LOCUS       NP_034707               1053 aa            linear   ROD 25-APR-2025
DEFINITION  integrin alpha-5 isoform 1 preproprotein [Mus musculus].
ACCESSION   NP_034707
VERSION     NP_034707.5
DBSOURCE    REFSEQ: accession NM_010577.4
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 1053)
  AUTHORS   Zouaghi,Y., Alpern,D., Gardeux,V., Russeil,J., Deplancke,B.,
            Santoni,F., Pitteloud,N. and Messina,A.
  TITLE     Transcriptomic profiling of murine GnRH neurons reveals
            developmental trajectories linked to human reproduction and
            infertility
  JOURNAL   Theranostics 15 (8), 3673-3692 (2025)
   PUBMED   40093908
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1053)
  AUTHORS   Arriagada,C., Lin,E., Schonning,M. and Astrof,S.
  TITLE     Mesodermal fibronectin controls cell shape, polarity, and
            mechanotransduction in the second heart field during cardiac
            outflow tract development
  JOURNAL   Dev Cell 60 (1), 62-84 (2025)
   PUBMED   39413783
REFERENCE   3  (residues 1 to 1053)
  AUTHORS   Ezzo,M., Spindler,K., Wang,J.B., Lee,D., Pecoraro,G., Cowen,J.,
            Pakshir,P. and Hinz,B.
  TITLE     Acute contact with profibrotic macrophages mechanically activates
            fibroblasts via alphavbeta3 integrin-mediated engagement of Piezo1
  JOURNAL   Sci Adv 10 (43), eadp4726 (2024)
   PUBMED   39441936
  REMARK    GeneRIF: Acute contact with profibrotic macrophages mechanically
            activates fibroblasts via alphavbeta3 integrin-mediated engagement
            of Piezo1.
REFERENCE   4  (residues 1 to 1053)
  AUTHORS   Miao,L., Lu,Y., Nusrat,A., Zhao,L., Castillo,M., Xiao,Y., Guo,H.,
            Liu,Y., Gunaratne,P., Schwartz,R.J., Burns,A.R., Kumar,A.,
            DiPersio,C.M. and Wu,M.
  TITLE     beta1 integrins regulate cellular behaviour and cardiomyocyte
            organization during ventricular wall formation
  JOURNAL   Cardiovasc Res 120 (11), 1279-1294 (2024)
   PUBMED   38794925
REFERENCE   5  (residues 1 to 1053)
  AUTHORS   Wang,X., Zhang,Y., Chi,K., Ji,Y., Zhang,K., Li,P., Fu,Z., Wang,X.,
            Cui,S., Shen,W., Cai,G., Chen,X., Zhu,H. and Hong,Q.
  TITLE     IGFBP2 induces podocyte apoptosis promoted by mitochondrial damage
            via integrin alpha5/FAK in diabetic kidney disease
  JOURNAL   Apoptosis 29 (7-8), 1109-1125 (2024)
   PUBMED   38796567
  REMARK    GeneRIF: IGFBP2 induces podocyte apoptosis promoted by
            mitochondrial damage via integrin alpha5/FAK in diabetic kidney
            disease.
REFERENCE   6  (residues 1 to 1053)
  AUTHORS   Watt,F.M. and Hodivala,K.J.
  TITLE     Cell adhesion. Fibronectin and integrin knockouts come unstuck
  JOURNAL   Curr Biol 4 (3), 270-272 (1994)
   PUBMED   7522915
  REMARK    Review article
REFERENCE   7  (residues 1 to 1053)
  AUTHORS   Yang,J.T., Rayburn,H. and Hynes,R.O.
  TITLE     Embryonic mesodermal defects in alpha 5 integrin-deficient mice
  JOURNAL   Development 119 (4), 1093-1105 (1993)
   PUBMED   7508365
REFERENCE   8  (residues 1 to 1053)
  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 1053)
  AUTHORS   Brannan,C.I., Gilbert,D.J., Ceci,J.D., Matsuda,Y., Chapman,V.M.,
            Mercer,J.A., Eisen,H., Johnston,L.A., Copeland,N.G. and
            Jenkins,N.A.
  TITLE     An interspecific linkage map of mouse chromosome 15 positioned with
            respect to the centromere
  JOURNAL   Genomics 13 (4), 1075-1081 (1992)
   PUBMED   1354638
REFERENCE   10 (residues 1 to 1053)
  AUTHORS   Holers,V.M., Ruff,T.G., Parks,D.L., McDonald,J.A., Ballard,L.L. and
            Brown,E.J.
  TITLE     Molecular cloning of a murine fibronectin receptor and its
            expression during inflammation. Expression of VLA-5 is increased in
            activated peritoneal macrophages in a manner discordant from major
            histocompatibility complex class II
  JOURNAL   J Exp Med 169 (5), 1589-1605 (1989)
   PUBMED   2523953
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC131721.4, BC050943.1 and
            AK142241.1.
            
            On Apr 19, 2016 this sequence version replaced NP_034707.4.
            
            Summary: The product of this gene belongs to the integrin alpha
            chain family. Integrins are heterodimeric integral membrane
            proteins composed of an alpha chain and a beta chain. This gene
            encodes the integrin alpha 5 chain, which is proteolytically
            processed to generate light and heavy chains that join with beta 1
            to form a fibronectin receptor. In addition to adhesion, integrins
            are known to participate in cell-surface mediated signaling.
            Integrin alpha 5 and integrin alpha V chains are produced by
            distinct genes. Homozygous knockout mice for this gene exhibit
            embryonic lethality. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Sep 2015].
            
            Transcript Variant: This variant (1) represents the shorter
            transcript and encodes the longer isoform (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 :: BC059829.1, AK142241.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164134 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            RefSeq Select criteria           :: based on conservation,
                                                expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1053
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="15"
                     /map="15 58.9 cM"
     Protein         1..1053
                     /product="integrin alpha-5 isoform 1 preproprotein"
                     /note="integrin alpha-5; integrin alpha-F; CD49
                     antigen-like family member E; fibronectin receptor subunit
                     alpha; fibronectin receptor alpha polypeptide"
                     /calculated_mol_wt=110119
     sig_peptide     1..44
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=4943
     mat_peptide     45..1053
                     /product="Integrin alpha-5. /id=PRO_0000016252"
                     /note="propagated from UniProtKB/Swiss-Prot (P11688.3)"
                     /calculated_mol_wt=110119
     mat_peptide     45..898
                     /product="Integrin alpha-5 heavy chain.
                     /id=PRO_0000016253"
                     /note="propagated from UniProtKB/Swiss-Prot (P11688.3)"
                     /calculated_mol_wt=92553
     Region          46..111
                     /region_name="FG-GAP 1.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00803"
                     /note="propagated from UniProtKB/Swiss-Prot (P11688.3)"
     Region          59..117
                     /region_name="Int_alpha"
                     /note="Integrin alpha (beta-propellor repeats);
                     smart00191"
                     /db_xref="CDD:214549"
     Site            87
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P11688.3)"
     Site            130
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P08648; propagated from
                     UniProtKB/Swiss-Prot (P11688.3)"
     Region          131..191
                     /region_name="FG-GAP 2.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00803"
                     /note="propagated from UniProtKB/Swiss-Prot (P11688.3)"
     Site            185
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19349973; propagated from
                     UniProtKB/Swiss-Prot (P11688.3)"
     Region          196..248
                     /region_name="FG-GAP 3.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00803"
                     /note="propagated from UniProtKB/Swiss-Prot (P11688.3)"
     Region          262..314
                     /region_name="FG-GAP 4.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00803"
                     /note="propagated from UniProtKB/Swiss-Prot (P11688.3)"
     Region          271..>313
                     /region_name="Int_alpha"
                     /note="Integrin alpha (beta-propellor repeats);
                     smart00191"
                     /db_xref="CDD:214549"
     Site            300
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19656770; propagated from
                     UniProtKB/Swiss-Prot (P11688.3)"
     Site            310
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19656770; propagated from
                     UniProtKB/Swiss-Prot (P11688.3)"
     Region          315..380
                     /region_name="FG-GAP 5.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00803"
                     /note="propagated from UniProtKB/Swiss-Prot (P11688.3)"
     Site            319
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P11688.3)"
     Region          325..382
                     /region_name="Int_alpha"
                     /note="Integrin alpha (beta-propellor repeats);
                     smart00191"
                     /db_xref="CDD:214549"
     Region          381..440
                     /region_name="FG-GAP 6.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00803"
                     /note="propagated from UniProtKB/Swiss-Prot (P11688.3)"
     Region          392..446
                     /region_name="Int_alpha"
                     /note="Integrin alpha (beta-propellor repeats);
                     smart00191"
                     /db_xref="CDD:214549"
     Region          444..507
                     /region_name="FG-GAP 7.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00803"
                     /note="propagated from UniProtKB/Swiss-Prot (P11688.3)"
     Region          458..510
                     /region_name="Int_alpha"
                     /note="Integrin alpha (beta-propellor repeats);
                     smart00191"
                     /db_xref="CDD:214549"
     Region          493..925
                     /region_name="Integrin_alpha2"
                     /note="Integrin alpha; pfam08441"
                     /db_xref="CDD:462478"
     Site            527
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P11688.3)"
     Site            533
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P11688.3)"
     Site            596
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19349973,
                     ECO:0000269|PubMed:19656770; propagated from
                     UniProtKB/Swiss-Prot (P11688.3)"
     Site            612
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19349973,
                     ECO:0000269|PubMed:19656770; propagated from
                     UniProtKB/Swiss-Prot (P11688.3)"
     Site            678
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19349973,
                     ECO:0000269|PubMed:19656770; propagated from
                     UniProtKB/Swiss-Prot (P11688.3)"
     Site            715
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19349973; propagated from
                     UniProtKB/Swiss-Prot (P11688.3)"
     Site            727
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19349973; propagated from
                     UniProtKB/Swiss-Prot (P11688.3)"
     Site            776
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P11688.3)"
     Site            872
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P11688.3)"
     Region          879..910
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P11688.3)"
     mat_peptide     899..1053
                     /product="Integrin alpha-5 light chain.
                     /id=PRO_0000016254"
                     /note="propagated from UniProtKB/Swiss-Prot (P11688.3)"
                     /calculated_mol_wt=17584
     Site            1000..1025
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P11688.3)"
     Region          1024..1028
                     /region_name="GFFKR motif. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (P11688.3)"
     Region          1025..1032
                     /region_name="Interaction with HPS5.
                     /evidence=ECO:0000250|UniProtKB:P08648"
                     /note="propagated from UniProtKB/Swiss-Prot (P11688.3)"
     CDS             1..1053
                     /gene="Itga5"
                     /gene_synonym="Cd49e; Fnra; VLA5"
                     /coded_by="NM_010577.4:266..3427"
                     /note="isoform 1 preproprotein is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS27903.1"
                     /db_xref="GeneID:16402"
                     /db_xref="MGI:MGI:96604"
ORIGIN      
        1 mgswtprspr splhavllrw gprrlppllp lllllwpppl qvggfnldae apavlsgppg
       61 slfgfsvefy rpgrdgvsvl vgapkantsq pgvlqggavy vcpwgtspiq cttiqfdskg
      121 srilesslys akgeepveyk slqwfgatvr ahgssilaca plyswrtekd pqndpvgtcy
      181 lstenftril eyapcrsdfg saagqgycqg gfsaeftktg rvvlggpgsy fwqgqilsat
      241 qeqisesyyp eylinpvqgq lqtrqassvy ddsylgysva vgefsgddte dfvagvpkgn
      301 ltygyvtvln gsdihslynv sgeqmasyfg yavaatdtng dglddllvga pllmertadg
      361 rpqevgrvyi ylqrpagidp tptltltgqd efsrfgsslt plgdldqdgy ndvaigapfg
      421 geaqqgvvfi fpggpgglst kpsqvlqplw aagrtpdffg salrggrdld gngypdlivg
      481 sfgvdkalvy rgrpiisasa sltifpsmfn peerscsleg npvscinlsf clnasgkhvp
      541 nsigfevelq ldwqkqkggv rralfltskq atltqtlliq ngaredcrem kiylrnesef
      601 rdklspihia lnfsldpkap mdshglrpvl hyqsksried kaqilldcge dnicvpdlql
      661 dvygekkhvy lgdknalnlt fhaqnlgegg ayeaelrvta pleaeysglv rhpgnfssls
      721 cdyfavnqsr qlvcdlgnpm kagtslwggl rftvphlqdt kktiqfdfqi lsknlnnsqs
      781 nvvsfplsve aqaqvslngv skpeavifpv sdwnpqdqpq keedlgpavh hvyelinqgp
      841 ssisqgvlel scpqalegqq llyvtkvtgl snctsnytpn sqgleldpet sphhlqkrea
      901 pgrsstasgt qvlkcpeakc frlrcefgpl hrqesrslql hfrvwaktfl qreyqpfslq
      961 ceavyealkm pyqilprqlp qkklqvatav qwtkaegsng vplwiiilai lfgllllgll
     1021 iyvlyklgff krslpygtam ekaqlkppat sda
//
