ITA9_MOUSE
ID ITA9_MOUSE Reviewed; 1036 AA.
AC B8JK39; B9EKC4;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Integrin alpha-9 {ECO:0000305};
DE Flags: Precursor;
GN Name=Itga9 {ECO:0000312|MGI:MGI:104756};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
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., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP INTERACTION WITH FBLN5.
RX PubMed=11805835; DOI=10.1038/415171a;
RA Nakamura T., Lozano P.R., Ikeda Y., Iwanaga Y., Hinek A., Minamisawa S.,
RA Cheng C.F., Kobuke K., Dalton N., Takada Y., Tashiro K., Ross J., Honjo T.,
RA Chien K.R.;
RT "Fibulin-5/DANCE is essential for elastogenesis in vivo.";
RL Nature 415:171-175(2002).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Integrin alpha-9/beta-1 (ITGA9:ITGB1) is a receptor for
CC VCAM1, cytotactin and osteopontin. It recognizes the sequence A-E-I-D-
CC G-I-E-L in cytotactin. {ECO:0000250}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Alpha-9 (ITGA9)
CC associates with beta-1 (ITGB1) (Probable). Integrin ITGA9:ITGB1
CC interacts with FBLN5 (via N-terminus) (PubMed:11805835).
CC {ECO:0000269|PubMed:11805835, ECO:0000305|PubMed:11805835}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I
CC membrane protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the integrin alpha chain family. {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; AC156800; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC159000; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC165257; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CT486004; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC150824; AAI50825.1; -; mRNA.
DR CCDS; CCDS23604.1; -.
DR RefSeq; NP_598482.2; NM_133721.2.
DR AlphaFoldDB; B8JK39; -.
DR SMR; B8JK39; -.
DR STRING; 10090.ENSMUSP00000044227; -.
DR GlyGen; B8JK39; 4 sites.
DR iPTMnet; B8JK39; -.
DR PhosphoSitePlus; B8JK39; -.
DR MaxQB; B8JK39; -.
DR PaxDb; B8JK39; -.
DR PeptideAtlas; B8JK39; -.
DR PRIDE; B8JK39; -.
DR ProteomicsDB; 301688; -.
DR Antibodypedia; 11893; 184 antibodies from 32 providers.
DR DNASU; 104099; -.
DR Ensembl; ENSMUST00000044165; ENSMUSP00000044227; ENSMUSG00000039115.
DR GeneID; 104099; -.
DR KEGG; mmu:104099; -.
DR UCSC; uc009rzw.2; mouse.
DR CTD; 3680; -.
DR MGI; MGI:104756; Itga9.
DR VEuPathDB; HostDB:ENSMUSG00000039115; -.
DR eggNOG; KOG3637; Eukaryota.
DR GeneTree; ENSGT00940000156503; -.
DR HOGENOM; CLU_004111_5_0_1; -.
DR InParanoid; B8JK39; -.
DR OMA; DKENIFH; -.
DR OrthoDB; 189377at2759; -.
DR PhylomeDB; B8JK39; -.
DR TreeFam; TF105391; -.
DR Reactome; R-MMU-216083; Integrin cell surface interactions.
DR Reactome; R-MMU-3000178; ECM proteoglycans.
DR Reactome; R-MMU-445144; Signal transduction by L1.
DR BioGRID-ORCS; 104099; 0 hits in 69 CRISPR screens.
DR ChiTaRS; Itga9; mouse.
DR PRO; PR:B8JK39; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; B8JK39; protein.
DR Bgee; ENSMUSG00000039115; Expressed in animal zygote and 240 other tissues.
DR ExpressionAtlas; B8JK39; baseline and differential.
DR Genevisible; B8JK39; MM.
DR GO; GO:0009925; C:basal plasma membrane; IDA:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0034679; C:integrin alpha9-beta1 complex; IEA:Ensembl.
DR GO; GO:0008305; C:integrin complex; IBA:GO_Central.
DR GO; GO:0005518; F:collagen binding; IEA:Ensembl.
DR GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR GO; GO:0043236; F:laminin binding; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; ISO:MGI.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; IBA:GO_Central.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0007160; P:cell-matrix adhesion; IBA:GO_Central.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0050900; P:leukocyte migration; IBA:GO_Central.
DR GO; GO:0030593; P:neutrophil chemotaxis; IGI:MGI.
DR GO; GO:0042060; P:wound healing; IEA:Ensembl.
DR Gene3D; 2.130.10.130; -; 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; IPR018184; Integrin_alpha_C_CS.
DR InterPro; IPR028994; Integrin_alpha_N.
DR InterPro; IPR032695; Integrin_dom_sf.
DR Pfam; PF01839; FG-GAP; 2.
DR Pfam; PF08441; Integrin_alpha2; 1.
DR PRINTS; PR01185; INTEGRINA.
DR SMART; SM00191; Int_alpha; 5.
DR SUPFAM; SSF69179; SSF69179; 3.
DR SUPFAM; SSF69318; SSF69318; 1.
DR PROSITE; PS51470; FG_GAP; 7.
DR PROSITE; PS00242; INTEGRIN_ALPHA; 1.
PE 1: Evidence at protein level;
KW Calcium; Cell adhesion; Disulfide bond; Glycoprotein; Integrin; Membrane;
KW Metal-binding; Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..1036
FT /note="Integrin alpha-9"
FT /evidence="ECO:0000255"
FT /id="PRO_0000431914"
FT TOPO_DOM 29..981
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 982..1002
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1003..1036
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REPEAT 36..97
FT /note="FG-GAP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 109..175
FT /note="FG-GAP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 183..233
FT /note="FG-GAP 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 234..290
FT /note="FG-GAP 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 291..350
FT /note="FG-GAP 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 352..409
FT /note="FG-GAP 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 412..475
FT /note="FG-GAP 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT MOTIF 1006..1010
FT /note="GFFKR motif"
FT /evidence="ECO:0000250|UniProtKB:Q13797"
FT BINDING 313
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 315
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 317
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 321
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 374
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 376
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 378
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 382
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 436
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 438
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 440
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 444
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT SITE 566..567
FT /note="Cleavage"
FT /evidence="ECO:0000255"
FT CARBOHYD 226
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 494
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 515
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 808
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 88..98
FT /evidence="ECO:0000250"
FT DISULFID 143..163
FT /evidence="ECO:0000250"
FT DISULFID 180..195
FT /evidence="ECO:0000250"
FT DISULFID 483..492
FT /evidence="ECO:0000250"
FT DISULFID 498..556
FT /evidence="ECO:0000250"
FT DISULFID 621..626
FT /evidence="ECO:0000250"
FT DISULFID 697..707
FT /evidence="ECO:0000250"
FT DISULFID 856..892
FT /evidence="ECO:0000250"
FT DISULFID 899..904
FT /evidence="ECO:0000250"
FT CONFLICT 291
FT /note="I -> V (in Ref. 2; AAI50825)"
FT /evidence="ECO:0000305"
FT CONFLICT 918
FT /note="N -> D (in Ref. 2; AAI50825)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1036 AA; 114416 MW; F14BDEA82670FFCD CRC64;
MGGPAAARTG AGGLRALLLA LVAAGVPAGA YNLDAQRPVR FQGPSGSFFG YAVLEHFHDN
TRWVLVGAPK ADSKYSTSVK SPGAVFKCRV HTNPDRRCTE LDMARGRTRG APCGKTCRGD
RDDEWMGVSL ARQPRADGRV LACAHRWKNI YYEADHILPH GFCYLIPSNL QAKGKVLIPC
YEEYKKKYGE EHGSCQAGIA GFFTEELVVM GAPGSFYWAG TLKVLNLTDN TYFKLNDEAI
MNRRYTYLGY AVTAGHFSHP SITDVVGGAP QDEGIGKVYI FRADRRSGTL IKIFQASGKK
MGSYFGSSLC AVDLNMDGLS DLLVGAPMFS EIRDEGQVTV YLNQGHGALE EQLTLTGDAA
YNAHFGESIA NLGDIDDDGF PDVAVGAPKE EDFAGAVYIY HGDANGIVPK YSMKLSGRRL
NPTLRMFGQS ISGGIDMDGN GYPDVTIGAF LSDSVVLLRA RPVITVDVSI FLPGSINITA
PQCHDGQQPV NCLNVTVCFR FHGKNVPGEI GLNYNLTADV AQKEKGQLPR VYFVLFGETA
GQVSERLQLS HMDEVCHHYV AHVKRRVQDV ISPIVFEAAY SLDEHVMGEE DRELPDLTPV
LRWKKGQRIS QKNQTVFERN CQSEDCAADL QLRGKLLLSS VDEKTPHLAL GAVKNISLNI
SISNLGDDAY DANVSFNVSR ELFFINMWQK EEMGISCELL ESDFLKCSVG FPFMRSKSKY
EFSVIFDTSH LSGEEEILSF IVTAQSGNLE RSEALHDNTL TLTVPLVHEV DTSITGIVSP
TSFVYGESVD ASNFIQLDDQ ECHFQPVNIT LQVYNMGPST LPGSSVSISF PSRLSPGGAE
MFQVQDMVVS QEKGNCSLQR NPTPCIIPQE QENIFHTIFA FFSKSGRKVL DCEKPGSFCL
TLHCNLSALP KEESRTINLY MLLNTEILKK DSSSVIQFMA RAKVKVEPAL RVVEIANGNP
EETLVVFEAL HNLEPRGYVV GWIIAISLLV GILIFLLLAV LLWKMGFFRR RYKEIIEAEK
NRKENEDGWD WVQKNQ
