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Database: UniProt
Entry: Q61092
LinkDB: Q61092
Original site: Q61092 
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   13-FEB-2019, entry version 147.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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
RT   subunit 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
RP   ARG-76; 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.,
RA   Faessler R., 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
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. Gamma-2 is a subunit of laminin-5 (laminin-332 or
CC       epiligrin/kalinin/nicein). Binds to fibulin-1, fibulin-1c,
CC       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
CC       high levels in tongue, hair follicles and kidney. Basement
CC       membranes of the collecting tubules of kidney and pancreas.
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 IV is globular.
CC   -!- MISCELLANEOUS: Binds heparin.
DR   EMBL; U43327; AAA85256.2; -; mRNA.
DR   UniGene; Mm.329272; -.
DR   ProteinModelPortal; 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   MaxQB; Q61092; -.
DR   PaxDb; Q61092; -.
DR   PRIDE; Q61092; -.
DR   MGI; MGI:99913; Lamc2.
DR   eggNOG; ENOG410IP6C; Eukaryota.
DR   eggNOG; ENOG4110QI9; LUCA.
DR   HOGENOM; HOG000019301; -.
DR   HOVERGEN; HBG062127; -.
DR   InParanoid; Q61092; -.
DR   PhylomeDB; Q61092; -.
DR   PMAP-CutDB; Q61092; -.
DR   PRO; PR:Q61092; -.
DR   Proteomes; UP000000589; Unplaced.
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:0005201; F:extracellular matrix structural constituent; HDA:BHF-UCL.
DR   GO; GO:0008201; F:heparin binding; IDA:MGI.
DR   GO; GO:0070831; P:basement membrane assembly; IEA:InterPro.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
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:0048731; P:system development; IEA:InterPro.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR002049; Laminin_EGF.
DR   InterPro; IPR031082; Laminin_gamma-2.
DR   InterPro; IPR000034; Laminin_IV.
DR   PANTHER; PTHR10574:SF313; PTHR10574:SF313; 1.
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; Complete proteome;
KW   Disulfide bond; Extracellular matrix; Glycoprotein; Heparin-binding;
KW   Laminin EGF-like domain; Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL        1     21       {ECO:0000255}.
FT   CHAIN        22   1191       Laminin subunit gamma-2.
FT                                /FTId=PRO_0000017078.
FT   DOMAIN       28     83       Laminin EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN       84    130       Laminin EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      139    186       Laminin EGF-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      187    196       Laminin EGF-like 4; first part.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DOMAIN      213    381       Laminin IV type A. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00458}.
FT   DOMAIN      382    415       Laminin EGF-like 4; second part.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DOMAIN      416    461       Laminin EGF-like 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      462    516       Laminin EGF-like 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      517    572       Laminin EGF-like 7. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      573    602       Laminin EGF-like 8; truncated.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   REGION      603   1191       Domain II and I.
FT   COILED      612    710       {ECO:0000255}.
FT   COILED      759    786       {ECO:0000255}.
FT   COILED      946    996       {ECO:0000255}.
FT   COILED     1139   1178       {ECO:0000255}.
FT   MOTIF       586    588       Cell attachment site. {ECO:0000255}.
FT   CARBOHYD    342    342       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    362    362       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    526    526       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    941    941       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1032   1032       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     28     37       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID     30     53       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID     56     65       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID     68     81       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID     84     96       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID     86    102       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    104    113       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    116    128       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    139    150       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    141    155       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    157    166       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    169    184       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    462    470       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    464    481       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    484    493       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    496    514       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    517    531       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    519    538       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    541    550       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    553    570       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    573    585       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    575    591       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    593    602       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    610    610       Interchain. {ECO:0000305}.
FT   DISULFID    613    613       Interchain. {ECO:0000305}.
FT   DISULFID   1182   1182       Interchain (with beta-3 chain).
FT                                {ECO:0000305}.
FT   MUTAGEN      76     76       R->A: No change to herarin-binding.
FT                                {ECO:0000269|PubMed:11733994}.
FT   MUTAGEN      78     78       R->A: No change to herarin-binding.
FT                                {ECO:0000269|PubMed:11733994}.
FT   MUTAGEN     202    202       F->A: No fibulin-1C binding. No change to
FT                                fibulin-2 binding.
FT                                {ECO:0000269|PubMed:11733994}.
FT   MUTAGEN     206    206       K->A: No fibulin-1C binding. No change to
FT                                fibulin-2 binding.
FT                                {ECO:0000269|PubMed:11733994}.
FT   MUTAGEN     442    442       C->S: 20-fold reduction to fibulin-2
FT                                binding. {ECO:0000269|PubMed:11733994}.
FT   MUTAGEN     445    445       C->S: 20-fold reduction to fibulin-2
FT                                binding. {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
//
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