LOCUS       NP_034811               1816 aa            linear   ROD 14-JAN-2025
DEFINITION  laminin subunit alpha-4 precursor [Mus musculus].
ACCESSION   NP_034811 XP_125563
VERSION     NP_034811.2
DBSOURCE    REFSEQ: accession NM_010681.4
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 1816)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 1816)
  AUTHORS   Sandhow,L., Cai,H., Leonard,E., Xiao,P., Tomaipitinca,L.,
            Mansson,A., Kondo,M., Sun,X., Johansson,A.S., Tryggvason,K.,
            Kasper,M., Jaras,M. and Qian,H.
  TITLE     Skin mesenchymal niches maintain and protect AML-initiating stem
            cells
  JOURNAL   J Exp Med 220 (10) (2023)
   PUBMED   37516911
REFERENCE   3  (residues 1 to 1816)
  AUTHORS   Feng,J., Han,X., Yuan,Y., Cho,C.K., Janeckova,E., Guo,T.,
            Pareek,S., Rahman,M.S., Zheng,B., Bi,J., Jing,J., Zhang,M., Xu,J.,
            Ho,T.V. and Chai,Y.
  TITLE     TGF-beta signaling and Creb5 cooperatively regulate Fgf18 to
            control pharyngeal muscle development
  JOURNAL   Elife 11, e80405 (2022)
   PUBMED   36542062
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1816)
  AUTHORS   Ramadan,R., Wouters,V.M., van Neerven,S.M., de Groot,N.E.,
            Garcia,T.M., Muncan,V., Franklin,O.D., Battle,M., Carlson,K.S.,
            Leach,J., Sansom,O.J., Boulard,O., Chamaillard,M., Vermeulen,L.,
            Medema,J.P. and Huels,D.J.
  TITLE     The extracellular matrix controls stem cell specification and crypt
            morphology in the developing and adult mouse gut
  JOURNAL   Biol Open 11 (12) (2022)
   PUBMED   36350252
REFERENCE   5  (residues 1 to 1816)
  AUTHORS   Hazra,R., Brine,L., Garcia,L., Benz,B., Chirathivat,N., Shen,M.M.,
            Wilkinson,J.E., Lyons,S.K. and Spector,D.L.
  TITLE     Platr4 is an early embryonic lncRNA that exerts its function
            downstream on cardiogenic mesodermal lineage commitment
  JOURNAL   Dev Cell 57 (21), 2450-2468 (2022)
   PUBMED   36347239
REFERENCE   6  (residues 1 to 1816)
  AUTHORS   Frieser,M., Nockel,H., Pausch,F., Roder,C., Hahn,A., Deutzmann,R.
            and Sorokin,L.M.
  TITLE     Cloning of the mouse laminin alpha 4 cDNA. Expression in a subset
            of endothelium
  JOURNAL   Eur J Biochem 246 (3), 727-735 (1997)
   PUBMED   9219532
REFERENCE   7  (residues 1 to 1816)
  AUTHORS   Miner,J.H., Patton,B.L., Lentz,S.I., Gilbert,D.J., Snider,W.D.,
            Jenkins,N.A., Copeland,N.G. and Sanes,J.R.
  TITLE     The laminin alpha chains: expression, developmental transitions,
            and chromosomal locations of alpha1-5, identification of
            heterotrimeric laminins 8-11, and cloning of a novel alpha3 isoform
  JOURNAL   J Cell Biol 137 (3), 685-701 (1997)
   PUBMED   9151674
REFERENCE   8  (residues 1 to 1816)
  AUTHORS   Hirohata,S., Kusachi,S., Kondo,J., Sano,I., Murakami,M., Doi,M.,
            Ninomiya,Y. and Tsuji,T.
  TITLE     Laminin alpha 1, alpha 2, alpha 4 and beta 1 chain mRNA expression
            in mouse embryonic, neonatal, and adult hearts
  JOURNAL   Jpn Heart J 38 (2), 281-289 (1997)
   PUBMED   9201115
REFERENCE   9  (residues 1 to 1816)
  AUTHORS   Lentz,S.I., Miner,J.H., Sanes,J.R. and Snider,W.D.
  TITLE     Distribution of the ten known laminin chains in the pathways and
            targets of developing sensory axons
  JOURNAL   J Comp Neurol 378 (4), 547-561 (1997)
   PUBMED   9034910
REFERENCE   10 (residues 1 to 1816)
  AUTHORS   Liu,J. and Mayne,R.
  TITLE     The complete cDNA coding sequence and tissue-specific expression of
            the mouse laminin alpha 4 chain
  JOURNAL   Matrix Biol 15 (6), 433-437 (1996)
   PUBMED   9049981
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC118224.8, BC115942.1 and AC153958.2.
            
            On Jun 10, 2007 this sequence version replaced NP_034811.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            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 :: BC115942.1, U59865.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1816
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="10"
                     /map="10 20.02 cM"
     Protein         1..1816
                     /product="laminin subunit alpha-4 precursor"
                     /note="laminin subunit alpha-4; laminin-8 subunit alpha;
                     laminin-9 subunit alpha; laminin-14 subunit alpha; laminin
                     [a]4"
                     /calculated_mol_wt=199166
     sig_peptide     1..24
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2672
     mat_peptide     25..1816
                     /product="Laminin subunit alpha-4. /id=PRO_0000017061"
                     /note="propagated from UniProtKB/Swiss-Prot (P97927.2)"
                     /calculated_mol_wt=199166
     Site            39
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000250|UniProtKB:Q16363; propagated from
                     UniProtKB/Swiss-Prot (P97927.2)"
     Region          81..130
                     /region_name="EGF_Lam"
                     /note="Laminin-type epidermal growth factor-like domain;
                     laminins are the major noncollagenous components of
                     basement membranes that mediate cell adhesion, growth
                     migration, and differentiation; the laminin-type epidermal
                     growth factor-like module occurs in...; cd00055"
                     /db_xref="CDD:238012"
     Site            order(82,84,91,98,101,110)
                     /site_type="active"
                     /note="EGF-like motif [active]"
                     /db_xref="CDD:238012"
     Site            104
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P97927.2)"
     Region          131..185
                     /region_name="EGF_Lam"
                     /note="Laminin-type epidermal growth factor-like domain;
                     laminins are the major noncollagenous components of
                     basement membranes that mediate cell adhesion, growth
                     migration, and differentiation; the laminin-type epidermal
                     growth factor-like module occurs in...; cd00055"
                     /db_xref="CDD:238012"
     Site            order(132,134,146,155,157,166)
                     /site_type="active"
                     /note="EGF-like motif [active]"
                     /db_xref="CDD:238012"
     Region          187..238
                     /region_name="EGF_Lam"
                     /note="Laminin-type epidermal growth factor-like domain;
                     laminins are the major noncollagenous components of
                     basement membranes that mediate cell adhesion, growth
                     migration, and differentiation; the laminin-type epidermal
                     growth factor-like module occurs in...; cd00055"
                     /db_xref="CDD:238012"
     Site            order(187,189,202,209,212,221)
                     /site_type="active"
                     /note="EGF-like motif [active]"
                     /db_xref="CDD:238012"
     Site            215
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P97927.2)"
     Region          256..825
                     /region_name="Domain II and I"
                     /note="propagated from UniProtKB/Swiss-Prot (P97927.2)"
     Region          291..547
                     /region_name="Laminin_I"
                     /note="Laminin Domain I; pfam06008"
                     /db_xref="CDD:310534"
     Site            308
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P97927.2)"
     Site            333
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P97927.2)"
     Region          <432..>716
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Site            458
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P97927.2)"
     Site            550
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P97927.2)"
     Site            571
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P97927.2)"
     Site            574
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P97927.2)"
     Site            631
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P97927.2)"
     Site            639
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P97927.2)"
     Region          717..719
                     /region_name="Cell attachment site. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P97927.2)"
     Region          727..854
                     /region_name="Laminin_II"
                     /note="Laminin Domain II; pfam06009"
                     /db_xref="CDD:368703"
     Site            735
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P97927.2)"
     Site            751
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P97927.2)"
     Site            754
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P97927.2)"
     Site            780
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P97927.2)"
     Site            803
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P97927.2)"
     Region          853..1008
                     /region_name="LamG"
                     /note="Laminin G domain; smart00282"
                     /db_xref="CDD:214598"
     Region          1044..1202
                     /region_name="LamG"
                     /note="Laminin G domain; Laminin G-like domains are
                     usually Ca++ mediated receptors that can have binding
                     sites for steroids, beta1 integrins, heparin, sulfatides,
                     fibulin-1, and alpha-dystroglycans. Proteins that contain
                     LamG domains serve a variety of...; cd00110"
                     /db_xref="CDD:238058"
     Site            1088
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P97927.2)"
     Region          1232..1371
                     /region_name="LamG"
                     /note="Laminin G domain; Laminin G-like domains are
                     usually Ca++ mediated receptors that can have binding
                     sites for steroids, beta1 integrins, heparin, sulfatides,
                     fibulin-1, and alpha-dystroglycans. Proteins that contain
                     LamG domains serve a variety of...; cd00110"
                     /db_xref="CDD:238058"
     Site            1283
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P97927.2)"
     Site            1361
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P97927.2)"
     Region          1409..1433
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P97927.2)"
     Region          1482..1617
                     /region_name="LamG"
                     /note="Laminin G domain; Laminin G-like domains are
                     usually Ca++ mediated receptors that can have binding
                     sites for steroids, beta1 integrins, heparin, sulfatides,
                     fibulin-1, and alpha-dystroglycans. Proteins that contain
                     LamG domains serve a variety of...; cd00110"
                     /db_xref="CDD:238058"
     Region          1641..1792
                     /region_name="LamG"
                     /note="Laminin G domain; Laminin G-like domains are
                     usually Ca++ mediated receptors that can have binding
                     sites for steroids, beta1 integrins, heparin, sulfatides,
                     fibulin-1, and alpha-dystroglycans. Proteins that contain
                     LamG domains serve a variety of...; cd00110"
                     /db_xref="CDD:238058"
     CDS             1..1816
                     /gene="Lama4"
                     /coded_by="NM_010681.4:441..5891"
                     /db_xref="CCDS:CCDS35882.1"
                     /db_xref="GeneID:16775"
                     /db_xref="MGI:MGI:109321"
ORIGIN      
        1 mgwstawcsv lalwllwcav csnaasgdgn afpfdiegsa vvgrqdpset sdsgvtlgrl
       61 ppaaercdag ffrtlsgeca pcdcngnshe cldgsgfclh cqrnttgehc ekcldgyigd
      121 sirgtprfcq pcpcplphla nfaescyrkn gavrcicken yvgpncerca pgyygnplli
      181 gstckkcdcs gnsdpnlife dcdeitgqcr nclrnttgfk cercapgyyg dartakncav
      241 cncgggpcds vtgecleegf evptgcdkcv wdltddlrla alsieesksg llsvssgaaa
      301 hrhvtdmnst ihllrtrlse renqytlrki qinnsentlr sllpdveglh ekgsqasrkg
      361 mlvekesmdt idqathlveq ahnmrdkiqe inskmlyyge nqelgpeeia eklvlaqkml
      421 eeirsrqpfl threlvdeea deaqellsqa enwqrlhndt rslfpvvleq lddynaklsd
      481 lqesinqald hvrdaedmnr aitfkqrdhe kqhervkeqm evvgaslsms adsltipqlt
      541 leeldeiikn asgiyaeidg aknelqgkls nlsnlshdlv qeatdhaynl qqeadelsrn
      601 lhssdmnglv qkaldasnvy enianyvsea netaelalni tdriydavsg idtqiiyhkd
      661 esdnllnqar elqakadssn deavadtsrr vggalwrkga lrdrlndavk qlqaaergda
      721 hqrlgqsklf ieeankttaa vqqvttpman nlsnwsqnlq tfdssaynta vdsardavrn
      781 ltevvpqlld qlrtveqkrp asnisasiqr ireliaqtrs vaskiqvsmm fdgqsavevh
      841 pkvsvddlka ftsislymkp ppkpaeptga wvadqfvlyl gsknakkeym glaikndnlv
      901 yvynlgmkdv eilldskpvs swpayfsivk iervgkhgkv fltvpslsst aeekfikkge
      961 fagddslldl tpedtvfyvg gvpanfklpa slnlpsysgc lelatlnndv islynfkhiy
     1021 nmdpsksvpc ardklaftqs raasyffdgs syavvrditr rgkfgqvtrf dieirtpadn
     1081 glvllmvngs mffslemrng ylhvfydfgf sngpvhledt lkkaqindak yheisiiyhn
     1141 dkkmilvvdr rhvkstdnek kkipftdiyi ggapqevlqs rtlrahlpld infrgcmkgf
     1201 qfqkkdfnll eqtetlgvgy gcpedslisr rayfngqsfi asiqkisffd gfeggfnfrt
     1261 lqpngllfyy tsgsdvfsis ldngtvvmdv kgikvmstdk qyhdglphfv vtsisdtrye
     1321 lvvdksrlrg knptkgkaeq tqttekkfyf ggspispqya nftgcisnay ftrldrdvev
     1381 edfqrysekv htslyecpie ssplfllhkk gknsskpktn kqgekskdap swdpiglkfl
     1441 eqkaprdshc hlssspraie hayqyggtan srqefeheqg dfgeksqfai rlktrsshgm
     1501 ifyvsdqeen dfmtlflahg rlvfmfnvgh kklkirsqek yndglwhdvi firekssgrl
     1561 vidglrvlee rlppsgaawk ikgpiylggv apgravknvq itsvysfsgc lgnlqlngas
     1621 itsasqtfsv tpcfegpmet gtyfsteggy vvldesfnig lkfeiafevr prsssgtlvh
     1681 ghsvngeyln vhmrngqviv kvnngvrdfs tsvtpkqnlc dgrwhritvi rdsnvvqldv
     1741 dsevnhvvgp lnpkpvdhre pvfvggvpes lltprlapsk pftgcirhfv idsrpvsfsk
     1801 aalvsgavsi nscpta
//
