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EFNA1_PIG
ID   EFNA1_PIG               Reviewed;         205 AA.
AC   Q06AS9;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=Ephrin-A1;
DE   Contains:
DE     RecName: Full=Ephrin-A1, secreted form;
DE   Flags: Precursor;
GN   Name=EFNA1;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Liu G.Y.;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cell surface GPI-bound ligand for Eph receptors, a family of
CC       receptor tyrosine kinases which are crucial for migration, repulsion
CC       and adhesion during neuronal, vascular and epithelial development.
CC       Binds promiscuously Eph receptors residing on adjacent cells, leading
CC       to contact-dependent bidirectional signaling into neighboring cells.
CC       Plays an important role in angiogenesis and tumor neovascularization.
CC       The recruitment of VAV2, VAV3 and PI3-kinase p85 subunit by
CC       phosphorylated EPHA2 is critical for EFNA1-induced RAC1 GTPase
CC       activation and vascular endothelial cell migration and assembly. Exerts
CC       anti-oncogenic effects in tumor cells through activation and down-
CC       regulation of EPHA2. Activates EPHA2 by inducing tyrosine
CC       phosphorylation which leads to its internalization and degradation.
CC       Acts as a negative regulator in the tumorigenesis of gliomas by down-
CC       regulating EPHA2 and FAK. Can evoke collapse of embryonic neuronal
CC       growth cone and regulates dendritic spine morphogenesis (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Monomer. Homodimer. Forms heterodimers with EPHA2. Binds to
CC       the receptor tyrosine kinases EPHA2, EPHA3, EPHA4, EPHA5, EPHA6 and
CC       EPHA7. Also binds with low affinity to EPHA1 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P20827};
CC       Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:P20827}.
CC   -!- SUBCELLULAR LOCATION: [Ephrin-A1, secreted form]: Secreted
CC       {ECO:0000250|UniProtKB:P20827}.
CC   -!- PTM: Undergoes proteolysis by a metalloprotease to give rise to a
CC       soluble monomeric form. {ECO:0000250}.
CC   -!- PTM: N-Glycosylation is required for binding to EPHA2 receptor and
CC       inducing its internalization. {ECO:0000250|UniProtKB:P20827}.
CC   -!- SIMILARITY: Belongs to the ephrin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00884}.
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DR   EMBL; DQ917646; ABI97191.1; -; mRNA.
DR   RefSeq; NP_001116582.1; NM_001123110.1.
DR   AlphaFoldDB; Q06AS9; -.
DR   SMR; Q06AS9; -.
DR   STRING; 9823.ENSSSCP00000006959; -.
DR   PaxDb; Q06AS9; -.
DR   PeptideAtlas; Q06AS9; -.
DR   GeneID; 100144501; -.
DR   KEGG; ssc:100144501; -.
DR   CTD; 1942; -.
DR   eggNOG; KOG3858; Eukaryota.
DR   InParanoid; Q06AS9; -.
DR   OrthoDB; 1094764at2759; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   GO; GO:0046658; C:anchored component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0046875; F:ephrin receptor binding; IBA:GO_Central.
DR   GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR   GO; GO:0048013; P:ephrin receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0061002; P:negative regulation of dendritic spine morphogenesis; ISS:UniProtKB.
DR   GO; GO:0050730; P:regulation of peptidyl-tyrosine phosphorylation; ISS:UniProtKB.
DR   CDD; cd10425; Ephrin-A_Ectodomain; 1.
DR   Gene3D; 2.60.40.420; -; 1.
DR   InterPro; IPR008972; Cupredoxin.
DR   InterPro; IPR031328; Ephrin.
DR   InterPro; IPR034252; Ephrin-A_Ecto.
DR   InterPro; IPR019765; Ephrin_CS.
DR   InterPro; IPR001799; Ephrin_RBD.
DR   PANTHER; PTHR11304; PTHR11304; 1.
DR   Pfam; PF00812; Ephrin; 1.
DR   PRINTS; PR01347; EPHRIN.
DR   SUPFAM; SSF49503; SSF49503; 1.
DR   PROSITE; PS01299; EPHRIN_RBD_1; 1.
DR   PROSITE; PS51551; EPHRIN_RBD_2; 1.
PE   2: Evidence at transcript level;
KW   Angiogenesis; Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor;
KW   Lipoprotein; Membrane; Reference proteome; Secreted; Signal;
KW   Tumor suppressor.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000250"
FT   CHAIN           19..182
FT                   /note="Ephrin-A1"
FT                   /id="PRO_0000288608"
FT   CHAIN           19..?
FT                   /note="Ephrin-A1, secreted form"
FT                   /id="PRO_0000389632"
FT   PROPEP          183..205
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000288609"
FT   DOMAIN          19..151
FT                   /note="Ephrin RBD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00884"
FT   LIPID           182
FT                   /note="GPI-anchor amidated serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        26
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        51..92
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00884"
FT   DISULFID        80..140
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00884"
SQ   SEQUENCE   205 AA;  23745 MW;  91D08A935741D56C CRC64;
     MEFLWAPLLG LCCSLAAADR HTVFWNSSEP KFWNEDYTVH VRLNDYLDII CPHYEDDSVA
     EAAMERYTLY LVEREQYQLC QPQSKDQVRW QCNQPNARHG PEKLSEKFQR FTPFTLGKEF
     KEGHSYYYIS KPIHHQEDQC LKLKVTVSGK ITHSPQAHAN PQEKRLPADD PEVQVLHSIG
     HSAAPRLSPL AWAVLLLPFL LLQTS
 
 
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