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Protein

Laminin subunit gamma-2

Gene

Lamc2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

  • heparin binding Source: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Heparin-binding

Enzyme and pathway databases

ReactomeiR-MMU-1474228. Degradation of the extracellular matrix.
R-MMU-3000157. Laminin interactions.

Names & Taxonomyi

Protein namesi
Recommended name:
Laminin subunit gamma-2
Alternative name(s):
Epiligrin subunit gamma
Kalinin subunit gamma
Kalinin/nicein/epiligrin 100 kDa subunit
Laminin B2t chain
Laminin-5 subunit gamma
Nicein subunit gamma
Gene namesi
Name:Lamc2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:99913. Lamc2.

Subcellular locationi

GO - Cellular componenti

  • basement membrane Source: MGI
  • extracellular region Source: Reactome
  • laminin-5 complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Basement membrane, Extracellular matrix, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi76 – 761R → A: No change to herarin-binding. 1 Publication
Mutagenesisi78 – 781R → A: No change to herarin-binding. 1 Publication
Mutagenesisi202 – 2021F → A: No fibulin-1C binding. No change to fibulin-2 binding. 1 Publication
Mutagenesisi206 – 2061K → A: No fibulin-1C binding. No change to fibulin-2 binding. 1 Publication
Mutagenesisi442 – 4421C → S: 20-fold reduction to fibulin-2 binding. 1 Publication
Mutagenesisi445 – 4451C → S: 20-fold reduction to fibulin-2 binding. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence analysisAdd
BLAST
Chaini22 – 11911170Laminin subunit gamma-2PRO_0000017078Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi28 ↔ 37PROSITE-ProRule annotation
Disulfide bondi30 ↔ 53PROSITE-ProRule annotation
Disulfide bondi56 ↔ 65PROSITE-ProRule annotation
Disulfide bondi68 ↔ 81PROSITE-ProRule annotation
Disulfide bondi84 ↔ 96PROSITE-ProRule annotation
Disulfide bondi86 ↔ 102PROSITE-ProRule annotation
Disulfide bondi104 ↔ 113PROSITE-ProRule annotation
Disulfide bondi116 ↔ 128PROSITE-ProRule annotation
Disulfide bondi139 ↔ 150PROSITE-ProRule annotation
Disulfide bondi141 ↔ 155PROSITE-ProRule annotation
Disulfide bondi157 ↔ 166PROSITE-ProRule annotation
Disulfide bondi169 ↔ 184PROSITE-ProRule annotation
Glycosylationi342 – 3421N-linked (GlcNAc...)Sequence analysis
Glycosylationi362 – 3621N-linked (GlcNAc...)Sequence analysis
Disulfide bondi462 ↔ 470PROSITE-ProRule annotation
Disulfide bondi464 ↔ 481PROSITE-ProRule annotation
Disulfide bondi484 ↔ 493PROSITE-ProRule annotation
Disulfide bondi496 ↔ 514PROSITE-ProRule annotation
Disulfide bondi517 ↔ 531PROSITE-ProRule annotation
Disulfide bondi519 ↔ 538PROSITE-ProRule annotation
Glycosylationi526 – 5261N-linked (GlcNAc...)Sequence analysis
Disulfide bondi541 ↔ 550PROSITE-ProRule annotation
Disulfide bondi553 ↔ 570PROSITE-ProRule annotation
Disulfide bondi573 ↔ 585PROSITE-ProRule annotation
Disulfide bondi575 ↔ 591PROSITE-ProRule annotation
Disulfide bondi593 ↔ 602PROSITE-ProRule annotation
Disulfide bondi610 – 610InterchainCurated
Disulfide bondi613 – 613InterchainCurated
Glycosylationi941 – 9411N-linked (GlcNAc...)Sequence analysis
Glycosylationi1032 – 10321N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1182 – 1182Interchain (with beta-3 chain)Curated

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ61092.
PaxDbiQ61092.
PRIDEiQ61092.

PTM databases

PhosphoSiteiQ61092.

Miscellaneous databases

PMAP-CutDBQ61092.

Expressioni

Tissue specificityi

Epithelial cells of many tissues, particularly high levels in tongue, hair follicles and kidney. Basement membranes of the collecting tubules of kidney and pancreas.

Gene expression databases

CleanExiMM_LAMC2.

Interactioni

Subunit structurei

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-2 is a subunit of laminin-5 (laminin-332 or epiligrin/kalinin/nicein). Binds to fibulin-1, fibulin-1c, fibulin-2 and nidogen.

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000027753.

Structurei

3D structure databases

ProteinModelPortaliQ61092.
SMRiQ61092. Positions 517-572.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini28 – 8356Laminin EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini84 – 13047Laminin EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini139 – 18648Laminin EGF-like 3PROSITE-ProRule annotationAdd
BLAST
Domaini187 – 19610Laminin EGF-like 4; first partPROSITE-ProRule annotation
Domaini213 – 381169Laminin IV type APROSITE-ProRule annotationAdd
BLAST
Domaini382 – 41534Laminin EGF-like 4; second partPROSITE-ProRule annotationAdd
BLAST
Domaini416 – 46146Laminin EGF-like 5PROSITE-ProRule annotationAdd
BLAST
Domaini462 – 51655Laminin EGF-like 6PROSITE-ProRule annotationAdd
BLAST
Domaini517 – 57256Laminin EGF-like 7PROSITE-ProRule annotationAdd
BLAST
Domaini573 – 60230Laminin EGF-like 8; truncatedPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni603 – 1191589Domain II and IAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili612 – 71099Sequence analysisAdd
BLAST
Coiled coili759 – 78628Sequence analysisAdd
BLAST
Coiled coili946 – 99651Sequence analysisAdd
BLAST
Coiled coili1139 – 117840Sequence analysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi586 – 5883Cell attachment siteSequence analysis

Domaini

The alpha-helical domains I and II are thought to interact with other laminin chains to form a coiled coil structure.
Domain IV is globular.

Sequence similaritiesi

Contains 8 laminin EGF-like domains.PROSITE-ProRule annotation
Contains 1 laminin IV type A domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Laminin EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiENOG410IP6C. Eukaryota.
ENOG4110QI9. LUCA.
HOGENOMiHOG000019301.
HOVERGENiHBG062127.
InParanoidiQ61092.
PhylomeDBiQ61092.

Family and domain databases

InterProiIPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR002049. Laminin_EGF.
IPR000034. Laminin_IV.
[Graphical view]
PfamiPF00052. Laminin_B. 1 hit.
PF00053. Laminin_EGF. 7 hits.
[Graphical view]
SMARTiSM00181. EGF. 7 hits.
SM00180. EGF_Lam. 7 hits.
SM00281. LamB. 1 hit.
[Graphical view]
PROSITEiPS00022. EGF_1. 4 hits.
PS01186. EGF_2. 2 hits.
PS01248. EGF_LAM_1. 6 hits.
PS50027. EGF_LAM_2. 6 hits.
PS51115. LAMININ_IVA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q61092-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPALWLSCCL GVALLLPAAQ ATSRREVCDC NGKSRQCVFD QELHRQTGSG
60 70 80 90 100
FRCLNCNDNT AGVHCERCRE GFYRHRDRDR CLPCNCHSKG SLSAGCDNSG
110 120 130 140 150
QCRCKPGVTG QRCDRCQPGF HMLTDAGCTR DQGQLDSKCD CDPAGISGPC
160 170 180 190 200
DSGRCVCKPA VTGERCDRCR PGYYHLDRAN PEGCTQCFCY GHSASCHASA
210 220 230 240 250
DFSVHKITST FSQDVDGWKA VQRNGAPAKL HWSQRHRDVF SSARRSDPVY
260 270 280 290 300
FVAPAKFLGN QQVSYGQSLS FDYRVDRGGR QPSAYDVILE GAGLQIRAPL
310 320 330 340 350
MAPGKTLPCG ITKTYTFRLN EHPSSHWSPQ LSYFEYRRLL RNLTALLIRA
360 370 380 390 400
TYGEYSTGYI DNVTLVSARP VSGAPAPWVE RCVCPAGYKG QFCQECASGY
410 420 430 440 450
KRDSARLGPF GACVPCNCQG GGACDPDTGD CYSGDENPDI ECADCPIGFY
460 470 480 490 500
NDPHDPRSCK PCPCHNGFSC SVMPETEEVV CNNCPPGVTG ARCELCADGF
510 520 530 540 550
FGDPFGERGP VRPCQRCQCN NNVDPNASGN CDQLTGRCLK CIYNTAGVYC
560 570 580 590 600
DQCKAGYFGD PLAPNPADKC RACNCSPMGS EPGECRGDGS CVCKPGFGGL
610 620 630 640 650
NCDHAALTSC PACYNQVKIQ MDQFTQQLQS LEALVSKAQG GGGGGTVPVQ
660 670 680 690 700
LEGRIEQAEQ ALQDILGEAQ ISEGAMRAVA VRLAKARSQE NDYKTRLDDL
710 720 730 740 750
KMTAERIRAL GSQHQNRVQD TSRLISQMRL SLAGSEALLE NTNIHSSEHY
760 770 780 790 800
VGPNDFKSLA QEATRKADSH AESANAMKQL ARETEDYSKQ ALSLARKLLS
810 820 830 840 850
GGGGSGSWDS SVVQGLMGKL EKTKSLSQQL SLEGTQADIE ADRSYQHSLR
860 870 880 890 900
LLDSASQLQG VSDLSFQVEA KRIRQKADSL SNLVTRQTDA FTRVRNNLGN
910 920 930 940 950
WEKETRQLLQ TGKDRRQTSD QLLSRANLAK NRAQEALSMG NATFYEVENI
960 970 980 990 1000
LKNLREFDLQ VEDRKAEAEE AMKRLSSISQ KVADASDKTQ QAETALGSAT
1010 1020 1030 1040 1050
ADTQRAKNAA REALEISSEI ELEIGSLNLE ANVTADGALA MEKGTATLKS
1060 1070 1080 1090 1100
EMREMIELAR KELEFDTDKD TVQLVITEAQ QADARATSAG VTIQDTLNTL
1110 1120 1130 1140 1150
DGILHLIDQP GSVDEEGMML LEQGLFQAKT QINSRLRPLM SDLEERVRRQ
1160 1170 1180 1190
RNHLHLLETS IDGILADVKN LENIRDNLPP GCYNTQALEQ Q
Length:1,191
Mass (Da):130,161
Last modified:January 17, 2003 - v2
Checksum:i7016C1F851D909B9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U43327 mRNA. Translation: AAA85256.2.
UniGeneiMm.329272.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U43327 mRNA. Translation: AAA85256.2.
UniGeneiMm.329272.

3D structure databases

ProteinModelPortaliQ61092.
SMRiQ61092. Positions 517-572.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000027753.

PTM databases

PhosphoSiteiQ61092.

Proteomic databases

MaxQBiQ61092.
PaxDbiQ61092.
PRIDEiQ61092.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

MGIiMGI:99913. Lamc2.

Phylogenomic databases

eggNOGiENOG410IP6C. Eukaryota.
ENOG4110QI9. LUCA.
HOGENOMiHOG000019301.
HOVERGENiHBG062127.
InParanoidiQ61092.
PhylomeDBiQ61092.

Enzyme and pathway databases

ReactomeiR-MMU-1474228. Degradation of the extracellular matrix.
R-MMU-3000157. Laminin interactions.

Miscellaneous databases

PMAP-CutDBQ61092.
PROiQ61092.
SOURCEiSearch...

Gene expression databases

CleanExiMM_LAMC2.

Family and domain databases

InterProiIPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR002049. Laminin_EGF.
IPR000034. Laminin_IV.
[Graphical view]
PfamiPF00052. Laminin_B. 1 hit.
PF00053. Laminin_EGF. 7 hits.
[Graphical view]
SMARTiSM00181. EGF. 7 hits.
SM00180. EGF_Lam. 7 hits.
SM00281. LamB. 1 hit.
[Graphical view]
PROSITEiPS00022. EGF_1. 4 hits.
PS01186. EGF_2. 2 hits.
PS01248. EGF_LAM_1. 6 hits.
PS50027. EGF_LAM_2. 6 hits.
PS51115. LAMININ_IVA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and expression of the mouse laminin gamma 2 (B2t) chain, a subunit of epithelial cell laminin."
    Sugiyama S., Utani A., Yamada S., Kozak C.A., Yamada Y.
    Eur. J. Biochem. 228:120-128(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: FVB/NJ.
    Tissue: Lung.
  2. Sasaki T., Yamada Y.
    Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  3. "Short arm region of laminin-5 gamma2 chain: structure, mechanism of processing and binding to heparin and proteins."
    Sasaki T., Goehring W., Mann K., Brakebusch C., Yamada Y., Faessler R., Timpl R.
    J. Mol. Biol. 314:751-763(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HEPARIN; FIBULIN AND NIDOGEN, MUTAGENESIS OF ARG-76; ARG-78; PHE-202; LYS-206; CYS-442 AND CYS-445.
    Strain: FVB/NJ.
    Tissue: Lung.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Lung.

Entry informationi

Entry nameiLAMC2_MOUSE
AccessioniPrimary (citable) accession number: Q61092
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 17, 2003
Last modified: June 8, 2016
This is version 131 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Binds heparin.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.