LAMA4_MOUSE
ID LAMA4_MOUSE Reviewed; 1816 AA.
AC P97927; O88785; P70409; Q14BF2;
DT 13-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 13-DEC-2001, sequence version 2.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Laminin subunit alpha-4;
DE AltName: Full=Laminin-14 subunit alpha;
DE AltName: Full=Laminin-8 subunit alpha;
DE AltName: Full=Laminin-9 subunit alpha;
DE Flags: Precursor;
GN Name=Lama4;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 462-469; 478-483;
RP 776-782 AND 940-945.
RC STRAIN=BALB/cJ; TISSUE=Endothelial cell;
RX PubMed=9219532; DOI=10.1111/j.1432-1033.1997.t01-1-00727.x;
RA Frieser M., Noeckel H., Pausch F., Roeder C., Hahn A., Deutzmann R.,
RA Sorokin L.M.;
RT "Cloning of the mouse laminin alpha 4 cDNA. Expression in a subset of
RT endothelium.";
RL Eur. J. Biochem. 246:727-735(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Heart;
RX PubMed=9049981; DOI=10.1016/s0945-053x(96)90162-6;
RA Liu J., Mayne R.;
RT "The complete cDNA coding sequence and tissue-specific expression of the
RT mouse laminin alpha 4 chain.";
RL Matrix Biol. 15:433-437(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ;
RX PubMed=9346933; DOI=10.1074/jbc.272.44.27862;
RA Iivanainen A., Kortesmaa J., Sahlberg C., Morita T., Bergmann U.,
RA Thesleff I., Tryggvason K.;
RT "Primary structure, developmental expression, and immunolocalization of the
RT murine laminin alpha4 chain.";
RL J. Biol. Chem. 272:27862-27868(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 836-1106.
RC STRAIN=ICR; TISSUE=Placenta;
RX PubMed=9151674; DOI=10.1083/jcb.137.3.685;
RA Miner J.H., Patton B.L., Lentz S.I., Gilbert D.J., Snider W.D.,
RA Jenkins N.A., Copeland N.G., Sanes J.R.;
RT "The laminin alpha chains: expression, developmental transitions, and
RT chromosomal locations of alpha1-5, identification of heterotrimeric
RT laminins 8-11, and cloning of a novel alpha3 isoform.";
RL J. Cell Biol. 137:685-701(1997).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1467-1691.
RC TISSUE=Placenta;
RX PubMed=9034910;
RX DOI=10.1002/(sici)1096-9861(19970224)378:4<547::aid-cne9>3.0.co;2-2;
RA Lentz S.I., Miner J.H., Sanes J.R., Snider W.D.;
RT "Distribution of the ten known laminin chains in the pathways and targets
RT of developing sensory axons.";
RL J. Comp. Neurol. 378:547-561(1997).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Lung, Pancreas, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Binding to cells via a high affinity receptor, laminin is
CC thought to mediate the attachment, migration and organization of cells
CC into tissues during embryonic development by interacting with other
CC extracellular matrix components.
CC -!- SUBUNIT: Laminin is a complex glycoprotein, consisting of three
CC different polypeptide chains (alpha, beta, gamma), which are bound to
CC each other by disulfide bonds into a cross-shaped molecule comprising
CC one long and three short arms with globules at each end. Alpha-4 is a
CC subunit of laminin-8 (laminin-411), laminin-9 (laminin-421) and
CC laminin-14 (laminin-423).
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix, basement membrane. Note=Major component.
CC -!- TISSUE SPECIFICITY: Strongly expressed in peripheral nerves, cardiac
CC muscle, fat, dermis, lung stroma, aortic endothelium, endocardium and
CC endothelium of blood vessels in skin and brain.
CC -!- DOMAIN: The alpha-helical domains I and II are thought to interact with
CC other laminin chains to form a coiled coil structure.
CC -!- DOMAIN: Domain G is globular.
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DR EMBL; U58950; AAB41840.1; -; mRNA.
DR EMBL; Y09827; CAA70970.1; -; mRNA.
DR EMBL; U59865; AAC24725.1; -; mRNA.
DR EMBL; BC115942; AAI15943.1; -; mRNA.
DR EMBL; U88352; AAC53178.1; -; mRNA.
DR EMBL; U69176; AAC52982.1; -; mRNA.
DR CCDS; CCDS35882.1; -.
DR RefSeq; NP_034811.2; NM_010681.4.
DR AlphaFoldDB; P97927; -.
DR SMR; P97927; -.
DR BioGRID; 201099; 1.
DR ComplexPortal; CPX-3015; Laminin-411 complex.
DR ComplexPortal; CPX-3019; Laminin-423 complex.
DR ComplexPortal; CPX-3031; Laminin-421 complex.
DR STRING; 10090.ENSMUSP00000019992; -.
DR GlyConnect; 2457; 3 N-Linked glycans (3 sites).
DR GlyGen; P97927; 18 sites, 3 N-linked glycans (3 sites).
DR iPTMnet; P97927; -.
DR PhosphoSitePlus; P97927; -.
DR MaxQB; P97927; -.
DR PaxDb; P97927; -.
DR PeptideAtlas; P97927; -.
DR PRIDE; P97927; -.
DR ProteomicsDB; 265035; -.
DR Antibodypedia; 2846; 350 antibodies from 29 providers.
DR DNASU; 16775; -.
DR Ensembl; ENSMUST00000019992; ENSMUSP00000019992; ENSMUSG00000019846.
DR GeneID; 16775; -.
DR KEGG; mmu:16775; -.
DR UCSC; uc007evq.2; mouse.
DR CTD; 3910; -.
DR MGI; MGI:109321; Lama4.
DR VEuPathDB; HostDB:ENSMUSG00000019846; -.
DR eggNOG; KOG1836; Eukaryota.
DR GeneTree; ENSGT00940000159970; -.
DR HOGENOM; CLU_002814_0_0_1; -.
DR InParanoid; P97927; -.
DR OMA; VEQAHNM; -.
DR OrthoDB; 2342at2759; -.
DR PhylomeDB; P97927; -.
DR TreeFam; TF335359; -.
DR Reactome; R-MMU-3000157; Laminin interactions.
DR Reactome; R-MMU-8874081; MET activates PTK2 signaling.
DR BioGRID-ORCS; 16775; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Lama4; mouse.
DR PRO; PR:P97927; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; P97927; protein.
DR Bgee; ENSMUSG00000019846; Expressed in external carotid artery and 200 other tissues.
DR Genevisible; P97927; MM.
DR GO; GO:0005604; C:basement membrane; IDA:MGI.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0031594; C:neuromuscular junction; IDA:SynGO.
DR GO; GO:0043083; C:synaptic cleft; IDA:SynGO.
DR GO; GO:0005102; F:signaling receptor binding; IEA:InterPro.
DR GO; GO:0001568; P:blood vessel development; IMP:MGI.
DR GO; GO:0050873; P:brown fat cell differentiation; IDA:MGI.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR GO; GO:0030155; P:regulation of cell adhesion; IEA:InterPro.
DR GO; GO:0030334; P:regulation of cell migration; IEA:InterPro.
DR GO; GO:0045995; P:regulation of embryonic development; IEA:InterPro.
DR CDD; cd00055; EGF_Lam; 3.
DR CDD; cd00110; LamG; 5.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR009254; Laminin_aI.
DR InterPro; IPR010307; Laminin_dom_II.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR002049; LE_dom.
DR Pfam; PF00053; Laminin_EGF; 3.
DR Pfam; PF02210; Laminin_G_2; 5.
DR Pfam; PF06008; Laminin_I; 1.
DR Pfam; PF06009; Laminin_II; 1.
DR SMART; SM00181; EGF; 3.
DR SMART; SM00180; EGF_Lam; 3.
DR SMART; SM00282; LamG; 5.
DR SUPFAM; SSF49899; SSF49899; 5.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01248; EGF_LAM_1; 3.
DR PROSITE; PS50027; EGF_LAM_2; 3.
DR PROSITE; PS50025; LAM_G_DOMAIN; 5.
PE 1: Evidence at protein level;
KW Basement membrane; Cell adhesion; Coiled coil; Direct protein sequencing;
KW Disulfide bond; Extracellular matrix; Glycoprotein;
KW Laminin EGF-like domain; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..1816
FT /note="Laminin subunit alpha-4"
FT /id="PRO_0000017061"
FT DOMAIN 82..131
FT /note="Laminin EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 132..186
FT /note="Laminin EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 187..240
FT /note="Laminin EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 241..255
FT /note="Laminin EGF-like 4; truncated"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 826..1030
FT /note="Laminin G-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 1042..1222
FT /note="Laminin G-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 1229..1397
FT /note="Laminin G-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 1462..1633
FT /note="Laminin G-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 1640..1813
FT /note="Laminin G-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT REGION 256..825
FT /note="Domain II and I"
FT REGION 1409..1433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 431..523
FT /evidence="ECO:0000255"
FT COILED 556..604
FT /evidence="ECO:0000255"
FT COILED 655..717
FT /evidence="ECO:0000255"
FT COILED 770..799
FT /evidence="ECO:0000255"
FT MOTIF 717..719
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 215
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 308
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 333
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 458
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 550
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 571
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 574
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 631
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 639
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 735
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 751
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 754
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 780
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 803
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1088
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1283
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1361
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 82..91
FT /evidence="ECO:0000250"
FT DISULFID 84..98
FT /evidence="ECO:0000250"
FT DISULFID 101..110
FT /evidence="ECO:0000250"
FT DISULFID 113..129
FT /evidence="ECO:0000250"
FT DISULFID 132..146
FT /evidence="ECO:0000250"
FT DISULFID 134..155
FT /evidence="ECO:0000250"
FT DISULFID 157..166
FT /evidence="ECO:0000250"
FT DISULFID 169..184
FT /evidence="ECO:0000250"
FT DISULFID 187..202
FT /evidence="ECO:0000250"
FT DISULFID 189..209
FT /evidence="ECO:0000250"
FT DISULFID 212..221
FT /evidence="ECO:0000250"
FT DISULFID 224..238
FT /evidence="ECO:0000250"
FT DISULFID 266
FT /note="Interchain"
FT /evidence="ECO:0000305"
FT DISULFID 269
FT /note="Interchain"
FT /evidence="ECO:0000305"
FT DISULFID 1000..1030
FT /evidence="ECO:0000250"
FT DISULFID 1196..1222
FT /evidence="ECO:0000250"
FT DISULFID 1365..1397
FT /evidence="ECO:0000250"
FT DISULFID 1610..1633
FT /evidence="ECO:0000250"
FT DISULFID 1785..1813
FT /evidence="ECO:0000250"
FT CONFLICT 8
FT /note="C -> S (in Ref. 2; AAC52982)"
FT /evidence="ECO:0000305"
FT CONFLICT 18
FT /note="C -> Y (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 248
FT /note="C -> R (in Ref. 3; AAC24725)"
FT /evidence="ECO:0000305"
FT CONFLICT 297
FT /note="G -> A (in Ref. 3; AAC24725)"
FT /evidence="ECO:0000305"
FT CONFLICT 431..433
FT /note="THR -> HPS (in Ref. 2; AAC52982)"
FT /evidence="ECO:0000305"
FT CONFLICT 679
FT /note="S -> C (in Ref. 3; AAC24725)"
FT /evidence="ECO:0000305"
FT CONFLICT 703
FT /note="D -> G (in Ref. 2; AAC52982)"
FT /evidence="ECO:0000305"
FT CONFLICT 706
FT /note="N -> H (in Ref. 2; AAC52982)"
FT /evidence="ECO:0000305"
FT CONFLICT 728
FT /note="K -> R (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 730
FT /note="F -> I (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 779
FT /note="R -> G (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 810
FT /note="R -> S (in Ref. 3; AAC24725)"
FT /evidence="ECO:0000305"
FT CONFLICT 865..867
FT /note="AEP -> QT (in Ref. 2; AAC52982)"
FT /evidence="ECO:0000305"
FT CONFLICT 936
FT /note="K -> E (in Ref. 3; AAC24725)"
FT /evidence="ECO:0000305"
FT CONFLICT 970
FT /note="L -> V (in Ref. 3; AAC24725)"
FT /evidence="ECO:0000305"
FT CONFLICT 1132
FT /note="H -> R (in Ref. 2; AAC52982)"
FT /evidence="ECO:0000305"
FT CONFLICT 1200
FT /note="F -> I (in Ref. 2; AAC52982)"
FT /evidence="ECO:0000305"
FT CONFLICT 1382
FT /note="D -> A (in Ref. 2; AAC52982)"
FT /evidence="ECO:0000305"
FT CONFLICT 1413..1414
FT /note="NS -> EF (in Ref. 1; CAA70970)"
FT /evidence="ECO:0000305"
FT CONFLICT 1489
FT /note="A -> S (in Ref. 2; AAC52982)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1816 AA; 201819 MW; B49C45F3A45999D8 CRC64;
MGWSTAWCSV LALWLLWCAV CSNAASGDGN AFPFDIEGSA VVGRQDPSET SDSGVTLGRL
PPAAERCDAG FFRTLSGECA PCDCNGNSHE CLDGSGFCLH CQRNTTGEHC EKCLDGYIGD
SIRGTPRFCQ PCPCPLPHLA NFAESCYRKN GAVRCICKEN YVGPNCERCA PGYYGNPLLI
GSTCKKCDCS GNSDPNLIFE DCDEITGQCR NCLRNTTGFK CERCAPGYYG DARTAKNCAV
CNCGGGPCDS VTGECLEEGF EVPTGCDKCV WDLTDDLRLA ALSIEESKSG LLSVSSGAAA
HRHVTDMNST IHLLRTRLSE RENQYTLRKI QINNSENTLR SLLPDVEGLH EKGSQASRKG
MLVEKESMDT IDQATHLVEQ AHNMRDKIQE INSKMLYYGE NQELGPEEIA EKLVLAQKML
EEIRSRQPFL THRELVDEEA DEAQELLSQA ENWQRLHNDT RSLFPVVLEQ LDDYNAKLSD
LQESINQALD HVRDAEDMNR AITFKQRDHE KQHERVKEQM EVVGASLSMS ADSLTIPQLT
LEELDEIIKN ASGIYAEIDG AKNELQGKLS NLSNLSHDLV QEATDHAYNL QQEADELSRN
LHSSDMNGLV QKALDASNVY ENIANYVSEA NETAELALNI TDRIYDAVSG IDTQIIYHKD
ESDNLLNQAR ELQAKADSSN DEAVADTSRR VGGALWRKGA LRDRLNDAVK QLQAAERGDA
HQRLGQSKLF IEEANKTTAA VQQVTTPMAN NLSNWSQNLQ TFDSSAYNTA VDSARDAVRN
LTEVVPQLLD QLRTVEQKRP ASNISASIQR IRELIAQTRS VASKIQVSMM FDGQSAVEVH
PKVSVDDLKA FTSISLYMKP PPKPAEPTGA WVADQFVLYL GSKNAKKEYM GLAIKNDNLV
YVYNLGMKDV EILLDSKPVS SWPAYFSIVK IERVGKHGKV FLTVPSLSST AEEKFIKKGE
FAGDDSLLDL TPEDTVFYVG GVPANFKLPA SLNLPSYSGC LELATLNNDV ISLYNFKHIY
NMDPSKSVPC ARDKLAFTQS RAASYFFDGS SYAVVRDITR RGKFGQVTRF DIEIRTPADN
GLVLLMVNGS MFFSLEMRNG YLHVFYDFGF SNGPVHLEDT LKKAQINDAK YHEISIIYHN
DKKMILVVDR RHVKSTDNEK KKIPFTDIYI GGAPQEVLQS RTLRAHLPLD INFRGCMKGF
QFQKKDFNLL EQTETLGVGY GCPEDSLISR RAYFNGQSFI ASIQKISFFD GFEGGFNFRT
LQPNGLLFYY TSGSDVFSIS LDNGTVVMDV KGIKVMSTDK QYHDGLPHFV VTSISDTRYE
LVVDKSRLRG KNPTKGKAEQ TQTTEKKFYF GGSPISPQYA NFTGCISNAY FTRLDRDVEV
EDFQRYSEKV HTSLYECPIE SSPLFLLHKK GKNSSKPKTN KQGEKSKDAP SWDPIGLKFL
EQKAPRDSHC HLSSSPRAIE HAYQYGGTAN SRQEFEHEQG DFGEKSQFAI RLKTRSSHGM
IFYVSDQEEN DFMTLFLAHG RLVFMFNVGH KKLKIRSQEK YNDGLWHDVI FIREKSSGRL
VIDGLRVLEE RLPPSGAAWK IKGPIYLGGV APGRAVKNVQ ITSVYSFSGC LGNLQLNGAS
ITSASQTFSV TPCFEGPMET GTYFSTEGGY VVLDESFNIG LKFEIAFEVR PRSSSGTLVH
GHSVNGEYLN VHMRNGQVIV KVNNGVRDFS TSVTPKQNLC DGRWHRITVI RDSNVVQLDV
DSEVNHVVGP LNPKPVDHRE PVFVGGVPES LLTPRLAPSK PFTGCIRHFV IDSRPVSFSK
AALVSGAVSI NSCPTA
