GenomeNet

Database: UniProt
Entry: P97927
LinkDB: P97927
Original site: P97927 
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   13-FEB-2019, entry version 167.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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
RT   the 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
RT   of the 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
RT   project: 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
RT   targets 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
RC   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
RT   expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Binding to cells via a high affinity receptor, laminin
CC       is thought to mediate the attachment, migration and organization
CC       of cells into tissues during embryonic development by interacting
CC       with other extracellular matrix components.
CC   -!- SUBUNIT: Laminin is a complex glycoprotein, consisting of three
CC       different polypeptide chains (alpha, beta, gamma), which are bound
CC       to each other by disulfide bonds into a cross-shaped molecule
CC       comprising one long and three short arms with globules at each
CC       end. Alpha-4 is a subunit of laminin-8 (laminin-411), laminin-9
CC       (laminin-421) and 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,
CC       cardiac muscle, fat, dermis, lung stroma, aortic endothelium,
CC       endocardium and endothelium of blood vessels in skin and brain.
CC   -!- DOMAIN: The alpha-helical domains I and II are thought to interact
CC       with other laminin chains to form a coiled coil structure.
CC   -!- DOMAIN: Domain G is globular.
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   UniGene; Mm.258065; -.
DR   ProteinModelPortal; P97927; -.
DR   SMR; P97927; -.
DR   ComplexPortal; CPX-3015; Laminin-411 complex.
DR   ComplexPortal; CPX-3019; Laminin-423 complex.
DR   ComplexPortal; CPX-3031; Laminin-421 complex.
DR   IntAct; P97927; 1.
DR   MINT; P97927; -.
DR   STRING; 10090.ENSMUSP00000019992; -.
DR   PhosphoSitePlus; P97927; -.
DR   MaxQB; P97927; -.
DR   PaxDb; P97927; -.
DR   PeptideAtlas; P97927; -.
DR   PRIDE; P97927; -.
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   eggNOG; ENOG410KCXD; Eukaryota.
DR   eggNOG; ENOG410Z3D5; LUCA.
DR   GeneTree; ENSGT00940000159970; -.
DR   HOGENOM; HOG000113278; -.
DR   HOVERGEN; HBG052299; -.
DR   InParanoid; P97927; -.
DR   KO; K06241; -.
DR   OMA; GMDCPTI; -.
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   ChiTaRS; Lama4; mouse.
DR   PRO; PR:P97927; -.
DR   Proteomes; UP000000589; Chromosome 10.
DR   Bgee; ENSMUSG00000019846; Expressed in 228 organ(s), highest expression level in sciatic nerve.
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:0005615; C:extracellular space; HDA:BHF-UCL.
DR   GO; GO:0031594; C:neuromuscular junction; IDA:SynGO.
DR   GO; GO:0043083; C:synaptic cleft; IDA:SynGO.
DR   GO; GO:0005201; F:extracellular matrix structural constituent; HDA:BHF-UCL.
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   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; IPR002049; Laminin_EGF.
DR   InterPro; IPR001791; Laminin_G.
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; Complete proteome;
KW   Direct protein sequencing; Disulfide bond; Extracellular matrix;
KW   Glycoprotein; Laminin EGF-like domain; Reference proteome; Repeat;
KW   Secreted; Signal.
FT   SIGNAL        1     24       {ECO:0000255}.
FT   CHAIN        25   1816       Laminin subunit alpha-4.
FT                                /FTId=PRO_0000017061.
FT   DOMAIN       82    131       Laminin EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      132    186       Laminin EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      187    240       Laminin EGF-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      241    255       Laminin EGF-like 4; truncated.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DOMAIN      826   1030       Laminin G-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   DOMAIN     1042   1222       Laminin G-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   DOMAIN     1229   1397       Laminin G-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   DOMAIN     1462   1633       Laminin G-like 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   DOMAIN     1640   1813       Laminin G-like 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   REGION      256    825       Domain II and I.
FT   COILED      431    523       {ECO:0000255}.
FT   COILED      556    604       {ECO:0000255}.
FT   COILED      655    717       {ECO:0000255}.
FT   COILED      770    799       {ECO:0000255}.
FT   MOTIF       717    719       Cell attachment site. {ECO:0000255}.
FT   CARBOHYD    104    104       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    215    215       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    308    308       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    333    333       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    458    458       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    550    550       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    571    571       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    574    574       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    631    631       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    639    639       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    735    735       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    751    751       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    754    754       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    780    780       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    803    803       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1088   1088       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1283   1283       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1361   1361       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     82     91       {ECO:0000250}.
FT   DISULFID     84     98       {ECO:0000250}.
FT   DISULFID    101    110       {ECO:0000250}.
FT   DISULFID    113    129       {ECO:0000250}.
FT   DISULFID    132    146       {ECO:0000250}.
FT   DISULFID    134    155       {ECO:0000250}.
FT   DISULFID    157    166       {ECO:0000250}.
FT   DISULFID    169    184       {ECO:0000250}.
FT   DISULFID    187    202       {ECO:0000250}.
FT   DISULFID    189    209       {ECO:0000250}.
FT   DISULFID    212    221       {ECO:0000250}.
FT   DISULFID    224    238       {ECO:0000250}.
FT   DISULFID    266    266       Interchain. {ECO:0000305}.
FT   DISULFID    269    269       Interchain. {ECO:0000305}.
FT   DISULFID   1000   1030       {ECO:0000250}.
FT   DISULFID   1196   1222       {ECO:0000250}.
FT   DISULFID   1365   1397       {ECO:0000250}.
FT   DISULFID   1610   1633       {ECO:0000250}.
FT   DISULFID   1785   1813       {ECO:0000250}.
FT   CONFLICT      8      8       C -> S (in Ref. 2; AAC52982).
FT                                {ECO:0000305}.
FT   CONFLICT     18     18       C -> Y (in Ref. 2). {ECO:0000305}.
FT   CONFLICT    248    248       C -> R (in Ref. 3; AAC24725).
FT                                {ECO:0000305}.
FT   CONFLICT    297    297       G -> A (in Ref. 3; AAC24725).
FT                                {ECO:0000305}.
FT   CONFLICT    431    433       THR -> HPS (in Ref. 2; AAC52982).
FT                                {ECO:0000305}.
FT   CONFLICT    679    679       S -> C (in Ref. 3; AAC24725).
FT                                {ECO:0000305}.
FT   CONFLICT    703    703       D -> G (in Ref. 2; AAC52982).
FT                                {ECO:0000305}.
FT   CONFLICT    706    706       N -> H (in Ref. 2; AAC52982).
FT                                {ECO:0000305}.
FT   CONFLICT    728    728       K -> R (in Ref. 2). {ECO:0000305}.
FT   CONFLICT    730    730       F -> I (in Ref. 2). {ECO:0000305}.
FT   CONFLICT    779    779       R -> G (in Ref. 1; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT    810    810       R -> S (in Ref. 3; AAC24725).
FT                                {ECO:0000305}.
FT   CONFLICT    865    867       AEP -> QT (in Ref. 2; AAC52982).
FT                                {ECO:0000305}.
FT   CONFLICT    936    936       K -> E (in Ref. 3; AAC24725).
FT                                {ECO:0000305}.
FT   CONFLICT    970    970       L -> V (in Ref. 3; AAC24725).
FT                                {ECO:0000305}.
FT   CONFLICT   1132   1132       H -> R (in Ref. 2; AAC52982).
FT                                {ECO:0000305}.
FT   CONFLICT   1200   1200       F -> I (in Ref. 2; AAC52982).
FT                                {ECO:0000305}.
FT   CONFLICT   1382   1382       D -> A (in Ref. 2; AAC52982).
FT                                {ECO:0000305}.
FT   CONFLICT   1413   1414       NS -> EF (in Ref. 1; CAA70970).
FT                                {ECO:0000305}.
FT   CONFLICT   1489   1489       A -> S (in Ref. 2; AAC52982).
FT                                {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
//
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