone)
|
P01522
|
O16A_CONGE
|
MKLTCVVIVAVLLLTACQLITADDSRGTQKHRALGSTTELSLSTRCKSPGSSCSPTSYNCCRSCNPYTKRCYG
| null | null | null |
extracellular region [GO:0005576]; host cell presynaptic membrane [GO:0044231]
|
calcium channel regulator activity [GO:0005246]; ion channel inhibitor activity [GO:0008200]; toxin activity [GO:0090729]
|
PF02950;
| null |
Conotoxin O1 superfamily
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:6509012}.
| null | null | null | null | null |
FUNCTION: [Omega-conotoxin GVIA]: Omega-conotoxins act at presynaptic membranes, they bind and block voltage-gated calcium channels (Cav). This toxin blocks N-type calcium channels (Cav2.2/CACNA1B) with a high potency (it displaces [125I]GVIA with an IC(50)=3.7-38 pM) (PubMed:10938268, PubMed:11724570). {ECO:0000269|PubMed:10938268, ECO:0000269|PubMed:11724570}.
|
Conus geographus (Geography cone) (Nubecula geographus)
|
P01523
|
CM3A_CONGE
|
MMSKLGVLLTICLLLFPLTALPMDGDEPANRPVERMQDNISSEQYPLFEKRRDCCTPPKKCKDRQCKPQRCCAGR
| null | null | null |
extracellular region [GO:0005576]
|
sodium channel inhibitor activity [GO:0019871]; toxin activity [GO:0090729]
|
PF05374;
| null |
Conotoxin M superfamily
|
PTM: Hydroxylated; hydroxylations improve the ability to block Nav1.4/SCN4A sodium channels but does not affect folding. {ECO:0000269|PubMed:1991506, ECO:0000269|PubMed:2069951}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:6852238}.
| null | null | null | null | null |
FUNCTION: Mu-conotoxins block voltage-gated sodium channels (Nav). This toxin potently blocks rat Nav1.4/SCN4A (IC(50)= 19-110 nM) (PubMed:10627583, PubMed:1326324, PubMed:1654319, PubMed:21652775, PubMed:30360356). It also moderately blocks rNav1.1/SCN1A (Kd=260 nM), rNav1.2/SCN2A (IC(50)=2.7-17.8 uM), and mNav1.6/SCN8A (IC(50)=680 nM) (PubMed:10627583, PubMed:21652775). The inhibition is reversible. In vivo, induces paralysis to an isolated skeletal muscle preparation from frog (cutaneous pectoralis) within a few minutes (PubMed:2410412). {ECO:0000269|PubMed:10627583, ECO:0000269|PubMed:18950653, ECO:0000269|PubMed:21652775, ECO:0000269|PubMed:2410412, ECO:0000269|PubMed:30360356}.
|
Conus geographus (Geography cone) (Nubecula geographus)
|
P01525
|
NXB4_CERLA
|
ASATWGAAYPACENNCRKKYDLCIRCQGKWAGKRGKCAAHCIIQKNNCKGKCKKE
| null | null | null |
extracellular region [GO:0005576]
|
sodium channel inhibitor activity [GO:0019871]; toxin activity [GO:0090729]
|
PF07822;
|
1.10.287.120;
|
Worm B-toxin family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: This toxin increases the excitability of nerves by delaying the inactivation of the voltage-gated sodium channel (Nav). Only acts on some crustacean. Is more abundant, but 15-fold less toxic than neurotoxin B-II.
|
Cerebratulus lacteus (Milky ribbon worm) (Micrura lactea)
|
P01531
|
NA1B_ANTXA
|
GVPCLCDSDGPRPRGNTLSGILWFYPSGCPSGWHNCKAHGPNIGWCCKK
| null | null |
regulation of signal transduction [GO:0009966]
|
extracellular region [GO:0005576]; nematocyst [GO:0042151]
|
sodium channel regulator activity [GO:0017080]; toxin activity [GO:0090729]
|
PF00706;
|
2.20.20.10;
|
Sea anemone sodium channel inhibitory toxin family, Type I subfamily
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Nematocyst {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Binds specifically to voltage-gated sodium channels (Nav) (site 3), thereby delaying their inactivation. This toxin has the highest affinity of all anemone toxins for the mammalian sodium channel, whereas its paralog Anthopleurin-A retains the greatest capacity to discriminate between cardiac (Nav1.5/SCN5A) and neuronal sodium channels (PubMed:8916901). When tested electrophysiologically, this toxin exhibits a high affinity for multiple sodium channels with a 50-fold preference for rat cardiac (Nav1.5/SCN5A) over neuronal channels (0.1 nM versus 5 nM). When tested by ion flux, the affinities are similar and appear to have higher affinity (9 nM versus 22 nM) (PubMed:7612595, PubMed:8276803). The residue Lys-37 of this toxin has been shown to interact with channel Nav1.5 (residue Asp-1612 in rat and Asp-1610 in human), which is located in the DIV S3-S4 linker (corresponding to channel site 3) (PubMed:24898004, PubMed:9417050). Selectively modifies sodium channel inactivation from the open state with little effect on channel activation or on inactivation from closed states (By similarity). Does not display phospholipid-binding activities, suggesting that the domain IV S3-S4 linker is located at the extracellular surface and not buried in the phospholipid bilayer (PubMed:15632158). {ECO:0000250|UniProtKB:P01530, ECO:0000269|PubMed:15632158, ECO:0000269|PubMed:24898004, ECO:0000269|PubMed:7612595, ECO:0000269|PubMed:8276803, ECO:0000269|PubMed:8916901, ECO:0000269|PubMed:9306007, ECO:0000269|PubMed:9417050}.
|
Anthopleura xanthogrammica (Giant green sea anemone) (Actinia xanthogrammica)
|
P01535
|
STX3_ANESU
|
RSCCPCYWGGCPWGQNCYPEGCSGPKV
| null | null | null |
extracellular region [GO:0005576]; nematocyst [GO:0042151]
|
sodium channel inhibitor activity [GO:0019871]; toxin activity [GO:0090729]
|
PF08098;
| null |
Sea anemone short toxin (type III) family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Nematocyst {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Specific arthropod (crab and insect) toxin that inhibits inactivation of voltage-gated sodium channels. It competes well with the site-3 toxin LqhalphaIT (from the scorpion L.quinquestriatus (AC P17728)) on binding to cockroach neuronal membranes (Ki=21.4 nM), and inhibits the inactivation of D.melanogaster channel (DmNav1), but not that of mammalian Navs expressed in Xenopus oocytes. Its activity is synergically enhanced by ligands of receptor site-4 (Bj-xtrIT (AC P56637)). Its ability to inhibit the channel mutant DmNav1[D1701R] only decreases 5-fold, whereas the inhibition activity is completely lost by LqhalphaIT and Av2 when tested on DmNav1[D1701R]. {ECO:0000269|PubMed:17492942, ECO:0000269|PubMed:19609479, ECO:0000269|PubMed:2409523}.
|
Anemonia sulcata (Mediterranean snakelocks sea anemone)
|
P01555
|
CHTA_VIBCH
|
MVKIIFVFFIFLSSFSYANDDKLYRADSRPPDEIKQSGGLMPRGQSEYFDRGTQMNINLYDHARGTQTGFVRHDDGYVSTSISLRSAHLVGQTILSGHSTYYIYVIATAPNMFNVNDVLGAYSPHPDEQEVSALGGIPYSQIYGWYRVHFGVLDEQLHRNRGYRDRYYSNLDIAPAADGYGLAGFPPEHRAWREEPWIHHAPPGCGNAPRSSMSNTCDEKTQSLGVKFLDEYQSKVKRQIFSGYQSDIDTHNRIKDEL
|
2.4.2.-
| null |
localization [GO:0051179]; positive regulation of tyrosine phosphorylation of STAT protein [GO:0042531]
|
catalytic complex [GO:1902494]; extracellular space [GO:0005615]; periplasmic space [GO:0042597]
|
galactose binding [GO:0005534]; glycosyltransferase activity [GO:0016757]; lipid binding [GO:0008289]; nucleotidyltransferase activity [GO:0016779]; toxin activity [GO:0090729]
|
PF01375;
|
1.20.5.240;3.90.210.10;
|
Enterotoxin A family
| null | null | null | null | null | null | null |
FUNCTION: The A1 chain catalyzes the ADP-ribosylation of Gs alpha, a GTP-binding regulatory protein, to activate the adenylate cyclase. This leads to an overproduction of cAMP and eventually to a hypersecretion of chloride and bicarbonate followed by water, resulting in the characteristic cholera stool. The A2 chain tethers A1 to the pentameric ring.
|
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
|
P01556
|
CHTB_VIBCH
|
MIKLKFGVFFTVLLSSAYAHGTPQNITDLCAEYHNTQIYTLNDKIFSYTESLAGKREMAIITFKNGAIFQVEVPGSQHIDSQKKAIERMKDTLRIAYLTEAKVEKLCVWNNKTPHAIAAISMAN
| null | null |
positive regulation of tyrosine phosphorylation of STAT protein [GO:0042531]
|
catalytic complex [GO:1902494]; extracellular region [GO:0005576]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; periplasmic space [GO:0042597]
|
galactose binding [GO:0005534]; host cell surface binding [GO:0046812]; toxin activity [GO:0090729]
|
PF01376;
|
2.40.50.110;
| null | null |
SUBCELLULAR LOCATION: Secreted. Host cell membrane {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: The B subunit pentameric ring directs the A subunit to its target by binding to the GM1 gangliosides present on the surface of the intestinal epithelial cells. It can bind five GM1 gangliosides. It has no toxic activity by itself.
|
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
|
P01562
|
IFNA1_HUMAN
|
MASPFALLMVLVVLSCKSSCSLGCDLPETHSLDNRRTLMLLAQMSRISPSSCLMDRHDFGFPQEEFDGNQFQKAPAISVLHELIQQIFNLFTTKDSSAAWDEDLLDKFCTELYQQLNDLEACVMQEERVGETPLMNADSILAVKKYFRRITLYLTEKKYSPCAWEVVRAEIMRSLSLSTNLQERLRRKE
| null | null |
adaptive immune response [GO:0002250]; B cell differentiation [GO:0030183]; B cell proliferation [GO:0042100]; cellular response to virus [GO:0098586]; cytokine-mediated signaling pathway [GO:0019221]; defense response to virus [GO:0051607]; humoral immune response [GO:0006959]; natural killer cell activation involved in immune response [GO:0002323]; positive regulation of peptidyl-serine phosphorylation of STAT protein [GO:0033141]; response to exogenous dsRNA [GO:0043330]; T cell activation involved in immune response [GO:0002286]; type I interferon-mediated signaling pathway [GO:0060337]
|
extracellular region [GO:0005576]; extracellular space [GO:0005615]
|
cytokine activity [GO:0005125]; type I interferon receptor binding [GO:0005132]
|
PF00143;
|
1.20.1250.10;
|
Alpha/beta interferon family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Produced by macrophages, IFN-alpha have antiviral activities. Interferon stimulates the production of two enzymes: a protein kinase and an oligoadenylate synthetase. {ECO:0000269|PubMed:1634550}.
|
Homo sapiens (Human)
|
P01563
|
IFNA2_HUMAN
|
MALTFALLVALLVLSCKSSCSVGCDLPQTHSLGSRRTLMLLAQMRRISLFSCLKDRHDFGFPQEEFGNQFQKAETIPVLHEMIQQIFNLFSTKDSSAAWDETLLDKFYTELYQQLNDLEACVIQGVGVTETPLMKEDSILAVRKYFQRITLYLKEKKYSPCAWEVVRAEIMRSFSLSTNLQESLRSKE
| null | null |
adaptive immune response [GO:0002250]; apoptotic process [GO:0006915]; B cell differentiation [GO:0030183]; B cell proliferation [GO:0042100]; cell surface receptor signaling pathway [GO:0007166]; cell-cell signaling [GO:0007267]; cellular response to virus [GO:0098586]; cytokine-mediated signaling pathway [GO:0019221]; defense response to virus [GO:0051607]; humoral immune response [GO:0006959]; inflammatory response [GO:0006954]; natural killer cell activation involved in immune response [GO:0002323]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of gene expression [GO:0010629]; negative regulation of interleukin-13 production [GO:0032696]; negative regulation of interleukin-5 production [GO:0032714]; negative regulation of T cell differentiation [GO:0045581]; negative regulation of T-helper 2 cell cytokine production [GO:2000552]; negative regulation of viral entry into host cell [GO:0046597]; positive regulation of peptidyl-serine phosphorylation of STAT protein [GO:0033141]; receptor signaling pathway via STAT [GO:0097696]; response to exogenous dsRNA [GO:0043330]; T cell activation involved in immune response [GO:0002286]; type I interferon-mediated signaling pathway [GO:0060337]
|
collagen-containing extracellular matrix [GO:0062023]; extracellular region [GO:0005576]; extracellular space [GO:0005615]
|
cytokine activity [GO:0005125]; type I interferon receptor binding [GO:0005132]
|
PF00143;
|
1.20.1250.10;
|
Alpha/beta interferon family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:6159538}.
| null | null | null | null | null |
FUNCTION: Produced by macrophages, IFN-alpha have antiviral activities. {ECO:0000269|PubMed:6159538}.
|
Homo sapiens (Human)
|
P01566
|
IFN10_HUMAN
|
MALSFSLLMAVLVLSYKSICSLGCDLPQTHSLGNRRALILLGQMGRISPFSCLKDRHDFRIPQEEFDGNQFQKAQAISVLHEMIQQTFNLFSTEDSSAAWEQSLLEKFSTELYQQLNDLEACVIQEVGVEETPLMNEDSILAVRKYFQRITLYLIERKYSPCAWEVVRAEIMRSLSFSTNLQKRLRRKD
| null | null |
adaptive immune response [GO:0002250]; B cell differentiation [GO:0030183]; B cell proliferation [GO:0042100]; cellular response to virus [GO:0098586]; cytokine-mediated signaling pathway [GO:0019221]; defense response to virus [GO:0051607]; humoral immune response [GO:0006959]; natural killer cell activation involved in immune response [GO:0002323]; positive regulation of peptidyl-serine phosphorylation of STAT protein [GO:0033141]; response to exogenous dsRNA [GO:0043330]; T cell activation involved in immune response [GO:0002286]; type I interferon-mediated signaling pathway [GO:0060337]
|
extracellular region [GO:0005576]; extracellular space [GO:0005615]
|
cytokine activity [GO:0005125]; type I interferon receptor binding [GO:0005132]
|
PF00143;
|
1.20.1250.10;
|
Alpha/beta interferon family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Produced by macrophages, IFN-alpha have antiviral activities. Interferon stimulates the production of two enzymes: a protein kinase and an oligoadenylate synthetase.
|
Homo sapiens (Human)
|
P01567
|
IFNA7_HUMAN
|
MARSFSLLMVVLVLSYKSICSLGCDLPQTHSLRNRRALILLAQMGRISPFSCLKDRHEFRFPEEEFDGHQFQKTQAISVLHEMIQQTFNLFSTEDSSAAWEQSLLEKFSTELYQQLNDLEACVIQEVGVEETPLMNEDFILAVRKYFQRITLYLMEKKYSPCAWEVVRAEIMRSFSFSTNLKKGLRRKD
| null | null |
adaptive immune response [GO:0002250]; B cell differentiation [GO:0030183]; B cell proliferation [GO:0042100]; cell-cell signaling [GO:0007267]; cellular response to virus [GO:0098586]; cytokine-mediated signaling pathway [GO:0019221]; defense response to virus [GO:0051607]; humoral immune response [GO:0006959]; natural killer cell activation involved in immune response [GO:0002323]; positive regulation of peptidyl-serine phosphorylation of STAT protein [GO:0033141]; response to exogenous dsRNA [GO:0043330]; response to virus [GO:0009615]; T cell activation involved in immune response [GO:0002286]; type I interferon-mediated signaling pathway [GO:0060337]
|
extracellular region [GO:0005576]; extracellular space [GO:0005615]
|
cytokine activity [GO:0005125]; type I interferon receptor binding [GO:0005132]
|
PF00143;
|
1.20.1250.10;
|
Alpha/beta interferon family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Produced by macrophages, IFN-alpha have antiviral activities. Interferon stimulates the production of two enzymes: a protein kinase and an oligoadenylate synthetase.
|
Homo sapiens (Human)
|
P01568
|
IFN21_HUMAN
|
MALSFSLLMAVLVLSYKSICSLGCDLPQTHSLGNRRALILLAQMGRISPFSCLKDRHDFGFPQEEFDGNQFQKAQAISVLHEMIQQTFNLFSTKDSSATWEQSLLEKFSTELNQQLNDLEACVIQEVGVEETPLMNVDSILAVKKYFQRITLYLTEKKYSPCAWEVVRAEIMRSFSLSKIFQERLRRKE
| null | null |
adaptive immune response [GO:0002250]; B cell differentiation [GO:0030183]; B cell proliferation [GO:0042100]; cellular response to virus [GO:0098586]; cytokine-mediated signaling pathway [GO:0019221]; defense response to virus [GO:0051607]; humoral immune response [GO:0006959]; natural killer cell activation involved in immune response [GO:0002323]; positive regulation of peptidyl-serine phosphorylation of STAT protein [GO:0033141]; response to exogenous dsRNA [GO:0043330]; T cell activation involved in immune response [GO:0002286]; type I interferon-mediated signaling pathway [GO:0060337]
|
extracellular region [GO:0005576]; extracellular space [GO:0005615]
|
cytokine activity [GO:0005125]; cytokine receptor binding [GO:0005126]; type I interferon receptor binding [GO:0005132]
|
PF00143;
|
1.20.1250.10;
|
Alpha/beta interferon family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Produced by macrophages, IFN-alpha have antiviral activities. Interferon stimulates the production of two enzymes: a protein kinase and an oligoadenylate synthetase. {ECO:0000269|PubMed:1634550}.
|
Homo sapiens (Human)
|
P01569
|
IFNA5_HUMAN
|
MALPFVLLMALVVLNCKSICSLGCDLPQTHSLSNRRTLMIMAQMGRISPFSCLKDRHDFGFPQEEFDGNQFQKAQAISVLHEMIQQTFNLFSTKDSSATWDETLLDKFYTELYQQLNDLEACMMQEVGVEDTPLMNVDSILTVRKYFQRITLYLTEKKYSPCAWEVVRAEIMRSFSLSANLQERLRRKE
| null | null |
adaptive immune response [GO:0002250]; B cell differentiation [GO:0030183]; B cell proliferation [GO:0042100]; cellular response to virus [GO:0098586]; cytokine-mediated signaling pathway [GO:0019221]; defense response to virus [GO:0051607]; humoral immune response [GO:0006959]; natural killer cell activation involved in immune response [GO:0002323]; positive regulation of peptidyl-serine phosphorylation of STAT protein [GO:0033141]; response to exogenous dsRNA [GO:0043330]; T cell activation involved in immune response [GO:0002286]; type I interferon-mediated signaling pathway [GO:0060337]
|
extracellular region [GO:0005576]; extracellular space [GO:0005615]
|
cytokine activity [GO:0005125]; cytokine receptor binding [GO:0005126]; type I interferon receptor binding [GO:0005132]
|
PF00143;
|
1.20.1250.10;
|
Alpha/beta interferon family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Produced by macrophages, IFN-alpha have antiviral activities. Interferon stimulates the production of two enzymes: a protein kinase and an oligoadenylate synthetase.
|
Homo sapiens (Human)
|
P01570
|
IFN14_HUMAN
|
MALPFALMMALVVLSCKSSCSLGCNLSQTHSLNNRRTLMLMAQMRRISPFSCLKDRHDFEFPQEEFDGNQFQKAQAISVLHEMMQQTFNLFSTKNSSAAWDETLLEKFYIELFQQMNDLEACVIQEVGVEETPLMNEDSILAVKKYFQRITLYLMEKKYSPCAWEVVRAEIMRSLSFSTNLQKRLRRKD
| null | null |
adaptive immune response [GO:0002250]; B cell differentiation [GO:0030183]; B cell proliferation [GO:0042100]; cellular response to virus [GO:0098586]; cytokine-mediated signaling pathway [GO:0019221]; defense response to virus [GO:0051607]; humoral immune response [GO:0006959]; natural killer cell activation involved in immune response [GO:0002323]; positive regulation of peptidyl-serine phosphorylation of STAT protein [GO:0033141]; response to exogenous dsRNA [GO:0043330]; T cell activation involved in immune response [GO:0002286]; type I interferon-mediated signaling pathway [GO:0060337]
|
extracellular region [GO:0005576]; extracellular space [GO:0005615]
|
cytokine activity [GO:0005125]; cytokine receptor binding [GO:0005126]; type I interferon receptor binding [GO:0005132]
|
PF00143;
|
1.20.1250.10;
|
Alpha/beta interferon family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Produced by macrophages, IFN-alpha have antiviral activities. Interferon stimulates the production of two enzymes: a protein kinase and an oligoadenylate synthetase. {ECO:0000269|PubMed:1634550}.
|
Homo sapiens (Human)
|
P01571
|
IFN17_HUMAN
|
MALSFSLLMAVLVLSYKSICSLGCDLPQTHSLGNRRALILLAQMGRISPFSCLKDRHDFGLPQEEFDGNQFQKTQAISVLHEMIQQTFNLFSTEDSSAAWEQSLLEKFSTELYQQLNNLEACVIQEVGMEETPLMNEDSILAVRKYFQRITLYLTEKKYSPCAWEVVRAEIMRSLSFSTNLQKILRRKD
| null | null |
adaptive immune response [GO:0002250]; B cell differentiation [GO:0030183]; B cell proliferation [GO:0042100]; cellular response to virus [GO:0098586]; cytokine-mediated signaling pathway [GO:0019221]; defense response to virus [GO:0051607]; humoral immune response [GO:0006959]; natural killer cell activation involved in immune response [GO:0002323]; positive regulation of peptidyl-serine phosphorylation of STAT protein [GO:0033141]; response to exogenous dsRNA [GO:0043330]; response to virus [GO:0009615]; T cell activation involved in immune response [GO:0002286]; type I interferon-mediated signaling pathway [GO:0060337]
|
extracellular region [GO:0005576]; extracellular space [GO:0005615]
|
cytokine activity [GO:0005125]; type I interferon receptor binding [GO:0005132]
|
PF00143;
|
1.20.1250.10;
|
Alpha/beta interferon family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Produced by macrophages, IFN-alpha have antiviral activities. Interferon stimulates the production of two enzymes: a protein kinase and an oligoadenylate synthetase. {ECO:0000269|PubMed:1634550}.
|
Homo sapiens (Human)
|
P01572
|
IFNA1_MOUSE
|
MARLCAFLMVLAVLSYWPTCSLGCDLPQTHNLRNKRALTLLVQMRRLSPLSCLKDRKDFGFPQEKVDAQQIKKAQAIPVLSELTQQILNIFTSKDSSAAWNTTLLDSFCNDLHQQLNDLQGCLMQQVGVQEFPLTQEDALLAVRKYFHRITVYLREKKHSPCAWEVVRAEVWRALSSSANVLGRLREEK
| null | null |
adaptive immune response [GO:0002250]; B cell differentiation [GO:0030183]; B cell proliferation [GO:0042100]; cytokine-mediated signaling pathway [GO:0019221]; defense response to bacterium [GO:0042742]; defense response to virus [GO:0051607]; humoral immune response [GO:0006959]; natural killer cell activation involved in immune response [GO:0002323]; positive regulation of peptidyl-serine phosphorylation of STAT protein [GO:0033141]; regulation of defense response to virus by host [GO:0050691]; response to exogenous dsRNA [GO:0043330]; T cell activation involved in immune response [GO:0002286]; type I interferon-mediated signaling pathway [GO:0060337]
|
extracellular region [GO:0005576]; extracellular space [GO:0005615]
|
cytokine activity [GO:0005125]; type I interferon receptor binding [GO:0005132]
|
PF00143;
|
1.20.1250.10;
|
Alpha/beta interferon family
|
PTM: Glycosylated. {ECO:0000269|PubMed:15254193}.
|
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Produced by macrophages, IFN-alpha have antiviral activities. Interferon stimulates the production of two enzymes: a protein kinase and an oligoadenylate synthetase. {ECO:0000269|PubMed:15254193}.
|
Mus musculus (Mouse)
|
P01574
|
IFNB_HUMAN
|
MTNKCLLQIALLLCFSTTALSMSYNLLGFLQRSSNFQCQKLLWQLNGRLEYCLKDRMNFDIPEEIKQLQQFQKEDAALTIYEMLQNIFAIFRQDSSSTGWNETIVENLLANVYHQINHLKTVLEEKLEKEDFTRGKLMSSLHLKRYYGRILHYLKAKEYSHCAWTIVRVEILRNFYFINRLTGYLRN
| null | null |
adaptive immune response [GO:0002250]; B cell activation involved in immune response [GO:0002312]; B cell differentiation [GO:0030183]; B cell proliferation [GO:0042100]; cell surface receptor signaling pathway [GO:0007166]; cellular response to exogenous dsRNA [GO:0071360]; cellular response to interferon-beta [GO:0035458]; cellular response to virus [GO:0098586]; cytokine-mediated signaling pathway [GO:0019221]; defense response to virus [GO:0051607]; humoral immune response [GO:0006959]; innate immune response [GO:0045087]; natural killer cell activation [GO:0030101]; natural killer cell activation involved in immune response [GO:0002323]; negative regulation of Lewy body formation [GO:0140123]; negative regulation of T cell differentiation [GO:0045581]; negative regulation of T-helper 2 cell cytokine production [GO:2000552]; negative regulation of viral genome replication [GO:0045071]; neuron cellular homeostasis [GO:0070050]; positive regulation of apoptotic signaling pathway [GO:2001235]; positive regulation of autophagy [GO:0010508]; positive regulation of innate immune response [GO:0045089]; positive regulation of peptidyl-serine phosphorylation of STAT protein [GO:0033141]; positive regulation of transcription by RNA polymerase II [GO:0045944]; receptor signaling pathway via JAK-STAT [GO:0007259]; regulation of MHC class I biosynthetic process [GO:0045343]; response to exogenous dsRNA [GO:0043330]; response to virus [GO:0009615]; T cell activation involved in immune response [GO:0002286]; type I interferon-mediated signaling pathway [GO:0060337]
|
extracellular region [GO:0005576]; extracellular space [GO:0005615]
|
chloramphenicol O-acetyltransferase activity [GO:0008811]; cytokine activity [GO:0005125]; cytokine receptor binding [GO:0005126]; type I interferon receptor binding [GO:0005132]
|
PF00143;
|
1.20.1250.10;
|
Alpha/beta interferon family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:6157094}.
| null | null | null | null | null |
FUNCTION: Type I interferon cytokine that plays a key role in the innate immune response to infection, developing tumors and other inflammatory stimuli (PubMed:10049744, PubMed:10556041, PubMed:6157094, PubMed:6171735, PubMed:7665574, PubMed:8027027, PubMed:8969169). Signals via binding to high-affinity (IFNAR2) and low-affinity (IFNAR1) heterodimeric receptor, activating the canonical Jak-STAT signaling pathway resulting in transcriptional activation or repression of interferon-regulated genes that encode the effectors of the interferon response, such as antiviral proteins, regulators of cell proliferation and differentiation, and immunoregulatory proteins (PubMed:10049744, PubMed:10556041, PubMed:7665574, PubMed:8027027, PubMed:8969169). Signals mostly via binding to a IFNAR1-IFNAR2 heterodimeric receptor, but can also function with IFNAR1 alone and independently of Jak-STAT pathways (By similarity). Elicits a wide variety of responses, including antiviral and antibacterial activities, and can regulate the development of B-cells, myelopoiesis and lipopolysaccharide (LPS)-inducible production of tumor necrosis factor (By similarity). Plays a role in neuronal homeostasis by regulating dopamine turnover and protecting dopaminergic neurons: acts by promoting neuronal autophagy and alpha-synuclein clearance, thereby preventing dopaminergic neuron loss (By similarity). IFNB1 is more potent than interferon-alpha (IFN-alpha) in inducing the apoptotic and antiproliferative pathways required for control of tumor cell growth (By similarity). {ECO:0000250|UniProtKB:P01575, ECO:0000269|PubMed:10049744, ECO:0000269|PubMed:10556041, ECO:0000269|PubMed:6157094, ECO:0000269|PubMed:6171735, ECO:0000269|PubMed:7665574, ECO:0000269|PubMed:8027027, ECO:0000269|PubMed:8969169}.
|
Homo sapiens (Human)
|
P01575
|
IFNB_MOUSE
|
MNNRWILHAAFLLCFSTTALSINYKQLQLQERTNIRKCQELLEQLNGKINLTYRADFKIPMEMTEKMQKSYTAFAIQEMLQNVFLVFRNNFSSTGWNETIVVRLLDELHQQTVFLKTVLEEKQEERLTWEMSSTALHLKSYYWRVQRYLKLMKYNSYAWMVVRAEIFRNFLIIRRLTRNFQN
| null | null |
adaptive immune response [GO:0002250]; B cell differentiation [GO:0030183]; B cell proliferation [GO:0042100]; cellular response to dexamethasone stimulus [GO:0071549]; cellular response to dsRNA [GO:0071359]; cellular response to virus [GO:0098586]; cytokine-mediated signaling pathway [GO:0019221]; defense response to bacterium [GO:0042742]; defense response to virus [GO:0051607]; humoral immune response [GO:0006959]; macrophage activation involved in immune response [GO:0002281]; natural killer cell activation involved in immune response [GO:0002323]; negative regulation of blood-brain barrier permeability [GO:1905604]; negative regulation of cell adhesion molecule production [GO:0060354]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of immunoglobulin production [GO:0002638]; negative regulation of Lewy body formation [GO:0140123]; negative regulation of matrix metallopeptidase secretion [GO:1904465]; negative regulation of mononuclear cell migration [GO:0071676]; negative regulation of neuroinflammatory response [GO:0150079]; negative regulation of osteoclast differentiation [GO:0045671]; negative regulation of type II interferon production [GO:0032689]; neuron cellular homeostasis [GO:0070050]; positive regulation of autophagy [GO:0010508]; positive regulation of peptidyl-serine phosphorylation of STAT protein [GO:0033141]; positive regulation of transforming growth factor beta production [GO:0071636]; response to exogenous dsRNA [GO:0043330]; T cell activation involved in immune response [GO:0002286]; type I interferon-mediated signaling pathway [GO:0060337]
|
extracellular region [GO:0005576]; extracellular space [GO:0005615]
|
cytokine activity [GO:0005125]; type I interferon receptor binding [GO:0005132]
|
PF00143;
|
1.20.1250.10;
|
Alpha/beta interferon family
|
PTM: This beta interferon does not have a disulfide bond. {ECO:0000269|PubMed:1505514}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P01574}.
| null | null | null | null | null |
FUNCTION: Type I interferon cytokine that plays a key role in the innate immune response to infection, developing tumors and other inflammatory stimuli (PubMed:10708458, PubMed:23872679). Signals via binding to high-affinity (IFNAR2) and low-affinity (IFNAR1) heterodimeric receptor, activating the canonical Jak-STAT signaling pathway resulting in transcriptional activation or repression of interferon-regulated genes that encode the effectors of the interferon response, such as antiviral proteins, regulators of cell proliferation and differentiation, and immunoregulatory proteins (By similarity). Signals mostly via binding to a IFNAR1-IFNAR2 heterodimeric receptor, but can also function with IFNAR1 alone and independently of Jak-STAT pathways (PubMed:23872679). Elicits a wide variety of responses, including antiviral and antibacterial activities, and can regulate the development of B-cells, myelopoiesis and lipopolysaccharide (LPS)-inducible production of tumor necrosis factor (PubMed:10708458, PubMed:14597717). Plays a role in neuronal homeostasis by regulating dopamine turnover and protecting dopaminergic neurons: acts by promoting neuronal autophagy and alpha-synuclein clearance, thereby preventing dopaminergic neuron loss (PubMed:26451483). IFNB1 is more potent than interferon-alpha (IFN-alpha) in inducing the apoptotic and antiproliferative pathways required for control of tumor cell growth (PubMed:14597717). {ECO:0000250|UniProtKB:P01574, ECO:0000269|PubMed:10708458, ECO:0000269|PubMed:14597717, ECO:0000269|PubMed:23872679, ECO:0000269|PubMed:26451483}.
|
Mus musculus (Mouse)
|
P01579
|
IFNG_HUMAN
|
MKYTSYILAFQLCIVLGSLGCYCQDPYVKEAENLKKYFNAGHSDVADNGTLFLGILKNWKEESDRKIMQSQIVSFYFKLFKNFKDDQSIQKSVETIKEDMNVKFFNSNKKKRDDFEKLTNYSVTDLNVQRKAIHELIQVMAELSPAAKTGKRKRSQMLFRGRRASQ
| null | null |
adaptive immune response [GO:0002250]; apoptotic process [GO:0006915]; astrocyte activation [GO:0048143]; cell surface receptor signaling pathway [GO:0007166]; cellular response to virus [GO:0098586]; defense response to virus [GO:0051607]; extrinsic apoptotic signaling pathway [GO:0097191]; humoral immune response [GO:0006959]; macrophage activation involved in immune response [GO:0002281]; macrophage differentiation [GO:0030225]; microglial cell activation [GO:0001774]; negative regulation of amyloid-beta clearance [GO:1900222]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of epithelial cell differentiation [GO:0030857]; negative regulation of gene expression [GO:0010629]; negative regulation of interleukin-17 production [GO:0032700]; negative regulation of smooth muscle cell proliferation [GO:0048662]; negative regulation of tau-protein kinase activity [GO:1902948]; negative regulation of transcription by RNA polymerase II [GO:0000122]; neuroinflammatory response [GO:0150076]; positive regulation of amyloid-beta formation [GO:1902004]; positive regulation of autophagy [GO:0010508]; positive regulation of calcidiol 1-monooxygenase activity [GO:0060559]; positive regulation of CD4-positive, CD25-positive, alpha-beta regulatory T cell differentiation involved in immune response [GO:0032834]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of cellular respiration [GO:1901857]; positive regulation of chemokine production [GO:0032722]; positive regulation of core promoter binding [GO:1904798]; positive regulation of cytokine production [GO:0001819]; positive regulation of epithelial cell migration [GO:0010634]; positive regulation of exosomal secretion [GO:1903543]; positive regulation of fructose 1,6-bisphosphate 1-phosphatase activity [GO:0060550]; positive regulation of fructose 1,6-bisphosphate metabolic process [GO:0060552]; positive regulation of gene expression [GO:0010628]; positive regulation of glycolytic process [GO:0045821]; positive regulation of inflammatory response [GO:0050729]; positive regulation of interleukin-1 beta production [GO:0032731]; positive regulation of interleukin-12 production [GO:0032735]; positive regulation of interleukin-23 production [GO:0032747]; positive regulation of interleukin-6 production [GO:0032755]; positive regulation of iron ion import across plasma membrane [GO:1904440]; positive regulation of killing of cells of another organism [GO:0051712]; positive regulation of membrane protein ectodomain proteolysis [GO:0051044]; positive regulation of MHC class II biosynthetic process [GO:0045348]; positive regulation of neurogenesis [GO:0050769]; positive regulation of nitric oxide biosynthetic process [GO:0045429]; positive regulation of nitric-oxide synthase biosynthetic process [GO:0051770]; positive regulation of nitrogen compound metabolic process [GO:0051173]; positive regulation of NMDA glutamate receptor activity [GO:1904783]; positive regulation of osteoclast differentiation [GO:0045672]; positive regulation of peptidyl-serine phosphorylation of STAT protein [GO:0033141]; positive regulation of phagocytosis [GO:0050766]; positive regulation of protein deacetylation [GO:0090312]; positive regulation of protein import into nucleus [GO:0042307]; positive regulation of protein localization to plasma membrane [GO:1903078]; positive regulation of protein serine/threonine kinase activity [GO:0071902]; positive regulation of protein-containing complex assembly [GO:0031334]; positive regulation of signaling receptor activity [GO:2000273]; positive regulation of smooth muscle cell apoptotic process [GO:0034393]; positive regulation of tumor necrosis factor (ligand) superfamily member 11 production [GO:2000309]; positive regulation of tumor necrosis factor production [GO:0032760]; positive regulation of tyrosine phosphorylation of STAT protein [GO:0042531]; positive regulation of vitamin D biosynthetic process [GO:0060557]; receptor signaling pathway via JAK-STAT [GO:0007259]; regulation of insulin secretion [GO:0050796]; response to virus [GO:0009615]; type II interferon-mediated signaling pathway [GO:0060333]; type III interferon-mediated signaling pathway [GO:0038196]
|
extracellular region [GO:0005576]; extracellular space [GO:0005615]
|
cytokine activity [GO:0005125]; type II interferon receptor binding [GO:0005133]
|
PF00714;
|
1.20.1250.10;
|
Type II (or gamma) interferon family
|
PTM: Proteolytic processing produces C-terminal heterogeneity, with proteins ending alternatively at Gly-150, Met-157 or Gly-161. {ECO:0000269|PubMed:3109913}.
|
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Type II interferon produced by immune cells such as T-cells and NK cells that plays crucial roles in antimicrobial, antiviral, and antitumor responses by activating effector immune cells and enhancing antigen presentation (PubMed:16914093, PubMed:8666937). Primarily signals through the JAK-STAT pathway after interaction with its receptor IFNGR1 to affect gene regulation (PubMed:8349687). Upon IFNG binding, IFNGR1 intracellular domain opens out to allow association of downstream signaling components JAK2, JAK1 and STAT1, leading to STAT1 activation, nuclear translocation and transcription of IFNG-regulated genes. Many of the induced genes are transcription factors such as IRF1 that are able to further drive regulation of a next wave of transcription (PubMed:16914093). Plays a role in class I antigen presentation pathway by inducing a replacement of catalytic proteasome subunits with immunoproteasome subunits (PubMed:8666937). In turn, increases the quantity, quality, and repertoire of peptides for class I MHC loading (PubMed:8163024). Increases the efficiency of peptide generation also by inducing the expression of activator PA28 that associates with the proteasome and alters its proteolytic cleavage preference (PubMed:11112687). Up-regulates as well MHC II complexes on the cell surface by promoting expression of several key molecules such as cathepsins B/CTSB, H/CTSH, and L/CTSL (PubMed:7729559). Participates in the regulation of hematopoietic stem cells during development and under homeostatic conditions by affecting their development, quiescence, and differentiation (By similarity). {ECO:0000250|UniProtKB:P01580, ECO:0000269|PubMed:11112687, ECO:0000269|PubMed:16914093, ECO:0000269|PubMed:7729559, ECO:0000269|PubMed:8163024, ECO:0000269|PubMed:8349687, ECO:0000269|PubMed:8666937}.
|
Homo sapiens (Human)
|
P01580
|
IFNG_MOUSE
|
MNATHCILALQLFLMAVSGCYCHGTVIESLESLNNYFNSSGIDVEEKSLFLDIWRNWQKDGDMKILQSQIISFYLRLFEVLKDNQAISNNISVIESHLITTFFSNSKAKKDAFMSIAKFEVNNPQVQRQAFNELIRVVHQLLPESSLRKRKRSRC
| null | null |
adaptive immune response [GO:0002250]; antigen processing and presentation [GO:0019882]; apoptotic process [GO:0006915]; astrocyte activation [GO:0048143]; CD8-positive, alpha-beta T cell differentiation involved in immune response [GO:0002302]; cellular response to interleukin-18 [GO:0071351]; cellular response to lipopolysaccharide [GO:0071222]; defense response to bacterium [GO:0042742]; defense response to Gram-positive bacterium [GO:0050830]; defense response to protozoan [GO:0042832]; defense response to virus [GO:0051607]; endoplasmic reticulum unfolded protein response [GO:0030968]; humoral immune response [GO:0006959]; inflammatory cell apoptotic process [GO:0006925]; microglial cell activation [GO:0001774]; negative regulation of amyloid-beta clearance [GO:1900222]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of epithelial cell differentiation [GO:0030857]; negative regulation of fibroblast proliferation [GO:0048147]; negative regulation of gene expression [GO:0010629]; negative regulation of glomerular mesangial cell proliferation [GO:0072125]; negative regulation of myelination [GO:0031642]; negative regulation of osteoclast differentiation [GO:0045671]; negative regulation of transcription by RNA polymerase II [GO:0000122]; neuroinflammatory response [GO:0150076]; neutrophil apoptotic process [GO:0001781]; neutrophil chemotaxis [GO:0030593]; nitric oxide biosynthetic process [GO:0006809]; positive regulation by host of viral process [GO:0044794]; positive regulation of amyloid-beta formation [GO:1902004]; positive regulation of apoptotic process [GO:0043065]; positive regulation of autophagy [GO:0010508]; positive regulation of cell adhesion [GO:0045785]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of cellular respiration [GO:1901857]; positive regulation of chemokine production [GO:0032722]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of gene expression [GO:0010628]; positive regulation of glycolytic process [GO:0045821]; positive regulation of interleukin-1 beta production [GO:0032731]; positive regulation of interleukin-12 production [GO:0032735]; positive regulation of interleukin-6 production [GO:0032755]; positive regulation of iron ion import across plasma membrane [GO:1904440]; positive regulation of isotype switching to IgG isotypes [GO:0048304]; positive regulation of macrophage cytokine production [GO:0060907]; positive regulation of MHC class II biosynthetic process [GO:0045348]; positive regulation of neuron differentiation [GO:0045666]; positive regulation of nitric oxide biosynthetic process [GO:0045429]; positive regulation of nitric-oxide synthase biosynthetic process [GO:0051770]; positive regulation of nitrogen compound metabolic process [GO:0051173]; positive regulation of peptidyl-serine phosphorylation of STAT protein [GO:0033141]; positive regulation of phagocytosis [GO:0050766]; positive regulation of protein deacetylation [GO:0090312]; positive regulation of signaling receptor activity [GO:2000273]; positive regulation of synaptic transmission, cholinergic [GO:0032224]; positive regulation of T cell proliferation [GO:0042102]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of tumor necrosis factor production [GO:0032760]; positive regulation of tyrosine phosphorylation of STAT protein [GO:0042531]; receptor signaling pathway via JAK-STAT [GO:0007259]; regulation of defense response to virus by host [GO:0050691]; regulation of DNA-templated transcription [GO:0006355]; regulation of glial cell proliferation [GO:0060251]; regulation of hepatocyte proliferation [GO:2000345]; regulation of immune response [GO:0050776]; regulation of neuronal action potential [GO:0098908]; regulation of the force of heart contraction [GO:0002026]; response to tacrolimus [GO:1901327]; response to virus [GO:0009615]; response to xenobiotic stimulus [GO:0009410]; sensory perception of mechanical stimulus [GO:0050954]; T cell proliferation [GO:0042098]; T cell receptor signaling pathway [GO:0050852]; type II interferon-mediated signaling pathway [GO:0060333]
|
external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; perikaryon [GO:0043204]
|
cytokine activity [GO:0005125]; type II interferon receptor binding [GO:0005133]
|
PF00714;
|
1.20.1250.10;
|
Type II (or gamma) interferon family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P01579}.
| null | null | null | null | null |
FUNCTION: Type II interferon produced by immune cells such as T-cells and NK cells that plays crucial roles in antimicrobial, antiviral, and antitumor responses by activating effector immune cells and enhancing antigen presentation (PubMed:11585387, PubMed:8456301). Primarily signals through the JAK-STAT pathway after interaction with its receptor IFNGR1 to affect gene regulation. Upon IFNG binding, IFNGR1 intracellular domain opens out to allow association of downstream signaling components JAK2, JAK1 and STAT1, leading to STAT1 activation, nuclear translocation and transcription of IFNG-regulated genes. Many of the induced genes are transcription factors such as IRF1 that are able to further drive regulation of a next wave of transcription. Plays a role in class I antigen presentation pathway by inducing a replacement of catalytic proteasome subunits with immunoproteasome subunits. In turn, increases the quantity, quality, and repertoire of peptides for class I MHC loading. Increases the efficiency of peptide generation also by inducing the expression of activator PA28 that associates with the proteasome and alters its proteolytic cleavage preference. Up-regulates as well MHC II complexes on the cell surface by promoting expression of several key molecules such as cathepsins B/CTSB, H/CTSH, and L/CTSL (By similarity). Participates in the regulation of hematopoietic stem cells during development and under homeostatic conditions by affecting their development, quiescence, and differentiation (PubMed:20535209, PubMed:25078851). {ECO:0000250|UniProtKB:P01579, ECO:0000269|PubMed:11585387, ECO:0000269|PubMed:20535209, ECO:0000269|PubMed:25078851, ECO:0000269|PubMed:8456301}.
|
Mus musculus (Mouse)
|
P01581
|
IFNG_RAT
|
MSATRRVLVLQLCLMALSGCYCQGTLIESLESLKNYFNSSSMDAMEGKSLLLDIWRNWQKDGNTKILESQIISFYLRLFEVLKDNQAISNNISVIESHLITNFFSNSKAKKDAFMSIAKFEVNNPQIQHKAVNELIRVIHQLSPESSLRKRKRSRC
| null | null |
adaptive immune response [GO:0002250]; antigen processing and presentation [GO:0019882]; apoptotic process [GO:0006915]; astrocyte activation [GO:0048143]; CD8-positive, alpha-beta T cell differentiation involved in immune response [GO:0002302]; cellular response to interleukin-18 [GO:0071351]; cellular response to lipopolysaccharide [GO:0071222]; defense response to bacterium [GO:0042742]; defense response to Gram-positive bacterium [GO:0050830]; defense response to protozoan [GO:0042832]; defense response to virus [GO:0051607]; endoplasmic reticulum unfolded protein response [GO:0030968]; extrinsic apoptotic signaling pathway [GO:0097191]; humoral immune response [GO:0006959]; inflammatory cell apoptotic process [GO:0006925]; macrophage activation involved in immune response [GO:0002281]; macrophage differentiation [GO:0030225]; microglial cell activation [GO:0001774]; negative regulation of amyloid-beta clearance [GO:1900222]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of epithelial cell differentiation [GO:0030857]; negative regulation of fibroblast proliferation [GO:0048147]; negative regulation of gene expression [GO:0010629]; negative regulation of glomerular mesangial cell proliferation [GO:0072125]; negative regulation of interleukin-17 production [GO:0032700]; negative regulation of myelination [GO:0031642]; negative regulation of osteoclast differentiation [GO:0045671]; negative regulation of smooth muscle cell proliferation [GO:0048662]; negative regulation of transcription by RNA polymerase II [GO:0000122]; neuroinflammatory response [GO:0150076]; neutrophil apoptotic process [GO:0001781]; neutrophil chemotaxis [GO:0030593]; nitric oxide biosynthetic process [GO:0006809]; positive regulation by host of viral process [GO:0044794]; positive regulation of amyloid-beta formation [GO:1902004]; positive regulation of apoptotic process [GO:0043065]; positive regulation of autophagy [GO:0010508]; positive regulation of CD4-positive, CD25-positive, alpha-beta regulatory T cell differentiation involved in immune response [GO:0032834]; positive regulation of cell adhesion [GO:0045785]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of cellular respiration [GO:1901857]; positive regulation of chemokine production [GO:0032722]; positive regulation of cytokine production [GO:0001819]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of epithelial cell migration [GO:0010634]; positive regulation of fructose 1,6-bisphosphate metabolic process [GO:0060552]; positive regulation of gene expression [GO:0010628]; positive regulation of glycolytic process [GO:0045821]; positive regulation of inflammatory response [GO:0050729]; positive regulation of interleukin-1 beta production [GO:0032731]; positive regulation of interleukin-12 production [GO:0032735]; positive regulation of interleukin-23 production [GO:0032747]; positive regulation of interleukin-6 production [GO:0032755]; positive regulation of iron ion import across plasma membrane [GO:1904440]; positive regulation of isotype switching to IgG isotypes [GO:0048304]; positive regulation of killing of cells of another organism [GO:0051712]; positive regulation of macrophage cytokine production [GO:0060907]; positive regulation of membrane protein ectodomain proteolysis [GO:0051044]; positive regulation of MHC class II biosynthetic process [GO:0045348]; positive regulation of neurogenesis [GO:0050769]; positive regulation of neuron differentiation [GO:0045666]; positive regulation of nitric oxide biosynthetic process [GO:0045429]; positive regulation of nitric-oxide synthase biosynthetic process [GO:0051770]; positive regulation of nitrogen compound metabolic process [GO:0051173]; positive regulation of NMDA glutamate receptor activity [GO:1904783]; positive regulation of osteoclast differentiation [GO:0045672]; positive regulation of peptidyl-serine phosphorylation of STAT protein [GO:0033141]; positive regulation of phagocytosis [GO:0050766]; positive regulation of protein deacetylation [GO:0090312]; positive regulation of protein import into nucleus [GO:0042307]; positive regulation of protein-containing complex assembly [GO:0031334]; positive regulation of smooth muscle cell apoptotic process [GO:0034393]; positive regulation of synaptic transmission, cholinergic [GO:0032224]; positive regulation of T cell proliferation [GO:0042102]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of tumor necrosis factor (ligand) superfamily member 11 production [GO:2000309]; positive regulation of tumor necrosis factor production [GO:0032760]; positive regulation of tyrosine phosphorylation of STAT protein [GO:0042531]; positive regulation of vitamin D biosynthetic process [GO:0060557]; receptor signaling pathway via JAK-STAT [GO:0007259]; regulation of defense response to virus by host [GO:0050691]; regulation of DNA-templated transcription [GO:0006355]; regulation of glial cell proliferation [GO:0060251]; regulation of hepatocyte proliferation [GO:2000345]; regulation of immune response [GO:0050776]; regulation of insulin secretion [GO:0050796]; regulation of neuronal action potential [GO:0098908]; regulation of the force of heart contraction [GO:0002026]; response to tacrolimus [GO:1901327]; response to virus [GO:0009615]; response to xenobiotic stimulus [GO:0009410]; sensory perception of mechanical stimulus [GO:0050954]; T cell proliferation [GO:0042098]; T cell receptor signaling pathway [GO:0050852]; type II interferon-mediated signaling pathway [GO:0060333]; type III interferon-mediated signaling pathway [GO:0038196]
|
external side of plasma membrane [GO:0009897]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; perikaryon [GO:0043204]
|
cytokine activity [GO:0005125]; type II interferon receptor binding [GO:0005133]
|
PF00714;
|
1.20.1250.10;
|
Type II (or gamma) interferon family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P01579}.
| null | null | null | null | null |
FUNCTION: Type II interferon produced by immune cells such as T-cells and NK cells that plays crucial roles in antimicrobial, antiviral, and antitumor responses by activating effector immune cells and enhancing antigen presentation. Primarily signals through the JAK-STAT pathway after interaction with its receptor IFNGR1 to affect gene regulation. Upon IFNG binding, IFNGR1 intracellular domain opens out to allow association of downstream signaling components JAK2, JAK1 and STAT1, leading to STAT1 activation, nuclear translocation and transcription of IFNG-regulated genes. Many of the induced genes are transcription factors such as IRF1 that are able to further drive regulation of a next wave of transcription. Plays a role in class I antigen presentation pathway by inducing a replacement of catalytic proteasome subunits with immunoproteasome subunits. In turn, increases the quantity, quality, and repertoire of peptides for class I MHC loading. Increases the efficiency of peptide generation also by inducing the expression of activator PA28 that associates with the proteasome and alters its proteolytic cleavage preference. Up-regulates as well MHC II complexes on the cell surface by promoting expression of several key molecules such as cathepsins B/CTSB, H/CTSH, and L/CTSL (By similarity). Participates in the regulation of hematopoietic stem cells during development and under homeostatic conditions by affecting their development, quiescence, and differentiation (By similarity). {ECO:0000250|UniProtKB:P01579, ECO:0000250|UniProtKB:P01580}.
|
Rattus norvegicus (Rat)
|
P01582
|
IL1A_MOUSE
|
MAKVPDLFEDLKNCYSENEDYSSAIDHLSLNQKSFYDASYGSLHETCTDQFVSLRTSETSKMSNFTFKESRVTVSATSSNGKILKKRRLSFSETFTEDDLQSITHDLEETIQPRSAPYTYQSDLRYKLMKLVRQKFVMNDSLNQTIYQDVDKHYLSTTWLNDLQQEVKFDMYAYSSGGDDSKYPVTLKISDSQLFVSAQGEDQPVLLKELPETPKLITGSETDLIFFWKSINSKNYFTSAAYPELFIATKEQSRVHLARGLPSMTDFQIS
| null | null |
cellular response to heat [GO:0034605]; cellular response to lipopolysaccharide [GO:0071222]; connective tissue replacement involved in inflammatory response wound healing [GO:0002248]; cytokine-mediated signaling pathway [GO:0019221]; ectopic germ cell programmed cell death [GO:0035234]; extrinsic apoptotic signaling pathway in absence of ligand [GO:0097192]; fever generation [GO:0001660]; heart development [GO:0007507]; immune response [GO:0006955]; inflammatory response [GO:0006954]; intracellular sodium ion homeostasis [GO:0006883]; keratinization [GO:0031424]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of establishment of Sertoli cell barrier [GO:1904445]; positive regulation of angiogenesis [GO:0045766]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of cell division [GO:0051781]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of gene expression [GO:0010628]; positive regulation of immature T cell proliferation in thymus [GO:0033092]; positive regulation of interleukin-2 production [GO:0032743]; positive regulation of interleukin-6 production [GO:0032755]; positive regulation of JNK cascade [GO:0046330]; positive regulation of mitotic nuclear division [GO:0045840]; positive regulation of neutrophil migration [GO:1902624]; positive regulation of prostaglandin secretion [GO:0032308]; positive regulation of protein secretion [GO:0050714]; positive regulation of steroid biosynthetic process [GO:0010893]; positive regulation of stress-activated MAPK cascade [GO:0032874]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of tumor necrosis factor production [GO:0032760]; positive regulation of vascular endothelial growth factor production [GO:0010575]; regulation of actin cytoskeleton organization [GO:0032956]; response to copper ion [GO:0046688]; response to gamma radiation [GO:0010332]; response to hypoxia [GO:0001666]; response to L-ascorbic acid [GO:0033591]; response to organonitrogen compound [GO:0010243]; response to ozone [GO:0010193]; spermatogenesis [GO:0007283]
|
cell surface [GO:0009986]; cytosol [GO:0005829]; extracellular space [GO:0005615]; nucleus [GO:0005634]
|
copper ion binding [GO:0005507]; cytokine activity [GO:0005125]; interleukin-1 receptor binding [GO:0005149]
|
PF00340;PF02394;
|
2.80.10.50;
|
IL-1 family
|
PTM: Acetylated within its nuclear localization sequence, which impacts subcellular localization. {ECO:0000250|UniProtKB:P01583}.; PTM: Proteolytic processed by CAPN1 in a calcium-dependent manner. Cleavage from 31 kDa precursor to 18 kDa biologically active molecules. {ECO:0000250|UniProtKB:P01583}.; PTM: Phosphorylated. Phosphorylation greatly enhances susceptibility to digestion and promotes the conversion of pre-IL1A alpha to the biologically active IL1A. {ECO:0000250|UniProtKB:P01583}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P01583}. Cytoplasm {ECO:0000250|UniProtKB:P01583}. Secreted {ECO:0000250|UniProtKB:P01583}. Note=The lack of a specific hydrophobic segment in the precursor sequence suggests that IL-1 is released by damaged cells or is secreted by a mechanism differing from that used for other secretory proteins. The secretion is dependent on protein unfolding and facilitated by the cargo receptor TMED10; it results in protein translocation from the cytoplasm into the ERGIC (endoplasmic reticulum-Golgi intermediate compartment) followed by vesicle entry and secretion. Recruited to DNA damage sites and secreted after genotoxic stress. {ECO:0000250|UniProtKB:P01583}.
| null | null | null | null | null |
FUNCTION: Cytokine constitutively present intracellularly in nearly all resting non-hematopoietic cells that plays an important role in inflammation and bridges the innate and adaptive immune systems (PubMed:16256210). After binding to its receptor IL1R1 together with its accessory protein IL1RAP, forms the high affinity interleukin-1 receptor complex. Signaling involves the recruitment of adapter molecules such as MYD88, IRAK1 or IRAK4. In turn, mediates the activation of NF-kappa-B and the three MAPK pathways p38, p42/p44 and JNK pathways (PubMed:1386364). Within the cell, acts as an alarmin and cell death results in its liberation in the extracellular space after disruption of the cell membrane to induce inflammation and alert the host to injury or damage. In addition to its role as a danger signal, which occurs when the cytokine is passively released by cell necrosis, directly senses DNA damage and acts as a signal for genotoxic stress without loss of cell integrity (By similarity). {ECO:0000250|UniProtKB:P01583, ECO:0000269|PubMed:1386364, ECO:0000269|PubMed:16256210}.
|
Mus musculus (Mouse)
|
P01583
|
IL1A_HUMAN
|
MAKVPDMFEDLKNCYSENEEDSSSIDHLSLNQKSFYHVSYGPLHEGCMDQSVSLSISETSKTSKLTFKESMVVVATNGKVLKKRRLSLSQSITDDDLEAIANDSEEEIIKPRSAPFSFLSNVKYNFMRIIKYEFILNDALNQSIIRANDQYLTAAALHNLDEAVKFDMGAYKSSKDDAKITVILRISKTQLYVTAQDEDQPVLLKEMPEIPKTITGSETNLLFFWETHGTKNYFTSVAHPNLFIATKQDYWVCLAGGPPSITDFQILENQA
| null | null |
apoptotic process [GO:0006915]; cellular response to heat [GO:0034605]; cellular response to lipopolysaccharide [GO:0071222]; connective tissue replacement involved in inflammatory response wound healing [GO:0002248]; cytokine-mediated signaling pathway [GO:0019221]; ectopic germ cell programmed cell death [GO:0035234]; extrinsic apoptotic signaling pathway in absence of ligand [GO:0097192]; fever generation [GO:0001660]; heart development [GO:0007507]; immune response [GO:0006955]; inflammatory response [GO:0006954]; intracellular sodium ion homeostasis [GO:0006883]; keratinization [GO:0031424]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of establishment of Sertoli cell barrier [GO:1904445]; negative regulation of extrinsic apoptotic signaling pathway in absence of ligand [GO:2001240]; positive regulation of angiogenesis [GO:0045766]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of cell division [GO:0051781]; positive regulation of cytokine production [GO:0001819]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of gene expression [GO:0010628]; positive regulation of immature T cell proliferation in thymus [GO:0033092]; positive regulation of interleukin-2 production [GO:0032743]; positive regulation of interleukin-6 production [GO:0032755]; positive regulation of JNK cascade [GO:0046330]; positive regulation of mitotic nuclear division [GO:0045840]; positive regulation of neutrophil migration [GO:1902624]; positive regulation of prostaglandin secretion [GO:0032308]; positive regulation of protein secretion [GO:0050714]; positive regulation of steroid biosynthetic process [GO:0010893]; positive regulation of stress-activated MAPK cascade [GO:0032874]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of tumor necrosis factor production [GO:0032760]; positive regulation of vascular endothelial growth factor production [GO:0010575]; regulation of actin cytoskeleton organization [GO:0032956]; response to copper ion [GO:0046688]; response to gamma radiation [GO:0010332]; response to hypoxia [GO:0001666]; response to L-ascorbic acid [GO:0033591]; response to organonitrogen compound [GO:0010243]; response to ozone [GO:0010193]; spermatogenesis [GO:0007283]
|
cell surface [GO:0009986]; cytosol [GO:0005829]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; nucleus [GO:0005634]
|
copper ion binding [GO:0005507]; cytokine activity [GO:0005125]; interleukin-1 receptor binding [GO:0005149]
|
PF00340;PF02394;
|
2.80.10.50;
|
IL-1 family
|
PTM: Acetylated within its nuclear localization sequence, which impacts subcellular localization. {ECO:0000269|PubMed:26439902}.; PTM: Proteolytic processed by CAPN1 in a calcium-dependent manner. Cleavage from 31 kDa precursor to 18 kDa biologically active molecules. {ECO:0000269|PubMed:2115174}.; PTM: Phosphorylated. Phosphorylation greatly enhances susceptibility to digestion and promotes the conversion of pre-IL1A alpha to the biologically active IL1A. {ECO:0000269|PubMed:3258335}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26439902}. Cytoplasm {ECO:0000269|PubMed:32272059}. Secreted {ECO:0000269|PubMed:26439902}. Note=The lack of a specific hydrophobic segment in the precursor sequence suggests that IL-1 is released by damaged cells or is secreted by a mechanism differing from that used for other secretory proteins. The secretion is dependent on protein unfolding and facilitated by the cargo receptor TMED10; it results in protein translocation from the cytoplasm into the ERGIC (endoplasmic reticulum-Golgi intermediate compartment) followed by vesicle entry and secretion (PubMed:32272059). Recruited to DNA damage sites and secreted after genotoxic stress. {ECO:0000269|PubMed:32272059}.
| null | null | null | null | null |
FUNCTION: Cytokine constitutively present intracellularly in nearly all resting non-hematopoietic cells that plays an important role in inflammation and bridges the innate and adaptive immune systems (PubMed:26439902). After binding to its receptor IL1R1 together with its accessory protein IL1RAP, forms the high affinity interleukin-1 receptor complex (PubMed:17507369, PubMed:2950091). Signaling involves the recruitment of adapter molecules such as MYD88, IRAK1 or IRAK4 (PubMed:17507369). In turn, mediates the activation of NF-kappa-B and the three MAPK pathways p38, p42/p44 and JNK pathways (PubMed:14687581). Within the cell, acts as an alarmin and cell death results in its liberation in the extracellular space after disruption of the cell membrane to induce inflammation and alert the host to injury or damage (PubMed:15679580). In addition to its role as a danger signal, which occurs when the cytokine is passively released by cell necrosis, directly senses DNA damage and acts as a signal for genotoxic stress without loss of cell integrity (PubMed:26439902). {ECO:0000269|PubMed:14687581, ECO:0000269|PubMed:15679580, ECO:0000269|PubMed:17507369, ECO:0000269|PubMed:26439902, ECO:0000269|PubMed:2950091, ECO:0000269|PubMed:3258335}.
|
Homo sapiens (Human)
|
P01584
|
IL1B_HUMAN
|
MAEVPELASEMMAYYSGNEDDLFFEADGPKQMKCSFQDLDLCPLDGGIQLRISDHHYSKGFRQAASVVVAMDKLRKMLVPCPQTFQENDLSTFFPFIFEEEPIFFDTWDNEAYVHDAPVRSLNCTLRDSQQKSLVMSGPYELKALHLQGQDMEQQVVFSMSFVQGEESNDKIPVALGLKEKNLYLSCVLKDDKPTLQLESVDPKNYPKKKMEKRFVFNKIEINNKLEFESAQFPNWYISTSQAENMPVFLGGTKGGQDITDFTMQFVSS
| null | null |
apoptotic process [GO:0006915]; astrocyte activation [GO:0048143]; cell-cell signaling [GO:0007267]; cellular response to interleukin-17 [GO:0097398]; cellular response to lipopolysaccharide [GO:0071222]; cellular response to mechanical stimulus [GO:0071260]; cellular response to organic substance [GO:0071310]; cellular response to xenobiotic stimulus [GO:0071466]; cytokine-mediated signaling pathway [GO:0019221]; defense response to Gram-positive bacterium [GO:0050830]; ectopic germ cell programmed cell death [GO:0035234]; embryo implantation [GO:0007566]; extrinsic apoptotic signaling pathway in absence of ligand [GO:0097192]; fever generation [GO:0001660]; hyaluronan biosynthetic process [GO:0030213]; immune response [GO:0006955]; inflammatory response [GO:0006954]; interleukin-1-mediated signaling pathway [GO:0070498]; JNK cascade [GO:0007254]; macrophage chemotaxis [GO:0048246]; monocyte aggregation [GO:0070487]; negative regulation of adiponectin secretion [GO:0070164]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of extrinsic apoptotic signaling pathway in absence of ligand [GO:2001240]; negative regulation of gap junction assembly [GO:1903597]; negative regulation of glucose transmembrane transport [GO:0010829]; negative regulation of insulin receptor signaling pathway [GO:0046627]; negative regulation of lipid catabolic process [GO:0050995]; negative regulation of lipid metabolic process [GO:0045833]; negative regulation of MAP kinase activity [GO:0043407]; negative regulation of neurogenesis [GO:0050768]; negative regulation of synaptic transmission [GO:0050805]; neutrophil activation [GO:0042119]; neutrophil chemotaxis [GO:0030593]; positive regulation of angiogenesis [GO:0045766]; positive regulation of calcidiol 1-monooxygenase activity [GO:0060559]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of cell adhesion molecule production [GO:0060355]; positive regulation of cell division [GO:0051781]; positive regulation of cell migration [GO:0030335]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of complement activation [GO:0045917]; positive regulation of DNA-binding transcription factor activity [GO:0051091]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of epithelial to mesenchymal transition [GO:0010718]; positive regulation of fever generation [GO:0031622]; positive regulation of gene expression [GO:0010628]; positive regulation of glial cell proliferation [GO:0060252]; positive regulation of granulocyte macrophage colony-stimulating factor production [GO:0032725]; positive regulation of heterotypic cell-cell adhesion [GO:0034116]; positive regulation of immature T cell proliferation in thymus [GO:0033092]; positive regulation of inflammatory response [GO:0050729]; positive regulation of interleukin-2 production [GO:0032743]; positive regulation of interleukin-6 production [GO:0032755]; positive regulation of interleukin-8 production [GO:0032757]; positive regulation of JNK cascade [GO:0046330]; positive regulation of lipid catabolic process [GO:0050996]; positive regulation of MAP kinase activity [GO:0043406]; positive regulation of membrane protein ectodomain proteolysis [GO:0051044]; positive regulation of mitotic nuclear division [GO:0045840]; positive regulation of monocyte chemotactic protein-1 production [GO:0071639]; positive regulation of myosin light chain kinase activity [GO:0035505]; positive regulation of neuroinflammatory response [GO:0150078]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of nitric oxide biosynthetic process [GO:0045429]; positive regulation of non-canonical NF-kappaB signal transduction [GO:1901224]; positive regulation of p38MAPK cascade [GO:1900745]; positive regulation of prostaglandin biosynthetic process [GO:0031394]; positive regulation of prostaglandin secretion [GO:0032308]; positive regulation of protein export from nucleus [GO:0046827]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of RNA biosynthetic process [GO:1902680]; positive regulation of T cell mediated immunity [GO:0002711]; positive regulation of T cell proliferation [GO:0042102]; positive regulation of T-helper 1 cell cytokine production [GO:2000556]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of type II interferon production [GO:0032729]; positive regulation of vascular endothelial growth factor production [GO:0010575]; positive regulation of vascular endothelial growth factor receptor signaling pathway [GO:0030949]; regulation of canonical NF-kappaB signal transduction [GO:0043122]; regulation of defense response to virus by host [GO:0050691]; regulation of ERK1 and ERK2 cascade [GO:0070372]; regulation of establishment of endothelial barrier [GO:1903140]; regulation of insulin secretion [GO:0050796]; regulation of neurogenesis [GO:0050767]; regulation of nitric-oxide synthase activity [GO:0050999]; response to ATP [GO:0033198]; response to carbohydrate [GO:0009743]; response to interleukin-1 [GO:0070555]; response to lipopolysaccharide [GO:0032496]; sequestering of triglyceride [GO:0030730]; signal transduction [GO:0007165]; smooth muscle adaptation [GO:0014805]; vascular endothelial growth factor production [GO:0010573]
|
cytosol [GO:0005829]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; lysosome [GO:0005764]; secretory granule [GO:0030141]
|
cytokine activity [GO:0005125]; integrin binding [GO:0005178]; interleukin-1 receptor binding [GO:0005149]; protein domain specific binding [GO:0019904]
|
PF00340;PF02394;
|
2.80.10.50;
|
IL-1 family
|
PTM: Activation of the IL1B precursor involves a CASP1-catalyzed proteolytic cleavage. Processing and secretion are temporarily associated. {ECO:0000269|PubMed:15192144}.; PTM: (Microbial infection) Cleavage by S.pyogenes cysteine protease SpeB promotes its activation independently of CASP1. {ECO:0000269|PubMed:28331908, ECO:0000269|PubMed:32719155, ECO:0000269|PubMed:7689226}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:15192144}. Secreted {ECO:0000269|PubMed:11728343, ECO:0000269|PubMed:15192144, ECO:0000269|PubMed:33883744}. Lysosome {ECO:0000269|PubMed:15192144}. Secreted, extracellular exosome {ECO:0000250|UniProtKB:P10749}. Note=The precursor is cytosolic (PubMed:15192144). In response to inflammasome-activating signals, such as ATP for NLRP3 inflammasome or bacterial flagellin for NLRC4 inflammasome, cleaved and secreted (PubMed:24201029, PubMed:33377178, PubMed:33883744). Mature form is secreted and released in the extracellular milieu by passing through the gasdermin-D (GSDMD) pore (PubMed:33883744). In contrast, the precursor form is not released, due to the presence of an acidic region that is proteolytically removed by CASP1 during maturation (PubMed:33883744). The secretion is dependent on protein unfolding and facilitated by the cargo receptor TMED10 (PubMed:32272059). {ECO:0000269|PubMed:15192144, ECO:0000269|PubMed:24201029, ECO:0000269|PubMed:32272059, ECO:0000269|PubMed:33377178, ECO:0000269|PubMed:33883744}.
| null | null | null | null | null |
FUNCTION: Potent pro-inflammatory cytokine (PubMed:10653850, PubMed:12794819, PubMed:28331908, PubMed:3920526). Initially discovered as the major endogenous pyrogen, induces prostaglandin synthesis, neutrophil influx and activation, T-cell activation and cytokine production, B-cell activation and antibody production, and fibroblast proliferation and collagen production (PubMed:3920526). Promotes Th17 differentiation of T-cells. Synergizes with IL12/interleukin-12 to induce IFNG synthesis from T-helper 1 (Th1) cells (PubMed:10653850). Plays a role in angiogenesis by inducing VEGF production synergistically with TNF and IL6 (PubMed:12794819). Involved in transduction of inflammation downstream of pyroptosis: its mature form is specifically released in the extracellular milieu by passing through the gasdermin-D (GSDMD) pore (PubMed:33377178, PubMed:33883744). Acts as a sensor of S.pyogenes infection in skin: cleaved and activated by pyogenes SpeB protease, leading to an inflammatory response that prevents bacterial growth during invasive skin infection (PubMed:28331908). {ECO:0000269|PubMed:10653850, ECO:0000269|PubMed:12794819, ECO:0000269|PubMed:28331908, ECO:0000269|PubMed:33377178, ECO:0000269|PubMed:33883744, ECO:0000269|PubMed:3920526}.
|
Homo sapiens (Human)
|
P01586
|
IL3_MOUSE
|
MVLASSTTSIHTMLLLLLMLFHLGLQASISGRDTHRLTRTLNCSSIVKEIIGKLPEPELKTDDEGPSLRNKSFRRVNLSKFVESQGEVDPEDRYVIKSNLQKLNCCLPTSANDSALPGVFIRDLDDFRKKLRFYMVHLNDLETVLTSRPPQPASGSVSPNRGTVEC
| null | null |
B cell apoptotic process [GO:0001783]; B cell proliferation [GO:0042100]; cell population proliferation [GO:0008283]; cytokine-mediated signaling pathway [GO:0019221]; extrinsic apoptotic signaling pathway in absence of ligand [GO:0097192]; hematopoietic progenitor cell differentiation [GO:0002244]; hemopoiesis [GO:0030097]; immune response [GO:0006955]; interleukin-3-mediated signaling pathway [GO:0038156]; JNK cascade [GO:0007254]; mast cell apoptotic process [GO:0033024]; mast cell proliferation [GO:0070662]; monocyte differentiation [GO:0030224]; myeloid cell apoptotic process [GO:0033028]; myeloid leukocyte differentiation [GO:0002573]; negative regulation of autophagy [GO:0010507]; negative regulation of B cell apoptotic process [GO:0002903]; negative regulation of mast cell apoptotic process [GO:0033026]; negative regulation of myeloid cell apoptotic process [GO:0033033]; positive regulation of B cell proliferation [GO:0030890]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of hematopoietic progenitor cell differentiation [GO:1901534]; positive regulation of JNK cascade [GO:0046330]; positive regulation of mast cell proliferation [GO:0070668]; positive regulation of myeloid leukocyte differentiation [GO:0002763]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of T cell proliferation [GO:0042102]; regulation of cell growth [GO:0001558]; regulation of gene expression [GO:0010468]; regulation of glycolytic process [GO:0006110]; regulation of protein dephosphorylation [GO:0035304]; response to hormone [GO:0009725]; response to hypoxia [GO:0001666]; T cell proliferation [GO:0042098]
|
extracellular space [GO:0005615]
|
cytokine activity [GO:0005125]; growth factor activity [GO:0008083]; interleukin-3 receptor binding [GO:0005135]
|
PF02059;
|
1.20.1250.10;
|
IL-3 family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Cytokine secreted predominantly by activated T-lymphocytes as well as mast cells and osteoblastic cells that controls the production and differentiation of hematopoietic progenitor cells into lineage-restricted cells. Stimulates also mature basophils, eosinophils, and monocytes to become functionally activated. In addition, plays an important role in neural cell proliferation and survival. Participates as well in bone homeostasis and inhibits osteoclast differentiation by preventing NF-kappa-B nuclear translocation and activation. Mechanistically, exerts its biological effects through a receptor composed of IL3RA subunit and a signal transducing subunit IL3RB (By similarity). Receptor stimulation results in the rapid activation of JAK2 kinase activity leading to STAT5-mediated transcriptional program (PubMed:10376805, PubMed:31990690, PubMed:8378315). Alternatively, contributes to cell survival under oxidative stress in non-hematopoietic systems by activating pathways mediated by PI3K/AKT and ERK (By similarity). {ECO:0000250|UniProtKB:P08700, ECO:0000269|PubMed:10376805, ECO:0000269|PubMed:31990690, ECO:0000269|PubMed:8378315, ECO:0000269|PubMed:9446636}.
|
Mus musculus (Mouse)
|
P01587
|
CSF2_MOUSE
|
MWLQNLLFLGIVVYSLSAPTRSPITVTRPWKHVEAIKEALNLLDDMPVTLNEEVEVVSNEFSFKKLTCVQTRLKIFEQGLRGNFTKLKGALNMTASYYQTYCPPTPETDCETQVTTYADFIDSLKTFLTDIPFECKKPGQK
| null | null |
cell population proliferation [GO:0008283]; cellular response to granulocyte macrophage colony-stimulating factor stimulus [GO:0097011]; dendritic cell differentiation [GO:0097028]; embryonic placenta development [GO:0001892]; epithelial fluid transport [GO:0042045]; granulocyte-macrophage colony-stimulating factor signaling pathway [GO:0038157]; histamine secretion [GO:0001821]; immune response [GO:0006955]; macrophage differentiation [GO:0030225]; monocyte differentiation [GO:0030224]; myeloid cell differentiation [GO:0030099]; myeloid dendritic cell differentiation [GO:0043011]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of extrinsic apoptotic signaling pathway in absence of ligand [GO:2001240]; neutrophil differentiation [GO:0030223]; positive regulation of cell migration [GO:0030335]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of interleukin-23 production [GO:0032747]; positive regulation of leukocyte proliferation [GO:0070665]; positive regulation of macrophage derived foam cell differentiation [GO:0010744]; positive regulation of podosome assembly [GO:0071803]; positive regulation of tyrosine phosphorylation of STAT protein [GO:0042531]; receptor signaling pathway via JAK-STAT [GO:0007259]; regulation of cell population proliferation [GO:0042127]; regulation of circadian sleep/wake cycle, sleep [GO:0045187]; regulation of gene expression [GO:0010468]
|
extracellular region [GO:0005576]; extracellular space [GO:0005615]; granulocyte macrophage colony-stimulating factor receptor complex [GO:0030526]; intracellular membrane-bounded organelle [GO:0043231]
|
cytokine activity [GO:0005125]; granulocyte macrophage colony-stimulating factor receptor binding [GO:0005129]; growth factor activity [GO:0008083]
|
PF01109;
|
1.20.1250.10;
|
GM-CSF family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Cytokine that stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes.
|
Mus musculus (Mouse)
|
P01588
|
EPO_HUMAN
|
MGVHECPAWLWLLLSLLSLPLGLPVLGAPPRLICDSRVLERYLLEAKEAENITTGCAEHCSLNENITVPDTKVNFYAWKRMEVGQQAVEVWQGLALLSEAVLRGQALLVNSSQPWEPLQLHVDKAVSGLRSLTTLLRALGAQKEAISPPDAASAAPLRTITADTFRKLFRVYSNFLRGKLKLYTGEACRTGDR
| null | null |
acute-phase response [GO:0006953]; blood circulation [GO:0008015]; cellular hyperosmotic response [GO:0071474]; embryo implantation [GO:0007566]; erythrocyte differentiation [GO:0030218]; erythrocyte maturation [GO:0043249]; erythropoietin-mediated signaling pathway [GO:0038162]; hemoglobin biosynthetic process [GO:0042541]; myeloid cell apoptotic process [GO:0033028]; negative regulation of calcium ion transport into cytosol [GO:0010523]; negative regulation of cation channel activity [GO:2001258]; negative regulation of erythrocyte apoptotic process [GO:1902251]; negative regulation of intrinsic apoptotic signaling pathway in response to osmotic stress [GO:1902219]; negative regulation of transcription by RNA polymerase II [GO:0000122]; nucleate erythrocyte development [GO:0048823]; positive regulation of activated T cell proliferation [GO:0042104]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of neuron differentiation [GO:0045666]; positive regulation of neuron projection development [GO:0010976]; positive regulation of Ras protein signal transduction [GO:0046579]; positive regulation of tyrosine phosphorylation of STAT protein [GO:0042531]; response to axon injury [GO:0048678]; response to dexamethasone [GO:0071548]; response to electrical stimulus [GO:0051602]; response to estrogen [GO:0043627]; response to hyperoxia [GO:0055093]; response to hypoxia [GO:0001666]; response to interleukin-1 [GO:0070555]; response to lipopolysaccharide [GO:0032496]; response to salt stress [GO:0009651]; response to testosterone [GO:0033574]; response to vitamin A [GO:0033189]; signal transduction [GO:0007165]
|
cell body [GO:0044297]; cell surface [GO:0009986]; extracellular region [GO:0005576]; extracellular space [GO:0005615]
|
cytokine activity [GO:0005125]; erythropoietin receptor binding [GO:0005128]; hormone activity [GO:0005179]; protein kinase activator activity [GO:0030295]
|
PF00758;
|
1.20.1250.10;
|
EPO/TPO family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:32989016}.
| null | null | null | null | null |
FUNCTION: Hormone involved in the regulation of erythrocyte proliferation and differentiation and the maintenance of a physiological level of circulating erythrocyte mass. Binds to EPOR leading to EPOR dimerization and JAK2 activation thereby activating specific downstream effectors, including STAT1 and STAT3. {ECO:0000269|PubMed:28283061}.
|
Homo sapiens (Human)
|
P01589
|
IL2RA_HUMAN
|
MDSYLLMWGLLTFIMVPGCQAELCDDDPPEIPHATFKAMAYKEGTMLNCECKRGFRRIKSGSLYMLCTGNSSHSSWDNQCQCTSSATRNTTKQVTPQPEEQKERKTTEMQSPMQPVDQASLPGHCREPPPWENEATERIYHFVVGQMVYYQCVQGYRALHRGPAESVCKMTHGKTRWTQPQLICTGEMETSQFPGEEKPQASPEGRPESETSCLVTTTDFQIQTEMAATMETSIFTTEYQVAVAGCVFLLISVLLLSGLTWQRRQRKSRRTI
| null | null |
activated T cell proliferation [GO:0050798]; activation-induced cell death of T cells [GO:0006924]; apoptotic process [GO:0006915]; cell surface receptor signaling pathway [GO:0007166]; immune response [GO:0006955]; inflammatory response [GO:0006954]; inflammatory response to antigenic stimulus [GO:0002437]; interleukin-2-mediated signaling pathway [GO:0038110]; negative regulation of inflammatory response [GO:0050728]; negative regulation of T cell proliferation [GO:0042130]; Notch signaling pathway [GO:0007219]; positive regulation of activated T cell proliferation [GO:0042104]; positive regulation of T cell differentiation [GO:0045582]; regulation of CD4-positive, alpha-beta T cell proliferation [GO:2000561]; regulation of T cell homeostatic proliferation [GO:0046013]; regulation of T cell tolerance induction [GO:0002664]
|
external side of plasma membrane [GO:0009897]; interleukin-2 receptor complex [GO:0005893]; plasma membrane [GO:0005886]
|
interleukin-2 binding [GO:0019976]; interleukin-2 receptor activity [GO:0004911]
|
PF00084;
|
2.20.28.230;
| null | null |
SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
| null | null | null | null | null |
FUNCTION: Receptor for interleukin-2. The receptor is involved in the regulation of immune tolerance by controlling regulatory T cells (TREGs) activity. TREGs suppress the activation and expansion of autoreactive T-cells. {ECO:0000269|PubMed:23416241, ECO:0000269|PubMed:24116927}.
|
Homo sapiens (Human)
|
P01590
|
IL2RA_MOUSE
|
MEPRLLMLGFLSLTIVPSCRAELCLYDPPEVPNATFKALSYKNGTILNCECKRGFRRLKELVYMRCLGNSWSSNCQCTSNSHDKSRKQVTAQLEHQKEQQTTTDMQKPTQSMHQENLTGHCREPPPWKHEDSKRIYHFVEGQSVHYECIPGYKALQRGPAISICKMKCGKTGWTQPQLTCVDEREHHRFLASEESQGSRNSSPESETSCPITTTDFPQPTETTAMTETFVLTMEYKVAVASCLFLLISILLLSGLTWQHRWRKSRRTI
| null | null |
activated T cell proliferation [GO:0050798]; activation-induced cell death of T cells [GO:0006924]; inflammatory response [GO:0006954]; inflammatory response to antigenic stimulus [GO:0002437]; lymphocyte proliferation [GO:0046651]; negative regulation of inflammatory response [GO:0050728]; negative regulation of lymphocyte proliferation [GO:0050672]; negative regulation of T cell proliferation [GO:0042130]; Notch signaling pathway [GO:0007219]; positive regulation of activated T cell proliferation [GO:0042104]; positive regulation of T cell differentiation [GO:0045582]; positive regulation of T cell proliferation [GO:0042102]; regulation of CD4-positive, alpha-beta T cell proliferation [GO:2000561]; regulation of T cell homeostatic proliferation [GO:0046013]; regulation of T cell tolerance induction [GO:0002664]; T cell homeostasis [GO:0043029]
|
cell surface [GO:0009986]; external side of plasma membrane [GO:0009897]
|
interleukin-2 binding [GO:0019976]; interleukin-2 receptor activity [GO:0004911]
|
PF00084;
|
2.20.28.230;
| null | null |
SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
| null | null | null | null | null |
FUNCTION: Receptor for interleukin-2. The receptor is involved in the regulation of immune tolerance by controlling regulatory T cells (TREGs) activity. TREGs suppress the activation and expansion of autoreactive T-cells. {ECO:0000250|UniProtKB:P01589}.
|
Mus musculus (Mouse)
|
P01591
|
IGJ_HUMAN
|
MKNHLLFWGVLAVFIKAVHVKAQEDERIVLVDNKCKCARITSRIIRSSEDPNEDIVERNIRIIVPLNNRENISDPTSPLRTRFVYHLSDLCKKCDPTEVELDNQIVTATQSNICDEDSATETCYTYDRNKCYTAVVPLVYGGETKMVETALTPDACYPD
| null | null |
adaptive immune response [GO:0002250]; antibacterial humoral response [GO:0019731]; glomerular filtration [GO:0003094]; humoral immune response [GO:0006959]; immune response [GO:0006955]; innate immune response [GO:0045087]; positive regulation of respiratory burst [GO:0060267]; protein-containing complex assembly [GO:0065003]
|
blood microparticle [GO:0072562]; dimeric IgA immunoglobulin complex [GO:0071750]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; monomeric IgA immunoglobulin complex [GO:0071748]; pentameric IgM immunoglobulin complex [GO:0071756]; secretory dimeric IgA immunoglobulin complex [GO:0071752]; secretory IgA immunoglobulin complex [GO:0071751]
|
antigen binding [GO:0003823]; IgA binding [GO:0019862]; immunoglobulin receptor binding [GO:0034987]; protein homodimerization activity [GO:0042803]; protein-macromolecule adaptor activity [GO:0030674]
|
PF15097;
| null | null | null |
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P01592}.
| null | null | null | null | null |
FUNCTION: Serves to link two monomer units of either IgM or IgA. In the case of IgM, the J chain-joined dimer is a nucleating unit for the IgM pentamer, and in the case of IgA it induces dimers and/or larger polymers. It also helps to bind these immunoglobulins to secretory component. {ECO:0000250|UniProtKB:P01592}.
|
Homo sapiens (Human)
|
P01592
|
IGJ_MOUSE
|
MKTHLLLWGVLAIFVKAVLVTGDDEATILADNKCMCTRVTSRIIPSTEDPNEDIVERNIRIVVPLNNRENISDPTSPLRRNFVYHLSDVCKKCDPVEVELEDQVVTATQSNICNEDDGVPETCYMYDRNKCYTTMVPLRYHGETKMVQAALTPDSCYPD
| null | null |
adaptive immune response [GO:0002250]; antibacterial humoral response [GO:0019731]; glomerular filtration [GO:0003094]; humoral immune response [GO:0006959]; innate immune response [GO:0045087]; positive regulation of respiratory burst [GO:0060267]; protein-containing complex assembly [GO:0065003]
|
dimeric IgA immunoglobulin complex [GO:0071750]; monomeric IgA immunoglobulin complex [GO:0071748]; pentameric IgM immunoglobulin complex [GO:0071756]; secretory dimeric IgA immunoglobulin complex [GO:0071752]; secretory IgA immunoglobulin complex [GO:0071751]
|
antigen binding [GO:0003823]; IgA binding [GO:0019862]; immunoglobulin receptor binding [GO:0034987]; peptidoglycan binding [GO:0042834]; phosphatidylcholine binding [GO:0031210]; protein homodimerization activity [GO:0042803]; protein-macromolecule adaptor activity [GO:0030674]; single-stranded DNA binding [GO:0003697]
|
PF15097;
| null | null | null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1517233}.
| null | null | null | null | null |
FUNCTION: Serves to link two monomer units of either IgM or IgA. In the case of IgM, the J chain-joined dimer is a nucleating unit for the IgM pentamer, and in the case of IgA it induces dimers and/or larger polymers. It also helps to bind these immunoglobulins to secretory component. {ECO:0000269|PubMed:1517233}.
|
Mus musculus (Mouse)
|
P01593
|
KVD33_HUMAN
|
MDMRVPAQLLGLLLLWLSGARCDIQMTQSPSSLSASVGDRVTITCQASQDISNYLNWYQQKPGKAPKLLIYDASNLETGVPSRFSGSGSGTDFTFTISSLQPEDIATYYCQQYDNLP
| null | null |
adaptive immune response [GO:0002250]; immune response [GO:0006955]
|
blood microparticle [GO:0072562]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; immunoglobulin complex [GO:0019814]; plasma membrane [GO:0005886]
|
antigen binding [GO:0003823]
|
PF07686;
|
2.60.40.10;
| null | null |
SUBCELLULAR LOCATION: Secreted {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. Cell membrane {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
| null | null | null | null | null |
FUNCTION: V region of the variable domain of immunoglobulin light chains that participates in the antigen recognition (PubMed:24600447). Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens (PubMed:20176268, PubMed:22158414). The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen (PubMed:17576170, PubMed:20176268). {ECO:0000303|PubMed:17576170, ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414, ECO:0000303|PubMed:24600447}.
|
Homo sapiens (Human)
|
P01594
|
KV133_HUMAN
|
MDMRVPAQLLGLLLLWLSGARCDIQMTQSPSSLSASVGDRVTITCQASQDISNYLNWYQQKPGKAPKLLIYDASNLETGVPSRFSGSGSGTDFTFTISSLQPEDIATYYCQQYDNLP
| null | null |
adaptive immune response [GO:0002250]; immune response [GO:0006955]
|
blood microparticle [GO:0072562]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; immunoglobulin complex [GO:0019814]; plasma membrane [GO:0005886]
|
antigen binding [GO:0003823]; identical protein binding [GO:0042802]
|
PF07686;
|
2.60.40.10;
| null | null |
SUBCELLULAR LOCATION: Secreted {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. Cell membrane {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
| null | null | null | null | null |
FUNCTION: V region of the variable domain of immunoglobulin light chains that participates in the antigen recognition (PubMed:24600447). Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens (PubMed:20176268, PubMed:22158414). The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen (PubMed:17576170, PubMed:20176268). {ECO:0000303|PubMed:17576170, ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414, ECO:0000303|PubMed:24600447}.
|
Homo sapiens (Human)
|
P01597
|
KV139_HUMAN
|
MDMRVPAQLLGLLLLWLRGARCDIQMTQSPSSLSASVGDRVTITCRASQSISSYLNWYQQKPGKAPKLLIYAASSLQSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQSYSTP
| null | null |
adaptive immune response [GO:0002250]; immune response [GO:0006955]
|
blood microparticle [GO:0072562]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; immunoglobulin complex [GO:0019814]; plasma membrane [GO:0005886]
|
antigen binding [GO:0003823]
|
PF07686;
|
2.60.40.10;
| null | null |
SUBCELLULAR LOCATION: Secreted {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. Cell membrane {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
| null | null | null | null | null |
FUNCTION: V region of the variable domain of immunoglobulin light chains that participates in the antigen recognition (PubMed:24600447). Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens (PubMed:20176268, PubMed:22158414). The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen (PubMed:17576170, PubMed:20176268). {ECO:0000303|PubMed:17576170, ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414, ECO:0000303|PubMed:24600447}.
|
Homo sapiens (Human)
|
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