P18564 (ITB6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Integrin beta-6

Gene names

Name:

ITGB6

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	788 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	Integrin alpha-V/beta-6 is a receptor for fibronectin and cytotactin. It recognizes the sequence R-G-D in its ligands. Internalisation of integrin alpha-V/beta-6 via clathrin-mediated endocytosis promotes carcinoma cell invasion. Ref.13
Subunit structure	Heterodimer of an alpha and a beta subunit. Beta-6 associates with alpha-V. Interacts with FLNB. Interacts with HAX1. Alpha-V/beta-6 binds to foot-and-mouth disease virus (FMDV) VP1 protein, coxsackievirus A9, coxsackievirus B1 capsid proteins and acts as a receptor for these viruses. Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13
Subcellular location	Membrane; Single-pass type I membrane protein.
Sequence similarities	Belongs to the integrin beta chain family. Contains 1 VWFA domain.

Ontologies

Keywords
Biological process	Cell adhesion Host-virus interaction
Cellular component	Membrane
Coding sequence diversity	Polymorphism
Domain	Repeat Signal Transmembrane Transmembrane helix
Molecular function	Host cell receptor for virus entry Integrin Receptor
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell adhesion Traceable author statement Ref.1. Source: ProtInc cell-matrix adhesion Inferred from electronic annotation. Source: InterPro inflammatory response Inferred from electronic annotation. Source: Compara integrin-mediated signaling pathway Inferred from electronic annotation. Source: UniProtKB-KW multicellular organismal development Inferred from electronic annotation. Source: InterPro virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	integrin complex Traceable author statement Ref.1. Source: ProtInc
Molecular_function	receptor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 21

21

Potential

Chain

22 – 788

767

Integrin beta-6

PRO_0000016350

Regions

Topological domain

22 – 709

688

Extracellular Potential

Transmembrane

710 – 730

21

Helical; Potential

Topological domain

731 – 788

58

Cytoplasmic Potential

Domain

131 – 371

241

VWFA

Repeat

456 – 501

46

I

Repeat

502 – 543

42

II

Repeat

544 – 582

39

III

Repeat

583 – 619

37

IV

Region

456 – 619

164

Cysteine-rich tandem repeats

Region

731 – 758

28

Interaction with HAX1

Amino acid modifications

Glycosylation

48

1

N-linked (GlcNAc...) Potential

Glycosylation

97

1

N-linked (GlcNAc...) Potential

Glycosylation

260

1

N-linked (GlcNAc...) Potential

Glycosylation

387

1

N-linked (GlcNAc...) Potential

Glycosylation

396

1

N-linked (GlcNAc...) Potential

Glycosylation

463

1

N-linked (GlcNAc...) Potential

Glycosylation

471

1

N-linked (GlcNAc...) Potential

Glycosylation

541

1

N-linked (GlcNAc...) Potential

Glycosylation

575

1

N-linked (GlcNAc...) Potential

Disulfide bond

23 ↔ 454

By similarity

Disulfide bond

31 ↔ 41

By similarity

Disulfide bond

34 ↔ 70

By similarity

Disulfide bond

44 ↔ 59

By similarity

Disulfide bond

197 ↔ 204

By similarity

Disulfide bond

252 ↔ 293

By similarity

Disulfide bond

394 ↔ 406

By similarity

Disulfide bond

426 ↔ 670

By similarity

Disulfide bond

452 ↔ 456

By similarity

Disulfide bond

467 ↔ 479

By similarity

Disulfide bond

476 ↔ 511

By similarity

Disulfide bond

481 ↔ 490

By similarity

Disulfide bond

492 ↔ 502

By similarity

Disulfide bond

517 ↔ 522

By similarity

Disulfide bond

519 ↔ 552

By similarity

Disulfide bond

524 ↔ 537

By similarity

Disulfide bond

539 ↔ 544

By similarity

Disulfide bond

558 ↔ 563

By similarity

Disulfide bond

560 ↔ 591

By similarity

Disulfide bond

565 ↔ 574

By similarity

Disulfide bond

576 ↔ 583

By similarity

Disulfide bond

597 ↔ 602

By similarity

Disulfide bond

599 ↔ 645

By similarity

Disulfide bond

604 ↔ 614

By similarity

Disulfide bond

617 ↔ 620

By similarity

Disulfide bond

624 ↔ 633

By similarity

Disulfide bond

630 ↔ 702

By similarity

Disulfide bond

649 ↔ 678

By similarity

Natural variations

Natural variant

437

1

P → T.
Corresponds to variant rs2305820 [ dbSNP | Ensembl ].

VAR_049636

Secondary structure

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788

Helix Strand Turn

Details...

Beta strand

97 – 99

3

Beta strand

103 – 105

3

Beta strand

109 – 113

5

Beta strand

118 – 121

4

Beta strand

124 – 126

3

Beta strand

133 – 140

8

Helix

143 – 145

3

Turn

146 – 152

7

Helix

157 – 164

8

Beta strand

168 – 177

10

Helix

183 – 185

3

Helix

191 – 193

3

Beta strand

199 – 201

3

Beta strand

209 – 211

3

Beta strand

216 – 218

3

Helix

222 – 228

7

Beta strand

236 – 240

5

Helix

243 – 251

9

Helix

253 – 256

4

Beta strand

260 – 272

13

Helix

279 – 281

3

Turn

282 – 284

3

Helix

302 – 305

4

Helix

312 – 321

10

Beta strand

326 – 331

6

Helix

332 – 334

3

Helix

335 – 344

10

Beta strand

349 – 353

5

Helix

358 – 360

3

Helix

361 – 371

11

Beta strand

377 – 380

4

Beta strand

384 – 386

3

Beta strand

414 – 416

3

Beta strand

419 – 422

4

Beta strand

431 – 437

7

Beta strand

444 – 450

7

Beta strand

487 – 490

4

Beta strand

492 – 494

3

Beta strand

505 – 507

3

Helix

510 – 513

4

Beta strand

515 – 518

4

Beta strand

521 – 523

3

Helix

542 – 544

3

Sequences

	Sequence		Length	Mass (Da)
	P18564 [UniParc]. Last modified April 27, 2001. Version 2. Checksum: EDB7D533EC4C8C4D	FASTA	788	85,936
	10 20 30 40 50 60 MGIELLCLFF LFLGRNDHVQ GGCALGGAET CEDCLLIGPQ CAWCAQENFT HPSGVGERCD 70 80 90 100 110 120 TPANLLAKGC QLNFIENPVS QVEILKNKPL SVGRQKNSSD IVQIAPQSLI LKLRPGGAQT 130 140 150 160 170 180 LQVHVRQTED YPVDLYYLMD LSASMDDDLN TIKELGSRLS KEMSKLTSNF RLGFGSFVEK 190 200 210 220 230 240 PVSPFVKTTP EEIANPCSSI PYFCLPTFGF KHILPLTNDA ERFNEIVKNQ KISANIDTPE 250 260 270 280 290 300 GGFDAIMQAA VCKEKIGWRN DSLHLLVFVS DADSHFGMDS KLAGIVIPND GLCHLDSKNE 310 320 330 340 350 360 YSMSTVLEYP TIGQLIDKLV QNNVLLIFAV TQEQVHLYEN YAKLIPGATV GLLQKDSGNI 370 380 390 400 410 420 LQLIISAYEE LRSEVELEVL GDTEGLNLSF TAICNNGTLF QHQKKCSHMK VGDTASFSVT 430 440 450 460 470 480 VNIPHCERRS RHIIIKPVGL GDALELLVSP ECNCDCQKEV EVNSSKCHHG NGSFQCGVCA 490 500 510 520 530 540 CHPGHMGPRC ECGEDMLSTD SCKEAPDHPS CSGRGDCYCG QCICHLSPYG NIYGPYCQCD 550 560 570 580 590 600 NFSCVRHKGL LCGGNGDCDC GECVCRSGWT GEYCNCTTST DSCVSEDGVL CSGRGDCVCG 610 620 630 640 650 660 KCVCTNPGAS GPTCERCPTC GDPCNSKRSC IECHLSAAGQ AREECVDKCK LAGATISEEE 670 680 690 700 710 720 DFSKDGSVSC SLQGENECLI TFLITTDNEG KTIIHSINEK DCPKPPNIPM IMLGVSLAIL 730 740 750 760 770 780 LIGVVLLCIW KLLVSFHDRK EVAKFEAERS KAKWQTGTNP LYRGSTSTFK NVTYKHREKQ KVDLSTDC

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete amino acid sequence of a novel integrin beta subunit (beta 6) identified in epithelial cells using the polymerase chain reaction." Sheppard D., Rozzo C., Starr L., Quaranta V., Erle D.J., Pytela R. J. Biol. Chem. 265:11502-11507(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Pancreas.
[2]	Askins J. Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION TO 18-24; 158; 642 AND 719.
[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]. Tissue: Placenta.
[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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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].
[7]	"The gene organization of the human beta 7 subunit, the common beta subunit of the leukocyte integrins HML-1 and LPAM-1." Jiang W.-M., Jenkins D., Yuan Q., Leung E., Choo K.H., Watson J.D., Krissansen G.W. Int. Immunol. 4:1031-1040(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 116-197.
[8]	"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.
[9]	"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.
[10]	"Different splice variants of filamin-B affect myogenesis, subcellular distribution, and determine binding to integrin (beta) subunits." van Der Flier A., Kuikman I., Kramer D., Geerts D., Kreft M., Takafuta T., Shapiro S.S., Sonnenberg A. J. Cell Biol. 156:361-376(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH FLNB. Tissue: Keratinocyte and Skeletal muscle.
[11]	"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.
[12]	"Specificity of the VP1 GH loop of Foot-and-Mouth Disease virus for alphav integrins." Burman A., Clark S., Abrescia N.G., Fry E.E., Stuart D.I., Jackson T. J. Virol. 80:9798-9810(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH FMDV VP1.
[13]	"HS1-associated protein X-1 regulates carcinoma cell migration and invasion via clathrin-mediated endocytosis of integrin alphavbeta6." Ramsay A.G., Keppler M.D., Jazayeri M., Thomas G.J., Parsons M., Violette S., Weinreb P., Hart I.R., Marshall J.F. Cancer Res. 67:5275-5284(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HAX1, FUNCTION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M35198 mRNA. Translation: AAA36122.2.
AC092153 Genomic DNA. Translation: AAX93093.1.
AK313944 mRNA. Translation: BAG36662.1.
AC080166 Genomic DNA. Translation: AAY24053.1.
CH471058 Genomic DNA. Translation: EAX11390.1.
BC121178 mRNA. Translation: AAI21179.1.
S49380 Genomic DNA. Translation: AAB23690.1.

IPI

IPI00000151.

PIR

A37057.

RefSeq

NP_000879.2. NM_000888.3.

UniGene

Hs.470399.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1LH9	model	-	A	76-546	[»]

ProteinModelPortal

P18564.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-59187N.

STRING

9606.ENSP00000283249.

PTM databases

PhosphoSite

P18564.

Polymorphism databases

DMDM

13432176.

Proteomic databases

PaxDb

P18564.

PeptideAtlas

P18564.

PRIDE

P18564.

Protocols and materials databases

DNASU

3694.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000283249; ENSP00000283249; ENSG00000115221.
ENST00000409872; ENSP00000386367; ENSG00000115221.

GeneID

3694.

KEGG

hsa:3694.

UCSC

uc002ubh.2. human.

Organism-specific databases

CTD

3694.

GeneCards

GC02M160920.

HGNC

HGNC:6161. ITGB6.

HPA

HPA023626.

MIM

147558. gene.

neXtProt

NX_P18564.

PharmGKB

PA29960.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG145803.

HOGENOM

HOG000252936.

HOVERGEN

HBG006190.

InParanoid

P18564.

KO

K06589.

OMA

EYCNCTT.

OrthoDB

EOG49GKFZ.

PhylomeDB

P18564.

Enzyme and pathway databases

Reactome

REACT_111102. Signal Transduction.
REACT_118779. Extracellular matrix organization.

Gene expression databases

ArrayExpress

P18564.

Bgee

P18564.

CleanEx

HS_ITGB6.

Genevestigator

P18564.

GermOnline

ENSG00000115221. Homo sapiens.

Family and domain databases

Gene3D

1.20.5.630. 1 hit.

InterPro

IPR013111. EGF_extracell.
IPR015812. Integrin_bsu.
IPR015436. Integrin_bsu-6.
IPR014836. Integrin_bsu_cyt_dom.
IPR002369. Integrin_bsu_N.
IPR012896. Integrin_bsu_tail.
IPR003659. Plexin-like.
IPR016201. Plexin-like_fold.
IPR002035. VWF_A.
[Graphical view]

PANTHER

PTHR10082. PTHR10082. 1 hit.
PTHR10082:SF11. PTHR10082:SF11. 1 hit.

Pfam

PF07974. EGF_2. 1 hit.
PF08725. Integrin_b_cyt. 1 hit.
PF07965. Integrin_B_tail. 1 hit.
PF00362. Integrin_beta. 1 hit.
[Graphical view]

PIRSF

PIRSF002512. Integrin_B. 1 hit.

PRINTS

PR01186. INTEGRINB.

SMART

SM00187. INB. 1 hit.
SM00423. PSI. 1 hit.
SM00327. VWA. 1 hit.
[Graphical view]

SUPFAM

SSF69687. Integrin_bsu_tail. 1 hit.
SSF103575. Plexin-like_fold. 1 hit.

PROSITE

PS00022. EGF_1. 2 hits. Uncertain.
PS01186. EGF_2. 1 hit. Uncertain.
PS00243. INTEGRIN_BETA. 3 hits.
PS50234. VWFA. False negative.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P18564.

ChEMBL

CHEMBL4876.

GenomeRNAi

3694.

NextBio

14479.

SOURCE

Search...

Entry information

Entry name

ITB6_HUMAN

Accession

Primary (citable) accession number: P18564
Secondary accession number(s): B2R9W5 , Q0VA95, Q16500, Q53RG5, Q53RR6

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1990
Last sequence update:	April 27, 2001
Last modified:	May 1, 2013
This is version 142 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.