(data stored in ACNUC4482 zone)

HOGENOM: BOVIN20_29_PE2

ID   BOVIN20_29_PE2                       STANDARD;      PRT;   1179 AA.
AC   BOVIN20_29_PE2; P53710;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   Flags: Fragments;
DE   RecName: Full=Integrin alpha-2;AltName: Full=CD49 antigen-like family
DE   member B;AltName: Full=Collagen receptor;AltName: Full=Platelet membrane
DE   glycoprotein Ia; Short=GPIa;AltName: Full=VLA-2 subunit alpha;AltName:
DE   CD_antigen=CD49b;Flags: Precursor; Fragment; (BOVIN20_29.PE2).
GN   Name=ITGA2;
OS   BOS TAURUS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Laurasiatheria; Cetartiodactyla; Ruminantia; Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS BOVIN20_29.PE2.
CC       Bos taurus chromosome 20 Btau_4.0 partial sequence 27566957..28566956
CC       annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:ITA2_BOVIN
CC   -!- FUNCTION: Integrin alpha-2/beta-1 is a receptor for laminin,
CC       collagen, collagen C-propeptides, fibronectin and E-cadherin. It
CC       recognizes the proline-hydroxylated sequence G-F-P-G-E-R in
CC       collagen. It is responsible for adhesion of platelets and other
CC       cells to collagens, modulation of collagen and collagenase gene
CC       expression, force generation and organization of newly synthesized
CC       extracellular matrix.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Alpha-2
CC       associates with beta-1. Interacts with HPS5 and RAB21 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- DOMAIN: The integrin I-domain (insert) is a VWFA domain. Integrins
CC       with I-domains do not undergo protease cleavage.
CC   -!- SIMILARITY: Belongs to the integrin alpha chain family.
CC   -!- SIMILARITY: Contains 7 FG-GAP repeats.
CC   -!- SIMILARITY: Contains 1 VWFA domain.
CC   -!- GENE_FAMILY: HOG000059610 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Bos_taurus;ENSBTAG00000019289;ENSBTAT00000025685;ENSBTAP00000025685.
DR   EMBL; L25886; - ;
DR   UniProtKB/Swiss-Prot; P53710; -.
DR   EMBL; L25886; AAB59255.1; -; mRNA.
DR   IPI; IPI00953862; -.
DR   PIR; I45914; I45914.
DR   UniGene; Bt.12761; -.
DR   ProteinModelPortal; P53710; -.
DR   SMR; P53710; 157-355.
DR   STRING; P53710; -.
DR   PRIDE; P53710; -.
DR   eggNOG; maNOG13795; -.
DR   GeneTree; ENSGT00600000084333; -.
DR   InParanoid; P53710; -.
DR   OrthoDB; EOG45B1DV; -.
DR   GO; GO:0008305; C:integrin complex; IEA:InterPro.
DR   GO; GO:0004872; F:receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR   InterPro; IPR013517; FG-GAP.
DR   InterPro; IPR013519; Int_alpha_beta-p.
DR   InterPro; IPR000413; Integrin_alpha.
DR   InterPro; IPR013649; Integrin_alpha-2.
DR   InterPro; IPR018184; Integrin_alpha_C_CS.
DR   InterPro; IPR002035; VWF_A.
DR   Pfam; PF01839; FG-GAP; 1.
DR   Pfam; PF08441; Integrin_alpha2; 1.
DR   Pfam; PF00092; VWA; 1.
DR   PRINTS; PR01185; INTEGRINA.
DR   SMART; SM00191; Int_alpha; 5.
DR   SMART; SM00327; VWA; 1.
DR   PROSITE; PS51470; FG_GAP; 7.
DR   PROSITE; PS00242; INTEGRIN_ALPHA; 1.
DR   PROSITE; PS50234; VWFA; 1.
DR   HOGENOMDNA; BOVIN20_29.PE2; -.
KW   ENSBTAG00000019289fold_1320000031; ENSBTAP00000025685fold_1320000031;
KW   L25886;
KW   Calcium; Cell adhesion; Complete proteome; Disulfide bond;
KW   Glycoprotein; Integrin; Magnesium; Membrane; Phosphoprotein;
KW   Polymorphism; Receptor; Reference proteome; Repeat; Signal;
KW   Transmembrane; Transmembrane helix.
SQ   SEQUENCE   1179 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     IYPGFILSGP LLFLKFSLIG ILNCCVAYNV GLPKAKIFSG PSSEQFGYAV QQFINPKGNW
     LLVGSPWSGF PKNRMGDVYK CPVDLSTTTC EKLNLQTSTS MSNVTEMKTN MSLGLTLTRN
     VGTGGFLTCG PLWAQQCGSQ YYTTGVCSDV SPDFQLRTSF APAVQTCPSF IDVVVVCDES
     NSIYPWDAVK NFLEKFVQGL DIGPTKTQMG LIQYANNPRV VFNLNTFKSK DEMIKATSQT
     FQYGGDLTNT FKAIQYARDT AYSTAAGGRP GATKVMVVVT DGESHDGSKL KAVIDQCNKD
     NILRFGIAVL GYLNRNALDT KNLIKEIKAI ASIPTERHFF NVSDEADLLE KAGTIGEQIF
     SIEGTVQGGD NFQMEMSQVG FSAEYSPQNN ILMLGAVGAY DWSGTVVQKT PHGHLIFSKQ
     AFEQILQDRN HSSYLGYSVA SISTGNSVHF VAGAPRANYT GQIVLYSVNE NGNVTVIQSH
     RGDQIGSYFG SVLCAVDVNK DTITDVLLVG APMYMNDLKK EEGRVYLFTI TKGILNWHQF
     LEGPKGLENA RFGSAIAALS DINMDGFNDV IVGSPLENQN SGAVYIYNGH EGMIRLRYSQ
     KILGSDRAFS SHLQYFGRSL DGYGDLNGDS ITDVSVGAFG QVVQLWSQSI ADVSVDASFT
     PKKITLLNKN AEIKLKLCFS AKFRPTNQNN QVAIVYNITI DEDQFSSRVI SRGLFKENNE
     RCLQKTMIVS QAQRCSEYII HIQEPSDIIS PLNLCMNISL ENPGTNPALE AYSETVKVFS
     IPFHKDCGDD GVCISDLVLN VQQLPATQQQ PFIVSNQNKR LTFSVQLKNK KESAYNTEIV
     VDFSENLFFA SWSMPVDGTE VTCQIASSQK SVTCNVGYPA LKSKQQVTFT INFDFNLQNL
     QNQASISFRA LSESQEENMA DNSVNLKLSL LYDAEIHITR STNINFYEVS LDGNVSSVVH
     SFEDIGPKFI FSIKVTTGSV PVSMASVIIH IPQYTKDKNP LMYLTGVHTD QAGDISCEAE
     INPLKIGQTS SSVSFKSENF RHIKELNCRT ASCSNIMCWL RDLQVKGEYF LNVSTRIWNG
     TFAASTFQTV QLTAAAEIDT YNPQIYVIEE NTVTIPLTIM KPHEKVEVPT GVIVGSVIAG
     ILLLLALVAI LWKLGFFKRK YEKMAKNPDE TDETTELNS
//

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