ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P02468


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name LAMC1_MOUSE
Primary accession number P02468
Secondary accession numbers None
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on July 1, 1989 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 98)
Name and origin of the protein
Protein name Laminin subunit gamma-1 [Precursor]
Synonym Laminin B2 chain
Gene name
Name: Lamc1
Synonyms: Lamb-2, Lamc-1
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3680290 [NCBI, ExPASy, EBI, Israel, Japan]
Sasaki M., Yamada Y.;
"The laminin B2 chain has a multidomain structure homologous to the B1 chain.";
J. Biol. Chem. 262:17111-17117(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1021/bi00414a038; PubMed=3167041 [NCBI, ExPASy, EBI, Israel, Japan]
Durkin M.E., Bartos B.B., Liu S.-H., Phillips S.L., Chung A.E.;
"Primary structure of the mouse laminin B2 chain and comparison with laminin B1.";
Biochemistry 27:5198-5204(1988).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-239.
PubMed=2836421 [NCBI, ExPASy, EBI, Israel, Japan]
Ogawa K., Burbelo P.D., Sasaki M., Yamada Y.;
"The laminin B2 chain promoter contains unique repeat sequences and is active in transient transfection.";
J. Biol. Chem. 263:8384-8389(1988).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 1391-1607.
PubMed=6209134 [NCBI, ExPASy, EBI, Israel, Japan]
Barlow D.P., Green N.M., Kurkinen M., Hogan B.L.M.;
"Sequencing of laminin B chain cDNAs reveals C-terminal regions of coiled-coil alpha-helix.";
EMBO J. 3:2355-2362(1984).
[5]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 771-932.
DOI=10.1006/jmbi.1996.0191; PubMed=8648630 [NCBI, ExPASy, EBI, Israel, Japan]
Stetefeld J., Mayer U., Timpl R., Huber R.;
"Crystal structure of three consecutive laminin-type epidermal growth factor-like (LE) modules of laminin gamma1 chain harboring the nidogen binding site.";
J. Mol. Biol. 257:644-657(1996).
[6]
STRUCTURE BY NMR OF 824-881.
DOI=10.1006/jmbi.1996.0192; PubMed=8648631 [NCBI, ExPASy, EBI, Israel, Japan]
Baumgartner R., Czisch M., Mayer U., Poeschl E., Huber R., Timpl R., Holak T.A.;
"Structure of the nidogen binding LE module of the laminin gamma1 chain in solution.";
J. Mol. Biol. 257:658-668(1996).
Comments
  • FUNCTION: Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components.
  • SUBUNIT: Laminin is a complex glycoprotein, consisting of three different polypeptide chains (alpha, beta, gamma), which are bound to each other by disulfide bonds into a cross-shaped molecule comprising one long and three short arms with globules at each end. Gamma-1 is a subunit of laminin-1 (EHS laminin), laminin-2 (merosin), laminin-3 (S-laminin), laminin-4 (S-merosin), laminin-6 (K-laminin) and laminin-7 (KS-laminin).
  • SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane.
  • TISSUE SPECIFICITY: Found in the basement membranes (major component).
  • DOMAIN: The alpha-helical domains I and II are thought to interact with other laminin chains to form a coiled coil structure.
  • DOMAIN: Domains VI and IV are globular.
  • SIMILARITY: Contains 11 laminin EGF-like domains.
  • SIMILARITY: Contains 1 laminin IV type A domain.
  • SIMILARITY: Contains 1 laminin N-terminal domain.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X05211; CAA28838.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
J03484; AAA39405.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
J02930; AAA39408.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
J03749; AAA39409.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A28469; MMMSB2.
S55783; S55783.
UniGene Mm.1249
3D structure databases
PDB
1KLO; X-ray; 2.10 A; A=771-932.[ExPASy / RCSB / EBI]
1NPE; X-ray; 2.30 A; B=769-932.[ExPASy / RCSB / EBI]
1TLE; NMR; -; A=824-881.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1KLO; -.
1NPE; -.
1TLE; -.
ModBase P02468.
Organism-specific databases
MGI MGI:99914; Lamc1.
Gene expression databases
ArrayExpress P02468; -.
CleanEx MM_LAMC1; -.
GermOnline ENSMUSG00000026478; Mus musculus.
Ontologies
GO
GO:0043259; Cellular component: laminin-10 complex (inferred from physical interaction from MGI).
GO:0005201; Molecular function: extracellular matrix structural constituent (inferred from sequence or structural similarity from HGNC).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from MGI).
GO:0007155; Biological process: cell adhesion (inferred from sequence or structural similarity from HGNC).
GO:0016477; Biological process: cell migration (inferred from sequence or structural similarity from HGNC).
GO:0022617; Biological process: extracellular matrix disassembly (inferred from sequence or structural similarity from HGNC).
GO:0031581; Biological process: hemidesmosome assembly (inferred from sequence or structural similarity from HGNC).
GO:0006461; Biological process: protein complex assembly (inferred from sequence or structural similarity from HGNC).
QuickGo view.
Family and domain databases
InterPro IPR002049; EGF_laminin.
IPR013032; EGF_like_reg_CS.
IPR000034; Laminin_B.
IPR008211; Laminin_N.
Graphical view of domain structure.
Pfam PF00052; Laminin_B; 1.
PF00053; Laminin_EGF; 10.
PF00055; Laminin_N; 1.
Pfam graphical view of domain structure.
PRINTS PR00011; EGFLAMININ.
ProDom PD003031; Laminin_B; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00180; EGF_Lam; 10.
SM00281; LamB; 1.
SM00136; LamNT; 1.
SMART graphical view of domain structure.
PROSITE PS00022; EGF_1; 8.
PS01186; EGF_2; 2.
PS01248; EGF_LAM_1; 10.
PS50027; EGF_LAM_2; 10.
PS51115; LAMININ_IVA; 1.
PS51117; LAMININ_NTER; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P02468.
Genome annotation databases
Ensembl ENSMUSG00000026478; Mus musculus. [Contig view]
Phylogenomic databases
HOGENOM P02468; -.
HOVERGEN P02468; -.
Other
LinkHub P02468; -.
SOURCE Lamc1; Mus musculus.
ProtoNet P02468.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Basement membrane; Cell adhesion; Coiled coil; Extracellular matrix; Glycoprotein; Laminin EGF-like domain; Repeat; Secreted; Signal.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
SIGNAL   1     33  33      
CHAIN   34   1607  1574     Laminin subunit gamma-1. PRO_0000017075
DOMAIN   44    283  240     Laminin N-terminal. 
DOMAIN   284    339  56     Laminin EGF-like 1. 
DOMAIN   340    395  56     Laminin EGF-like 2. 
DOMAIN   396    442  47     Laminin EGF-like 3. 
DOMAIN   443    492  50     Laminin EGF-like 4. 
DOMAIN   493    502  10     Laminin EGF-like 5; first part. 
DOMAIN   512    687  176     Laminin IV type A. 
DOMAIN   688    721  34     Laminin EGF-like 5; second part. 
DOMAIN   722    770  49     Laminin EGF-like 6. 
DOMAIN   771    825  55     Laminin EGF-like 7. 
DOMAIN   826    881  56     Laminin EGF-like 8; nidogen-binding. 
DOMAIN   882    932  51     Laminin EGF-like 9. 
DOMAIN   933    980  48     Laminin EGF-like 10. 
DOMAIN   981   1028  48     Laminin EGF-like 11. 
REGION   1029   1607  579     Domain II and I. 
COILED   1034   1594  561     Potential. 
CARBOHYD   58     58        N-linked (GlcNAc...) (Potential). 
CARBOHYD   132    132        N-linked (GlcNAc...) (Potential). 
CARBOHYD   574    574        N-linked (GlcNAc...) (Potential). 
CARBOHYD   648    648        N-linked (GlcNAc...) (Potential). 
CARBOHYD   1020   1020        N-linked (GlcNAc...) (Potential). 
CARBOHYD   1105   1105        N-linked (GlcNAc...) (Potential). 
CARBOHYD   1159   1159        N-linked (GlcNAc...) (Potential). 
CARBOHYD   1173   1173        N-linked (GlcNAc...) (Potential). 
CARBOHYD   1203   1203        N-linked (GlcNAc...) (Potential). 
CARBOHYD   1221   1221        N-linked (GlcNAc...) (Potential). 
CARBOHYD   1239   1239        N-linked (GlcNAc...) (Potential). 
CARBOHYD   1378   1378        N-linked (GlcNAc...) (Potential). 
CARBOHYD   1393   1393        N-linked (GlcNAc...) (Potential). 
CARBOHYD   1437   1437        N-linked (GlcNAc...) (Potential). 
DISULFID   284    293        By similarity. 
DISULFID   286    303        By similarity. 
DISULFID   305    314        By similarity. 
DISULFID   340    349        By similarity. 
DISULFID   342    365        By similarity. 
DISULFID   368    377        By similarity. 
DISULFID   380    393        By similarity. 
DISULFID   396    408        By similarity. 
DISULFID   398    414        By similarity. 
DISULFID   416    425        By similarity. 
DISULFID   428    440        By similarity. 
DISULFID   443    454        By similarity. 
DISULFID   445    461        By similarity. 
DISULFID   463    472        By similarity. 
DISULFID   475    490        By similarity. 
DISULFID   722    731        By similarity. 
DISULFID   724    738        By similarity. 
DISULFID   740    749        By similarity. 
DISULFID   752    768        By similarity. 
DISULFID   771    779         
DISULFID   773    790         
DISULFID   793    802         
DISULFID   805    823         
DISULFID   826    840         
DISULFID   828    847         
DISULFID   850    859         
DISULFID   862    879         
DISULFID   882    896         
DISULFID   884    903         
DISULFID   905    914         
DISULFID   917    930         
DISULFID   933    945        By similarity. 
DISULFID   935    952        By similarity. 
DISULFID   954    963        By similarity. 
DISULFID   966    978        By similarity. 
DISULFID   981    993        By similarity. 
DISULFID   983    999        By similarity. 
DISULFID   1001   1010        By similarity. 
DISULFID   1013   1026        By similarity. 
DISULFID   1029   1029        Interchain (Probable). 
DISULFID   1032   1032        Interchain (Probable). 
DISULFID   1598   1598        Interchain (with beta-1 chain). 
CONFLICT   216    216        G -> A (in Ref. 3; AAA39409). 
CONFLICT   260    260        E -> D (in Ref. 2). 
CONFLICT   337    337        S -> C (in Ref. 2; AAA39408). 
CONFLICT   447    448        LR -> PS (in Ref. 2; AAA39408). 
CONFLICT   544    544        D -> Y (in Ref. 2; AAA39408). 
CONFLICT   662    662        T -> S (in Ref. 2; AAA39408). 
CONFLICT   886    886        Missing (in Ref. 2; AAA39408). 
CONFLICT   1158   1158        Missing (in Ref. 2; AAA39408). 
CONFLICT   1434   1434        V -> A (in Ref. 2; AAA39408). 
CONFLICT   1475   1475        R -> K (in Ref. 4; CAA28838). 
CONFLICT   1576   1576        D -> N (in Ref. 4; CAA28838). 
STRAND   779    781  3      
STRAND   783    785  3      
STRAND   788    790  3      
STRAND   797    799  3      
STRAND   809    812  4      
STRAND   821    825  5      
TURN   842    844  3      
TURN   856    859  4      
STRAND   866    868  3      
HELIX   875    877  3      
STRAND   878    881  4      
TURN   886    888  3      
HELIX   890    892  3      
TURN   898    900  3      
STRAND   909    911  3      
HELIX   924    926  3      
Sequence information
Length: 1607 AA [This is the length of the unprocessed precursor] Molecular weight: 177298 Da [This is the MW of the unprocessed precursor] CRC64: 81B7B08E4869F242 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MTGGGRAALA LQPRGRLWPL LAVLAAVAGC VRAAMDECAD EGGRPQRCMP EFVNAAFNVT 

        70         80         90        100        110        120 
VVATNTCGTP PEEYCVQTGV TGVTKSCHLC DAGQQHLQHG AAFLTDYNNQ ADTTWWQSQT 

       130        140        150        160        170        180 
MLAGVQYPNS INLTLHLGKA FDITYVRLKF HTSRPESFAI YKRTREDGPW IPYQYYSGSC 

       190        200        210        220        230        240 
ENTYSKANRG FIRTGGDEQQ ALCTDEFSDI SPLTGGNVAF STLEGRPSAY NFDNSPVLQE 

       250        260        270        280        290        300 
WVTATDIRVT LNRLNTFGDE VFNEPKVLKS YYYAISDFAV GGRCKCNGHA SECVKNEFDK 

       310        320        330        340        350        360 
LMCNCKHNTY GVDCEKCLPF FNDRPWRRAT AESASESLPC DCNGRSQECY FDPELYRSTG 

       370        380        390        400        410        420 
HGGHCTNCRD NTDGAKCERC RENFFRLGNT EACSPCHCSP VGSLSTQCDS YGRCSCKPGV 

       430        440        450        460        470        480 
MGDKCDRCQP GFHSLTEAGC RPCSCDLRGS TDECNVETGR CVCKDNVEGF NCERCKPGFF 

       490        500        510        520        530        540 
NLESSNPKGC TPCFCFGHSS VCTNAVGYSV YDISSTFQID EDGWRVEQRD GSEASLEWSS 

       550        560        570        580        590        600 
DRQDIAVISD SYFPRYFIAP VKFLGNQVLS YGQNLSFSFR VDRRDTRLSA EDLVLEGAGL 

       610        620        630        640        650        660 
RVSVPLIAQG NSYPSETTVK YIFRLHEATD YPWRPALSPF EFQKLLNNLT SIKIRGTYSE 

       670        680        690        700        710        720 
RTAGYLDDVT LQSARPGPGV PATWVESCTC PVGYGGQFCE TCLPGYRRET PSLGPYSPCV 

       730        740        750        760        770        780 
LCTCNGHSET CDPETGVCDC RDNTAGPHCE KCSDGYYGDS TLGTSSDCQP CPCPGGSSCA 

       790        800        810        820        830        840 
IVPKTKEVVC THCPTGTAGK RCELCDDGYF GDPLGSNGPV RLCRPCQCND NIDPNAVGNC 

       850        860        870        880        890        900 
NRLTGECLKC IYNTAGFYCD RCKEGFFGNP LAPNPADKCK ACACNPYGTV QQQSSCNPVT 

       910        920        930        940        950        960 
GQCQCLPHVS GRDCGTCDPG YYNLQSGQGC ERCDCHALGS TNGQCDIRTG QCECQPGITG 

       970        980        990       1000       1010       1020 
QHCERCETNH FGFGPEGCKP CDCHHEGSLS LQCKDDGRCE CREGFVGNRC DQCEENYFYN 

      1030       1040       1050       1060       1070       1080 
RSWPGCQECP ACYRLVKDKA AEHRVKLQEL ESLIANLGTG DDMVTDQAFE DRLKEAEREV 

      1090       1100       1110       1120       1130       1140 
TDLLREAQEV KDVDQNLMDR LQRVNSSLHS QISRLQNIRN TIEETGILAE RARSRVESTE 

      1150       1160       1170       1180       1190       1200 
QLIEIASREL EKAKMAAANV SITQPESTGE PNNMTLLAEE ARRLAERHKQ EADDIVRVAK 

      1210