P53708 (ITA8_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Integrin alpha-8

Cleaved into the following 2 chains:

1. Integrin alpha-8 heavy chain
2. Integrin alpha-8 light chain

Gene names

Name:

ITGA8

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	1063 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-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 process	Cell adhesion Differentiation Neurogenesis
Cellular component	Membrane
Coding sequence diversity	Polymorphism
Domain	Repeat Signal Transmembrane Transmembrane helix
Ligand	Calcium Metal-binding
Molecular function	Developmental protein Integrin Receptor
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell projection organization Inferred from electronic annotation. Source: Compara cell-cell adhesion Non-traceable author statement Ref.5. Source: UniProtKB cell-matrix adhesion Non-traceable author statement Ref.5. Source: UniProtKB establishment of protein localization Inferred from electronic annotation. Source: Compara extracellular matrix organization Inferred from electronic annotation. Source: Compara inner ear morphogenesis Inferred from electronic annotation. Source: Compara integrin-mediated signaling pathway Inferred from electronic annotation. Source: UniProtKB-KW memory Inferred from electronic annotation. Source: Compara metanephros development Inferred from electronic annotation. Source: Compara nervous system development Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of transcription from RNA polymerase II promoter involved in smooth muscle cell differentiation Inferred from electronic annotation. Source: Compara positive regulation of transforming growth factor beta receptor signaling pathway Inferred from electronic annotation. Source: Compara smooth muscle tissue development Inferred from electronic annotation. Source: Compara
Cellular_component	alpha8-beta1 integrin complex Traceable author statement PubMed 21335239. Source: BHF-UCL apical part of cell Inferred from electronic annotation. Source: Compara
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 38	38	Potential
	Chain	39 – 1063	1025	Integrin alpha-8		PRO_0000016310
	Chain	39 – 906	868	Integrin alpha-8 heavy chain Potential		PRO_0000016311
	Chain	907 – 1063	157	Integrin alpha-8 light chain Potential		PRO_0000016312
Regions
	Topological domain	39 – 1012	974	Extracellular Potential
	Transmembrane	1013 – 1033	21	Helical; Potential
	Topological domain	1034 – 1063	30	Cytoplasmic Potential
	Repeat	44 – 105	62	FG-GAP 1
	Repeat	122 – 183	62	FG-GAP 2
	Repeat	188 – 240	53	FG-GAP 3
	Repeat	253 – 310	58	FG-GAP 4
	Repeat	311 – 372	62	FG-GAP 5
	Repeat	373 – 431	59	FG-GAP 6
	Repeat	435 – 498	64	FG-GAP 7
	Calcium binding	329 – 337	9	Potential
	Calcium binding	395 – 403	9	Potential
	Calcium binding	459 – 467	9	Potential
	Motif	455 – 457	3	Cell attachment site Potential
Amino acid modifications
	Glycosylation	81	1	N-linked (GlcNAc...) Potential
	Glycosylation	122	1	N-linked (GlcNAc...) Potential
	Glycosylation	177	1	N-linked (GlcNAc...) Potential
	Glycosylation	239	1	N-linked (GlcNAc...) Potential
	Glycosylation	302	1	N-linked (GlcNAc...) Potential
	Glycosylation	311	1	N-linked (GlcNAc...) Potential
	Glycosylation	504	1	N-linked (GlcNAc...) Potential
	Glycosylation	601	1	N-linked (GlcNAc...) Potential
	Glycosylation	605	1	N-linked (GlcNAc...) Potential
	Glycosylation	719	1	N-linked (GlcNAc...) Potential
	Glycosylation	737	1	N-linked (GlcNAc...) Potential
	Glycosylation	753	1	N-linked (GlcNAc...) Potential
	Glycosylation	780	1	N-linked (GlcNAc...) Potential
	Glycosylation	896	1	N-linked (GlcNAc...) Potential
	Glycosylation	923	1	N-linked (GlcNAc...) Potential
	Glycosylation	1005	1	N-linked (GlcNAc...) Potential
	Disulfide bond	96 ↔ 106		By similarity
	Disulfide bond	150 ↔ 171		By similarity
	Disulfide bond	187 ↔ 200		By similarity
	Disulfide bond	507 ↔ 518		By similarity
	Disulfide bond	524 ↔ 580		By similarity
	Disulfide bond	641 ↔ 647		By similarity
	Disulfide bond	713 ↔ 726		By similarity
	Disulfide bond	867 ↔ 924		Interchain (between heavy and light chains) By similarity
	Disulfide bond	929 ↔ 934		By similarity
Natural variations
	Natural variant	216	1	V → L. Ref.1 Corresponds to variant rs7895372 [ dbSNP | Ensembl ].		VAR_018673
	Natural variant	567	1	V → L. Ref.9		VAR_034682
	Natural variant	577	1	S → F. Ref.1 Ref.9 Corresponds to variant rs2298033 [ dbSNP | Ensembl ].		VAR_018674
	Natural variant	581	1	Q → P. Ref.1 Ref.9 Corresponds to variant rs9333269 [ dbSNP | Ensembl ].		VAR_018675
	Natural variant	748	1	R → H. Ref.1 Ref.9 Corresponds to variant rs9333174 [ dbSNP | Ensembl ].		VAR_018676
	Natural variant	993	1	I → V. Ref.1 Ref.9 Corresponds to variant rs9333241 [ dbSNP | Ensembl ].		VAR_018677
	Natural variant	994	1	V → A. Ref.1 Ref.5 Ref.9 Corresponds to variant rs1041135 [ dbSNP | Ensembl ].		VAR_018678
Experimental info
	Sequence conflict	47	1	T → A in AAA93514. Ref.5
	Sequence conflict	166	1	D → G in AAA93514. Ref.5
	Sequence conflict	188	1	R → G in AAA93514. Ref.5
	Sequence conflict	304	1	T → Y in AAA93514. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	P53708 [UniParc]. Last modified November 2, 2010. Version 3. Checksum: 8F9614BDBB897D77	FASTA	1,063	117,474
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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

SeattleSNPs

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.
IPI	IPI00023410.
RefSeq	NP_003629.1. NM_003638.1.
UniGene	Hs.171311.
3D structure databases
ProteinModelPortal	P53708.
SMR	P53708. Positions 39-1002.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000367316.
PTM databases
PhosphoSite	P53708.
Polymorphism databases
DMDM	311033437.
Proteomic databases
PaxDb	P53708.
PRIDE	P53708.
Protocols and materials databases
DNASU	8516.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000378076; ENSP00000367316; ENSG00000077943.
GeneID	8516.
KEGG	hsa:8516.
UCSC	uc001ioc.1. human.
Organism-specific databases
CTD	8516.
GeneCards	GC10M015599.
H-InvDB	HIX0035424.
HGNC	HGNC:6144. ITGA8.
HPA	HPA003432.
MIM	604063. gene.
neXtProt	NX_P53708.
PharmGKB	PA29944.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG26407.
HOGENOM	HOG000231603.
HOVERGEN	HBG006186.
InParanoid	P53708.
KO	K06584.
OMA	ESNPREV.
OrthoDB	EOG4548XV.
PhylomeDB	P53708.
Enzyme and pathway databases
Pathway_Interaction_DB	arf6_traffickingpathway. Arf6 trafficking events.
Reactome	REACT_111102. Signal Transduction. REACT_118779. Extracellular matrix organization.
Gene expression databases
ArrayExpress	P53708.
Bgee	P53708.
CleanEx	HS_ITGA8.
Genevestigator	P53708.
GermOnline	ENSG00000077943. Homo sapiens.
Family and domain databases
InterPro	IPR013517. FG-GAP. IPR013519. Int_alpha_beta-p. IPR000413. Integrin_alpha. IPR013649. Integrin_alpha-2. IPR018184. Integrin_alpha_C_CS. [Graphical view]
Pfam	PF01839. FG-GAP. 2 hits. PF00357. Integrin_alpha. 1 hit. PF08441. Integrin_alpha2. 1 hit. [Graphical view]
PRINTS	PR01185. INTEGRINA.
SMART	SM00191. Int_alpha. 6 hits. [Graphical view]
PROSITE	PS51470. FG_GAP. 7 hits. PS00242. INTEGRIN_ALPHA. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	8516.
NextBio	31878.
SOURCE	Search...

Entry information

Entry name

ITA8_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 117 of the entry and version 3 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.