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Protein

Integrin alpha-V

Gene

ITGAV

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

The alpha-V (ITGAV) integrins are receptors for vitronectin, cytotactin, fibronectin, fibrinogen, laminin, matrix metalloproteinase-2, osteopontin, osteomodulin, prothrombin, thrombospondin and vWF. They recognize the sequence R-G-D in a wide array of ligands. ITGAV:ITGB3 binds to fractalkine (CX3CL1) and may act as its coreceptor in CX3CR1-dependent fractalkine signaling (PubMed:23125415). ITGAV:ITGB3 binds to NRG1 (via EGF domain) and this binding is essential for NRG1-ERBB signaling (PubMed:20682778). ITGAV:ITGB3 binds to FGF1 and this binding is essential for FGF1 signaling (PubMed:18441324). ITGAV:ITGB3 binds to IGF1 and this binding is essential for IGF1 signaling (PubMed:19578119). ITGAV:ITGB3 binds to PLA2G2A via a site (site 2) which is distinct from the classical ligand-binding site (site 1) and this induces integrin conformational changes and enhanced ligand binding to site 1 (PubMed:18635536, PubMed:25398877). ITGAV:ITGB3 and ITGAV:ITGB6 act as a receptor for fibrillin-1 (FBN1) and mediate R-G-D-dependent cell adhesion to FBN1 (PubMed:12807887, PubMed:17158881).8 Publications
(Microbial infection) Integrin ITGAV:ITGB5 acts as a receptor for adenovirus type C (PubMed:20615244). Integrin ITGAV:ITGB5 and ITGAV:ITGB3 act as receptors for coxsackievirus A9 and B1 (PubMed:9426447, PubMed:15194773, PubMed:7519807). Integrin ITGAV:ITGB3 acts as a receptor for herpes virus 8/HHV-8 (PubMed:18045938). Integrin ITGAV:ITGB6 acts as a receptor for herpes simplex 1/HHV-1 (PubMed:24367260). Integrin ITGAV:ITGB3 acts as a receptor for Human parechovirus 1 (PubMed:11160695). Integrin ITGAV:ITGB3 acts as a receptor for West nile virus (PubMed:23658209). In case of HIV-1 infection, the interaction with extracellular viral Tat protein seems to enhance angiogenesis in Kaposi's sarcoma lesions (PubMed:10397733).9 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Calcium bindingi260 – 268Sequence analysis9
Calcium bindingi314 – 322Sequence analysis9
Calcium bindingi379 – 387Sequence analysis9
Calcium bindingi443 – 451Sequence analysis9

GO - Molecular functioni

  • coreceptor activity Source: UniProtKB
  • extracellular matrix binding Source: UniProtKB
  • extracellular matrix protein binding Source: UniProtKB
  • fibronectin binding Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • protease binding Source: UniProtKB
  • transforming growth factor beta binding Source: BHF-UCL
  • virus receptor activity Source: UniProtKB-KW
  • voltage-gated calcium channel activity Source: UniProtKB

GO - Biological processi

  • angiogenesis Source: UniProtKB
  • antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent Source: Reactome
  • apolipoprotein A-I-mediated signaling pathway Source: UniProtKB
  • apoptotic cell clearance Source: Ensembl
  • calcium ion transmembrane transport Source: UniProtKB
  • cell adhesion Source: BHF-UCL
  • cell adhesion mediated by integrin Source: UniProtKB
  • cell growth Source: UniProtKB
  • cell-matrix adhesion Source: UniProtKB
  • cell migration Source: UniProtKB
  • cell-substrate adhesion Source: UniProtKB
  • endodermal cell differentiation Source: UniProtKB
  • entry of symbiont into host cell by promotion of host phagocytosis Source: BHF-UCL
  • ERK1 and ERK2 cascade Source: BHF-UCL
  • extracellular matrix organization Source: Reactome
  • extrinsic apoptotic signaling pathway in absence of ligand Source: BHF-UCL
  • heterotypic cell-cell adhesion Source: UniProtKB
  • integrin-mediated signaling pathway Source: UniProtKB
  • leukocyte migration Source: Reactome
  • negative chemotaxis Source: UniProtKB
  • negative regulation of entry of bacterium into host cell Source: BHF-UCL
  • negative regulation of extrinsic apoptotic signaling pathway Source: BHF-UCL
  • negative regulation of lipid storage Source: BHF-UCL
  • negative regulation of lipid transport Source: BHF-UCL
  • negative regulation of lipoprotein metabolic process Source: BHF-UCL
  • negative regulation of low-density lipoprotein particle receptor biosynthetic process Source: BHF-UCL
  • negative regulation of macrophage derived foam cell differentiation Source: BHF-UCL
  • positive regulation of cell adhesion Source: BHF-UCL
  • positive regulation of cell migration Source: Ensembl
  • positive regulation of cell proliferation Source: BHF-UCL
  • positive regulation of osteoblast proliferation Source: Ensembl
  • regulation of apoptotic cell clearance Source: BHF-UCL
  • regulation of phagocytosis Source: BHF-UCL
  • substrate adhesion-dependent cell spreading Source: UniProtKB
  • vascular endothelial growth factor receptor signaling pathway Source: Reactome
  • viral entry into host cell Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Host cell receptor for virus entry, Integrin, Receptor

Keywords - Biological processi

Cell adhesion, Host-virus interaction

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000138448-MONOMER.
ReactomeiR-HSA-1236973. Cross-presentation of particulate exogenous antigens (phagosomes).
R-HSA-1566948. Elastic fibre formation.
R-HSA-210990. PECAM1 interactions.
R-HSA-2129379. Molecules associated with elastic fibres.
R-HSA-216083. Integrin cell surface interactions.
R-HSA-3000157. Laminin interactions.
R-HSA-3000170. Syndecan interactions.
R-HSA-3000178. ECM proteoglycans.
R-HSA-4420097. VEGFA-VEGFR2 Pathway.
R-HSA-445144. Signal transduction by L1.
R-HSA-6798695. Neutrophil degranulation.
SignaLinkiP06756.
SIGNORiP06756.

Names & Taxonomyi

Protein namesi
Recommended name:
Integrin alpha-V
Alternative name(s):
Vitronectin receptor subunit alpha
CD_antigen: CD51
Cleaved into the following 2 chains:
Gene namesi
Name:ITGAV
Synonyms:MSK8, VNRA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:6150. ITGAV.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini31 – 992ExtracellularSequence analysisAdd BLAST962
Transmembranei993 – 1016HelicalSequence analysisAdd BLAST24
Topological domaini1017 – 1048CytoplasmicSequence analysisAdd BLAST32

GO - Cellular componenti

  • alphav-beta3 integrin-IGF-1-IGF1R complex Source: BHF-UCL
  • cell surface Source: UniProtKB
  • external side of plasma membrane Source: Ensembl
  • extracellular exosome Source: UniProtKB
  • filopodium membrane Source: UniProtKB
  • focal adhesion Source: UniProtKB
  • integral component of plasma membrane Source: UniProtKB
  • integrin alphav-beta3 complex Source: UniProtKB
  • integrin alphav-beta5 complex Source: UniProtKB
  • integrin alphav-beta8 complex Source: UniProtKB
  • integrin complex Source: UniProtKB
  • lamellipodium membrane Source: UniProtKB
  • membrane Source: BHF-UCL
  • microvillus membrane Source: UniProtKB
  • phagocytic vesicle Source: Reactome
  • plasma membrane Source: BHF-UCL
  • ruffle membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Membrane

Pathology & Biotechi

Organism-specific databases

DisGeNETi3685.
OpenTargetsiENSG00000138448.
PharmGKBiPA37336.

Chemistry databases

ChEMBLiCHEMBL3660.
DrugBankiDB00098. Anti-thymocyte Globulin (Rabbit).

Polymorphism and mutation databases

DMDMi143811408.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 301 PublicationAdd BLAST30
ChainiPRO_000001630131 – 1048Integrin alpha-VAdd BLAST1018
ChainiPRO_000001630231 – 889Integrin alpha-V heavy chainAdd BLAST859
ChainiPRO_0000016303891 – 1048Integrin alpha-V light chainAdd BLAST158

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi74N-linked (GlcNAc...)2 Publications1
Disulfide bondi89 ↔ 971 Publication
Disulfide bondi138 ↔ 1581 Publication
Disulfide bondi172 ↔ 1851 Publication
Glycosylationi290N-linked (GlcNAc...)Sequence analysis1
Glycosylationi296N-linked (GlcNAc...)Sequence analysis1
Glycosylationi488N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi491 ↔ 5021 Publication
Disulfide bondi508 ↔ 5651 Publication
Glycosylationi554N-linked (GlcNAc...)Sequence analysis1
Glycosylationi615N-linked (GlcNAc...)2 Publications1
Disulfide bondi626 ↔ 6321 Publication
Disulfide bondi698 ↔ 7111 Publication
Glycosylationi704N-linked (GlcNAc...)1 Publication1
Glycosylationi835N-linked (GlcNAc...)Sequence analysis1
Glycosylationi851N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi852 ↔ 914Interchain (between heavy and light chains)1 Publication
Glycosylationi874N-linked (GlcNAc...)2 Publications1
Disulfide bondi904 ↔ 9091 Publication
Glycosylationi945N-linked (GlcNAc...)Sequence analysis1
Glycosylationi973N-linked (GlcNAc...)Sequence analysis1
Glycosylationi980N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

Proteomic databases

EPDiP06756.
MaxQBiP06756.
PaxDbiP06756.
PeptideAtlasiP06756.
PRIDEiP06756.

PTM databases

iPTMnetiP06756.
PhosphoSitePlusiP06756.

Miscellaneous databases

PMAP-CutDBB0LPF4.

Expressioni

Gene expression databases

BgeeiENSG00000138448.
CleanExiHS_ITGAV.
ExpressionAtlasiP06756. baseline and differential.
GenevisibleiP06756. HS.

Organism-specific databases

HPAiCAB002499.
HPA004856.

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta subunit. The alpha subunit is composed of a heavy and a light chain linked by a disulfide bond. Alpha-V (ITGAV) associates with either beta-1 (ITGB1), beta-3 (ITGB3), beta-5 (ITGB5), beta-6 (ITGB6) or beta-8 (ITGB8). Interacts with CIB1 (PubMed:24011356). Interacts with RAB25 (PubMed:17925226). Integrins ITGAV:ITGB3 and ITGAV:ITGB5 interact with FBLN5 (via N-terminus) (By similarity). ITGAV:ITGB3 and ITGAV:ITGB5 interact with NOV (PubMed:12695522). ITGAV:ITGB3 interacts with ADGRA2 (PubMed:16982628). ITGAV:ITGB3 is found in a ternary complex with CX3CR1 and CX3CL1 (PubMed:23125415). ITGAV:ITGB3 is found in a ternary complex with NRG1 and ERBB3 (PubMed:20682778). ITGAV:ITGB3 is found in a ternary complex with FGF1 and FGFR1 (PubMed:18441324). ITGAV:ITGB3 is found in a ternary complex with IGF1 and IGF1R (PubMed:19578119). ITGAV:ITGB3 and ITGAV:ITGB6 interact with FBN1 (PubMed:12807887, PubMed:17158881).By similarity12 Publications
(Microbial infection) Integrin ITGAV:ITGB3 interacts with herpes virus 8/HHV-8 envelope glycoprotein B.1 Publication
(Microbial infection) Integrin ITGAV:ITGB3 and ITGAV:ITGB6 bind to coxsackievirus A9 and coxsackievirus B1 capsid proteins (PubMed:9426447, PubMed:15194773, PubMed:7519807).3 Publications
(Microbial infection) Integrin ITGAV:ITGB6 interacts with herpes simplex 1/HHV-1 envelope glycoprotein H.1 Publication
(Microbial infection) Integrin ITGAV:ITGB5 interacts with adenovirus type C penton protein.1 Publication
(Microbial infection) Integrin ITGAV:ITGB3 interacts with Human parechovirus 1 capsid proteins.1 Publication
(Microbial infection) Integrin ITGAV:ITGB3 interacts with West nile virus envelope protein E.1 Publication
(Microbial infection) Interacts with HIV-1 Tat.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
ITGB3P0510611EBI-298282,EBI-702847
ITGB5P180842EBI-298282,EBI-1223434

GO - Molecular functioni

  • extracellular matrix protein binding Source: UniProtKB
  • fibronectin binding Source: UniProtKB
  • protease binding Source: UniProtKB
  • transforming growth factor beta binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi109891. 45 interactors.
DIPiDIP-31785N.
IntActiP06756. 14 interactors.
MINTiMINT-209462.
STRINGi9606.ENSP00000261023.

Chemistry databases

BindingDBiP06756.

Structurei

Secondary structure

11048
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi39 – 42Combined sources4
Turni45 – 50Combined sources6
Beta strandi51 – 56Combined sources6
Beta strandi60 – 62Combined sources3
Beta strandi65 – 70Combined sources6
Beta strandi85 – 90Combined sources6
Beta strandi92 – 94Combined sources3
Beta strandi97 – 99Combined sources3
Beta strandi109 – 111Combined sources3
Beta strandi114 – 118Combined sources5
Beta strandi126 – 131Combined sources6
Beta strandi134 – 139Combined sources6
Beta strandi147 – 150Combined sources4
Beta strandi157 – 162Combined sources6
Beta strandi165 – 169Combined sources5
Beta strandi174 – 176Combined sources3
Turni178 – 184Combined sources7
Beta strandi189 – 193Combined sources5
Beta strandi197 – 203Combined sources7
Helixi206 – 209Combined sources4
Beta strandi211 – 217Combined sources7
Helixi218 – 223Combined sources6
Beta strandi235 – 239Combined sources5
Helixi245 – 247Combined sources3
Beta strandi254 – 259Combined sources6
Beta strandi261 – 266Combined sources6
Beta strandi268 – 273Combined sources6
Helixi276 – 279Combined sources4
Beta strandi282 – 286Combined sources5
Turni288 – 290Combined sources3
Beta strandi293 – 298Combined sources6
Beta strandi308 – 313Combined sources6
Beta strandi315 – 319Combined sources5
Beta strandi322 – 327Combined sources6
Beta strandi331 – 333Combined sources3
Beta strandi335 – 337Combined sources3
Beta strandi339 – 341Combined sources3
Beta strandi344 – 350Combined sources7
Beta strandi352 – 354Combined sources3
Beta strandi356 – 362Combined sources7
Beta strandi364 – 368Combined sources5
Helixi370 – 372Combined sources3
Beta strandi374 – 379Combined sources6
Beta strandi383 – 385Combined sources3
Beta strandi387 – 392Combined sources6
Helixi397 – 399Combined sources3
Beta strandi402 – 409Combined sources8
Beta strandi410 – 413Combined sources4
Beta strandi418 – 422Combined sources5
Beta strandi428 – 430Combined sources3
Beta strandi434 – 442Combined sources9
Beta strandi447 – 449Combined sources3
Beta strandi451 – 456Combined sources6
Helixi457 – 459Combined sources3
Beta strandi461 – 465Combined sources5
Beta strandi470 – 484Combined sources15
Beta strandi494 – 499Combined sources6
Beta strandi502 – 516Combined sources15
Beta strandi519 – 528Combined sources10
Turni529 – 532Combined sources4
Beta strandi535 – 537Combined sources3
Beta strandi541 – 543Combined sources3
Turni544 – 547Combined sources4
Beta strandi548 – 558Combined sources11
Beta strandi559 – 561Combined sources3
Beta strandi564 – 572Combined sources9
Helixi575 – 577Combined sources3
Beta strandi585 – 593Combined sources9
Turni595 – 597Combined sources3
Beta strandi601 – 603Combined sources3
Beta strandi610 – 612Combined sources3
Beta strandi614 – 622Combined sources9
Turni627 – 630Combined sources4
Beta strandi636 – 641Combined sources6
Beta strandi646 – 648Combined sources3
Beta strandi653 – 663Combined sources11
Beta strandi668 – 670Combined sources3
Beta strandi672 – 676Combined sources5
Beta strandi681 – 686Combined sources6
Beta strandi691 – 693Combined sources3
Beta strandi697 – 701Combined sources5
Beta strandi703 – 705Combined sources3
Beta strandi708 – 712Combined sources5
Beta strandi715 – 717Combined sources3
Beta strandi722 – 731Combined sources10
Beta strandi735 – 737Combined sources3
Beta strandi739 – 748Combined sources10
Beta strandi752 – 754Combined sources3
Beta strandi760 – 767Combined sources8
Beta strandi772 – 786Combined sources15
Turni798 – 802Combined sources5
Beta strandi805 – 814Combined sources10
Beta strandi816 – 818Combined sources3
Beta strandi820 – 833Combined sources14
Beta strandi839 – 856Combined sources18
Beta strandi900 – 902Combined sources3
Turni904 – 906Combined sources3
Beta strandi907 – 916Combined sources10
Beta strandi923 – 933Combined sources11
Helixi935 – 938Combined sources4
Beta strandi941 – 944Combined sources4
Beta strandi948 – 960Combined sources13
Beta strandi964 – 966Combined sources3
Beta strandi971 – 982Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1JV2X-ray3.10A31-987[»]
1L5GX-ray3.20A31-987[»]
1M1XX-ray3.30A31-987[»]
1U8CX-ray3.10A31-987[»]
3IJEX-ray2.90A31-997[»]
4G1EX-ray3.00A31-989[»]
4G1MX-ray2.90A31-989[»]
4MMXX-ray3.32A31-989[»]
4MMYX-ray3.18A31-989[»]
4MMZX-ray3.10A31-989[»]
4O02X-ray3.60A31-992[»]
4UM8X-ray2.85A/C31-625[»]
4UM9X-ray2.50A/C31-625[»]
ProteinModelPortaliP06756.
SMRiP06756.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06756.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati32 – 98FG-GAP 1PROSITE-ProRule annotationAdd BLAST67
Repeati109 – 170FG-GAP 2PROSITE-ProRule annotationAdd BLAST62
Repeati173 – 225FG-GAP 3PROSITE-ProRule annotationAdd BLAST53
Repeati237 – 291FG-GAP 4PROSITE-ProRule annotationAdd BLAST55
Repeati292 – 357FG-GAP 5PROSITE-ProRule annotationAdd BLAST66
Repeati358 – 415FG-GAP 6PROSITE-ProRule annotationAdd BLAST58
Repeati419 – 482FG-GAP 7PROSITE-ProRule annotationAdd BLAST64

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1019 – 1023GFFKR motif5

Sequence similaritiesi

Belongs to the integrin alpha chain family.Curated
Contains 7 FG-GAP repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IPB5. Eukaryota.
ENOG410YR19. LUCA.
GeneTreeiENSGT00760000118782.
HOGENOMiHOG000231603.
HOVERGENiHBG006186.
InParanoidiP06756.
KOiK06487.
OMAiSCFNVRF.
OrthoDBiEOG091G05Z4.
PhylomeDBiP06756.
TreeFamiTF105391.

Family and domain databases

InterProiIPR013517. FG-GAP.
IPR013519. Int_alpha_beta-p.
IPR000413. Integrin_alpha.
IPR013649. Integrin_alpha-2.
IPR018184. Integrin_alpha_C_CS.
IPR032695. Integrin_dom.
[Graphical view]
PfamiPF01839. FG-GAP. 3 hits.
PF00357. Integrin_alpha. 1 hit.
PF08441. Integrin_alpha2. 1 hit.
[Graphical view]
PRINTSiPR01185. INTEGRINA.
SMARTiSM00191. Int_alpha. 5 hits.
[Graphical view]
SUPFAMiSSF69179. SSF69179. 3 hits.
PROSITEiPS51470. FG_GAP. 7 hits.
PS00242. INTEGRIN_ALPHA. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P06756-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAFPPRRRLR LGPRGLPLLL SGLLLPLCRA FNLDVDSPAE YSGPEGSYFG
60 70 80 90 100
FAVDFFVPSA SSRMFLLVGA PKANTTQPGI VEGGQVLKCD WSSTRRCQPI
110 120 130 140 150
EFDATGNRDY AKDDPLEFKS HQWFGASVRS KQDKILACAP LYHWRTEMKQ
160 170 180 190 200
EREPVGTCFL QDGTKTVEYA PCRSQDIDAD GQGFCQGGFS IDFTKADRVL
210 220 230 240 250
LGGPGSFYWQ GQLISDQVAE IVSKYDPNVY SIKYNNQLAT RTAQAIFDDS
260 270 280 290 300
YLGYSVAVGD FNGDGIDDFV SGVPRAARTL GMVYIYDGKN MSSLYNFTGE
310 320 330 340 350
QMAAYFGFSV AATDINGDDY ADVFIGAPLF MDRGSDGKLQ EVGQVSVSLQ
360 370 380 390 400
RASGDFQTTK LNGFEVFARF GSAIAPLGDL DQDGFNDIAI AAPYGGEDKK
410 420 430 440 450
GIVYIFNGRS TGLNAVPSQI LEGQWAARSM PPSFGYSMKG ATDIDKNGYP
460 470 480 490 500
DLIVGAFGVD RAILYRARPV ITVNAGLEVY PSILNQDNKT CSLPGTALKV
510 520 530 540 550
SCFNVRFCLK ADGKGVLPRK LNFQVELLLD KLKQKGAIRR ALFLYSRSPS
560 570 580 590 600
HSKNMTISRG GLMQCEELIA YLRDESEFRD KLTPITIFME YRLDYRTAAD
610 620 630 640 650
TTGLQPILNQ FTPANISRQA HILLDCGEDN VCKPKLEVSV DSDQKKIYIG
660 670 680 690 700
DDNPLTLIVK AQNQGEGAYE AELIVSIPLQ ADFIGVVRNN EALARLSCAF
710 720 730 740 750
KTENQTRQVV CDLGNPMKAG TQLLAGLRFS VHQQSEMDTS VKFDLQIQSS
760 770 780 790 800
NLFDKVSPVV SHKVDLAVLA AVEIRGVSSP DHVFLPIPNW EHKENPETEE
810 820 830 840 850
DVGPVVQHIY ELRNNGPSSF SKAMLHLQWP YKYNNNTLLY ILHYDIDGPM
860 870 880 890 900
NCTSDMEINP LRIKISSLQT TEKNDTVAGQ GERDHLITKR DLALSEGDIH
910 920 930 940 950
TLGCGVAQCL KIVCQVGRLD RGKSAILYVK SLLWTETFMN KENQNHSYSL
960 970 980 990 1000
KSSASFNVIE FPYKNLPIED ITNSTLVTTN VTWGIQPAPM PVPVWVIILA
1010 1020 1030 1040
VLAGLLLLAV LVFVMYRMGF FKRVRPPQEE QEREQLQPHE NGEGNSET
Length:1,048
Mass (Da):116,038
Last modified:April 3, 2007 - v2
Checksum:i364EE25C5303A2D7
GO
Isoform 2 (identifier: P06756-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     175-211: QDIDADGQGFCQGGFSIDFTKADRVLLGGPGSFYWQG → R

Note: No experimental confirmation available.
Show »
Length:1,012
Mass (Da):112,258
Checksum:i132A3F554FCDE8B6
GO
Isoform 3 (identifier: P06756-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-62: MAFPPRRRLR...VDFFVPSASS → MLLGTLLLILYILMLC

Note: No experimental confirmation available.
Show »
Length:1,002
Mass (Da):111,132
Checksum:iD6178F9822C83829
GO

Sequence cautioni

The sequence BAD93131 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti425W → R in AAG03000 (PubMed:10965141).Curated1
Sequence conflicti700F → L in AAI44101 (PubMed:15489334).Curated1
Sequence conflicti1039H → R in AAG03000 (PubMed:10965141).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_024289405I → V.Corresponds to variant rs3738918dbSNPEnsembl.1
Natural variantiVAR_055970548S → A.Corresponds to variant rs2230615dbSNPEnsembl.1
Natural variantiVAR_031547783V → I.7 PublicationsCorresponds to variant rs2230616dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0449141 – 62MAFPP…PSASS → MLLGTLLLILYILMLC in isoform 3. 1 PublicationAdd BLAST62
Alternative sequenceiVSP_024351175 – 211QDIDA…FYWQG → R in isoform 2. 2 PublicationsAdd BLAST37

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14648 mRNA. Translation: AAA36808.1.
AF251841
, AF251818, AF251819, AF251820, AF251821, AF251822, AF251823, AF251824, AF251825, AF251826, AF251827, AF251828, AF251829, AF251830, AF251831, AF251832, AF251833, AF251834, AF251835, AF251836, AF251837, AF251838, AF251839, AF251840 Genomic DNA. Translation: AAG03000.1.
AK302990 mRNA. Translation: BAH13869.1.
AB209894 mRNA. Translation: BAD93131.1. Different initiation.
AC017101 Genomic DNA. Translation: AAY24257.1.
EU332844 Genomic DNA. Translation: ABY87533.1.
CH471058 Genomic DNA. Translation: EAX10934.1.
BC126231 mRNA. Translation: AAI26232.1.
BC136442 mRNA. Translation: AAI36443.1.
BC144100 mRNA. Translation: AAI44101.1.
U07375 Genomic DNA. Translation: AAA61631.1.
CCDSiCCDS2292.1. [P06756-1]
CCDS46470.1. [P06756-2]
CCDS46471.1. [P06756-3]
PIRiA27421.
RefSeqiNP_001138471.1. NM_001144999.2.
NP_001138472.1. NM_001145000.2.
NP_002201.1. NM_002210.4.
UniGeneiHs.436873.

Genome annotation databases

EnsembliENST00000261023; ENSP00000261023; ENSG00000138448. [P06756-1]
ENST00000374907; ENSP00000364042; ENSG00000138448. [P06756-2]
ENST00000433736; ENSP00000404291; ENSG00000138448. [P06756-3]
GeneIDi3685.
KEGGihsa:3685.
UCSCiuc002upq.5. human. [P06756-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14648 mRNA. Translation: AAA36808.1.
AF251841
, AF251818, AF251819, AF251820, AF251821, AF251822, AF251823, AF251824, AF251825, AF251826, AF251827, AF251828, AF251829, AF251830, AF251831, AF251832, AF251833, AF251834, AF251835, AF251836, AF251837, AF251838, AF251839, AF251840 Genomic DNA. Translation: AAG03000.1.
AK302990 mRNA. Translation: BAH13869.1.
AB209894 mRNA. Translation: BAD93131.1. Different initiation.
AC017101 Genomic DNA. Translation: AAY24257.1.
EU332844 Genomic DNA. Translation: ABY87533.1.
CH471058 Genomic DNA. Translation: EAX10934.1.
BC126231 mRNA. Translation: AAI26232.1.
BC136442 mRNA. Translation: AAI36443.1.
BC144100 mRNA. Translation: AAI44101.1.
U07375 Genomic DNA. Translation: AAA61631.1.
CCDSiCCDS2292.1. [P06756-1]
CCDS46470.1. [P06756-2]
CCDS46471.1. [P06756-3]
PIRiA27421.
RefSeqiNP_001138471.1. NM_001144999.2.
NP_001138472.1. NM_001145000.2.
NP_002201.1. NM_002210.4.
UniGeneiHs.436873.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1JV2X-ray3.10A31-987[»]
1L5GX-ray3.20A31-987[»]
1M1XX-ray3.30A31-987[»]
1U8CX-ray3.10A31-987[»]
3IJEX-ray2.90A31-997[»]
4G1EX-ray3.00A31-989[»]
4G1MX-ray2.90A31-989[»]
4MMXX-ray3.32A31-989[»]
4MMYX-ray3.18A31-989[»]
4MMZX-ray3.10A31-989[»]
4O02X-ray3.60A31-992[»]
4UM8X-ray2.85A/C31-625[»]
4UM9X-ray2.50A/C31-625[»]
ProteinModelPortaliP06756.
SMRiP06756.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109891. 45 interactors.
DIPiDIP-31785N.
IntActiP06756. 14 interactors.
MINTiMINT-209462.
STRINGi9606.ENSP00000261023.

Chemistry databases

BindingDBiP06756.
ChEMBLiCHEMBL3660.
DrugBankiDB00098. Anti-thymocyte Globulin (Rabbit).

PTM databases

iPTMnetiP06756.
PhosphoSitePlusiP06756.

Polymorphism and mutation databases

DMDMi143811408.

Proteomic databases

EPDiP06756.
MaxQBiP06756.
PaxDbiP06756.
PeptideAtlasiP06756.
PRIDEiP06756.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000261023; ENSP00000261023; ENSG00000138448. [P06756-1]
ENST00000374907; ENSP00000364042; ENSG00000138448. [P06756-2]
ENST00000433736; ENSP00000404291; ENSG00000138448. [P06756-3]
GeneIDi3685.
KEGGihsa:3685.
UCSCiuc002upq.5. human. [P06756-1]

Organism-specific databases

CTDi3685.
DisGeNETi3685.
GeneCardsiITGAV.
HGNCiHGNC:6150. ITGAV.
HPAiCAB002499.
HPA004856.
MIMi193210. gene.
neXtProtiNX_P06756.
OpenTargetsiENSG00000138448.
PharmGKBiPA37336.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IPB5. Eukaryota.
ENOG410YR19. LUCA.
GeneTreeiENSGT00760000118782.
HOGENOMiHOG000231603.
HOVERGENiHBG006186.
InParanoidiP06756.
KOiK06487.
OMAiSCFNVRF.
OrthoDBiEOG091G05Z4.
PhylomeDBiP06756.
TreeFamiTF105391.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000138448-MONOMER.
ReactomeiR-HSA-1236973. Cross-presentation of particulate exogenous antigens (phagosomes).
R-HSA-1566948. Elastic fibre formation.
R-HSA-210990. PECAM1 interactions.
R-HSA-2129379. Molecules associated with elastic fibres.
R-HSA-216083. Integrin cell surface interactions.
R-HSA-3000157. Laminin interactions.
R-HSA-3000170. Syndecan interactions.
R-HSA-3000178. ECM proteoglycans.
R-HSA-4420097. VEGFA-VEGFR2 Pathway.
R-HSA-445144. Signal transduction by L1.
R-HSA-6798695. Neutrophil degranulation.
SignaLinkiP06756.
SIGNORiP06756.

Miscellaneous databases

ChiTaRSiITGAV. human.
EvolutionaryTraceiP06756.
GeneWikiiITGAV.
GenomeRNAii3685.
PMAP-CutDBB0LPF4.
PROiP06756.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000138448.
CleanExiHS_ITGAV.
ExpressionAtlasiP06756. baseline and differential.
GenevisibleiP06756. HS.

Family and domain databases

InterProiIPR013517. FG-GAP.
IPR013519. Int_alpha_beta-p.
IPR000413. Integrin_alpha.
IPR013649. Integrin_alpha-2.
IPR018184. Integrin_alpha_C_CS.
IPR032695. Integrin_dom.
[Graphical view]
PfamiPF01839. FG-GAP. 3 hits.
PF00357. Integrin_alpha. 1 hit.
PF08441. Integrin_alpha2. 1 hit.
[Graphical view]
PRINTSiPR01185. INTEGRINA.
SMARTiSM00191. Int_alpha. 5 hits.
[Graphical view]
SUPFAMiSSF69179. SSF69179. 3 hits.
PROSITEiPS51470. FG_GAP. 7 hits.
PS00242. INTEGRIN_ALPHA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiITAV_HUMAN
AccessioniPrimary (citable) accession number: P06756
Secondary accession number(s): A0AV67
, B0LPF4, B7Z883, B7ZLX0, D3DPG8, E7EWZ6, Q53SK4, Q59EB7, Q6LD15
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: April 3, 2007
Last modified: November 30, 2016
This is version 204 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  2. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.