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P06756

- ITAV_HUMAN

UniProt

P06756 - ITAV_HUMAN

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Protein

Integrin alpha-V

Gene

ITGAV

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

Functioni

The alpha-V 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. In case of HIV-1 infection, the interaction with extracellular viral Tat protein seems to enhance angiogenesis in Kaposi's sarcoma lesions.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi260 – 2689Sequence Analysis
Calcium bindingi314 – 3229Sequence Analysis
Calcium bindingi379 – 3879Sequence Analysis
Calcium bindingi443 – 4519Sequence Analysis

GO - Molecular functioni

  1. extracellular matrix binding Source: UniProtKB
  2. extracellular matrix protein binding Source: UniProtKB
  3. fibronectin binding Source: UniProtKB
  4. metal ion binding Source: UniProtKB-KW
  5. protease binding Source: UniProtKB
  6. transforming growth factor beta binding Source: BHF-UCL
  7. virus receptor activity Source: UniProtKB-KW
  8. voltage-gated calcium channel activity Source: UniProtKB

GO - Biological processi

  1. angiogenesis Source: UniProtKB
  2. antigen processing and presentation of exogenous peptide antigen via MHC class I Source: Reactome
  3. antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent Source: Reactome
  4. antigen processing and presentation of peptide antigen via MHC class I Source: Reactome
  5. apolipoprotein A-I-mediated signaling pathway Source: UniProtKB
  6. apoptotic cell clearance Source: Ensembl
  7. axon guidance Source: Reactome
  8. blood coagulation Source: Reactome
  9. calcium ion transmembrane transport Source: UniProtKB
  10. cell adhesion Source: BHF-UCL
  11. cell growth Source: UniProtKB
  12. cell-matrix adhesion Source: UniProtKB
  13. cell migration Source: UniProtKB
  14. cell-substrate adhesion Source: UniProtKB
  15. endodermal cell differentiation Source: UniProtKB
  16. entry of symbiont into host cell by promotion of host phagocytosis Source: BHF-UCL
  17. ERK1 and ERK2 cascade Source: BHF-UCL
  18. extracellular matrix organization Source: Reactome
  19. extrinsic apoptotic signaling pathway in absence of ligand Source: BHF-UCL
  20. heterotypic cell-cell adhesion Source: UniProtKB
  21. integrin-mediated signaling pathway Source: UniProtKB
  22. leukocyte migration Source: Reactome
  23. negative chemotaxis Source: UniProtKB
  24. negative regulation of entry of bacterium into host cell Source: BHF-UCL
  25. negative regulation of extrinsic apoptotic signaling pathway Source: BHF-UCL
  26. negative regulation of lipid storage Source: BHF-UCL
  27. negative regulation of lipid transport Source: BHF-UCL
  28. negative regulation of lipoprotein metabolic process Source: BHF-UCL
  29. negative regulation of low-density lipoprotein particle receptor biosynthetic process Source: BHF-UCL
  30. negative regulation of macrophage derived foam cell differentiation Source: BHF-UCL
  31. positive regulation of cell adhesion Source: BHF-UCL
  32. positive regulation of cell migration Source: Ensembl
  33. positive regulation of cell proliferation Source: BHF-UCL
  34. positive regulation of osteoblast proliferation Source: Ensembl
  35. regulation of apoptotic cell clearance Source: BHF-UCL
  36. regulation of phagocytosis Source: BHF-UCL
  37. substrate adhesion-dependent cell spreading Source: UniProtKB
  38. 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

ReactomeiREACT_111174. Cross-presentation of particulate exogenous antigens (phagosomes).
REACT_12519. PECAM1 interactions.
REACT_13552. Integrin cell surface interactions.
REACT_150331. Molecules associated with elastic fibres.
REACT_150366. Elastic fibre formation.
REACT_163906. ECM proteoglycans.
REACT_163942. Syndecan interactions.
REACT_169262. Laminin interactions.
REACT_22272. Signal transduction by L1.
REACT_228166. VEGFA-VEGFR2 Pathway.
SignaLinkiP06756.

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
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:6150. ITGAV.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini31 – 992962ExtracellularSequence AnalysisAdd
BLAST
Transmembranei993 – 101624HelicalSequence AnalysisAdd
BLAST
Topological domaini1017 – 104832CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. alphav-beta3 integrin-IGF-1-IGF1R complex Source: BHF-UCL
  2. cell surface Source: UniProtKB
  3. external side of plasma membrane Source: Ensembl
  4. extracellular vesicular exosome Source: UniProtKB
  5. filopodium membrane Source: UniProtKB
  6. focal adhesion Source: UniProtKB
  7. integral component of plasma membrane Source: UniProtKB
  8. integrin alphav-beta3 complex Source: UniProtKB
  9. integrin alphav-beta5 complex Source: UniProtKB
  10. integrin alphav-beta8 complex Source: UniProtKB
  11. integrin complex Source: UniProtKB
  12. lamellipodium membrane Source: UniProtKB
  13. membrane Source: BHF-UCL
  14. microvillus membrane Source: UniProtKB
  15. phagocytic vesicle Source: Reactome
  16. plasma membrane Source: BHF-UCL
  17. ruffle membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA37336.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 30301 PublicationAdd
BLAST
Chaini31 – 10481018Integrin alpha-VPRO_0000016301Add
BLAST
Chaini31 – 889859Integrin alpha-V heavy chainPRO_0000016302Add
BLAST
Chaini891 – 1048158Integrin alpha-V light chainPRO_0000016303Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi74 – 741N-linked (GlcNAc...)2 Publications
Disulfide bondi89 ↔ 971 Publication
Disulfide bondi138 ↔ 1581 Publication
Disulfide bondi172 ↔ 1851 Publication
Glycosylationi290 – 2901N-linked (GlcNAc...)Sequence Analysis
Glycosylationi296 – 2961N-linked (GlcNAc...)Sequence Analysis
Glycosylationi488 – 4881N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi491 ↔ 5021 Publication
Disulfide bondi508 ↔ 5651 Publication
Glycosylationi554 – 5541N-linked (GlcNAc...)Sequence Analysis
Glycosylationi615 – 6151N-linked (GlcNAc...)2 Publications
Disulfide bondi626 ↔ 6321 Publication
Disulfide bondi698 ↔ 7111 Publication
Glycosylationi704 – 7041N-linked (GlcNAc...)1 Publication
Glycosylationi835 – 8351N-linked (GlcNAc...)Sequence Analysis
Glycosylationi851 – 8511N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi852 ↔ 914Interchain (between heavy and light chains)1 Publication
Glycosylationi874 – 8741N-linked (GlcNAc...)2 Publications
Disulfide bondi904 ↔ 9091 Publication
Glycosylationi945 – 9451N-linked (GlcNAc...)Sequence Analysis
Glycosylationi973 – 9731N-linked (GlcNAc...)Sequence Analysis
Glycosylationi980 – 9801N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP06756.
PaxDbiP06756.
PRIDEiP06756.

PTM databases

PhosphoSiteiP06756.

Miscellaneous databases

PMAP-CutDBB0LPF4.

Expressioni

Gene expression databases

BgeeiP06756.
CleanExiHS_ITGAV.
ExpressionAtlasiP06756. baseline and differential.
GenevestigatoriP06756.

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 associates with either beta-1, beta-3, beta-5, beta-6 or beta-8 subunit. Interacts with HIV-1 Tat. Alpha-V/beta-6 binds to foot-and-mouth disease virus (FMDV) VP1 protein and acts as a receptor for this virus (By similarity). Alpha-V/beta-6 binds to coxsackievirus A9 and coxsackievirus B1 capsid proteins and acts as a receptor for these viruses. Interacts with RAB25. Alpha-V/beta-3 interacts with herpes virus 8/HHV-8 glycoprotein B and acts as a receptor for the virus. Interacts with CIB1.By similarity7 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi109891. 23 interactions.
DIPiDIP-31785N.
IntActiP06756. 11 interactions.
MINTiMINT-209462.
STRINGi9606.ENSP00000261023.

Structurei

Secondary structure

1
1048
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi39 – 424Combined sources
Turni45 – 506Combined sources
Beta strandi51 – 566Combined sources
Beta strandi65 – 706Combined sources
Beta strandi85 – 906Combined sources
Beta strandi92 – 943Combined sources
Beta strandi97 – 993Combined sources
Beta strandi109 – 1113Combined sources
Beta strandi114 – 1185Combined sources
Beta strandi126 – 1316Combined sources
Beta strandi134 – 1396Combined sources
Beta strandi147 – 1493Combined sources
Beta strandi157 – 1626Combined sources
Beta strandi165 – 1695Combined sources
Beta strandi174 – 1763Combined sources
Turni179 – 1846Combined sources
Beta strandi189 – 1935Combined sources
Beta strandi195 – 2039Combined sources
Helixi206 – 2094Combined sources
Beta strandi211 – 2177Combined sources
Helixi218 – 2247Combined sources
Beta strandi235 – 2395Combined sources
Helixi245 – 2473Combined sources
Beta strandi254 – 2596Combined sources
Beta strandi262 – 2665Combined sources
Beta strandi268 – 2736Combined sources
Helixi276 – 2794Combined sources
Beta strandi282 – 2865Combined sources
Beta strandi288 – 2914Combined sources
Beta strandi293 – 2986Combined sources
Beta strandi310 – 3134Combined sources
Beta strandi317 – 3193Combined sources
Beta strandi322 – 3276Combined sources
Beta strandi331 – 3333Combined sources
Beta strandi335 – 3373Combined sources
Beta strandi339 – 3413Combined sources
Beta strandi344 – 3496Combined sources
Beta strandi352 – 3543Combined sources
Beta strandi357 – 3626Combined sources
Beta strandi364 – 3685Combined sources
Beta strandi372 – 3798Combined sources
Beta strandi383 – 3853Combined sources
Beta strandi387 – 3926Combined sources
Beta strandi396 – 3994Combined sources
Beta strandi402 – 4098Combined sources
Beta strandi410 – 4134Combined sources
Beta strandi418 – 4225Combined sources
Beta strandi428 – 4303Combined sources
Beta strandi434 – 4429Combined sources
Beta strandi445 – 4495Combined sources
Beta strandi451 – 4566Combined sources
Helixi457 – 4593Combined sources
Beta strandi461 – 4655Combined sources
Beta strandi470 – 48112Combined sources
Beta strandi482 – 4843Combined sources
Beta strandi494 – 4996Combined sources
Beta strandi501 – 51212Combined sources
Beta strandi514 – 5163Combined sources
Beta strandi519 – 53012Combined sources
Helixi531 – 5344Combined sources
Beta strandi535 – 5373Combined sources
Beta strandi541 – 5433Combined sources
Turni544 – 5463Combined sources
Beta strandi548 – 56114Combined sources
Beta strandi564 – 5729Combined sources
Turni575 – 5773Combined sources
Beta strandi585 – 5939Combined sources
Turni595 – 5973Combined sources
Beta strandi601 – 6033Combined sources
Beta strandi614 – 6229Combined sources
Turni627 – 6304Combined sources
Beta strandi636 – 6416Combined sources
Beta strandi646 – 6483Combined sources
Beta strandi653 – 66311Combined sources
Beta strandi668 – 6703Combined sources
Beta strandi672 – 6765Combined sources
Beta strandi681 – 6866Combined sources
Beta strandi691 – 6933Combined sources
Beta strandi697 – 7015Combined sources
Beta strandi703 – 7053Combined sources
Beta strandi708 – 7125Combined sources
Beta strandi715 – 7173Combined sources
Beta strandi722 – 73110Combined sources
Beta strandi735 – 7373Combined sources
Beta strandi739 – 74810Combined sources
Beta strandi752 – 7543Combined sources
Beta strandi760 – 7678Combined sources
Beta strandi772 – 78615Combined sources
Turni798 – 8025Combined sources
Beta strandi805 – 81410Combined sources
Beta strandi816 – 8183Combined sources
Beta strandi820 – 83314Combined sources
Beta strandi839 – 85618Combined sources
Beta strandi900 – 9023Combined sources
Turni904 – 9063Combined sources
Beta strandi907 – 91610Combined sources
Beta strandi923 – 93311Combined sources
Helixi935 – 9384Combined sources
Beta strandi941 – 9444Combined sources
Beta strandi948 – 96013Combined sources
Beta strandi964 – 9663Combined sources
Beta strandi971 – 98212Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP06756.
SMRiP06756. Positions 31-989.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06756.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati32 – 9867FG-GAP 1Add
BLAST
Repeati109 – 17062FG-GAP 2Add
BLAST
Repeati173 – 22553FG-GAP 3Add
BLAST
Repeati237 – 29559FG-GAP 4Add
BLAST
Repeati296 – 35762FG-GAP 5Add
BLAST
Repeati358 – 41558FG-GAP 6Add
BLAST
Repeati419 – 48264FG-GAP 7Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1019 – 10235GFFKR motif

Sequence similaritiesi

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

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG26407.
GeneTreeiENSGT00760000118782.
HOVERGENiHBG006186.
InParanoidiP06756.
KOiK06487.
OMAiDKNGYPD.
OrthoDBiEOG7R830R.
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.
[Graphical view]
PfamiPF01839. FG-GAP. 2 hits.
PF00357. Integrin_alpha. 1 hit.
PF08441. Integrin_alpha2. 1 hit.
[Graphical view]
PRINTSiPR01185. INTEGRINA.
SMARTiSM00191. Int_alpha. 5 hits.
[Graphical view]
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. Align

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 BAD93131.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti425 – 4251W → R in AAG03000. (PubMed:10965141)Curated
Sequence conflicti700 – 7001F → L in AAI44101. (PubMed:15489334)Curated
Sequence conflicti1039 – 10391H → R in AAG03000. (PubMed:10965141)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti405 – 4051I → V.
Corresponds to variant rs3738918 [ dbSNP | Ensembl ].
VAR_024289
Natural varianti548 – 5481S → A.
Corresponds to variant rs2230615 [ dbSNP | Ensembl ].
VAR_055970
Natural varianti783 – 7831V → I.7 Publications
Corresponds to variant rs2230616 [ dbSNP | Ensembl ].
VAR_031547

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 6262MAFPP…PSASS → MLLGTLLLILYILMLC in isoform 3. 1 PublicationVSP_044914Add
BLAST
Alternative sequencei175 – 21137QDIDA…FYWQG → R in isoform 2. 2 PublicationsVSP_024351Add
BLAST

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.4. human. [P06756-1]

Polymorphism databases

DMDMi143811408.

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 .
CCDSi CCDS2292.1. [P06756-1 ]
CCDS46470.1. [P06756-2 ]
CCDS46471.1. [P06756-3 ]
PIRi A27421.
RefSeqi NP_001138471.1. NM_001144999.2.
NP_001138472.1. NM_001145000.2.
NP_002201.1. NM_002210.4.
UniGenei Hs.436873.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1JV2 X-ray 3.10 A 31-987 [» ]
1L5G X-ray 3.20 A 31-987 [» ]
1M1X X-ray 3.30 A 31-987 [» ]
1U8C X-ray 3.10 A 31-987 [» ]
3IJE X-ray 2.90 A 31-997 [» ]
4G1E X-ray 3.00 A 31-989 [» ]
4G1M X-ray 2.90 A 31-989 [» ]
4MMX X-ray 3.32 A 31-989 [» ]
4MMY X-ray 3.18 A 31-989 [» ]
4MMZ X-ray 3.10 A 31-989 [» ]
4O02 X-ray 3.60 A 31-992 [» ]
ProteinModelPortali P06756.
SMRi P06756. Positions 31-989.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109891. 23 interactions.
DIPi DIP-31785N.
IntActi P06756. 11 interactions.
MINTi MINT-209462.
STRINGi 9606.ENSP00000261023.

Chemistry

BindingDBi P06756.
ChEMBLi CHEMBL1907598.
DrugBanki DB00098. Antithymocyte globulin.

PTM databases

PhosphoSitei P06756.

Polymorphism databases

DMDMi 143811408.

Proteomic databases

MaxQBi P06756.
PaxDbi P06756.
PRIDEi P06756.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000261023 ; ENSP00000261023 ; ENSG00000138448 . [P06756-1 ]
ENST00000374907 ; ENSP00000364042 ; ENSG00000138448 . [P06756-2 ]
ENST00000433736 ; ENSP00000404291 ; ENSG00000138448 . [P06756-3 ]
GeneIDi 3685.
KEGGi hsa:3685.
UCSCi uc002upq.4. human. [P06756-1 ]

Organism-specific databases

CTDi 3685.
GeneCardsi GC02P187418.
HGNCi HGNC:6150. ITGAV.
HPAi CAB002499.
HPA004856.
MIMi 193210. gene.
neXtProti NX_P06756.
PharmGKBi PA37336.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG26407.
GeneTreei ENSGT00760000118782.
HOVERGENi HBG006186.
InParanoidi P06756.
KOi K06487.
OMAi DKNGYPD.
OrthoDBi EOG7R830R.
PhylomeDBi P06756.
TreeFami TF105391.

Enzyme and pathway databases

Reactomei REACT_111174. Cross-presentation of particulate exogenous antigens (phagosomes).
REACT_12519. PECAM1 interactions.
REACT_13552. Integrin cell surface interactions.
REACT_150331. Molecules associated with elastic fibres.
REACT_150366. Elastic fibre formation.
REACT_163906. ECM proteoglycans.
REACT_163942. Syndecan interactions.
REACT_169262. Laminin interactions.
REACT_22272. Signal transduction by L1.
REACT_228166. VEGFA-VEGFR2 Pathway.
SignaLinki P06756.

Miscellaneous databases

ChiTaRSi ITGAV. human.
EvolutionaryTracei P06756.
GeneWikii ITGAV.
GenomeRNAii 3685.
NextBioi 14423.
PMAP-CutDB B0LPF4.
PROi P06756.
SOURCEi Search...

Gene expression databases

Bgeei P06756.
CleanExi HS_ITGAV.
ExpressionAtlasi P06756. baseline and differential.
Genevestigatori P06756.

Family and domain databases

InterProi IPR013517. FG-GAP.
IPR013519. Int_alpha_beta-p.
IPR000413. Integrin_alpha.
IPR013649. Integrin_alpha-2.
IPR018184. Integrin_alpha_C_CS.
[Graphical view ]
Pfami PF01839. FG-GAP. 2 hits.
PF00357. Integrin_alpha. 1 hit.
PF08441. Integrin_alpha2. 1 hit.
[Graphical view ]
PRINTSi PR01185. INTEGRINA.
SMARTi SM00191. Int_alpha. 5 hits.
[Graphical view ]
PROSITEi PS51470. FG_GAP. 7 hits.
PS00242. INTEGRIN_ALPHA. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Amino acid sequence of the vitronectin receptor alpha subunit and comparative expression of adhesion receptor mRNAs."
    Suzuki S., Argraves W.S., Arai H., Languino L.R., Pierschbacher M.D., Ruoslahti E.
    J. Biol. Chem. 262:14080-14085(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ILE-783.
  2. "Cloning and characterisation of ITGAV, the genomic sequence for human cell adhesion protein (vitronectin) receptor alpha subunit, CD51."
    Sims M.A., Field S., Barnes M.R., Shaikh N., Ellington K., Murphy K.E., Spurr N.K., Campbell D.A.
    Cytogenet. Cell Genet. 89:268-271(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), VARIANT ILE-783.
    Tissue: Testis.
  4. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT ILE-783.
    Tissue: Aortic endothelium.
  5. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ILE-783.
  7. NHLBI resequencing and genotyping service (RS&G)
    Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ILE-783.
  8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), VARIANT ILE-783.
  9. "The integrin alpha v gene: identification and characterization of the promoter region."
    Donahue J.P., Sugg N., Hawiger J.
    Biochim. Biophys. Acta 1219:228-232(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-62.
  10. "cDNA and amino acid sequences of the cell adhesion protein receptor recognizing vitronectin reveal a transmembrane domain and homologies with other adhesion protein receptors."
    Suzuki S., Argraves W.S., Pytela R., Arai H., Krusius T., Pierschbacher M.D., Ruoslahti E.
    Proc. Natl. Acad. Sci. U.S.A. 83:8614-8618(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 413-1048, VARIANT ILE-783.
  11. "A novel vitronectin receptor integrin (alpha v beta x) is responsible for distinct adhesive properties of carcinoma cells."
    Cheresh D.A., Smith J.W., Cooper H.M., Quaranta V.
    Cell 57:59-69(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 31-41.
  12. "Integrin alpha v beta 6 enhances coxsackievirus B1 lytic infection of human colon cancer cells."
    Agrez M.V., Shafren D.R., Gu X., Cox K., Sheppard D., Barry R.D.
    Virology 239:71-77(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH COXSACKIEVIRUS B1 CAPSID PROTEINS.
  13. "The Tat protein of human immunodeficiency virus type-1 promotes vascular cell growth and locomotion by engaging the alpha5beta1 and alphavbeta3 integrins and by mobilizing sequestered basic fibroblast growth factor."
    Barillari G., Sgadari C., Fiorelli V., Samaniego F., Colombini S., Manzari V., Modesti A., Nair B.C., Cafaro A., Stuerzl M., Ensoli B.
    Blood 94:663-672(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HIV-1 TAT.
  14. "The epithelial integrin alphavbeta6 is a receptor for foot-and-mouth disease virus."
    Jackson T., Sheppard D., Denyer M., Blakemore W., King A.M.
    J. Virol. 74:4949-4956(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FMDV VP1.
  15. "Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry."
    Zhang H., Li X.-J., Martin D.B., Aebersold R.
    Nat. Biotechnol. 21:660-666(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT ASN-615.
  16. "Mass spectrometric based mapping of the disulfide bonding patterns of integrin alpha chains."
    Krokhin O.V., Cheng K., Sousa S.L., Ens W., Standing K.G., Wilkins J.A.
    Biochemistry 42:12950-12959(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISULFIDE BONDS.
  17. "Integrin alpha v beta 6 is an RGD-dependent receptor for coxsackievirus A9."
    Williams C.H., Kajander T., Hyypia T., Jackson T., Sheppard D., Stanway G.
    J. Virol. 78:6967-6973(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH COXSACKIEVIRUS A9 CAPSID PROTEINS.
  18. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  19. "Rab25 associates with alpha5beta1 integrin to promote invasive migration in 3D microenvironments."
    Caswell P.T., Spence H.J., Parsons M., White D.P., Clark K., Cheng K.W., Mills G.B., Humphries M.J., Messent A.J., Anderson K.I., McCaffrey M.W., Ozanne B.W., Norman J.C.
    Dev. Cell 13:496-510(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RAB25.
  20. "Integrin alphaVbeta3 Binds to the RGD motif of glycoprotein B of Kaposi's sarcoma-associated herpesvirus and functions as an RGD-dependent entry receptor."
    Garrigues H.J., Rubinchikova Y.E., Dipersio C.M., Rose T.M.
    J. Virol. 82:1570-1580(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HHV-8 GLYCOPROTEIN B.
  21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  22. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
    Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
    J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-74; ASN-615; ASN-704 AND ASN-874.
    Tissue: Liver.
  23. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
    Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
    Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-74 AND ASN-874.
    Tissue: Leukemic T-cell.
  24. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  25. "Identification of novel integrin binding partners for calcium and integrin binding protein 1 (CIB1): structural and thermodynamic basis of CIB1 promiscuity."
    Freeman T.C. Jr., Black J.L., Bray H.G., Dagliyan O., Wu Y.I., Tripathy A., Dokholyan N.V., Leisner T.M., Parise L.V.
    Biochemistry 52:7082-7090(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CIB1.
  26. "Crystal structure of the extracellular segment of integrin alpha Vbeta3."
    Xiong J.P., Stehle T., Diefenbach B., Zhang R., Dunker R., Scott D.L., Joachimiak A., Goodman S.L., Arnaout M.A.
    Science 294:339-345(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 31-987.

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 26, 2014
This is version 182 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

External Data

Dasty 3