ITA9_HUMAN
ID ITA9_HUMAN Reviewed; 1035 AA.
AC Q13797; Q14638;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Integrin alpha-9;
DE AltName: Full=Integrin alpha-RLC;
DE Flags: Precursor;
GN Name=ITGA9;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], VARIANT GLU-507, TISSUE SPECIFICITY, AND
RP INDUCTION.
RC TISSUE=Lung;
RX PubMed=8290272;
RA Hibi K., Yamakawa K., Ueda R., Horio Y., Murata Y., Tamari M., Uchida K.,
RA Takahashi T., Nakamura Y., Takahashi T.;
RT "Aberrant upregulation of a novel integrin alpha subunit gene at 3p21.3 in
RT small cell lung cancer.";
RL Oncogene 9:611-619(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 36-1035, PROTEIN SEQUENCE OF 30-35, VARIANT
RP GLU-507, AND TISSUE SPECIFICITY.
RC TISSUE=Intestine, and Lung;
RX PubMed=8245132; DOI=10.1083/jcb.123.5.1289;
RA Palmer E.L., Rueegg C., Ferrando R., Pytela R., Sheppard D.;
RT "Sequence and tissue distribution of the integrin alpha 9 subunit, a novel
RT partner of beta 1 that is widely distributed in epithelia and muscle.";
RL J. Cell Biol. 123:1289-1297(1993).
RN [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-225.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [5]
RP VARIANT [LARGE SCALE ANALYSIS] CYS-750.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
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). Integrin ITGA9:ITGB1 interacts with
CC FBLN5 (via N-terminus). {ECO:0000250, ECO:0000250|UniProtKB:B8JK39}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I
CC membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: In airway epithelium, in the basal layer of
CC squamous epithelium, and in smooth muscle, skeletal muscle, and
CC hepatocytes. Abundantly expressed in fetal lung and lung cancers.
CC {ECO:0000269|PubMed:8245132, ECO:0000269|PubMed:8290272}.
CC -!- INDUCTION: Up-regulated in small cell lung cancers (SCLC).
CC {ECO:0000269|PubMed:8290272}.
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; D25303; BAA04984.1; -; mRNA.
DR EMBL; AC092055; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC093415; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP006240; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; L24158; AAA16099.1; -; mRNA.
DR CCDS; CCDS2669.1; -.
DR PIR; I58409; I58409.
DR RefSeq; NP_002198.2; NM_002207.2.
DR AlphaFoldDB; Q13797; -.
DR SMR; Q13797; -.
DR BioGRID; 109886; 32.
DR ComplexPortal; CPX-1816; Integrin alpha9-beta1 complex.
DR CORUM; Q13797; -.
DR IntAct; Q13797; 1.
DR STRING; 9606.ENSP00000264741; -.
DR ChEMBL; CHEMBL3170; -.
DR GlyGen; Q13797; 11 sites.
DR iPTMnet; Q13797; -.
DR PhosphoSitePlus; Q13797; -.
DR BioMuta; ITGA9; -.
DR DMDM; 229462922; -.
DR CPTAC; CPTAC-1492; -.
DR EPD; Q13797; -.
DR jPOST; Q13797; -.
DR MassIVE; Q13797; -.
DR PaxDb; Q13797; -.
DR PeptideAtlas; Q13797; -.
DR PRIDE; Q13797; -.
DR ProteomicsDB; 59688; -.
DR ABCD; Q13797; 3 sequenced antibodies.
DR Antibodypedia; 11893; 184 antibodies from 32 providers.
DR DNASU; 3680; -.
DR Ensembl; ENST00000264741.10; ENSP00000264741.5; ENSG00000144668.12.
DR GeneID; 3680; -.
DR KEGG; hsa:3680; -.
DR MANE-Select; ENST00000264741.10; ENSP00000264741.5; NM_002207.3; NP_002198.2.
DR UCSC; uc003chd.4; human.
DR CTD; 3680; -.
DR DisGeNET; 3680; -.
DR GeneCards; ITGA9; -.
DR HGNC; HGNC:6145; ITGA9.
DR HPA; ENSG00000144668; Low tissue specificity.
DR MIM; 603963; gene.
DR neXtProt; NX_Q13797; -.
DR OpenTargets; ENSG00000144668; -.
DR PharmGKB; PA29945; -.
DR VEuPathDB; HostDB:ENSG00000144668; -.
DR eggNOG; KOG3637; Eukaryota.
DR GeneTree; ENSGT00940000156503; -.
DR HOGENOM; CLU_004111_5_0_1; -.
DR InParanoid; Q13797; -.
DR OMA; DKENIFH; -.
DR OrthoDB; 189377at2759; -.
DR PhylomeDB; Q13797; -.
DR TreeFam; TF105391; -.
DR PathwayCommons; Q13797; -.
DR Reactome; R-HSA-216083; Integrin cell surface interactions.
DR Reactome; R-HSA-3000178; ECM proteoglycans.
DR Reactome; R-HSA-445144; Signal transduction by L1.
DR SignaLink; Q13797; -.
DR SIGNOR; Q13797; -.
DR BioGRID-ORCS; 3680; 13 hits in 1061 CRISPR screens.
DR ChiTaRS; ITGA9; human.
DR GeneWiki; ITGA9; -.
DR GenomeRNAi; 3680; -.
DR Pharos; Q13797; Tbio.
DR PRO; PR:Q13797; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q13797; protein.
DR Bgee; ENSG00000144668; Expressed in urethra and 172 other tissues.
DR ExpressionAtlas; Q13797; baseline and differential.
DR Genevisible; Q13797; HS.
DR GO; GO:0009925; C:basal plasma membrane; IEA:Ensembl.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0008305; C:integrin complex; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IGI: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; 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; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Integrin; Membrane; Metal-binding; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..1035
FT /note="Integrin alpha-9"
FT /id="PRO_0000016316"
FT TOPO_DOM 30..981
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 982..1002
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1003..1035
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 35..96
FT /note="FG-GAP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 111..174
FT /note="FG-GAP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 182..232
FT /note="FG-GAP 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 233..289
FT /note="FG-GAP 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 290..349
FT /note="FG-GAP 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 351..408
FT /note="FG-GAP 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 411..474
FT /note="FG-GAP 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT MOTIF 1005..1009
FT /note="GFFKR motif"
FT BINDING 312
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 314
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 316
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 320
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 373
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 375
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 377
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 381
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 435
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 437
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 439
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 443
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT SITE 565..566
FT /note="Cleavage"
FT /evidence="ECO:0000255"
FT CARBOHYD 225
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 476
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 493
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 612
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 654
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 658
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 672
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 676
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 807
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 854
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 904
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 87..97
FT /evidence="ECO:0000250"
FT DISULFID 142..162
FT /evidence="ECO:0000250"
FT DISULFID 179..194
FT /evidence="ECO:0000250"
FT DISULFID 482..491
FT /evidence="ECO:0000250"
FT DISULFID 497..555
FT /evidence="ECO:0000250"
FT DISULFID 620..625
FT /evidence="ECO:0000250"
FT DISULFID 696..706
FT /evidence="ECO:0000250"
FT DISULFID 855..891
FT /evidence="ECO:0000250"
FT DISULFID 898..903
FT /evidence="ECO:0000250"
FT VARIANT 507
FT /note="G -> E (in dbSNP:rs267561)"
FT /evidence="ECO:0000269|PubMed:8245132,
FT ECO:0000269|PubMed:8290272"
FT /id="VAR_055091"
FT VARIANT 750
FT /note="R -> C (in a breast cancer sample; somatic mutation;
FT dbSNP:rs781472543)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036073"
SQ SEQUENCE 1035 AA; 114489 MW; B812EDA867A3E836 CRC64;
MGGPAAPRGA GRLRALLLAL VVAGIPAGAY NLDPQRPVHF QGPADSFFGY AVLEHFHDNT
RWVLVGAPKA DSKYSPSVKS PGAVFKCRVH TNPDRRCTEL DMARGKNRGT SCGKTCREDR
DDEWMGVSLA RQPKADGRVL ACAHRWKNIY YEADHILPHG FCYIIPSNLQ AKGRTLIPCY
EEYKKKYGEE HGSCQAGIAG FFTEELVVMG APGSFYWAGT IKVLNLTDNT YLKLNDEVIM
NRRYTYLGYA VTAGHFSHPS TIDVVGGAPQ DKGIGKVYIF RADRRSGTLI KIFQASGKKM
GSYFGSSLCA VDLNGDGLSD LLVGAPMFSE IRDEGQVTVY INRGNGALEE QLALTGDGAY
NAHFGESIAS LDDLDNDGFP DVAIGAPKED DFAGAVYIYH GDAGGIVPQY SMKLSGQKIN
PVLRMFGQSI SGGIDMDGNG YPDVTVGAFM SDSVVLLRAR PVITVDVSIF LPGSINITAP
QCHDGQQPVN CLNVTTCFSF HGKHVPGEIG LNYVLMADVA KKEKGQMPRV YFVLLGETMG
QVTEKLQLTY MEETCRHYVA HVKRRVQDVI SPIVFEAAYS LSEHVTGEEE RELPPLTPVL
RWKKGQKIAQ KNQTVFERNC RSEDCAADLQ LQGKLLLSSM DEKTLYLALG AVKNISLNIS
ISNLGDDAYD ANVSFNVSRE LFFINMWQKE EMGISCELLE SDFLKCSVGF PFMRSKSKYE
FSVIFDTSHL SGEEEVLSFI VTAQSGNTER SESLHDNTLV LMVPLMHEVD TSITGIMSPT
SFVYGESVDA ANFIQLDDLE CHFQPINITL QVYNTGPSTL PGSSVSISFP NRLSSGGAEM
FHVQEMVVGQ EKGNCSFQKN PTPCIIPQEQ ENIFHTIFAF FTKSGRKVLD CEKPGISCLT
AHCNFSALAK EESRTIDIYM LLNTEILKKD SSSVIQFMSR AKVKVDPALR VVEIAHGNPE
EVTVVFEALH NLEPRGYVVG WIIAISLLVG ILIFLLLAVL LWKMGFFRRR YKEIIEAEKN
RKENEDSWDW VQKNQ
