Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P06756

- ITAV_HUMAN

UniProt

P06756 - ITAV_HUMAN

Protein

Integrin alpha-V

Gene

ITGAV

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 180 (01 Oct 2014)
      Sequence version 2 (03 Apr 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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. metal ion binding Source: UniProtKB-KW
    2. protein binding Source: UniProtKB
    3. transforming growth factor beta binding Source: BHF-UCL
    4. virus receptor activity Source: UniProtKB-KW
    5. 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. apoptotic cell clearance Source: Ensembl
    6. axon guidance Source: Reactome
    7. blood coagulation Source: Reactome
    8. calcium ion transmembrane transport Source: UniProtKB
    9. cell adhesion Source: BHF-UCL
    10. cell-matrix adhesion Source: UniProtKB
    11. cell-substrate adhesion Source: UniProtKB
    12. entry of symbiont into host cell by promotion of host phagocytosis Source: BHF-UCL
    13. ERK1 and ERK2 cascade Source: BHF-UCL
    14. extracellular matrix organization Source: Reactome
    15. extrinsic apoptotic signaling pathway in absence of ligand Source: BHF-UCL
    16. integrin-mediated signaling pathway Source: UniProtKB
    17. leukocyte migration Source: Reactome
    18. negative regulation of entry of bacterium into host cell Source: BHF-UCL
    19. negative regulation of extrinsic apoptotic signaling pathway Source: BHF-UCL
    20. negative regulation of lipid storage Source: BHF-UCL
    21. negative regulation of lipid transport Source: BHF-UCL
    22. negative regulation of lipoprotein metabolic process Source: BHF-UCL
    23. negative regulation of low-density lipoprotein particle receptor biosynthetic process Source: BHF-UCL
    24. negative regulation of macrophage derived foam cell differentiation Source: BHF-UCL
    25. positive regulation of cell adhesion Source: BHF-UCL
    26. positive regulation of cell migration Source: Ensembl
    27. positive regulation of cell proliferation Source: BHF-UCL
    28. positive regulation of osteoblast proliferation Source: Ensembl
    29. regulation of apoptotic cell clearance Source: BHF-UCL
    30. regulation of phagocytosis Source: BHF-UCL
    31. viral entry into host cell Source: BHF-UCL

    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.
    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

    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: UniProt
    5. integral component of plasma membrane Source: UniProtKB
    6. integrin complex Source: UniProtKB
    7. membrane Source: BHF-UCL
    8. phagocytic vesicle Source: Reactome
    9. plasma membrane Source: BHF-UCL

    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

    ArrayExpressiP06756.
    BgeeiP06756.
    CleanExiHS_ITGAV.
    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. 20 interactions.
    DIPiDIP-31785N.
    IntActiP06756. 12 interactions.
    MINTiMINT-209462.
    STRINGi9606.ENSP00000261023.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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, 992-1031.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP06756.

    Topological domain

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

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei993 – 101624HelicalSequence AnalysisAdd
    BLAST

    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.
    HOVERGENiHBG006186.
    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

    MAFPPRRRLR LGPRGLPLLL SGLLLPLCRA FNLDVDSPAE YSGPEGSYFG     50
    FAVDFFVPSA SSRMFLLVGA PKANTTQPGI VEGGQVLKCD WSSTRRCQPI 100
    EFDATGNRDY AKDDPLEFKS HQWFGASVRS KQDKILACAP LYHWRTEMKQ 150
    EREPVGTCFL QDGTKTVEYA PCRSQDIDAD GQGFCQGGFS IDFTKADRVL 200
    LGGPGSFYWQ GQLISDQVAE IVSKYDPNVY SIKYNNQLAT RTAQAIFDDS 250
    YLGYSVAVGD FNGDGIDDFV SGVPRAARTL GMVYIYDGKN MSSLYNFTGE 300
    QMAAYFGFSV AATDINGDDY ADVFIGAPLF MDRGSDGKLQ EVGQVSVSLQ 350
    RASGDFQTTK LNGFEVFARF GSAIAPLGDL DQDGFNDIAI AAPYGGEDKK 400
    GIVYIFNGRS TGLNAVPSQI LEGQWAARSM PPSFGYSMKG ATDIDKNGYP 450
    DLIVGAFGVD RAILYRARPV ITVNAGLEVY PSILNQDNKT CSLPGTALKV 500
    SCFNVRFCLK ADGKGVLPRK LNFQVELLLD KLKQKGAIRR ALFLYSRSPS 550
    HSKNMTISRG GLMQCEELIA YLRDESEFRD KLTPITIFME YRLDYRTAAD 600
    TTGLQPILNQ FTPANISRQA HILLDCGEDN VCKPKLEVSV DSDQKKIYIG 650
    DDNPLTLIVK AQNQGEGAYE AELIVSIPLQ ADFIGVVRNN EALARLSCAF 700
    KTENQTRQVV CDLGNPMKAG TQLLAGLRFS VHQQSEMDTS VKFDLQIQSS 750
    NLFDKVSPVV SHKVDLAVLA AVEIRGVSSP DHVFLPIPNW EHKENPETEE 800
    DVGPVVQHIY ELRNNGPSSF SKAMLHLQWP YKYNNNTLLY ILHYDIDGPM 850
    NCTSDMEINP LRIKISSLQT TEKNDTVAGQ GERDHLITKR DLALSEGDIH 900
    TLGCGVAQCL KIVCQVGRLD RGKSAILYVK SLLWTETFMN KENQNHSYSL 950
    KSSASFNVIE FPYKNLPIED ITNSTLVTTN VTWGIQPAPM PVPVWVIILA 1000
    VLAGLLLLAV LVFVMYRMGF FKRVRPPQEE QEREQLQPHE NGEGNSET 1048
    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.

    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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, 992-1031.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109891. 20 interactions.
    DIPi DIP-31785N.
    IntActi P06756. 12 interactions.
    MINTi MINT-209462.
    STRINGi 9606.ENSP00000261023.

    Chemistry

    BindingDBi P06756.
    ChEMBLi CHEMBL2096675.

    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.
    HOVERGENi HBG006186.
    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.
    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

    ArrayExpressi P06756.
    Bgeei P06756.
    CleanExi HS_ITGAV.
    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

    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: October 1, 2014
    This is version 180 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