LOCUS       NP_001028400            1179 aa            linear   ROD 31-DEC-2024
DEFINITION  integrin alpha-1 precursor [Mus musculus].
ACCESSION   NP_001028400 XP_913045 XP_925759 XP_925763 XP_925768
VERSION     NP_001028400.2
DBSOURCE    REFSEQ: accession NM_001033228.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 1179)
  AUTHORS   Ray,A.T. and Soriano,P.
  TITLE     FGF signaling regulates salivary gland branching morphogenesis by
            modulating cell adhesion
  JOURNAL   Development 150 (6) (2023)
   PUBMED   36861436
REFERENCE   2  (residues 1 to 1179)
  AUTHORS   Song,W., Li,Q., Wang,T., Li,Y., Fan,T., Zhang,J., Wang,Q., Pan,J.,
            Dong,Q., Sun,Z.S. and Wang,Y.
  TITLE     Putative complement control protein CSMD3 dysfunction impairs
            synaptogenesis and induces neurodevelopmental disorders
  JOURNAL   Brain Behav Immun 102, 237-250 (2022)
   PUBMED   35245678
REFERENCE   3  (residues 1 to 1179)
  AUTHORS   Eckert,I.N., Ribechini,E., Jarick,K.J., Strozniak,S., Potter,S.J.,
            Beilhack,A. and Lutz,M.B.
  TITLE     VLA-1 Binding to Collagen IV Controls Effector T Cell Suppression
            by Myeloid-Derived Suppressor Cells in the Splenic Red Pulp
  JOURNAL   Front Immunol 11, 616531 (2021)
   PUBMED   33584706
  REMARK    GeneRIF: VLA-1 Binding to Collagen IV Controls Effector T Cell
            Suppression by Myeloid-Derived Suppressor Cells in the Splenic Red
            Pulp.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1179)
  AUTHORS   Bromley,S.K., Akbaba,H., Mani,V., Mora-Buch,R., Chasse,A.Y.,
            Sama,A. and Luster,A.D.
  TITLE     CD49a Regulates Cutaneous Resident Memory CD8+ T Cell Persistence
            and Response
  JOURNAL   Cell Rep 32 (9), 108085 (2020)
   PUBMED   32877667
REFERENCE   5  (residues 1 to 1179)
  AUTHORS   Brignani,S., Raj,D.D.A., Schmidt,E.R.E., Dudukcu,O., Adolfs,Y., De
            Ruiter,A.A., Rybiczka-Tesulov,M., Verhagen,M.G., van der Meer,C.,
            Broekhoven,M.H., Moreno-Bravo,J.A., Grossouw,L.M., Dumontier,E.,
            Cloutier,J.F., Chedotal,A. and Pasterkamp,R.J.
  TITLE     Remotely Produced and Axon-Derived Netrin-1 Instructs GABAergic
            Neuron Migration and Dopaminergic Substantia Nigra Development
  JOURNAL   Neuron 107 (4), 684-702 (2020)
   PUBMED   32562661
REFERENCE   6  (residues 1 to 1179)
  AUTHORS   Shakibaei,M., Zimmermann,B. and Merker,H.J.
  TITLE     Changes in integrin expression during chondrogenesis in vitro: an
            immunomorphological study
  JOURNAL   J Histochem Cytochem 43 (10), 1061-1069 (1995)
   PUBMED   7560884
REFERENCE   7  (residues 1 to 1179)
  AUTHORS   Tarone,G., Russo,M.A., Hirsch,E., Odorisio,T., Altruda,F.,
            Silengo,L. and Siracusa,G.
  TITLE     Expression of beta 1 integrin complexes on the surface of
            unfertilized mouse oocyte
  JOURNAL   Development 117 (4), 1369-1375 (1993)
   PUBMED   7691492
REFERENCE   8  (residues 1 to 1179)
  AUTHORS   Morse,H.C. 3rd.
  TITLE     Genetic nomenclature for loci controlling surface antigens of mouse
            hemopoietic cells
  JOURNAL   J Immunol 149 (10), 3129-3134 (1992)
   PUBMED   1431091
  REMARK    Review article
            Erratum:[J Immunol 1993 Mar 15;150(6):2563]
REFERENCE   9  (residues 1 to 1179)
  AUTHORS   Douville,P., Seldin,M.F. and Carbonetto,S.
  TITLE     Genetic mapping of the integrin alpha 1 gene (Vla1) to mouse
            chromosome 13
  JOURNAL   Genomics 14 (2), 503-505 (1992)
   PUBMED   1427867
REFERENCE   10 (residues 1 to 1179)
  AUTHORS   Eicher,E.M. and Lee,B.K.
  TITLE     The NXSM recombinant inbred strains of mice: genetic profile for 58
            loci including the Mtv proviral loci
  JOURNAL   Genetics 125 (2), 431-446 (1990)
   PUBMED   2165966
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK035870.1, AK040830.1, AK053377.1 and AK033533.1.
            
            On Jul 25, 2007 this sequence version replaced NP_001028400.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK035870.1, SRR10223969.13192.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1179
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="13"
                     /map="13 64.61 cM"
     Protein         1..1179
                     /product="integrin alpha-1 precursor"
                     /note="VLA-1; laminin and collagen receptor; CD49
                     antigen-like family member A"
                     /calculated_mol_wt=127788
     sig_peptide     1..28
                     /note="/evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q3V3R4.2)"
                     /calculated_mol_wt=3041
     mat_peptide     29..1179
                     /product="Integrin alpha-1. /evidence=ECO:0000250.
                     /id=PRO_0000273722"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3V3R4.2)"
                     /calculated_mol_wt=127788
     Region          30..91
                     /region_name="FG-GAP 1.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00803"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3V3R4.2)"
     Site            100
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q3V3R4.2)"
     Region          101..160
                     /region_name="FG-GAP 2.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00803"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3V3R4.2)"
     Site            105
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q3V3R4.2)"
     Site            112
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q3V3R4.2)"
     Region          171..351
                     /region_name="vWA_integrins_alpha_subunit"
                     /note="Integrins are a class of adhesion receptors that
                     link the extracellular matrix to the cytoskeleton and
                     cooperate with growth factor receptors to promote celll
                     survival, cell cycle progression and cell migration.
                     Integrins consist of an alpha and a beta...; cd01469"
                     /db_xref="CDD:238746"
     Site            order(171,173,192,275,277,305,340)
                     /site_type="active"
                     /note="integrin inhibitor binding pocket [active]"
                     /db_xref="CDD:238746"
     Site            order(178,180,182,248,281)
                     /site_type="other"
                     /note="metal ion-dependent adhesion site (MIDAS)"
                     /db_xref="CDD:238746"
     Site            order(180..182,184,248)
                     /site_type="active"
                     /note="integrin-collagen binding site [active]"
                     /db_xref="CDD:238746"
     Site            217
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q3V3R4.2)"
     Site            317
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q3V3R4.2)"
     Site            341
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q3V3R4.2)"
     Region          365..417
                     /region_name="FG-GAP 3.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00803"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3V3R4.2)"
     Site            402
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q3V3R4.2)"
     Site            418
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q3V3R4.2)"
     Region          422..474
                     /region_name="FG-GAP 4.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00803"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3V3R4.2)"
     Site            459
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q3V3R4.2)"
     Region          475..537
                     /region_name="FG-GAP 5.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00803"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3V3R4.2)"
     Region          485..>528
                     /region_name="Int_alpha"
                     /note="Integrin alpha (beta-propellor repeats);
                     smart00191"
                     /db_xref="CDD:214549"
     Site            531
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q3V3R4.2)"
     Region          556..614
                     /region_name="FG-GAP 6.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00803"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3V3R4.2)"
     Region          567..620
                     /region_name="Int_alpha"
                     /note="Integrin alpha (beta-propellor repeats);
                     smart00191"
                     /db_xref="CDD:214549"
     Region          618..678
                     /region_name="FG-GAP 7.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00803"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3V3R4.2)"
     Region          664..1044
                     /region_name="Integrin_alpha2"
                     /note="Integrin alpha; pfam08441"
                     /db_xref="CDD:462478"
     Site            698
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q3V3R4.2)"
     Site            747
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q3V3R4.2)"
     Site            779
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q3V3R4.2)"
     Site            839
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q3V3R4.2)"
     Site            882
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q3V3R4.2)"
     Site            907
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q3V3R4.2)"
     Site            938
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q3V3R4.2)"
     Site            965
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q3V3R4.2)"
     Site            973
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q3V3R4.2)"
     Site            1007
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q3V3R4.2)"
     Site            1083
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q3V3R4.2)"
     Site            1102
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q3V3R4.2)"
     Site            1113
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q3V3R4.2)"
     Site            1142..1164
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3V3R4.2)"
     Region          1167..1171
                     /region_name="GFFKR motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3V3R4.2)"
     CDS             1..1179
                     /gene="Itga1"
                     /gene_synonym="CD49A; E130012M19Rik; Vla1"
                     /coded_by="NM_001033228.3:434..3973"
                     /db_xref="CCDS:CCDS36788.1"
                     /db_xref="GeneID:109700"
                     /db_xref="MGI:MGI:96599"
ORIGIN      
        1 mvprrpasle vtvaciwllt vilgvcisfn vdvknsmsfs gpvedmfgyt vqqyeneegk
       61 wvligsplvg qpkartgdvy kcpvgrersm pcvkldlpvn tsipnvteik enmtfgstlv
      121 tnpkggflac gplyayrcgh lhyttgicsd vsptfqvvns fapvqecstq ldivivldgs
      181 nsiypwesvt aflndllkrm digpkqtqvg ivqyganvth efnlnkysst eevlvaanki
      241 grrgglqtmt algidtarke afteargarr gvkkvmvivt dgeshdnyrl kqviqdcede
      301 niqrfsiail ghynrgnlst ekfveeiksi aseptekhff nvsdelalvt ivkalgerif
      361 aleatadqsa asfememsqt gfsahysqdw vmlgavgayd wngtvvmqka nqiviphntt
      421 fqteptkmne plasylgytv nsatipgdvl yiagqprynh tgqvviykme dgdvnilqtl
      481 sgeqigsyfg svlttididk dsytdlllvg apmymgteke eqgkvyvyav nqtrfeyqms
      541 lepikqtccs slkdnsctke nknepcgarf gtavaavkdl nvdgfndvvi gapleddhag
      601 avyiyhgsgk tirkeyaqri psggdgktlk ffgqsihgem dlngdgltdv tigglggaal
      661 fwardvavvk vtmnfepnkv niqkkncrve gketvcinat mcfhvklksk edsvyeadlq
      721 yrvtldslrq isrsffsgtq erriqrnltv resecirhsf ymldkhdfqd svrvtldfnl
      781 tdpengpvld dalpnsvhgh ipfakdcgnk ercvsdltld vstteknlli vrsqndkfnv
      841 sltvknkgds ayntrtvvqy spnlifsgie eiqkdscesn qnitcrvgyp flrtgdvvnf
      901 kiifqfntsh lsenaiihls atsdseeple slydnevnis ipvkyevglq fyssasehhi
      961 svaanetvpe linstkdigd einvfytirk rghfpmpelr laisfpnlts dgypvlyptg
     1021 wsssdnvncr prsledplgi nsgkkmtisk sevlkrgtiq dcstckiati tchllpsdvs
     1081 qvnvslilwk ptfikahfss lnltirgelq senssltlss snrkrelaiq iskdglpgrv
     1141 plwvillsaf agllllmlli lalwkigffk rplkkkmek
//
