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Reviewed, UniProtKB/Swiss-Prot P02468 (LAMC1_MOUSE)

Last modified October 13, 2009. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Laminin subunit gamma-1
Alternative name(s):
    Laminin B2 chain
Gene names
Name: Lamc1
Synonyms: Lamb-2, Lamc-1
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

Sequence length1607 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (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 structure

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.

Domains VI and IV are globular.

Sequence similarities

Contains 11 laminin EGF-like domains.

Contains 1 laminin IV type A domain.

Contains 1 laminin N-terminal domain.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3333
Chain34 – 16071574Laminin subunit gamma-1
PRO_0000017075

Regions

Domain44 – 283240Laminin N-terminal
Domain284 – 33956Laminin EGF-like 1
Domain340 – 39556Laminin EGF-like 2
Domain396 – 44247Laminin EGF-like 3
Domain443 – 49250Laminin EGF-like 4
Domain493 – 50210Laminin EGF-like 5; first part
Domain512 – 687176Laminin IV type A
Domain688 – 72134Laminin EGF-like 5; second part
Domain722 – 77049Laminin EGF-like 6
Domain771 – 82555Laminin EGF-like 7
Domain826 – 88156Laminin EGF-like 8; nidogen-binding
Domain882 – 93251Laminin EGF-like 9
Domain933 – 98048Laminin EGF-like 10
Domain981 – 102848Laminin EGF-like 11
Region1029 – 1607579Domain II and I
Coiled coil1034 – 1594561 Potential

Amino acid modifications

Glycosylation581N-linked (GlcNAc...) Potential
Glycosylation1321N-linked (GlcNAc...) Potential
Glycosylation5741N-linked (GlcNAc...) Potential
Glycosylation6481N-linked (GlcNAc...) Ref.5
Glycosylation10201N-linked (GlcNAc...) Potential
Glycosylation11051N-linked (GlcNAc...) Ref.5
Glycosylation11591N-linked (GlcNAc...) Potential
Glycosylation11731N-linked (GlcNAc...) Potential
Glycosylation12031N-linked (GlcNAc...) Ref.5
Glycosylation12211N-linked (GlcNAc...) Ref.5
Glycosylation12391N-linked (GlcNAc...) Potential
Glycosylation13781N-linked (GlcNAc...) Potential
Glycosylation13931N-linked (GlcNAc...) Ref.5
Glycosylation14371N-linked (GlcNAc...) Potential
Disulfide bond284 ↔ 293 By similarity
Disulfide bond286 ↔ 303 By similarity
Disulfide bond305 ↔ 314 By similarity
Disulfide bond340 ↔ 349 By similarity
Disulfide bond342 ↔ 365 By similarity
Disulfide bond368 ↔ 377 By similarity
Disulfide bond380 ↔ 393 By similarity
Disulfide bond396 ↔ 408 By similarity
Disulfide bond398 ↔ 414 By similarity
Disulfide bond416 ↔ 425 By similarity
Disulfide bond428 ↔ 440 By similarity
Disulfide bond443 ↔ 454 By similarity
Disulfide bond445 ↔ 461 By similarity
Disulfide bond463 ↔ 472 By similarity
Disulfide bond475 ↔ 490 By similarity
Disulfide bond722 ↔ 731 By similarity
Disulfide bond724 ↔ 738 By similarity
Disulfide bond740 ↔ 749 By similarity
Disulfide bond752 ↔ 768 By similarity
Disulfide bond771 ↔ 779
Disulfide bond773 ↔ 790
Disulfide bond793 ↔ 802
Disulfide bond805 ↔ 823
Disulfide bond826 ↔ 840
Disulfide bond828 ↔ 847
Disulfide bond850 ↔ 859
Disulfide bond862 ↔ 879
Disulfide bond882 ↔ 896
Disulfide bond884 ↔ 903
Disulfide bond905 ↔ 914
Disulfide bond917 ↔ 930
Disulfide bond933 ↔ 945 By similarity
Disulfide bond935 ↔ 952 By similarity
Disulfide bond954 ↔ 963 By similarity
Disulfide bond966 ↔ 978 By similarity
Disulfide bond981 ↔ 993 By similarity
Disulfide bond983 ↔ 999 By similarity
Disulfide bond1001 ↔ 1010 By similarity
Disulfide bond1013 ↔ 1026 By similarity
Disulfide bond1029Interchain Probable
Disulfide bond1032Interchain Probable
Disulfide bond1598Interchain (with beta-1 chain)

Experimental info

Sequence conflict2161G → A in AAA39409. Ref.3
Sequence conflict2601E → D Ref.2
Sequence conflict3371S → C in AAA39408. Ref.2
Sequence conflict447 – 4482LR → PS in AAA39408. Ref.2
Sequence conflict5441D → Y in AAA39408. Ref.2
Sequence conflict6621T → S in AAA39408. Ref.2
Sequence conflict8861Missing in AAA39408. Ref.2
Sequence conflict11581Missing in AAA39408. Ref.2
Sequence conflict14341V → A in AAA39408. Ref.2
Sequence conflict14751R → K in CAA28838. Ref.4
Sequence conflict15761D → N in CAA28838. Ref.4

Secondary structure

1 ................................ 1607
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P02468-1 [UniParc].

Last modified July 1, 1989. Version 2.
Checksum: 81B7B08E4869F242

FASTA1,607177,298
        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       1220       1230       1240       1250       1260 
TANETSAEAY NLLLRTLAGE NQTALEIEEL NRKYEQAKNI SQDLEKQAAR VHEEAKRAGD 

      1270       1280       1290       1300       1310       1320 
KAVEIYASVA QLTPVDSEAL ENEANKIKKE AADLDRLIDQ KLKDYEDLRE DMRGKEHEVK 

      1330       1340       1350       1360       1370       1380 
NLLEKGKAEQ QTADQLLARA DAAKALAEEA AKKGRSTLQE ANDILNNLKD FDRRVNDNKT 

      1390       1400       1410       1420       1430       1440 
AAEEALRRIP AINRTIAEAN EKTREAQLAL GNAAADATEA KNKAHEAERI ASAVQKNATS 

      1450       1460       1470       1480       1490       1500 
TKADAERTFG EVTDLDNEVN GMLRQLEEAE NELKRKQDDA DQDMMMAGMA SQAAQEAELN 

      1510       1520       1530       1540       1550       1560 
ARKAKNSVSS LLSQLNNLLD QLGQLDTVDL NKLNEIEGSL NKAKDEMKAS DLDRKVSDLE 

      1570       1580       1590       1600 
SEARKQEAAI MDYNRDIAEI IKDIHNLEDI KKTLPTGCFN TPSIEKP

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References

« Hide 'large scale' references
[1]"The laminin B2 chain has a multidomain structure homologous to the B1 chain."
Sasaki M., Yamada Y.
J. Biol. Chem. 262:17111-17117(1987) [PubMed: 3680290] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Primary structure of the mouse laminin B2 chain and comparison with laminin B1."
Durkin M.E., Bartos B.B., Liu S.-H., Phillips S.L., Chung A.E.
Biochemistry 27:5198-5204(1988) [PubMed: 3167041] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"The laminin B2 chain promoter contains unique repeat sequences and is active in transient transfection."
Ogawa K., Burbelo P.D., Sasaki M., Yamada Y.
J. Biol. Chem. 263:8384-8389(1988) [PubMed: 2836421] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-239.
[4]"Sequencing of laminin B chain cDNAs reveals C-terminal regions of coiled-coil alpha-helix."
Barlow D.P., Green N.M., Kurkinen M., Hogan B.L.M.
EMBO J. 3:2355-2362(1984) [PubMed: 6209134] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1391-1607.
[5]"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
Nat. Biotechnol. 27:378-386(2009) [PubMed: 19349973] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-648; ASN-1105; ASN-1203; ASN-1221 AND ASN-1393, MASS SPECTROMETRY.
[6]"Crystal structure of three consecutive laminin-type epidermal growth factor-like (LE) modules of laminin gamma1 chain harboring the nidogen binding site."
Stetefeld J., Mayer U., Timpl R., Huber R.
J. Mol. Biol. 257:644-657(1996) [PubMed: 8648630] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 771-932.
[7]"Structure of the nidogen binding LE module of the laminin gamma1 chain in solution."
Baumgartner R., Czisch M., Mayer U., Poeschl E., Huber R., Timpl R., Holak T.A.
J. Mol. Biol. 257:658-668(1996) [PubMed: 8648631] [Abstract]
Cited for: STRUCTURE BY NMR OF 824-881.
+Additional computationally mapped references.

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Cross-references

Sequence databases

X05211 mRNA. Translation: CAA28838.1.
J03484 mRNA. Translation: AAA39405.1.
J02930 mRNA. Translation: AAA39408.1.
J03749 Genomic DNA. Translation: AAA39409.1.
IPIIPI00400016.
PIRMMMSB2. A28469.
S55783.
UniGeneMm.1249

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1KLOX-ray2.10A771-932[»]
1NPEX-ray2.30B769-932[»]
1TLENMR-A824-881[»]
ModBaseSearch...

Protein-protein interaction databases

STRINGP02468.

Proteomic databases

PRIDEP02468.

Genome annotation databases

EnsemblENSMUST00000027752; ENSMUSP00000027752; ENSMUSG00000026478; Mus musculus. [Genome view]
UCSCuc007czu.1. mouse.

Organism-specific databases

MGIMGI:99914. Lamc1.

Phylogenomic databases

HOGENOMP02468.
HOVERGENP02468.

Gene expression databases

ArrayExpressP02468.
BgeeP02468.
CleanExMM_LAMC1.
GenevestigatorP02468.
GermOnlineENSMUSG00000026478. Mus musculus.

Family and domain databases

InterProIPR013032. EGF-like_reg_CS.
IPR002049. EGF_laminin.
IPR018031. Laminin_B.
IPR000034. Laminin_B_type_IV.
IPR008211. Laminin_N.
[Graphical view]
PfamPF00052. Laminin_B. 1 hit.
PF00053. Laminin_EGF. 10 hits.
PF00055. Laminin_N. 1 hit.
[Graphical view]
PRINTSPR00011. EGFLAMININ.
ProDomPD003031. Laminin_B. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00180. EGF_Lam. 10 hits.
SM00281. LamB. 1 hit.
SM00136. LamNT. 1 hit.
[Graphical view]
PROSITEPS00022. EGF_1. 8 hits.
PS01186. EGF_2. 2 hits.
PS01248. EGF_LAM_1. 10 hits.
PS50027. EGF_LAM_2. 10 hits.
PS51115. LAMININ_IVA. 1 hit.
PS51117. LAMININ_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

SOURCESearch...

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Entry information

Entry nameLAMC1_MOUSE
AccessionPrimary (citable) accession number: P02468
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 1, 1989
Last modified: October 13, 2009
This is version 108 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents