ID ITA10_HUMAN Reviewed; 1167 AA. AC O75578; B2RAM4; B2RTV5; Q6UXJ6; Q9UHZ8; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 03-OCT-2006, sequence version 2. DT 13-FEB-2019, entry version 173. DE RecName: Full=Integrin alpha-10; DE Flags: Precursor; GN Name=ITGA10; ORFNames=UNQ468/PRO827; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Articular chondrocyte; RX PubMed=9685391; DOI=10.1074/jbc.273.32.20383; RA Camper L., Hellman U., Lundgren-Aakerlund E.; RT "Isolation, cloning, and sequence analysis of the integrin subunit RT alpha10, a beta1-associated collagen binding integrin expressed on RT chondrocytes."; RL J. Biol. Chem. 273:20383-20389(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Endothelial cell, and Heart; RX PubMed=10702680; RA Lehnert K., Ni J., Leung E., Gough S.M., Morris C.M., Liu D., RA Wang S.-X., Langley R., Krissansen G.W.; RT "The integrin alpha10 subunit: expression pattern, partial gene RT structure, and chromosomal localization."; RL Cytogenet. Cell Genet. 87:238-244(1999). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RX PubMed=12975309; DOI=10.1101/gr.1293003; RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., RA Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., RA Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., RA Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., RA Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., RA Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., RA Wood W.I., Godowski P.J., Gray A.M.; RT "The secreted protein discovery initiative (SPDI), a large-scale RT effort to identify novel human secreted and transmembrane proteins: a RT bioinformatics assessment."; RL Genome Res. 13:2265-2270(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Trachea; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., RA Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Integrin alpha-10/beta-1 is a receptor for collagen. CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Alpha-10 CC associates with beta-1. CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane CC protein. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=O75578-1; Sequence=Displayed; CC Name=2; CC IsoId=O75578-2; Sequence=VSP_013114, VSP_013115; CC Note=No experimental confirmation available.; CC Name=3; CC IsoId=O75578-3; Sequence=VSP_054483; CC Note=No experimental confirmation available.; CC -!- TISSUE SPECIFICITY: Widely expressed with highest expression in CC muscle and heart. Found in articular cartilage. CC -!- DOMAIN: The integrin I-domain (insert) is a VWFA domain. Integrins CC with I-domains do not undergo protease cleavage. CC -!- SIMILARITY: Belongs to the integrin alpha chain family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AF074015; AAC31952.1; -; mRNA. DR EMBL; AF112345; AAF21944.1; -; mRNA. DR EMBL; AF172723; AAF61638.1; -; Genomic_DNA. DR EMBL; AY358325; AAQ88691.1; -; mRNA. DR EMBL; AK314255; BAG36921.1; -; mRNA. DR EMBL; AL160282; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471244; EAW71425.1; -; Genomic_DNA. DR EMBL; BC140831; AAI40832.1; -; mRNA. DR EMBL; BC144637; AAI44638.1; -; mRNA. DR CCDS; CCDS72869.1; -. [O75578-1] DR CCDS; CCDS76204.1; -. [O75578-3] DR RefSeq; NP_001289969.1; NM_001303040.1. DR RefSeq; NP_001289970.1; NM_001303041.1. [O75578-3] DR RefSeq; NP_003628.2; NM_003637.4. [O75578-1] DR UniGene; Hs.158237; -. DR ProteinModelPortal; O75578; -. DR SMR; O75578; -. DR BioGrid; 114087; 1. DR ComplexPortal; CPX-1817; Integrin alpha10-beta1 complex. DR CORUM; O75578; -. DR IntAct; O75578; 1. DR STRING; 9606.ENSP00000358310; -. DR ChEMBL; CHEMBL5882; -. DR iPTMnet; O75578; -. DR PhosphoSitePlus; O75578; -. DR BioMuta; ITGA10; -. DR EPD; O75578; -. DR jPOST; O75578; -. DR PaxDb; O75578; -. DR PeptideAtlas; O75578; -. DR PRIDE; O75578; -. DR ProteomicsDB; 50095; -. DR ProteomicsDB; 50096; -. [O75578-2] DR DNASU; 8515; -. DR Ensembl; ENST00000369304; ENSP00000358310; ENSG00000143127. [O75578-1] DR Ensembl; ENST00000539363; ENSP00000439894; ENSG00000143127. [O75578-3] DR GeneID; 8515; -. DR KEGG; hsa:8515; -. DR UCSC; uc001eoa.4; human. [O75578-1] DR CTD; 8515; -. DR DisGeNET; 8515; -. DR EuPathDB; HostDB:ENSG00000143127.12; -. DR GeneCards; ITGA10; -. DR HGNC; HGNC:6135; ITGA10. DR MIM; 604042; gene. DR neXtProt; NX_O75578; -. DR OpenTargets; ENSG00000143127; -. DR PharmGKB; PA29936; -. DR eggNOG; KOG3637; Eukaryota. DR eggNOG; ENOG410XPVZ; LUCA. DR GeneTree; ENSGT00940000158423; -. DR HOGENOM; HOG000059610; -. DR HOVERGEN; HBG006185; -. DR InParanoid; O75578; -. DR KO; K06586; -. DR OMA; PIVHLAP; -. DR OrthoDB; 52951at2759; -. DR PhylomeDB; O75578; -. DR TreeFam; TF105391; -. DR Reactome; R-HSA-216083; Integrin cell surface interactions. DR Reactome; R-HSA-447041; CHL1 interactions. DR Reactome; R-HSA-75892; Platelet Adhesion to exposed collagen. DR SIGNOR; O75578; -. DR ChiTaRS; ITGA10; human. DR GeneWiki; ITGA10; -. DR GenomeRNAi; 8515; -. DR PRO; PR:O75578; -. DR Proteomes; UP000005640; Chromosome 1. DR Bgee; ENSG00000143127; Expressed in 131 organ(s), highest expression level in tibia. DR Genevisible; O75578; HS. DR GO; GO:0034680; C:integrin alpha10-beta1 complex; IDA:UniProtKB. DR GO; GO:0008305; C:integrin complex; TAS:ProtInc. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0005518; F:collagen binding; TAS:ProtInc. DR GO; GO:0098639; F:collagen binding involved in cell-matrix adhesion; IMP:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0007160; P:cell-matrix adhesion; IMP:UniProtKB. DR GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome. DR GO; GO:0007229; P:integrin-mediated signaling pathway; IMP:UniProtKB. DR Gene3D; 2.130.10.130; -; 1. DR Gene3D; 3.40.50.410; -; 1. 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; IPR028994; Integrin_alpha_N. DR InterPro; IPR032695; Integrin_dom_sf. DR InterPro; IPR002035; VWF_A. DR InterPro; IPR036465; vWFA_dom_sf. DR Pfam; PF01839; FG-GAP; 2. DR Pfam; PF08441; Integrin_alpha2; 1. DR Pfam; PF00092; VWA; 1. DR PRINTS; PR01185; INTEGRINA. DR SMART; SM00191; Int_alpha; 5. DR SMART; SM00327; VWA; 1. DR SUPFAM; SSF53300; SSF53300; 1. DR SUPFAM; SSF69179; SSF69179; 3. DR PROSITE; PS51470; FG_GAP; 7. DR PROSITE; PS50234; VWFA; 1. PE 2: Evidence at transcript level; KW Alternative splicing; Calcium; Cell adhesion; Complete proteome; KW Disulfide bond; Glycoprotein; Integrin; Magnesium; Membrane; KW Metal-binding; Polymorphism; Receptor; Reference proteome; Repeat; KW Signal; Transmembrane; Transmembrane helix. FT SIGNAL 1 22 {ECO:0000255}. FT CHAIN 23 1167 Integrin alpha-10. FT /FTId=PRO_0000016317. FT TOPO_DOM 23 1122 Extracellular. {ECO:0000255}. FT TRANSMEM 1123 1145 Helical. {ECO:0000255}. FT TOPO_DOM 1146 1167 Cytoplasmic. {ECO:0000255}. FT REPEAT 24 85 FG-GAP 1. {ECO:0000255|PROSITE- FT ProRule:PRU00803}. FT REPEAT 95 154 FG-GAP 2. {ECO:0000255|PROSITE- FT ProRule:PRU00803}. FT DOMAIN 167 350 VWFA. {ECO:0000255|PROSITE- FT ProRule:PRU00219}. FT REPEAT 361 412 FG-GAP 3. {ECO:0000255|PROSITE- FT ProRule:PRU00803}. FT REPEAT 417 470 FG-GAP 4. {ECO:0000255|PROSITE- FT ProRule:PRU00803}. FT REPEAT 472 534 FG-GAP 5. {ECO:0000255|PROSITE- FT ProRule:PRU00803}. FT REPEAT 535 593 FG-GAP 6. {ECO:0000255|PROSITE- FT ProRule:PRU00803}. FT REPEAT 597 657 FG-GAP 7. {ECO:0000255|PROSITE- FT ProRule:PRU00803}. FT CA_BIND 494 502 {ECO:0000255}. FT CA_BIND 558 566 {ECO:0000255}. FT CA_BIND 620 628 {ECO:0000255}. FT COMPBIAS 1134 1140 Poly-Leu. FT CARBOHYD 98 98 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 234 234 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 336 336 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 364 364 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 733 733 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 763 763 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 839 839 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 921 921 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 1011 1011 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 1018 1018 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 1039 1039 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 76 86 {ECO:0000250}. FT DISULFID 666 675 {ECO:0000250}. FT DISULFID 681 736 {ECO:0000250}. FT DISULFID 789 795 {ECO:0000250}. FT VAR_SEQ 19 161 Missing (in isoform 3). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_054483. FT VAR_SEQ 123 124 AC -> VS (in isoform 2). FT {ECO:0000303|PubMed:12975309}. FT /FTId=VSP_013114. FT VAR_SEQ 125 1167 Missing (in isoform 2). FT {ECO:0000303|PubMed:12975309}. FT /FTId=VSP_013115. FT VARIANT 381 381 R -> Q (in dbSNP:rs6665210). FT /FTId=VAR_027768. FT VARIANT 668 668 R -> W (in dbSNP:rs36073645). FT /FTId=VAR_034026. FT VARIANT 691 691 R -> H (in dbSNP:rs2274618). FT /FTId=VAR_027769. FT VARIANT 702 702 A -> T (in dbSNP:rs35515885). FT /FTId=VAR_034027. FT VARIANT 725 725 R -> Q (in dbSNP:rs2274616). FT /FTId=VAR_027770. FT CONFLICT 844 844 L -> I (in Ref. 1; AAC31952). FT {ECO:0000305}. FT CONFLICT 909 909 V -> G (in Ref. 1; AAC31952). FT {ECO:0000305}. FT CONFLICT 926 926 D -> E (in Ref. 1; AAC31952). FT {ECO:0000305}. SQ SEQUENCE 1167 AA; 127602 MW; 2F7FF938B4C0CBAC CRC64; MELPFVTHLF LPLVFLTGLC SPFNLDEHHP RLFPGPPEAE FGYSVLQHVG GGQRWMLVGA PWDGPSGDRR GDVYRCPVGG AHNAPCAKGH LGDYQLGNSS HPAVNMHLGM SLLETDGDGG FMACAPLWSR ACGSSVFSSG ICARVDASFQ PQGSLAPTAQ RCPTYMDVVI VLDGSNSIYP WSEVQTFLRR LVGKLFIDPE QIQVGLVQYG ESPVHEWSLG DFRTKEEVVR AAKNLSRREG RETKTAQAIM VACTEGFSQS HGGRPEAARL LVVVTDGESH DGEELPAALK ACEAGRVTRY GIAVLGHYLR RQRDPSSFLR EIRTIASDPD ERFFFNVTDE AALTDIVDAL GDRIFGLEGS HAENESSFGL EMSQIGFSTH RLKDGILFGM VGAYDWGGSV LWLEGGHRLF PPRMALEDEF PPALQNHAAY LGYSVSSMLL RGGRRLFLSG APRFRHRGKV IAFQLKKDGA VRVAQSLQGE QIGSYFGSEL CPLDTDRDGT TDVLLVAAPM FLGPQNKETG RVYVYLVGQQ SLLTLQGTLQ PEPPQDARFG FAMGALPDLN QDGFADVAVG APLEDGHQGA LYLYHGTQSG VRPHPAQRIA AASMPHALSY FGRSVDGRLD LDGDDLVDVA VGAQGAAILL SSRPIVHLTP SLEVTPQAIS VVQRDCRRRG QEAVCLTAAL CFQVTSRTPG RWDHQFYMRF TASLDEWTAG ARAAFDGSGQ RLSPRRLRLS VGNVTCEQLH FHVLDTSDYL RPVALTVTFA LDNTTKPGPV LNEGSPTSIQ KLVPFSKDCG PDNECVTDLV LQVNMDIRGS RKAPFVVRGG RRKVLVSTTL ENRKENAYNT SLSLIFSRNL HLASLTPQRE SPIKVECAAP SAHARLCSVG HPVFQTGAKV TFLLEFEFSC SSLLSQVFVK LTASSDSLER NGTLQDNTAQ TSAYIQYEPH LLFSSESTLH RYEVHPYGTL PVGPGPEFKT TLRVQNLGCY VVSGLIISAL LPAVAHGGNY FLSLSQVITN NASCIVQNLT EPPGPPVHPE ELQHTNRLNG SNTQCQVVRC HLGQLAKGTE VSVGLLRLVH NEFFRRAKFK SLTVVSTFEL GTEEGSVLQL TEASRWSESL LEVVQTRPIL ISLWILIGSV LGGLLLLALL VFCLWKLGFF AHKKIPEEEK REEKLEQ //