LAMC2_MOUSE
ID LAMC2_MOUSE Reviewed; 1191 AA.
AC Q61092;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 17-JAN-2003, sequence version 2.
DT 25-MAY-2022, entry version 159.
DE RecName: Full=Laminin subunit gamma-2;
DE AltName: Full=Epiligrin subunit gamma;
DE AltName: Full=Kalinin subunit gamma;
DE AltName: Full=Kalinin/nicein/epiligrin 100 kDa subunit;
DE AltName: Full=Laminin B2t chain;
DE AltName: Full=Laminin-5 subunit gamma;
DE AltName: Full=Nicein subunit gamma;
DE Flags: Precursor;
GN Name=Lamc2;
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].
RC STRAIN=FVB/NJ; TISSUE=Lung;
RX PubMed=7882992; DOI=10.1111/j.1432-1033.1995.tb20239.x;
RA Sugiyama S., Utani A., Yamada S., Kozak C.A., Yamada Y.;
RT "Cloning and expression of the mouse laminin gamma 2 (B2t) chain, a subunit
RT of epithelial cell laminin.";
RL Eur. J. Biochem. 228:120-128(1995).
RN [2]
RP SEQUENCE REVISION.
RA Sasaki T., Yamada Y.;
RL Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP INTERACTION WITH HEPARIN; FIBULIN AND NIDOGEN, AND MUTAGENESIS OF ARG-76;
RP ARG-78; PHE-202; LYS-206; CYS-442 AND CYS-445.
RC STRAIN=FVB/NJ; TISSUE=Lung;
RX PubMed=11733994; DOI=10.1006/jmbi.2001.5176;
RA Sasaki T., Goehring W., Mann K., Brakebusch C., Yamada Y., Faessler R.,
RA Timpl R.;
RT "Short arm region of laminin-5 gamma2 chain: structure, mechanism of
RT processing and binding to heparin and proteins.";
RL J. Mol. Biol. 314:751-763(2001).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung;
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-2 is a
CC subunit of laminin-5 (laminin-332 or epiligrin/kalinin/nicein). Binds
CC to fibulin-1, fibulin-1c, fibulin-2 and nidogen.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix, basement membrane. Note=Major component.
CC -!- TISSUE SPECIFICITY: Epithelial cells of many tissues, particularly high
CC levels in tongue, hair follicles and kidney. Basement membranes of the
CC collecting tubules of kidney and pancreas.
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.
CC -!- MISCELLANEOUS: Binds heparin.
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DR EMBL; U43327; AAA85256.2; -; mRNA.
DR AlphaFoldDB; Q61092; -.
DR SMR; Q61092; -.
DR ComplexPortal; CPX-3012; Laminin-332 complex variant A.
DR ComplexPortal; CPX-3020; Laminin-522 complex.
DR ComplexPortal; CPX-3164; Laminin-332 complex variant B.
DR STRING; 10090.ENSMUSP00000027753; -.
DR GlyGen; Q61092; 5 sites.
DR jPOST; Q61092; -.
DR MaxQB; Q61092; -.
DR PaxDb; Q61092; -.
DR PRIDE; Q61092; -.
DR ProteomicsDB; 265037; -.
DR MGI; MGI:99913; Lamc2.
DR eggNOG; KOG1836; Eukaryota.
DR InParanoid; Q61092; -.
DR PhylomeDB; Q61092; -.
DR Reactome; R-MMU-1474228; Degradation of the extracellular matrix.
DR Reactome; R-MMU-2022090; Assembly of collagen fibrils and other multimeric structures.
DR Reactome; R-MMU-2214320; Anchoring fibril formation.
DR Reactome; R-MMU-3000157; Laminin interactions.
DR Reactome; R-MMU-446107; Type I hemidesmosome assembly.
DR Reactome; R-MMU-8874081; MET activates PTK2 signaling.
DR ChiTaRS; Lamc2; mouse.
DR PRO; PR:Q61092; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q61092; protein.
DR GO; GO:0005604; C:basement membrane; IDA:MGI.
DR GO; GO:0005938; C:cell cortex; ISO:MGI.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0031012; C:extracellular matrix; ISO:MGI.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0005607; C:laminin-2 complex; ISO:MGI.
DR GO; GO:0005610; C:laminin-5 complex; IDA:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0008201; F:heparin binding; IDA:MGI.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0016358; P:dendrite development; IBA:GO_Central.
DR GO; GO:0008045; P:motor neuron axon guidance; IBA:GO_Central.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0009888; P:tissue development; IBA:GO_Central.
DR CDD; cd00055; EGF_Lam; 6.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000034; Laminin_IV.
DR InterPro; IPR002049; LE_dom.
DR Pfam; PF00052; Laminin_B; 1.
DR Pfam; PF00053; Laminin_EGF; 7.
DR SMART; SM00181; EGF; 7.
DR SMART; SM00180; EGF_Lam; 7.
DR SMART; SM00281; LamB; 1.
DR PROSITE; PS00022; EGF_1; 4.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS01248; EGF_LAM_1; 6.
DR PROSITE; PS50027; EGF_LAM_2; 6.
DR PROSITE; PS51115; LAMININ_IVA; 1.
PE 1: Evidence at protein level;
KW Basement membrane; Cell adhesion; Coiled coil; Disulfide bond;
KW Extracellular matrix; Glycoprotein; Heparin-binding;
KW Laminin EGF-like domain; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..1191
FT /note="Laminin subunit gamma-2"
FT /id="PRO_0000017078"
FT DOMAIN 28..83
FT /note="Laminin EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 84..130
FT /note="Laminin EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 139..186
FT /note="Laminin EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 187..196
FT /note="Laminin EGF-like 4; first part"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 213..381
FT /note="Laminin IV type A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00458"
FT DOMAIN 382..415
FT /note="Laminin EGF-like 4; second part"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 416..461
FT /note="Laminin EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 462..516
FT /note="Laminin EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 517..572
FT /note="Laminin EGF-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 573..602
FT /note="Laminin EGF-like 8; truncated"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT REGION 603..1191
FT /note="Domain II and I"
FT COILED 612..710
FT /evidence="ECO:0000255"
FT COILED 759..786
FT /evidence="ECO:0000255"
FT COILED 946..996
FT /evidence="ECO:0000255"
FT COILED 1139..1178
FT /evidence="ECO:0000255"
FT MOTIF 586..588
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT CARBOHYD 342
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 362
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 526
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 941
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1032
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 28..37
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 30..53
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 56..65
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 68..81
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 84..96
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 86..102
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 104..113
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 116..128
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 139..150
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 141..155
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 157..166
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 169..184
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 462..470
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 464..481
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 484..493
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 496..514
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 517..531
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 519..538
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 541..550
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 553..570
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 573..585
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 575..591
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 593..602
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 610
FT /note="Interchain"
FT /evidence="ECO:0000305"
FT DISULFID 613
FT /note="Interchain"
FT /evidence="ECO:0000305"
FT DISULFID 1182
FT /note="Interchain (with beta-3 chain)"
FT /evidence="ECO:0000305"
FT MUTAGEN 76
FT /note="R->A: No change to herarin-binding."
FT /evidence="ECO:0000269|PubMed:11733994"
FT MUTAGEN 78
FT /note="R->A: No change to herarin-binding."
FT /evidence="ECO:0000269|PubMed:11733994"
FT MUTAGEN 202
FT /note="F->A: No fibulin-1C binding. No change to fibulin-2
FT binding."
FT /evidence="ECO:0000269|PubMed:11733994"
FT MUTAGEN 206
FT /note="K->A: No fibulin-1C binding. No change to fibulin-2
FT binding."
FT /evidence="ECO:0000269|PubMed:11733994"
FT MUTAGEN 442
FT /note="C->S: 20-fold reduction to fibulin-2 binding."
FT /evidence="ECO:0000269|PubMed:11733994"
FT MUTAGEN 445
FT /note="C->S: 20-fold reduction to fibulin-2 binding."
FT /evidence="ECO:0000269|PubMed:11733994"
SQ SEQUENCE 1191 AA; 130161 MW; 7016C1F851D909B9 CRC64;
MPALWLSCCL GVALLLPAAQ ATSRREVCDC NGKSRQCVFD QELHRQTGSG FRCLNCNDNT
AGVHCERCRE GFYRHRDRDR CLPCNCHSKG SLSAGCDNSG QCRCKPGVTG QRCDRCQPGF
HMLTDAGCTR DQGQLDSKCD CDPAGISGPC DSGRCVCKPA VTGERCDRCR PGYYHLDRAN
PEGCTQCFCY GHSASCHASA DFSVHKITST FSQDVDGWKA VQRNGAPAKL HWSQRHRDVF
SSARRSDPVY FVAPAKFLGN QQVSYGQSLS FDYRVDRGGR QPSAYDVILE GAGLQIRAPL
MAPGKTLPCG ITKTYTFRLN EHPSSHWSPQ LSYFEYRRLL RNLTALLIRA TYGEYSTGYI
DNVTLVSARP VSGAPAPWVE RCVCPAGYKG QFCQECASGY KRDSARLGPF GACVPCNCQG
GGACDPDTGD CYSGDENPDI ECADCPIGFY NDPHDPRSCK PCPCHNGFSC SVMPETEEVV
CNNCPPGVTG ARCELCADGF FGDPFGERGP VRPCQRCQCN NNVDPNASGN CDQLTGRCLK
CIYNTAGVYC DQCKAGYFGD PLAPNPADKC RACNCSPMGS EPGECRGDGS CVCKPGFGGL
NCDHAALTSC PACYNQVKIQ MDQFTQQLQS LEALVSKAQG GGGGGTVPVQ LEGRIEQAEQ
ALQDILGEAQ ISEGAMRAVA VRLAKARSQE NDYKTRLDDL KMTAERIRAL GSQHQNRVQD
TSRLISQMRL SLAGSEALLE NTNIHSSEHY VGPNDFKSLA QEATRKADSH AESANAMKQL
ARETEDYSKQ ALSLARKLLS GGGGSGSWDS SVVQGLMGKL EKTKSLSQQL SLEGTQADIE
ADRSYQHSLR LLDSASQLQG VSDLSFQVEA KRIRQKADSL SNLVTRQTDA FTRVRNNLGN
WEKETRQLLQ TGKDRRQTSD QLLSRANLAK NRAQEALSMG NATFYEVENI LKNLREFDLQ
VEDRKAEAEE AMKRLSSISQ KVADASDKTQ QAETALGSAT ADTQRAKNAA REALEISSEI
ELEIGSLNLE ANVTADGALA MEKGTATLKS EMREMIELAR KELEFDTDKD TVQLVITEAQ
QADARATSAG VTIQDTLNTL DGILHLIDQP GSVDEEGMML LEQGLFQAKT QINSRLRPLM
SDLEERVRRQ RNHLHLLETS IDGILADVKN LENIRDNLPP GCYNTQALEQ Q
