ITA1_RAT
ID ITA1_RAT Reviewed; 1180 AA.
AC P18614;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Integrin alpha-1;
DE AltName: Full=CD49 antigen-like family member A;
DE AltName: Full=Laminin and collagen receptor;
DE AltName: Full=VLA-1;
DE AltName: CD_antigen=CD49a;
DE Flags: Precursor;
GN Name=Itga1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2380249; DOI=10.1083/jcb.111.2.709;
RA Ignatius M.J., Large T.H., Houde M., Tawil J.W., Barton A., Esch F.,
RA Carbonetto S., Reichardt L.F.;
RT "Molecular cloning of the rat integrin alpha 1-subunit: a receptor for
RT laminin and collagen.";
RL J. Cell Biol. 111:709-720(1990).
RN [2]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-418, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24090084; DOI=10.1021/pr400783j;
RA Parker B.L., Thaysen-Andersen M., Solis N., Scott N.E., Larsen M.R.,
RA Graham M.E., Packer N.H., Cordwell S.J.;
RT "Site-specific glycan-peptide analysis for determination of N-glycoproteome
RT heterogeneity.";
RL J. Proteome Res. 12:5791-5800(2013).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 151-364.
RX PubMed=10386626; DOI=10.1016/s0014-5793(99)00666-3;
RA Nolte M., Pepinsky R.B., Venyaminov S.Y., Koteliansky V., Gotwals P.J.,
RA Karpusas M.;
RT "Crystal structure of the alpha1beta1 integrin I-domain: insights into
RT integrin I-domain function.";
RL FEBS Lett. 452:379-385(1999).
CC -!- FUNCTION: Integrin alpha-1/beta-1 is a receptor for laminin and
CC collagen. It recognizes the proline-hydroxylated sequence G-F-P-G-E-R
CC in collagen. Involved in anchorage-dependent, negative regulation of
CC EGF-stimulated cell growth (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Alpha-1 associates
CC with beta-1 (By similarity). Interacts with RAB21 (By similarity).
CC Interacts (via cytoplasmic domain) with PTPN2; activates PTPN2
CC phosphatase activity towards EGFR and negatively regulates EGF
CC signaling (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- DOMAIN: The integrin I-domain (insert) is a VWFA domain. Integrins with
CC I-domains do not undergo protease cleavage.
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; X52140; CAA36384.1; -; mRNA.
DR PIR; A35854; A35854.
DR RefSeq; NP_112256.1; NM_030994.2.
DR PDB; 1CK4; X-ray; 2.20 A; A/B=167-364.
DR PDB; 1MHP; X-ray; 2.80 A; A/B=169-360.
DR PDB; 2B2X; X-ray; 2.20 A; A/B=151-364.
DR PDBsum; 1CK4; -.
DR PDBsum; 1MHP; -.
DR PDBsum; 2B2X; -.
DR AlphaFoldDB; P18614; -.
DR BMRB; P18614; -.
DR SMR; P18614; -.
DR CORUM; P18614; -.
DR IntAct; P18614; 2.
DR STRING; 10116.ENSRNOP00000016353; -.
DR GlyGen; P18614; 24 sites, 3 N-linked glycans (2 sites).
DR iPTMnet; P18614; -.
DR PhosphoSitePlus; P18614; -.
DR jPOST; P18614; -.
DR PaxDb; P18614; -.
DR PRIDE; P18614; -.
DR Ensembl; ENSRNOT00000106157; ENSRNOP00000086956; ENSRNOG00000053550.
DR GeneID; 25118; -.
DR KEGG; rno:25118; -.
DR CTD; 3672; -.
DR RGD; 2923; Itga1.
DR eggNOG; KOG3637; Eukaryota.
DR GeneTree; ENSGT00940000157646; -.
DR HOGENOM; CLU_004111_2_1_1; -.
DR InParanoid; P18614; -.
DR OMA; THTFLAI; -.
DR OrthoDB; 66046at2759; -.
DR PhylomeDB; P18614; -.
DR Reactome; R-RNO-216083; Integrin cell surface interactions.
DR Reactome; R-RNO-445355; Smooth Muscle Contraction.
DR EvolutionaryTrace; P18614; -.
DR PRO; PR:P18614; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000053550; Expressed in adult mammalian kidney and 18 other tissues.
DR Genevisible; P18614; RN.
DR GO; GO:0001669; C:acrosomal vesicle; IDA:RGD.
DR GO; GO:0045178; C:basal part of cell; ISO:RGD.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:RGD.
DR GO; GO:0005925; C:focal adhesion; ISO:RGD.
DR GO; GO:0034665; C:integrin alpha1-beta1 complex; ISO:RGD.
DR GO; GO:0008305; C:integrin complex; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0045121; C:membrane raft; IDA:RGD.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0043204; C:perikaryon; IDA:RGD.
DR GO; GO:0005518; F:collagen binding; IMP:RGD.
DR GO; GO:0098639; F:collagen binding involved in cell-matrix adhesion; ISO:RGD.
DR GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019903; F:protein phosphatase binding; ISO:RGD.
DR GO; GO:0005102; F:signaling receptor binding; IPI:RGD.
DR GO; GO:0007155; P:cell adhesion; ISO:RGD.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; IBA:GO_Central.
DR GO; GO:0060326; P:cell chemotaxis; IMP:RGD.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0007160; P:cell-matrix adhesion; ISO:RGD.
DR GO; GO:0045123; P:cellular extravasation; ISO:RGD.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0048812; P:neuron projection morphogenesis; IMP:RGD.
DR GO; GO:0030593; P:neutrophil chemotaxis; ISO:RGD.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IMP:RGD.
DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; IMP:RGD.
DR GO; GO:0032516; P:positive regulation of phosphoprotein phosphatase activity; ISS:UniProtKB.
DR GO; GO:0042311; P:vasodilation; IMP:RGD.
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; IPR018184; Integrin_alpha_C_CS.
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 SUPFAM; SSF69318; SSF69318; 1.
DR PROSITE; PS51470; FG_GAP; 7.
DR PROSITE; PS00242; INTEGRIN_ALPHA; 1.
DR PROSITE; PS50234; VWFA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cell adhesion; Disulfide bond; Glycoprotein;
KW Integrin; Magnesium; Membrane; Metal-binding; Receptor; Reference proteome;
KW Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..28
FT CHAIN 29..1180
FT /note="Integrin alpha-1"
FT /id="PRO_0000016231"
FT TOPO_DOM 29..1142
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1143..1165
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1166..1180
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 30..91
FT /note="FG-GAP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 101..160
FT /note="FG-GAP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT DOMAIN 175..364
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT REPEAT 365..417
FT /note="FG-GAP 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 422..474
FT /note="FG-GAP 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 475..537
FT /note="FG-GAP 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 556..614
FT /note="FG-GAP 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 618..678
FT /note="FG-GAP 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT MOTIF 1168..1172
FT /note="GFFKR motif"
FT BINDING 497
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 499
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 501
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 505
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 579
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 581
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 583
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 587
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 641
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 643
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 645
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 649
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 217
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 317
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 341
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 402
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 418
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PubMed:24090084"
FT CARBOHYD 459
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 531
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 698
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 747
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 779
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 820
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 839
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 882
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 907
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 938
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 965
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 973
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1007
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1084
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 82..92
FT /evidence="ECO:0000250"
FT DISULFID 687..696
FT /evidence="ECO:0000250"
FT DISULFID 702..755
FT /evidence="ECO:0000250"
FT DISULFID 807..813
FT /evidence="ECO:0000250"
FT DISULFID 877..885
FT /evidence="ECO:0000250"
FT DISULFID 1029..1062
FT /evidence="ECO:0000250"
FT DISULFID 1066..1073
FT /evidence="ECO:0000250"
FT STRAND 171..178
FT /evidence="ECO:0007829|PDB:1CK4"
FT HELIX 186..197
FT /evidence="ECO:0007829|PDB:1CK4"
FT STRAND 208..222
FT /evidence="ECO:0007829|PDB:1CK4"
FT TURN 224..226
FT /evidence="ECO:0007829|PDB:1CK4"
FT HELIX 230..238
FT /evidence="ECO:0007829|PDB:1CK4"
FT HELIX 250..259
FT /evidence="ECO:0007829|PDB:1CK4"
FT TURN 260..262
FT /evidence="ECO:0007829|PDB:1MHP"
FT HELIX 264..266
FT /evidence="ECO:0007829|PDB:1CK4"
FT STRAND 273..282
FT /evidence="ECO:0007829|PDB:1CK4"
FT HELIX 287..289
FT /evidence="ECO:0007829|PDB:1CK4"
FT HELIX 290..299
FT /evidence="ECO:0007829|PDB:1CK4"
FT STRAND 302..309
FT /evidence="ECO:0007829|PDB:1CK4"
FT HELIX 311..315
FT /evidence="ECO:0007829|PDB:1CK4"
FT HELIX 321..328
FT /evidence="ECO:0007829|PDB:1CK4"
FT HELIX 335..338
FT /evidence="ECO:0007829|PDB:1CK4"
FT STRAND 339..345
FT /evidence="ECO:0007829|PDB:1CK4"
FT HELIX 346..350
FT /evidence="ECO:0007829|PDB:1CK4"
FT HELIX 352..359
FT /evidence="ECO:0007829|PDB:1CK4"
SQ SEQUENCE 1180 AA; 130809 MW; 8E5DA2BE02362EE4 CRC64;
MVPRRPASLE VTVACIWLLT VILGFCVSFN VDVKNSMSFS GPVEDMFGYT VQQYENEEGK
WVLIGSPLVG QPKARTGDVY KCPVGRERAM PCVKLDLPVN TSIPNVTEIK ENMTFGSTLV
TNPNGGFLAC GPLYAYRCGH LHYTTGICSD VSPTFQVVNS FAPVQECSTQ LDIVIVLDGS
NSIYPWESVI AFLNDLLKRM DIGPKQTQVG IVQYGENVTH EFNLNKYSST EEVLVAANKI
GRQGGLQTMT ALGIDTARKE AFTEARGARR GVKKVMVIVT DGESHDNYRL KQVIQDCEDE
NIQRFSIAIL GHYNRGNLST EKFVEEIKSI ASEPTEKHFF NVSDELALVT IVKALGERIF
ALEATADQSA ASFEMEMSQT GFSAHYSQDW VMLGAVGAYD WNGTVVMQKA NQMVIPHNTT
FQTEPAKMNE PLASYLGYTV NSATIPGDVL YIAGQPRYNH TGQVVIYKME DGNINILQTL
GGEQIGSYFG SVLTTIDIDK DSYTDLLLVG APMYMGTEKE EQGKVYVYAV NQTRFEYQMS
LEPIRQTCCS SLKDNSCTKE NKNEPCGARF GTAIAAVKDL NVDGFNDVVI GAPLEDDHAG
AVYIYHGSGK TIREAYAQRI PSGGDGKTLK FFGQSIHGEM DLNGDGLTDV TIGGLGGAAL
FWARDVAVVK VTMNFEPNKV NIQKKNCRVE GKETVCINAT MCFHVKLKSK EDSIYEADLQ
YRVTLDSLRQ ISRSFFSGTQ ERKIQRNITV RESECIRHSF YMLDKHDFQD SVRVTLDFNL
TDPENGPVLD DALPNSVHEH IPFAKDCGNK ERCISDLTLN VSTTEKSLLI VKSQHDKFNV
SLTVKNKGDS AYNTRTVVQH SPNLIFSGIE EIQKDSCESN QNITCRVGYP FLRAGETVTF
KIIFQFNTSH LSENAIIHLS ATSDSEEPLE SLNDNEVNIS IPVKYEVGLQ FYSSASEHHI
SVAANETIPE FINSTEDIGN EINVFYTIRK RGHFPMPELQ LSISFPNLTA DGYPVLYPIG
WSSSDNVNCR PRSLEDPFGI NSGKKMTISK SEVLKRGTIQ DCSSTCGVAT ITCSLLPSDL
SQVNVSLLLW KPTFIRAHFS SLNLTLRGEL KSENSSLTLS SSNRKRELAI QISKDGLPGR
VPLWVILLSA FAGLLLLMLL ILALWKIGFF KRPLKKKMEK
