(data stored in ACNUC4482 zone)

HOGENOM: HS5_PE689

ID   HS5_PE689                            STANDARD;      PRT;   1179 AA.
AC   HS5_PE689; P56199; B2RNU0;
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   RecName: Full=Integrin alpha-1;AltName: Full=CD49 antigen-like family
DE   member A;AltName: Full=Laminin and collagen receptor;AltName:
DE   Full=VLA-1;AltName: CD_antigen=CD49a;Flags: Precursor; (HS5.PE689).
GN   Name=ITGA1;
OS   HOMO SAPIENS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Primates; Haplorrhini; Simiiformes; Catarrhini;
OC   Hominoidea; Hominidae; Homininae; Homo.
OX   NCBI_TaxID=9606;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS HS5.PE689.
CC       Homo sapiens chromosome 5 GRCh37  sequence 1..180905260 annotated by
CC       Ensembl
CC   -!- ANNOTATIONS ORIGIN:ITA1_HUMAN
CC   -!- FUNCTION: Integrin alpha-1/beta-1 is a receptor for laminin and
CC       collagen. It recognizes the proline-hydroxylated sequence G-F-P-G-
CC       E-R in collagen.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Alpha-1
CC       associates with beta-1. Interacts with RAB21.
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:Homo_sapiens;ENSG00000213949;ENST00000282588;ENSP00000282588.
DR   EMBL; AC022133; - ;
DR   EMBL; AC025180; - ;
DR   EMBL; AC027326; - ;
DR   EMBL; AK300423; - ;
DR   EMBL; BC137121; - ;
DR   EMBL; BC137122; - ;
DR   EMBL; X68742; - ;
DR   UniProtKB/Swiss-Prot; P56199; B2RNU0; -.
DR   EMBL; AC027326; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC022133; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC025180; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC137121; AAI37122.1; -; mRNA.
DR   EMBL; BC137122; AAI37123.1; -; mRNA.
DR   EMBL; X68742; -; NOT_ANNOTATED_CDS; mRNA.
DR   IPI; IPI00743104; -.
DR   PIR; A45226; A45226.
DR   RefSeq; NP_852478.1; NM_181501.1.
DR   UniGene; Hs.644352; -.
DR   PDB; 1PT6; X-ray; 1.87 A; A/B=166-366.
DR   PDB; 1QC5; X-ray; 2.00 A; A/B=168-359.
DR   PDB; 1QCY; X-ray; 2.30 A; A=169-361.
DR   PDBsum; 1PT6; -.
DR   PDBsum; 1QC5; -.
DR   PDBsum; 1QCY; -.
DR   ProteinModelPortal; P56199; -.
DR   SMR; P56199; 170-359, 391-531, 569-665, 1136-1173.
DR   DIP; DIP-206N; -.
DR   IntAct; P56199; 5.
DR   STRING; P56199; -.
DR   PhosphoSite; P56199; -.
DR   Cornea-2DPAGE; P56199; -.
DR   PRIDE; P56199; -.
DR   Ensembl; ENST00000282588; ENSP00000282588; ENSG00000213949.
DR   GeneID; 3672; -.
DR   KEGG; hsa:3672; -.
DR   UCSC; uc003jou.1; human.
DR   CTD; 3672; -.
DR   GeneCards; GC05P049056; -.
DR   HGNC; HGNC:6134; ITGA1.
DR   HPA; HPA042555; -.
DR   MIM; 192968; gene.
DR   neXtProt; NX_P56199; -.
DR   PharmGKB; PA29935; -.
DR   eggNOG; prNOG08790; -.
DR   GeneTree; ENSGT00600000084333; -.
DR   InParanoid; P56199; -.
DR   OMA; YMGTEKE; -.
DR   OrthoDB; EOG4THVS7; -.
DR   PhylomeDB; P56199; -.
DR   Pathway_Interaction_DB; arf6_traffickingpathway; Arf6 trafficking events.
DR   Pathway_Interaction_DB; prlsignalingeventspathway; Signaling events mediated by PRL.
DR   Pathway_Interaction_DB; lymphangiogenesis_pathway; VEGFR3 signaling in lymphatic endothelium.
DR   Reactome; REACT_13552; Integrin cell surface interactions.
DR   Reactome; REACT_17044; Muscle contraction.
DR   Reactome; REACT_18266; Axon guidance.
DR   NextBio; 14373; -.
DR   ArrayExpress; P56199; -.
DR   Bgee; P56199; -.
DR   Genevestigator; P56199; -.
DR   GermOnline; ENSG00000152684; Homo sapiens.
DR   GO; GO:0008305; C:integrin complex; TAS:UniProtKB.
DR   GO; GO:0005518; F:collagen binding; TAS:UniProtKB.
DR   GO; GO:0004872; F:receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0007411; P:axon guidance; TAS:Reactome.
DR   GO; GO:0007160; P:cell-matrix adhesion; NAS:UniProtKB.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR   GO; GO:0006936; P:muscle contraction; EXP:Reactome.
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; HS5.PE689; -.
KW   ENSG000002139491755old_1320000031; ENSP000002825887901old_1320000031;
KW   B4DTY8_HUMAN; AC022133; AC025180; AC027326; AK300423; BC137121; BC137122;
KW   X68742;
KW   3D-structure; Calcium; Cell adhesion; Complete proteome;
KW   Disulfide bond; Glycoprotein; Integrin; Magnesium; Membrane;
KW   Polymorphism; Receptor; Reference proteome; Repeat; Signal;
KW   Transmembrane; Transmembrane helix.
SQ   SEQUENCE   1179 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MAPRPRARPG VAVACCWLLT VVLRCCVSFN VDVKNSMTFS GPVEDMFGYT VQQYENEEGK
     WVLIGSPLVG QPKNRTGDVY KCPVGRGESL PCVKLDLPVN TSIPNVTEVK ENMTFGSTLV
     TNPNGGFLAC GPLYAYRCGH LHYTTGICSD VSPTFQVVNS IAPVQECSTQ LDIVIVLDGS
     NSIYPWDSVT AFLNDLLERM DIGPKQTQVG IVQYGENVTH EFNLNKYSST EEVLVAAKKI
     VQRGGRQTMT ALGIDTARKE AFTEARGARR GVKKVMVIVT DGESHDNHRL KKVIQDCEDE
     NIQRFSIAIL GSYNRGNLST EKFVEEIKSI ASEPTEKHFF NVSDELALVT IVKTLGERIF
     ALEATADQSA ASFEMEMSQT GFSAHYSQDW VMLGAVGAYD WNGTVVMQKA SQIIIPRNTT
     FNVESTKKNE PLASYLGYTV NSATASSGDV LYIAGQPRYN HTGQVIIYRM EDGNIKILQT
     LSGEQIGSYF GSILTTTDID KDSNTDILLV GAPMYMGTEK EEQGKVYVYA LNQTRFEYQM
     SLEPIKQTCC SSRQHNSCTT ENKNEPCGAR FGTAIAAVKD LNLDGFNDIV IGAPLEDDHG
     GAVYIYHGSG KTIRKEYAQR IPSGGDGKTL KFFGQSIHGE MDLNGDGLTD VTIGGLGGAA
     LFWSRDVAVV KVTMNFEPNK VNIQKKNCHM EGKETVCINA TVCFDVKLKS KEDTIYEADL
     QYRVTLDSLR QISRSFFSGT QERKVQRNIT VRKSECTKHS FYMLDKHDFQ DSVRITLDFN
     LTDPENGPVL DDSLPNSVHE YIPFAKDCGN KEKCISDLSL HVATTEKDLL IVRSQNDKFN
     VSLTVKNTKD SAYNTRTIVH YSPNLVFSGI EAIQKDSCES NHNITCKVGY PFLRRGEMVT
     FKILFQFNTS YLMENVTIYL SATSDSEEPP ETLSDNVVNI SIPVKYEVGL QFYSSASEYH
     ISIAANETVP EVINSTEDIG NEINIFYLIR KSGSFPMPEL KLSISFPNMT SNGYPVLYPT
     GLSSSENANC RPHIFEDPFS INSGKKMTTS TDHLKRGTIL DCNTCKFATI TCNLTSSDIS
     QVNVSLILWK PTFIKSYFSS LNLTIRGELR SENASLVLSS SNQKRELAIQ ISKDGLPGRV
     PLWVILLSAF AGLLLLMLLI LALWKIGFFK RPLKKKMEK
//

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