ID ITA8_MOUSE Reviewed; 1062 AA.
AC A2ARA8; O70304; Q3UXV8; Q8BRG3; Q8C0H7;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 01-MAY-2013, entry version 60.
DE RecName: Full=Integrin alpha-8;
DE Contains:
DE RecName: Full=Integrin alpha-8 heavy chain;
DE Contains:
DE RecName: Full=Integrin alpha-8 light chain;
DE Flags: Precursor;
GN Name=Itga8;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC Muroidea; Muridae; Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Embryo, Testis, and Wolffian duct;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of
RT the mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 45-1056 (ISOFORM 1), FUNCTION,
RP DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
RC TISSUE=Fibroblast;
RX PubMed=9054500; DOI=10.1016/S0092-8674(00)81903-0;
RA Mueller U., Wang D., Denda S., Meneses J.J., Pedersen R.A.,
RA Reichardt L.F.;
RT "Integrin alpha8beta1 is critically important for epithelial-
RT mesenchymal interactions during kidney morphogenesis.";
RL Cell 88:603-613(1997).
RN [4]
RP FUNCTION.
RX PubMed=9548928; DOI=10.1021/bi9727489;
RA Denda S., Mueller U., Crossin K.L., Erickson H.P., Reichardt L.F.;
RT "Utilization of a soluble integrin-alkaline phosphatase chimera to
RT characterize integrin alpha 8 beta 1 receptor interactions with
RT tenascin: murine alpha 8 beta 1 binds to the RGD site in tenascin-C
RT fragments, but not to native tenascin-C.";
RL Biochemistry 37:5464-5474(1998).
RN [5]
RP FUNCTION.
RX PubMed=9614184;
RA Denda S., Reichardt L.F., Mueller U.;
RT "Identification of osteopontin as a novel ligand for the integrin
RT alpha8 beta1 and potential roles for this integrin-ligand interaction
RT in kidney morphogenesis.";
RL Mol. Biol. Cell 9:1425-1435(1998).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=10024342;
RA Pinkstaff J.K., Detterich J., Lynch G., Gall C.;
RT "Integrin subunit gene expression is regionally differentiated in
RT adult brain.";
RL J. Neurosci. 19:1541-1556(1999).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=10504498; DOI=10.1046/j.1523-1755.1999.00662.x;
RA Hartner A., Schoecklmann H., Proels F., Mueller U., Sterzel R.B.;
RT "Alpha8 integrin in glomerular mesangial cells and in experimental
RT glomerulonephritis.";
RL Kidney Int. 56:1468-1480(1999).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=10742111; DOI=10.1038/74286;
RA Littlewood Evans A., Mueller U.;
RT "Stereocilia defects in the sensory hair cells of the inner ear in
RT mice deficient in integrin alpha8beta1.";
RL Nat. Genet. 24:424-428(2000).
RN [9]
RP FUNCTION.
RX PubMed=11470831; DOI=10.1083/jcb.200103069;
RA Brandenberger R., Schmidt A., Linton J., Wang D., Backus C., Denda S.,
RA Mueller U., Reichardt L.F.;
RT "Identification and characterization of a novel extracellular matrix
RT protein nephronectin that is associated with integrin alpha8beta1 in
RT the embryonic kidney.";
RL J. Cell Biol. 154:447-458(2001).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11891185;
RA Hartner A., Cordasic N., Klanke B., Mueller U., Sterzel R.B.,
RA Hilgers K.F.;
RT "The alpha8 integrin chain affords mechanical stability to the
RT glomerular capillary tuft in hypertensive glomerular disease.";
RL Am. J. Pathol. 160:861-867(2002).
RN [11]
RP DEVELOPMENTAL STAGE.
RX PubMed=14500699;
RA Wagner T.E., Frevert C.W., Herzog E.L., Schnapp L.M.;
RT "Expression of the integrin subunit alpha8 in murine lung
RT development.";
RL J. Histochem. Cytochem. 51:1307-1315(2003).
RN [12]
RP FUNCTION.
RX PubMed=12787402; DOI=10.1046/j.1523-1755.2003.00057.x;
RA Bieritz B., Spessotto P., Colombatti A., Jahn A., Prols F.,
RA Hartner A.;
RT "Role of alpha8 integrin in mesangial cell adhesion, migration, and
RT proliferation.";
RL Kidney Int. 64:119-127(2003).
RN [13]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17537792; DOI=10.1242/dev.005033;
RA Linton J.M., Martin G.R., Reichardt L.F.;
RT "The ECM protein nephronectin promotes kidney development via integrin
RT alpha8beta1-mediated stimulation of Gdnf expression.";
RL Development 134:2501-2509(2007).
CC -!- FUNCTION: Integrin alpha-8/beta-1 functions in the genesis of
CC kidney and probably of other organs by regulating the recruitment
CC of mesenchymal cells into epithelial structures. It recognizes the
CC sequence R-G-D in a wide array of ligands including TNC, FN1, SPP1
CC TGFB1, TGFB3 and VTN. NPNT is probably its functional ligand in
CC kidney genesis. Neuronal receptor for TNC it mediates cell-cell
CC interactions and regulates neurite outgrowth of sensory and motor
CC neurons.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. The alpha
CC subunit is composed of a heavy and a light chain linked by a
CC disulfide bond. Alpha-8 associates with beta-1.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A2ARA8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A2ARA8-2; Sequence=VSP_027364, VSP_027365;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: In brain, expressed in deep cortex,
CC hippocampal CA1, basolateral amygdala and striatum. In kidney,
CC expressed in glomerular mesengium (at protein level).
CC -!- DEVELOPMENTAL STAGE: Expressed in mesenchymal cells of developing
CC organs such as gut, lung, gonads and nephrogenic cord.
CC -!- DISRUPTION PHENOTYPE: Mice display renal agenesis and dysgenesis.
CC This is associated with a reduced expression of Gdnf that is
CC similarly found in mice lacking Npnt. Adult mice also display
CC increased susceptibility to glomerular capillary destruction upon
CC mechanical stress. Mice lacking Itga8 also have difficulty
CC balancing associated with structural defects in the inner ear
CC where utricular hair cells lack stereocilia.
CC -!- SIMILARITY: Belongs to the integrin alpha chain family.
CC -!- SIMILARITY: Contains 7 FG-GAP repeats.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AK031326; BAC27348.1; -; mRNA.
DR EMBL; AK044910; BAC32137.1; -; mRNA.
DR EMBL; AK135193; BAE22455.1; -; mRNA.
DR EMBL; AL845313; CAM17354.1; -; Genomic_DNA.
DR EMBL; AF041409; AAC15665.1; -; mRNA.
DR IPI; IPI00345112; -.
DR IPI; IPI00857527; -.
DR RefSeq; NP_001001309.1; NM_001001309.2.
DR UniGene; Mm.329997; -.
DR ProteinModelPortal; A2ARA8; -.
DR SMR; A2ARA8; 38-1002.
DR PhosphoSite; A2ARA8; -.
DR PaxDb; A2ARA8; -.
DR PRIDE; A2ARA8; -.
DR Ensembl; ENSMUST00000028106; ENSMUSP00000028106; ENSMUSG00000026768.
DR GeneID; 241226; -.
DR KEGG; mmu:241226; -.
DR UCSC; uc008ijk.1; mouse.
DR UCSC; uc008ijl.1; mouse.
DR CTD; 8516; -.
DR MGI; MGI:109442; Itga8.
DR eggNOG; NOG26407; -.
DR GeneTree; ENSGT00700000104007; -.
DR HOGENOM; HOG000231603; -.
DR HOVERGEN; HBG006186; -.
DR InParanoid; A2ARA8; -.
DR KO; K06584; -.
DR OMA; ESNPREV; -.
DR OrthoDB; EOG4548XV; -.
DR NextBio; 384935; -.
DR ArrayExpress; A2ARA8; -.
DR Bgee; A2ARA8; -.
DR CleanEx; MM_ITGA8; -.
DR Genevestigator; A2ARA8; -.
DR GO; GO:0045177; C:apical part of cell; IDA:MGI.
DR GO; GO:0008305; C:integrin complex; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0030030; P:cell projection organization; IMP:MGI.
DR GO; GO:0045184; P:establishment of protein localization; IMP:BHF-UCL.
DR GO; GO:0030198; P:extracellular matrix organization; IMP:MGI.
DR GO; GO:0042472; P:inner ear morphogenesis; IMP:MGI.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0007613; P:memory; IMP:MGI.
DR GO; GO:0001656; P:metanephros development; IMP:MGI.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:2000721; P:positive regulation of transcription from RNA polymerase II promoter involved in smooth muscle cell differentiation; IDA:BHF-UCL.
DR GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; IMP:MGI.
DR GO; GO:0048745; P:smooth muscle tissue development; IMP:BHF-UCL.
DR InterPro; IPR013517; FG-GAP.
DR InterPro; IPR013519; Int_alpha_beta-p.
DR InterPro; IPR000413; Integrin_alpha.
DR InterPro; IPR013649; Integrin_alpha-2.
DR InterPro; IPR018184; Integrin_alpha_C_CS.
DR Pfam; PF01839; FG-GAP; 2.
DR Pfam; PF00357; Integrin_alpha; 1.
DR Pfam; PF08441; Integrin_alpha2; 1.
DR PRINTS; PR01185; INTEGRINA.
DR SMART; SM00191; Int_alpha; 6.
DR PROSITE; PS51470; FG_GAP; 7.
DR PROSITE; PS00242; INTEGRIN_ALPHA; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cell adhesion;
KW Cleavage on pair of basic residues; Complete proteome;
KW Developmental protein; Differentiation; Disulfide bond; Glycoprotein;
KW Integrin; Membrane; Metal-binding; Neurogenesis; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1 35 Potential.
FT CHAIN 36 1062 Integrin alpha-8.
FT /FTId=PRO_0000297709.
FT CHAIN 38 905 Integrin alpha-8 heavy chain (Potential).
FT /FTId=PRO_0000297710.
FT CHAIN 906 1062 Integrin alpha-8 light chain (Potential).
FT /FTId=PRO_0000297711.
FT TOPO_DOM 36 1010 Extracellular (Potential).
FT TRANSMEM 1011 1031 Helical; (Potential).
FT TOPO_DOM 1032 1062 Cytoplasmic (Potential).
FT REPEAT 41 104 FG-GAP 1.
FT REPEAT 121 182 FG-GAP 2.
FT REPEAT 187 239 FG-GAP 3.
FT REPEAT 252 309 FG-GAP 4.
FT REPEAT 310 371 FG-GAP 5.
FT REPEAT 372 430 FG-GAP 6.
FT REPEAT 434 497 FG-GAP 7.
FT CA_BIND 328 336 Potential.
FT CA_BIND 394 402 Potential.
FT CA_BIND 458 466 Potential.
FT MOTIF 454 456 Cell attachment site (Potential).
FT CARBOHYD 80 80 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 121 121 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 176 176 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 238 238 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 301 301 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 310 310 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 503 503 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 600 600 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 604 604 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 718 718 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 736 736 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 752 752 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 779 779 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 895 895 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 922 922 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 1004 1004 N-linked (GlcNAc...) (Potential).
FT DISULFID 95 105 By similarity.
FT DISULFID 149 170 By similarity.
FT DISULFID 186 199 By similarity.
FT DISULFID 506 517 By similarity.
FT DISULFID 523 579 By similarity.
FT DISULFID 640 646 By similarity.
FT DISULFID 712 725 By similarity.
FT DISULFID 866 923 Interchain (between heavy and light
FT chains) (By similarity).
FT DISULFID 928 933 By similarity.
FT VAR_SEQ 282 286 ELVAG -> GQRHP (in isoform 2).
FT /FTId=VSP_027364.
FT VAR_SEQ 287 1062 Missing (in isoform 2).
FT /FTId=VSP_027365.
FT CONFLICT 66 66 D -> G (in Ref. 1; BAE22455).
SQ SEQUENCE 1062 AA; 117556 MW; DB1ACA43FADD3AC0 CRC64;
MSAGTHCGPP GNRAPPFARL CCVSAALGML WSPACLAFNL DVDKLTVYSG PEGSYFGYSL
DFYIPDARTA SVLVGAPKAN TSQPDIVEGG AVYYCPWPSE RSAQCKQIPF DTTNNRKIRV
NGTKEPIEFK SNQWFGATVR AHKGKVVACA PLYHWRTLKP NPAKDPVGTC YVAIQNFSAY
AEHSPCRNSN ADPEGQGYCQ AGFSLDFYKN GDLIVGGPGS FYWQGQVITV SIADIIANYS
FKDILRKLAA EKQTDVAPAS YDDSYLGYSV AAGEFTGDSQ QELVAGIPRG AQNFGYVSII
NSTDMTFIQN FTGEQMASYF GYTVVVSDVN NDGMDDILVG APLFMEREFE SNPREVGQVY
LYLQASALLF QDPQVLTGTE TFGRFGSSVA HLGDLNQDGY NDIAIGVPFA GKDQRGKVLI
YNGNPRGLHS KPSQVLQGIW GSQTIPSGFG FSLRGDADID KNDYPDLLVG AFGKGKVAVY
RARPVVTVDA QLLLHPMIIN LENKTCQIPE FPTPVACFSV RVCASIAGQS ISNTIALLAE
VQLDFLKQKG AIKRTLFLHN HQSHFTFPFV MKQQKSLHCQ DFMVYLRDET EFRDKLSPIN
ISLNYSLDDS TFKDSLEVKP ILNHYRDNVV TEQAHILVDC GEDNLCVPDL KLSARPDKHQ
IIIGDENHLM LIINARNEGE GAYEAELFVI IPEEADYVGI ERNNKGLRPL SCEYKMENVT
RMVVCDLGNP MVTGTNFSLG LRFAVPRLEK TNMSINFDLQ IRSSNKDNPD SNFERVQINI
TAIAQVEIRG VSHPPQIVLP IHNWEPEKKP HKEEEVGPLV EHIYELHNIG PSTISDSILD
VGWPFSARDE FLLYIFHLQT LGPLQCQTNP EINPQDIKPA ASPEDTPELS AFLRNATIPH
LVRKRDVPVV QLHRQSPARI LNCTNIDCLQ ISCAVGRLGG GESAVLKVRS RLWAHTFLKR
KNDHYALASL VSFEVKKMPY KEQPAKLPAG STAVKTSVIW ATPNVSFSIP LWVIILAILL
GLLVLAILTL ALWKCGFFDR ARPPQDEMTD REQLTSDKTP EA
//
