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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)DescriptionActionsGraphical viewLength
Mutagenesisi76R → A: No change to herarin-binding. 1 Publication1
Mutagenesisi78R → A: No change to herarin-binding. 1 Publication1
Mutagenesisi202F → A: No fibulin-1C binding. No change to fibulin-2 binding. 1 Publication1
Mutagenesisi206K → A: No fibulin-1C binding. No change to fibulin-2 binding. 1 Publication1
Mutagenesisi442C → S: 20-fold reduction to fibulin-2 binding. 1 Publication1
Mutagenesisi445C → S: 20-fold reduction to fibulin-2 binding. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 21Sequence analysisAdd BLAST21
ChainiPRO_000001707822 – 1191Laminin subunit gamma-2Add BLAST1170

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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
Glycosylationi342N-linked (GlcNAc...)Sequence analysis1
Glycosylationi362N-linked (GlcNAc...)Sequence analysis1
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
Glycosylationi526N-linked (GlcNAc...)Sequence analysis1
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 bondi610InterchainCurated
Disulfide bondi613InterchainCurated
Glycosylationi941N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1032N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1182Interchain (with beta-3 chain)Curated

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ61092.
PaxDbiQ61092.
PRIDEiQ61092.

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.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini28 – 83Laminin EGF-like 1PROSITE-ProRule annotationAdd BLAST56
Domaini84 – 130Laminin EGF-like 2PROSITE-ProRule annotationAdd BLAST47
Domaini139 – 186Laminin EGF-like 3PROSITE-ProRule annotationAdd BLAST48
Domaini187 – 196Laminin EGF-like 4; first partPROSITE-ProRule annotation10
Domaini213 – 381Laminin IV type APROSITE-ProRule annotationAdd BLAST169
Domaini382 – 415Laminin EGF-like 4; second partPROSITE-ProRule annotationAdd BLAST34
Domaini416 – 461Laminin EGF-like 5PROSITE-ProRule annotationAdd BLAST46
Domaini462 – 516Laminin EGF-like 6PROSITE-ProRule annotationAdd BLAST55
Domaini517 – 572Laminin EGF-like 7PROSITE-ProRule annotationAdd BLAST56
Domaini573 – 602Laminin EGF-like 8; truncatedPROSITE-ProRule annotationAdd BLAST30

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni603 – 1191Domain II and IAdd BLAST589

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili612 – 710Sequence analysisAdd BLAST99
Coiled coili759 – 786Sequence analysisAdd BLAST28
Coiled coili946 – 996Sequence analysisAdd BLAST51
Coiled coili1139 – 1178Sequence analysisAdd BLAST40

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi586 – 588Cell attachment siteSequence analysis3

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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000027753.

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...

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: November 30, 2016
This is version 135 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.