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P53708 (ITA8_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Integrin alpha-8
Gene names
Name:ITGA8
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1063 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Integrin alpha-8/beta-1 functions in the genesis of kidney and probably of other organs by regulating the recruitment of mesenchymal cells into epithelial structures. It recognizes the sequence R-G-D in a wide array of ligands including TNC, FN1, SPP1 TGFB1, TGFB3 and VTN. NPNT is probably its functional ligand in kidney genesis. Neuronal receptor for TNC it mediates cell-cell interactions and regulates neurite outgrowth of sensory and motor neurons. Ref.7 Ref.8

Subunit structure

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-8 associates with beta-1.

Subcellular location

Membrane; Single-pass type I membrane protein.

Tissue specificity

Expressed in mesenchymal cells, including alveolar myofibroblasts, kidney mesangial cells and hepatic stellar cells and vascular and visceral smooth muscle (at protein level). Ref.5 Ref.6

Sequence similarities

Belongs to the integrin alpha chain family.

Contains 7 FG-GAP repeats.

Ontologies

Keywords
   Biological processCell adhesion
Differentiation
Neurogenesis
   Cellular componentMembrane
   Coding sequence diversityPolymorphism
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   LigandCalcium
Metal-binding
   Molecular functionDevelopmental protein
Integrin
Receptor
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbrain development

Inferred from electronic annotation. Source: Ensembl

cell projection organization

Inferred from electronic annotation. Source: Ensembl

cell-matrix adhesion

Non-traceable author statement Ref.5. Source: UniProtKB

establishment of protein localization

Inferred from electronic annotation. Source: Ensembl

extracellular matrix organization

Traceable author statement. Source: Reactome

inner ear morphogenesis

Inferred from electronic annotation. Source: Ensembl

integrin-mediated signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

memory

Inferred from electronic annotation. Source: Ensembl

metanephros development

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter involved in smooth muscle cell differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of transforming growth factor beta receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

single organismal cell-cell adhesion

Non-traceable author statement Ref.5. Source: UniProtKB

smooth muscle tissue development

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentalpha8-beta1 integrin complex

Traceable author statement PubMed 21335239. Source: BHF-UCL

apical part of cell

Inferred from electronic annotation. Source: Ensembl

dendritic spine membrane

Inferred from electronic annotation. Source: Ensembl

integrin complex

Traceable author statement Ref.5. Source: UniProtKB

perikaryon

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Traceable author statement. Source: Reactome

postsynaptic density

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3838 Potential
Chain39 – 10631025Integrin alpha-8
PRO_0000016310
Chain39 – 906868Integrin alpha-8 heavy chain Potential
PRO_0000016311
Chain907 – 1063157Integrin alpha-8 light chain Potential
PRO_0000016312

Regions

Topological domain39 – 1012974Extracellular Potential
Transmembrane1013 – 103321Helical; Potential
Topological domain1034 – 106330Cytoplasmic Potential
Repeat44 – 10562FG-GAP 1
Repeat122 – 18362FG-GAP 2
Repeat188 – 24053FG-GAP 3
Repeat253 – 31058FG-GAP 4
Repeat311 – 37262FG-GAP 5
Repeat373 – 43159FG-GAP 6
Repeat435 – 49864FG-GAP 7
Calcium binding329 – 3379 Potential
Calcium binding395 – 4039 Potential
Calcium binding459 – 4679 Potential
Motif455 – 4573Cell attachment site Potential

Amino acid modifications

Glycosylation811N-linked (GlcNAc...) Potential
Glycosylation1221N-linked (GlcNAc...) Potential
Glycosylation1771N-linked (GlcNAc...) Potential
Glycosylation2391N-linked (GlcNAc...) Potential
Glycosylation3021N-linked (GlcNAc...) Potential
Glycosylation3111N-linked (GlcNAc...) Potential
Glycosylation5041N-linked (GlcNAc...) Potential
Glycosylation6011N-linked (GlcNAc...) Potential
Glycosylation6051N-linked (GlcNAc...) Potential
Glycosylation7191N-linked (GlcNAc...) Potential
Glycosylation7371N-linked (GlcNAc...) Potential
Glycosylation7531N-linked (GlcNAc...) Potential
Glycosylation7801N-linked (GlcNAc...) Potential
Glycosylation8961N-linked (GlcNAc...) Potential
Glycosylation9231N-linked (GlcNAc...) Potential
Glycosylation10051N-linked (GlcNAc...) Potential
Disulfide bond96 ↔ 106 By similarity
Disulfide bond150 ↔ 171 By similarity
Disulfide bond187 ↔ 200 By similarity
Disulfide bond507 ↔ 518 By similarity
Disulfide bond524 ↔ 580 By similarity
Disulfide bond641 ↔ 647 By similarity
Disulfide bond713 ↔ 726 By similarity
Disulfide bond867 ↔ 924Interchain (between heavy and light chains) By similarity
Disulfide bond929 ↔ 934 By similarity

Natural variations

Natural variant2161V → L. Ref.1
Corresponds to variant rs7895372 [ dbSNP | Ensembl ].
VAR_018673
Natural variant5671V → L. Ref.9
VAR_034682
Natural variant5771S → F. Ref.1 Ref.9
Corresponds to variant rs2298033 [ dbSNP | Ensembl ].
VAR_018674
Natural variant5811Q → P. Ref.1 Ref.9
Corresponds to variant rs9333269 [ dbSNP | Ensembl ].
VAR_018675
Natural variant7481R → H. Ref.1 Ref.9
Corresponds to variant rs9333174 [ dbSNP | Ensembl ].
VAR_018676
Natural variant9931I → V. Ref.1 Ref.9
Corresponds to variant rs9333241 [ dbSNP | Ensembl ].
VAR_018677
Natural variant9941V → A. Ref.1 Ref.5 Ref.9
Corresponds to variant rs1041135 [ dbSNP | Ensembl ].
VAR_018678

Experimental info

Sequence conflict471T → A in AAA93514. Ref.5
Sequence conflict1661D → G in AAA93514. Ref.5
Sequence conflict1881R → G in AAA93514. Ref.5
Sequence conflict3041T → Y in AAA93514. Ref.5

Sequences

Sequence LengthMass (Da)Tools
P53708 [UniParc].

Last modified November 2, 2010. Version 3.
Checksum: 8F9614BDBB897D77

FASTA1,063117,474
        10         20         30         40         50         60 
MSPGASRGPR GSQAPLIAPL CCAAAALGML LWSPACQAFN LDVEKLTVYS GPKGSYFGYA 

        70         80         90        100        110        120 
VDFHIPDART ASVLVGAPKA NTSQPDIVEG GAVYYCPWPA EGSAQCRQIP FDTTNNRKIR 

       130        140        150        160        170        180 
VNGTKEPIEF KSNQWFGATV KAHKGKVVAC APLYHWRTLK PTPEKDPVGT CYVAIQNFSA 

       190        200        210        220        230        240 
YAEFSPCRNS NADPEGQGYC QAGFSLDFYK NGDLIVGGPG SFYWQGQVIT ASVADIIANY 

       250        260        270        280        290        300 
SFKDILRKLA GEKQTEVAPA SYDDSYLGYS VAAGEFTGDS QQELVAGIPR GAQNFGYVSI 

       310        320        330        340        350        360 
INSTDMTFIQ NFTGEQMASY FGYTVVVSDV NSDGLDDVLV GAPLFMEREF ESNPREVGQI 

       370        380        390        400        410        420 
YLYLQVSSLL FRDPQILTGT ETFGRFGSAM AHLGDLNQDG YNDIAIGVPF AGKDQRGKVL 

       430        440        450        460        470        480 
IYNGNKDGLN TKPSQVLQGV WASHAVPSGF GFTLRGDSDI DKNDYPDLIV GAFGTGKVAV 

       490        500        510        520        530        540 
YRARPVVTVD AQLLLHPMII NLENKTCQVP DSMTSAACFS LRVCASVTGQ SIANTIVLMA 

       550        560        570        580        590        600 
EVQLDSLKQK GAIKRTLFLD NHQAHRVFPL VIKRQKSHQC QDFIVYLRDE TEFRDKLSPI 

       610        620        630        640        650        660 
NISLNYSLDE STFKEGLEVK PILNYYRENI VSEQAHILVD CGEDNLCVPD LKLSARPDKH 

       670        680        690        700        710        720 
QVIIGDENHL MLIINARNEG EGAYEAELFV MIPEEADYVG IERNNKGFRP LSCEYKMENV 

       730        740        750        760        770        780 
TRMVVCDLGN PMVSGTNYSL GLRFAVPRLE KTNMSINFDL QIRSSNKDNP DSNFVSLQIN 

       790        800        810        820        830        840 
ITAVAQVEIR GVSHPPQIVL PIHNWEPEEE PHKEEEVGPL VEHIYELHNI GPSTISDTIL 

       850        860        870        880        890        900 
EVGWPFSARD EFLLYIFHIQ TLGPLQCQPN PNINPQDIKP AASPEDTPEL SAFLRNSTIP 

       910        920        930        940        950        960 
HLVRKRDVHV VEFHRQSPAK ILNCTNIECL QISCAVGRLE GGESAVLKVR SRLWAHTFLQ 

       970        980        990       1000       1010       1020 
RKNDPYALAS LVSFEVKKMP YTDQPAKLPE GSIVIKTSVI WATPNVSFSI PLWVIILAIL 

      1030       1040       1050       1060 
LGLLVLAILT LALWKCGFFD RARPPQEDMT DREQLTNDKT PEA 

« Hide

References

« Hide 'large scale' references
[1]SeattleSNPs variation discovery resource
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LEU-216; PHE-577; PRO-581; HIS-748; VAL-993 AND ALA-994.
[2]NHLBI resequencing and genotyping service (RS&G)
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The DNA sequence and comparative analysis of human chromosome 10."
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. expand/collapse author list , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]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. expand/collapse author list , 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].
[5]"Sequence and tissue distribution of the human integrin alpha 8 subunit: a beta 1-associated alpha subunit expressed in smooth muscle cells."
Schnapp L.M., Breuss J.M., Ramos D.M., Sheppard D., Pytela R.
J. Cell Sci. 108:537-544(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 39-1063, TISSUE SPECIFICITY, VARIANT ALA-994.
[6]"Alpha8 integrin in glomerular mesangial cells and in experimental glomerulonephritis."
Hartner A., Schoecklmann H., Proels F., Mueller U., Sterzel R.B.
Kidney Int. 56:1468-1480(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[7]"Integrin alpha8beta1 mediates adhesion to LAP-TGFbeta1."
Lu M., Munger J.S., Steadele M., Busald C., Tellier M., Schnapp L.M.
J. Cell Sci. 115:4641-4648(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"Integrin alpha8beta1-fibronectin interactions promote cell survival via PI3 kinase pathway."
Farias E., Lu M., Li X., Schnapp L.M.
Biochem. Biophys. Res. Commun. 329:305-311(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"Genomic organization and sequence variation of the human integrin subunit alpha8 gene (ITGA8)."
Ekwa-Ekoka C., Diaz G.A., Carlson C., Hasegawa T., Samudrala R., Lim K.-C., Yabu J.M., Levy B., Schnapp L.M.
Matrix Biol. 23:487-496(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LEU-567; PHE-577; PRO-581; HIS-748; VAL-993 AND ALA-994.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY371697 Genomic DNA. Translation: AAQ56848.2.
EF444991 Genomic DNA. Translation: ACA06009.1.
AL359645, AL590636 Genomic DNA. Translation: CAH73424.1.
AL590636, AL359645 Genomic DNA. Translation: CAI14955.1.
CH471072 Genomic DNA. Translation: EAW86235.1.
L36531 mRNA. Translation: AAA93514.1.
RefSeqNP_003629.2. NM_003638.2.
UniGeneHs.171311.
Hs.592472.

3D structure databases

ProteinModelPortalP53708.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114088. 3 interactions.
STRING9606.ENSP00000367316.

PTM databases

PhosphoSiteP53708.

Polymorphism databases

DMDM311033437.

Proteomic databases

PaxDbP53708.
PRIDEP53708.

Protocols and materials databases

DNASU8516.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000378076; ENSP00000367316; ENSG00000077943.
GeneID8516.
KEGGhsa:8516.
UCSCuc001ioc.1. human.

Organism-specific databases

CTD8516.
GeneCardsGC10M015599.
H-InvDBHIX0035424.
HGNCHGNC:6144. ITGA8.
HPAHPA003432.
MIM604063. gene.
neXtProtNX_P53708.
Orphanet1848. Bilateral renal agenesis.
PharmGKBPA29944.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG26407.
HOGENOMHOG000231603.
HOVERGENHBG006186.
InParanoidP53708.
KOK06584.
OMACRQIPFD.
OrthoDBEOG7HQN77.
PhylomeDBP53708.
TreeFamTF105391.

Enzyme and pathway databases

ReactomeREACT_118779. Extracellular matrix organization.
SignaLinkP53708.

Gene expression databases

BgeeP53708.
CleanExHS_ITGA8.
GenevestigatorP53708.

Family and domain databases

InterProIPR013517. FG-GAP.
IPR013519. Int_alpha_beta-p.
IPR000413. Integrin_alpha.
IPR013649. Integrin_alpha-2.
IPR018184. Integrin_alpha_C_CS.
[Graphical view]
PfamPF01839. FG-GAP. 1 hit.
PF00357. Integrin_alpha. 1 hit.
PF08441. Integrin_alpha2. 1 hit.
[Graphical view]
PRINTSPR01185. INTEGRINA.
SMARTSM00191. Int_alpha. 6 hits.
[Graphical view]
PROSITEPS51470. FG_GAP. 7 hits.
PS00242. INTEGRIN_ALPHA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiITGA8.
GenomeRNAi8516.
NextBio31878.
PROP53708.
SOURCESearch...

Entry information

Entry nameITA8_HUMAN
AccessionPrimary (citable) accession number: P53708
Secondary accession number(s): B0YJ31, Q5VX94
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: November 2, 2010
Last modified: July 9, 2014
This is version 127 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM