Reviewed, UniProtKB/Swiss-Prot P06756 (ITAV_HUMAN)

Names and origin

Protein names

Recommended name:
    Integrin alpha-V
Alternative name(s):
    Vitronectin receptor subunit alpha
    CD_antigen=CD51
Cleaved into the following 2 chains:
    1- Recommended name:
            Integrin alpha-V heavy chain
    2- Recommended name:
            Integrin alpha-V light chain

Gene names

Name:	ITGAV
Synonyms:	MSK8, VNRA

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1048 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	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.
Subunit structure	Heterodimer of an alpha and a beta subunit. The alpha subunit is composed of an 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.
Subcellular location	Membrane; Single-pass type I membrane protein.
Sequence similarities	Belongs to the integrin alpha chain family. Contains 7 FG-GAP repeats.

Ontologies

Keywords
Biological process	Cell adhesion Host-virus interaction
Cellular component	Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat Signal Transmembrane
Ligand	Calcium
Molecular function	Integrin Receptor
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	cell-matrix adhesion Non-traceable author statement. Source: UniProtKB integrin-mediated signaling pathway Non-traceable author statement. Source: UniProtKB interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of lipid storage Inferred from mutant phenotype. Source: UniProtKB negative regulation of lipid transport Inferred from mutant phenotype. Source: UniProtKB negative regulation of lipoprotein metabolic process Inferred from mutant phenotype. Source: UniProtKB negative regulation of low-density lipoprotein receptor biosynthetic process Inferred from mutant phenotype. Source: UniProtKB negative regulation of macrophage derived foam cell differentiation Inferred from mutant phenotype. Source: UniProtKB
Cellular component	integrin complex Non-traceable author statement. Source: UniProtKB
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: UniProtKB receptor activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ANGPTL3	Q9Y5C1	1	EBI-298282,EBI-298276
ITGB3	P05106	3	EBI-298282,EBI-702847
ITGB8	P26012	1	EBI-298282,EBI-2436381

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P06756-1)

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.

Isoform 2 (identifier: P06756-2)

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

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 30

30

Ref.8

Chain

31 – 1048

1018

Integrin alpha-V

PRO_0000016301

Chain

31 – 889

859

Integrin alpha-V heavy chain

PRO_0000016302

Chain

891 – 1048

158

Integrin alpha-V light chain

PRO_0000016303

Regions

Topological domain

31 – 992

962

Extracellular Potential

Transmembrane

993 – 1016

24

Potential

Topological domain

1017 – 1048

32

Cytoplasmic Potential

Repeat

46 – 108

63

FG-GAP 1

Repeat

113 – 178

66

FG-GAP 2

Repeat

179 – 236

58

FG-GAP 3

Repeat

249 – 302

54

FG-GAP 4

Repeat

303 – 362

60

FG-GAP 5

Repeat

367 – 427

61

FG-GAP 6

Repeat

432 – 483

52

FG-GAP 7

Calcium binding

260 – 268

9

Potential

Calcium binding

314 – 322

9

Potential

Calcium binding

379 – 387

9

Potential

Calcium binding

443 – 451

9

Potential

Motif

1019 – 1023

5

GFFKR motif

Amino acid modifications

Glycosylation

74

1

N-linked (GlcNAc...) Ref.16 Ref.17

Glycosylation

290

1

N-linked (GlcNAc...) Potential

Glycosylation

296

1

N-linked (GlcNAc...) Potential

Glycosylation

488

1

N-linked (GlcNAc...) Potential

Glycosylation

554

1

N-linked (GlcNAc...) Potential

Glycosylation

615

1

N-linked (GlcNAc...) Ref.16 Ref.12

Glycosylation

704

1

N-linked (GlcNAc...) Ref.16

Glycosylation

835

1

N-linked (GlcNAc...) Potential

Glycosylation

851

1

N-linked (GlcNAc...) Potential

Glycosylation

874

1

N-linked (GlcNAc...) Ref.16 Ref.17

Glycosylation

945

1

N-linked (GlcNAc...) Potential

Glycosylation

973

1

N-linked (GlcNAc...) Potential

Glycosylation

980

1

N-linked (GlcNAc...) Potential

Disulfide bond

89 ↔ 97

Ref.13

Disulfide bond

138 ↔ 158

Ref.13

Disulfide bond

172 ↔ 185

Ref.13

Disulfide bond

491 ↔ 502

Ref.13

Disulfide bond

508 ↔ 565

Ref.13

Disulfide bond

626 ↔ 632

Ref.13

Disulfide bond

698 ↔ 711

Ref.13

Disulfide bond

852 ↔ 914

Interchain (between heavy and light chains) Ref.13

Disulfide bond

904 ↔ 909

Ref.13

Natural variations

Alternative sequence

175 – 211

37

QDIDA…FYWQG → R in isoform 2.

VSP_024351

Natural variant

405

1

I → V: dbSNP rs3738918.

VAR_024289

Natural variant

548

1

S → A: dbSNP rs2230615.

VAR_055970

Natural variant

783

1

V → I: dbSNP rs2230616. Ref.1 Ref.3 Ref.5 Ref.7

VAR_031547

Experimental info

Sequence conflict

425

1

W → R in AAG03000. Ref.2

Sequence conflict

1039

1

H → R in AAG03000. Ref.2

Secondary structure

1

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1048

Helix Strand Turn

Details...

Beta strand

39 – 42

4

Beta strand

51 – 56

6

Beta strand

65 – 72

8

Beta strand

85 – 90

6

Turn

91 – 94

4

Beta strand

109 – 111

3

Beta strand

114 – 118

5

Beta strand

126 – 130

5

Beta strand

135 – 139

5

Beta strand

147 – 150

4

Beta strand

157 – 161

5

Beta strand

167 – 169

3

Turn

179 – 184

6

Beta strand

189 – 192

4

Beta strand

200 – 203

4

Helix

206 – 209

4

Beta strand

211 – 216

6

Helix

218 – 221

4

Beta strand

237 – 239

3

Helix

245 – 247

3

Beta strand

254 – 259

6

Beta strand

262 – 266

5

Beta strand

268 – 273

6

Helix

276 – 279

4

Beta strand

282 – 287

6

Turn

288 – 290

3

Beta strand

293 – 298

6

Beta strand

310 – 313

4

Beta strand

317 – 319

3

Beta strand

322 – 327

6

Beta strand

331 – 333

3

Beta strand

339 – 341

3

Beta strand

344 – 350

7

Beta strand

356 – 359

4

Beta strand

364 – 368

5

Beta strand

383 – 385

3

Beta strand

389 – 392

4

Helix

397 – 399

3

Beta strand

402 – 404

3

Beta strand

420 – 422

3

Beta strand

428 – 430

3

Beta strand

436 – 439

4

Beta strand

445 – 449

5

Beta strand

451 – 456

6

Turn

457 – 460

4

Beta strand

461 – 467

7

Beta strand

470 – 474

5

Beta strand

477 – 481

5

Beta strand

494 – 496

3

Beta strand

502 – 512

11

Beta strand

514 – 516

3

Beta strand

524 – 529

6

Beta strand

542 – 546

5

Beta strand

548 – 554

7

Beta strand

564 – 571

8

Helix

575 – 577

3

Beta strand

585 – 592

8

Beta strand

600 – 602

3

Beta strand

614 – 616

3

Beta strand

619 – 622

4

Beta strand

628 – 631

4

Beta strand

636 – 640

5

Beta strand

647 – 651

5

Beta strand

653 – 663

11

Beta strand

668 – 670

3

Beta strand

672 – 676

5

Beta strand

683 – 686

4

Beta strand

699 – 705

7

Beta strand

707 – 712

6

Beta strand

715 – 717

3

Beta strand

725 – 731

7

Beta strand

735 – 748

14

Beta strand

752 – 754

3

Beta strand

760 – 767

8

Beta strand

772 – 778

7

Beta strand

782 – 784

3

Helix

799 – 802

4

Beta strand

805 – 814

10

Beta strand

816 – 818

3

Beta strand

820 – 833

14

Beta strand

843 – 856

14

Beta strand

904 – 907

4

Beta strand

909 – 916

8

Beta strand

923 – 932

10

Beta strand

941 – 943

3

Beta strand

952 – 960

9

Beta strand

971 – 977

7

Beta strand

980 – 982

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified April 3, 2007. Version 2. Checksum: 364EE25C5303A2D7	FASTA	1,048	116,038
	10 20 30 40 50 60 MAFPPRRRLR LGPRGLPLLL SGLLLPLCRA FNLDVDSPAE YSGPEGSYFG FAVDFFVPSA 70 80 90 100 110 120 SSRMFLLVGA PKANTTQPGI VEGGQVLKCD WSSTRRCQPI EFDATGNRDY AKDDPLEFKS 130 140 150 160 170 180 HQWFGASVRS KQDKILACAP LYHWRTEMKQ EREPVGTCFL QDGTKTVEYA PCRSQDIDAD 190 200 210 220 230 240 GQGFCQGGFS IDFTKADRVL LGGPGSFYWQ GQLISDQVAE IVSKYDPNVY SIKYNNQLAT 250 260 270 280 290 300 RTAQAIFDDS YLGYSVAVGD FNGDGIDDFV SGVPRAARTL GMVYIYDGKN MSSLYNFTGE 310 320 330 340 350 360 QMAAYFGFSV AATDINGDDY ADVFIGAPLF MDRGSDGKLQ EVGQVSVSLQ RASGDFQTTK 370 380 390 400 410 420 LNGFEVFARF GSAIAPLGDL DQDGFNDIAI AAPYGGEDKK GIVYIFNGRS TGLNAVPSQI 430 440 450 460 470 480 LEGQWAARSM PPSFGYSMKG ATDIDKNGYP DLIVGAFGVD RAILYRARPV ITVNAGLEVY 490 500 510 520 530 540 PSILNQDNKT CSLPGTALKV SCFNVRFCLK ADGKGVLPRK LNFQVELLLD KLKQKGAIRR 550 560 570 580 590 600 ALFLYSRSPS HSKNMTISRG GLMQCEELIA YLRDESEFRD KLTPITIFME YRLDYRTAAD 610 620 630 640 650 660 TTGLQPILNQ FTPANISRQA HILLDCGEDN VCKPKLEVSV DSDQKKIYIG DDNPLTLIVK 670 680 690 700 710 720 AQNQGEGAYE AELIVSIPLQ ADFIGVVRNN EALARLSCAF KTENQTRQVV CDLGNPMKAG 730 740 750 760 770 780 TQLLAGLRFS VHQQSEMDTS VKFDLQIQSS NLFDKVSPVV SHKVDLAVLA AVEIRGVSSP 790 800 810 820 830 840 DHVFLPIPNW EHKENPETEE DVGPVVQHIY ELRNNGPSSF SKAMLHLQWP YKYNNNTLLY 850 860 870 880 890 900 ILHYDIDGPM NCTSDMEINP LRIKISSLQT TEKNDTVAGQ GERDHLITKR DLALSEGDIH 910 920 930 940 950 960 TLGCGVAQCL KIVCQVGRLD RGKSAILYVK SLLWTETFMN KENQNHSYSL KSSASFNVIE 970 980 990 1000 1010 1020 FPYKNLPIED ITNSTLVTTN VTWGIQPAPM PVPVWVIILA VLAGLLLLAV LVFVMYRMGF 1030 1040 FKRVRPPQEE QEREQLQPHE NGEGNSET
	Isoform 2. Checksum: 132A3F554FCDE8B6	FASTA	1,012	112,258
	10 20 30 40 50 60 MAFPPRRRLR LGPRGLPLLL SGLLLPLCRA FNLDVDSPAE YSGPEGSYFG FAVDFFVPSA 70 80 90 100 110 120 SSRMFLLVGA PKANTTQPGI VEGGQVLKCD WSSTRRCQPI EFDATGNRDY AKDDPLEFKS 130 140 150 160 170 180 HQWFGASVRS KQDKILACAP LYHWRTEMKQ EREPVGTCFL QDGTKTVEYA PCRSRQLISD 190 200 210 220 230 240 QVAEIVSKYD PNVYSIKYNN QLATRTAQAI FDDSYLGYSV AVGDFNGDGI DDFVSGVPRA 250 260 270 280 290 300 ARTLGMVYIY DGKNMSSLYN FTGEQMAAYF GFSVAATDIN GDDYADVFIG APLFMDRGSD 310 320 330 340 350 360 GKLQEVGQVS VSLQRASGDF QTTKLNGFEV FARFGSAIAP LGDLDQDGFN DIAIAAPYGG 370 380 390 400 410 420 EDKKGIVYIF NGRSTGLNAV PSQILEGQWA ARSMPPSFGY SMKGATDIDK NGYPDLIVGA 430 440 450 460 470 480 FGVDRAILYR ARPVITVNAG LEVYPSILNQ DNKTCSLPGT ALKVSCFNVR FCLKADGKGV 490 500 510 520 530 540 LPRKLNFQVE LLLDKLKQKG AIRRALFLYS RSPSHSKNMT ISRGGLMQCE ELIAYLRDES 550 560 570 580 590 600 EFRDKLTPIT IFMEYRLDYR TAADTTGLQP ILNQFTPANI SRQAHILLDC GEDNVCKPKL 610 620 630 640 650 660 EVSVDSDQKK IYIGDDNPLT LIVKAQNQGE GAYEAELIVS IPLQADFIGV VRNNEALARL 670 680 690 700 710 720 SCAFKTENQT RQVVCDLGNP MKAGTQLLAG LRFSVHQQSE MDTSVKFDLQ IQSSNLFDKV 730 740 750 760 770 780 SPVVSHKVDL AVLAAVEIRG VSSPDHVFLP IPNWEHKENP ETEEDVGPVV QHIYELRNNG 790 800 810 820 830 840 PSSFSKAMLH LQWPYKYNNN TLLYILHYDI DGPMNCTSDM EINPLRIKIS SLQTTEKNDT 850 860 870 880 890 900 VAGQGERDHL ITKRDLALSE GDIHTLGCGV AQCLKIVCQV GRLDRGKSAI LYVKSLLWTE 910 920 930 940 950 960 TFMNKENQNH SYSLKSSASF NVIEFPYKNL PIEDITNSTL VTTNVTWGIQ PAPMPVPVWV 970 980 990 1000 1010 IILAVLAGLL LLAVLVFVMY RMGFFKRVRP PQEEQEREQL QPHENGEGNS ET

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 2443500] [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: 10965141] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	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.
[4]	"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: 15815621] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ILE-783.
[6]	"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: 7522056] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-62.
[7]	"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: 2430295] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 413-1048, VARIANT ILE-783.
[8]	"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: 2467745] [Abstract] Cited for: PROTEIN SEQUENCE OF 31-41.
[9]	"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: 9426447] [Abstract] Cited for: INTERACTION WITH COXSACKIEVIRUS B1 CAPSID PROTEINS.
[10]	"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: 10397733] [Abstract] Cited for: INTERACTION WITH HIV-1 TAT.
[11]	"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: 10799568] [Abstract] Cited for: INTERACTION WITH FMDV VP1.
[12]	"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: 12754519] [Abstract] Cited for: GLYCOSYLATION AT ASN-615.
[13]	"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: 14596610] [Abstract] Cited for: DISULFIDE BONDS.
[14]	"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: 15194773] [Abstract] Cited for: INTERACTION WITH COXSACKIEVIRUS A9 CAPSID PROTEINS.
[15]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[16]	"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: 19159218] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-74; ASN-615; ASN-704 AND ASN-874, MASS SPECTROMETRY. Tissue: Liver.
[17]	"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: 19349973] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-74 AND ASN-874, MASS SPECTROMETRY.
[18]	"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: 11546839] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 31-987.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

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.
AB209894 mRNA. Translation: BAD93131.1. Different initiation.
AC017101 Genomic DNA. Translation: AAY24257.1.
BC126231 mRNA. Translation: AAI26232.1.
U07375 Genomic DNA. Translation: AAA61631.1.

IPI

IPI00027505.
IPI00555991.

PIR

A27421.

RefSeq

NP_002201.1.

UniGene

Hs.436873

3D structure databases

PDBPDBe

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	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P06756. 3 interactions.

STRING

P06756.

PTM databases

PhosphoSite

P06756.

Proteomic databases

PRIDE

P06756.

Genome annotation databases

Ensembl

ENST00000261023; ENSP00000261023; ENSG00000138448; Homo sapiens. [Genome view]
ENST00000374907; ENSP00000364042; ENSG00000138448; Homo sapiens. [Genome view]
ENST00000422543; ENSP00000400070; ENSG00000138448; Homo sapiens. [Genome view]
ENST00000430709; ENSP00000389442; ENSG00000138448; Homo sapiens. [Genome view]
ENST00000433736; ENSP00000404291; ENSG00000138448; Homo sapiens. [Genome view]

GeneID

3685.

NMPDR

fig|9606.3.peg.19030.

UCSC

uc010frs.1. human.

Organism-specific databases

GeneCards

GC02P187163.

H-InvDB

HIX0029959.

HGNC

HGNC:6150. ITGAV.

HPA

CAB002499.
HPA004856.

MIM

193210. gene.

PharmGKB

PA29950.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

P06756.

Enzyme and pathway databases

Pathway_Interaction_DB

arf6_traffickingpathway. Arf6 trafficking events.
avb3_integrin_pathway. Integrins in angiogenesis.
avb3_opn_pathway. Osteopontin-mediated events.
pdgfrapathway. PDGFR-alpha signaling pathway.
s1p_s1p1_pathway. S1P1 pathway.
s1p_s1p3_pathway. S1P3 pathway.
vegfr1_2_pathway. Signaling events mediated by VEGFR1 and VEGFR2.

Reactome

REACT_13552. Integrin cell surface interactions.
REACT_604. Hemostasis.
REACT_6900. Signaling in Immune system.

Gene expression databases

ArrayExpress

P06756.

Bgee

P06756.

CleanEx

HS_ITGAV.

Genevestigator

P06756.

GermOnline

ENSG00000138448. Homo sapiens.

Family and domain databases

InterPro

IPR013517. FG-GAP.
IPR013519. Int_alpha_beta-p.
IPR000413. Integrin_alpha.
IPR013649. Integrin_alpha-2.
IPR013513. Integrin_alpha_C.
IPR018184. Integrin_alpha_C_CS.
[Graphical view]

Pfam

PF01839. FG-GAP. 3 hits.
PF00357. Integrin_alpha. 1 hit.
PF08441. Integrin_alpha2. 1 hit.
[Graphical view]

PRINTS

PR01185. INTEGRINA.

SMART

SM00191. Int_alpha. 5 hits.
[Graphical view]

PROSITE

PS00242. INTEGRIN_ALPHA. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

14423.

SOURCE

Search...

Entry information

Entry name

ITAV_HUMAN

Accession

Primary (citable) accession number: P06756
Secondary accession number(s): A0AV67 , Q53SK4, Q59EB7, Q6LD15

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	April 3, 2007
Last modified:	November 3, 2009
This is version 126 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.