LAMC3_MOUSE
ID LAMC3_MOUSE Reviewed; 1581 AA.
AC Q9R0B6; Q4VAI3; Q9WTW6;
DT 13-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Laminin subunit gamma-3;
DE AltName: Full=Laminin-12 subunit gamma;
DE AltName: Full=Laminin-14 subunit gamma;
DE AltName: Full=Laminin-15 subunit gamma;
DE Flags: Precursor;
GN Name=Lamc3;
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].
RA Albus A.M., Burgeson B., Champliaud M.-F., Koch M., Olson P.;
RT "Mouse laminin 12 gamma 3 chain.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 1-1526.
RX PubMed=10318827; DOI=10.1074/jbc.274.20.14107;
RA Iivanainen A., Morita T., Tryggvason K.;
RT "Molecular cloning and tissue-specific expression of a novel murine laminin
RT gamma3 chain.";
RL J. Biol. Chem. 274:14107-14111(1999).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, 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. Gamma-3 is a
CC subunit of laminin-12 (laminin-213), laminin-14 (laminin-423) and
CC laminin-15 (laminin-523).
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix, basement membrane.
CC -!- TISSUE SPECIFICITY: Strongly expressed in capillaries and arterioles of
CC kidney as well as in interstitial Leydig cells of testis.
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 IV is globular.
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DR EMBL; AF083372; AAF08983.1; -; mRNA.
DR EMBL; AL928893; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX511243; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466542; EDL08519.1; -; Genomic_DNA.
DR EMBL; BC096366; AAH96366.1; -; mRNA.
DR EMBL; AF079520; AAD29851.1; -; mRNA.
DR CCDS; CCDS15903.1; -.
DR RefSeq; NP_035966.2; NM_011836.3.
DR AlphaFoldDB; Q9R0B6; -.
DR SMR; Q9R0B6; -.
DR BioGRID; 204801; 1.
DR ComplexPortal; CPX-3018; Laminin-213 complex.
DR ComplexPortal; CPX-3019; Laminin-423 complex.
DR ComplexPortal; CPX-3021; Laminin-523 complex.
DR STRING; 10090.ENSMUSP00000028187; -.
DR GlyConnect; 2462; 1 N-Linked glycan (2 sites).
DR GlyGen; Q9R0B6; 10 sites, 1 N-linked glycan (2 sites).
DR iPTMnet; Q9R0B6; -.
DR PhosphoSitePlus; Q9R0B6; -.
DR MaxQB; Q9R0B6; -.
DR PaxDb; Q9R0B6; -.
DR PRIDE; Q9R0B6; -.
DR ProteomicsDB; 264912; -.
DR Antibodypedia; 45184; 143 antibodies from 23 providers.
DR DNASU; 23928; -.
DR Ensembl; ENSMUST00000028187; ENSMUSP00000028187; ENSMUSG00000026840.
DR GeneID; 23928; -.
DR KEGG; mmu:23928; -.
DR UCSC; uc008jef.1; mouse.
DR CTD; 10319; -.
DR MGI; MGI:1344394; Lamc3.
DR VEuPathDB; HostDB:ENSMUSG00000026840; -.
DR eggNOG; KOG1836; Eukaryota.
DR GeneTree; ENSGT00940000161559; -.
DR InParanoid; Q9R0B6; -.
DR OMA; TCVQLAD; -.
DR OrthoDB; 156553at2759; -.
DR PhylomeDB; Q9R0B6; -.
DR TreeFam; TF352481; -.
DR Reactome; R-MMU-3000157; Laminin interactions.
DR Reactome; R-MMU-8874081; MET activates PTK2 signaling.
DR BioGRID-ORCS; 23928; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Lamc3; mouse.
DR PRO; PR:Q9R0B6; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9R0B6; protein.
DR Bgee; ENSMUSG00000026840; Expressed in meninx of hindbrain and 83 other tissues.
DR ExpressionAtlas; Q9R0B6; baseline and differential.
DR Genevisible; Q9R0B6; MM.
DR GO; GO:0005604; C:basement membrane; IDA:MGI.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR GO; GO:0014002; P:astrocyte development; IGI:MGI.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0000904; P:cell morphogenesis involved in differentiation; IGI:MGI.
DR GO; GO:0060041; P:retina development in camera-type eye; IGI:MGI.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IBA:GO_Central.
DR GO; GO:0009888; P:tissue development; IBA:GO_Central.
DR GO; GO:0007601; P:visual perception; IGI:MGI.
DR CDD; cd00055; EGF_Lam; 10.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000034; Laminin_IV.
DR InterPro; IPR008211; Laminin_N.
DR InterPro; IPR002049; LE_dom.
DR Pfam; PF00052; Laminin_B; 1.
DR Pfam; PF00053; Laminin_EGF; 11.
DR Pfam; PF00055; Laminin_N; 1.
DR SMART; SM00181; EGF; 6.
DR SMART; SM00180; EGF_Lam; 11.
DR SMART; SM00281; LamB; 1.
DR SMART; SM00136; LamNT; 1.
DR PROSITE; PS00022; EGF_1; 8.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS01248; EGF_LAM_1; 11.
DR PROSITE; PS50027; EGF_LAM_2; 10.
DR PROSITE; PS51115; LAMININ_IVA; 1.
DR PROSITE; PS51117; LAMININ_NTER; 1.
PE 1: Evidence at protein level;
KW Basement membrane; Cell adhesion; Coiled coil; Disulfide bond;
KW Extracellular matrix; Glycoprotein; Laminin EGF-like domain;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..1581
FT /note="Laminin subunit gamma-3"
FT /id="PRO_0000017080"
FT DOMAIN 40..279
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00466"
FT DOMAIN 280..335
FT /note="Laminin EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 336..391
FT /note="Laminin EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 392..438
FT /note="Laminin EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 439..488
FT /note="Laminin EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 489..498
FT /note="Laminin EGF-like 5; first part"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 508..684
FT /note="Laminin IV type A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00458"
FT DOMAIN 685..718
FT /note="Laminin EGF-like 5; second part"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 719..766
FT /note="Laminin EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 767..821
FT /note="Laminin EGF-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 822..877
FT /note="Laminin EGF-like 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 878..927
FT /note="Laminin EGF-like 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 928..975
FT /note="Laminin EGF-like 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 976..1024
FT /note="Laminin EGF-like 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT REGION 1025..1581
FT /note="Domain II and I"
FT REGION 1382..1413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1029..1046
FT /evidence="ECO:0000255"
FT COILED 1112..1153
FT /evidence="ECO:0000255"
FT COILED 1208..1231
FT /evidence="ECO:0000255"
FT COILED 1438..1468
FT /evidence="ECO:0000255"
FT COILED 1510..1575
FT /evidence="ECO:0000255"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 304
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 337
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 640
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 849
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 991
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1162
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1320
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1514
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 280..289
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 282..299
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 301..310
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 313..333
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 336..345
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 338..361
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 364..373
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 376..389
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 392..404
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 394..410
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 412..421
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 424..436
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 439..450
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 441..457
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 459..468
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 471..486
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 719..727
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 721..734
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 736..745
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 748..764
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 767..775
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 769..786
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 789..798
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 801..819
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 822..836
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 824..843
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 846..855
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 858..875
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 878..891
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 880..898
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 900..909
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 912..925
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 928..940
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 930..947
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 949..958
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 961..973
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 976..988
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 978..994
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 996..1005
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1008..1021
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT CONFLICT 9
FT /note="L -> F (in Ref. 5; AAD29851)"
FT /evidence="ECO:0000305"
FT CONFLICT 190
FT /note="P -> T (in Ref. 5; AAD29851)"
FT /evidence="ECO:0000305"
FT CONFLICT 195
FT /note="R -> K (in Ref. 5; AAD29851)"
FT /evidence="ECO:0000305"
FT CONFLICT 221
FT /note="G -> S (in Ref. 5; AAD29851)"
FT /evidence="ECO:0000305"
FT CONFLICT 394
FT /note="C -> R (in Ref. 5; AAD29851)"
FT /evidence="ECO:0000305"
FT CONFLICT 471
FT /note="C -> Y (in Ref. 5; AAD29851)"
FT /evidence="ECO:0000305"
FT CONFLICT 1150
FT /note="L -> LDEPQLFSLLLK (in Ref. 5; AAD29851)"
FT /evidence="ECO:0000305"
FT CONFLICT 1387
FT /note="Q -> H (in Ref. 1; AAF08983)"
FT /evidence="ECO:0000305"
FT CONFLICT 1438..1439
FT /note="AS -> TI (in Ref. 5; AAD29851)"
FT /evidence="ECO:0000305"
FT CONFLICT 1479
FT /note="I -> V (in Ref. 1; AAF08983)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1581 AA; 172322 MW; A6E83A8F9C678830 CRC64;
MAVSRVLSLL ATVASMALVI QETHFAAGAD MGSCYDGVGR AQRCLPEFEN AAFGRRAEAS
HTCGRPPEDF CPHVGAPGAG LQCQRCDDAD PGRRHDASYL TDFHSPDDST WWQSPSMAFG
VQYPTSVNLT LSLGKAYEIT YVRLKFHTSR PESFAIYKRT YASGPWEPYQ YYSASCQKTY
GRPEGHYLRP GEDERVAFCT SEFSDISPLN GGNVAFSTLE GRPSAYNFEE SPVLQEWVTS
TDILISLDRL NTFGDDIFKD PRVLQSYYYA VSDFSVGGRC KCNGHASECE PNAAGQLACR
CQHNTTGVDC ERCLPFFQDR PWARGTAEDA NECLPCNCSG HSEECTFDRE LYRSTGHGGH
CQRCRDHTTG PHCERCEKNY YRWSPKTPCQ PCDCHPAGSL SLQCDNSGVC PCKPTVTGWK
CDRCLPGFHS LSEGGCRPCA CNVAGSLGTC DPRSGNCPCK ENVEGSLCDR CRPGTFNLQP
HNPVGCSSCF CYGHSKVCSP AAGFQEHHIR SDFRHGAGGW QIRSMGVSKR PLQWSQSGLL
LGLRGGEELS APKKFLGDQR LSYGQPVILT LQVPPGGSPP PIQLRLEGAG LALSLRPSSL
PSPQDTRQPR RVQLQFLLQE TSEEAESPLP TFHFQRLLSN LTALSIWTSG QGPGHSGQVL
LCEVQLTSAW PQRELAPPAS WVETCLCPQG YTGQFCEFCA LGYKREIPHG GPYANCIPCT
CNQHGTCDPN TGICLCGHHT EGPSCERCMP GFYGNAFSGR ADDCQPCPCP GQSACATIPE
SGDVVCTHCP PGQRGRRCES CEDGFFGDPL GLSGAPQPCR RCQCSGNVDL NAVGNCDPHS
GHCLRCLYNT TGAHCEHCRE GFYGSAVATR PVDKCAPCSC DLRGSVSEKT CNPVTGQCVC
LPYVSGRDCS RCSPGFYDLQ SGRGCQSCKC HPLGSLENKC HPKTGQCPCR PGVTGQACDR
CQLGFFGFSI KGCRDCRCSP LGAASSQCHE NSTCVCRPGF VGYKCDRCQD NFFLADGDTG
CQECPTCYAL VKEEAAKLKA RLMLMEGWLQ RSDCGSPWGP LDILQGEAPL GDVYQGHHLL
QETRGTFLQQ MVGLEDSVKA TWEQLQVLRG HVHCAQAGAQ KTCIQLAELE ETLQSSEEEV
LRAASALSFL ASLQKGSSTP TNWSHLASEA QILARSHRDT ATKIEATSER ALLASNASYE
LLKLMEGRVA SEAQQELEDR YQEVQAAQTA LGIAVAEALP KAEKALATVK QVIGDAAPHL
GLLVTPEAMN FQARGLSWKV KALEQKLEQK EPEVGQSVGA LQVEAGRALE KMEPFMQLRN
KTTAAFTRAS SAVQAAKVTV IGAETLLADL EGMKLRSPLP KEQAALKKKA GSIRTRLLED
TKRKTKQAER MLGNAASLSS STKKKSKEAE LMSKDNAKLS RALLREGKQG YRHASRLASQ
TQATLRRASR LLLTSEAHKQ ELEEAKQVTS GLSTVERQIR ESRISLEKDT KVLSELLVKL
GSLGVHQAPA QTLNETQRAL ESLRLQLDSH GALHHKLRQL EEESARQELQ IQSFEDDLAE
IRADKHNLET ILSSLPENCA S
