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Protein

Laminin subunit gamma-3

Gene

Lamc3

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 - Biological processi

  • astrocyte development Source: MGI
  • cell adhesion Source: UniProtKB-KW
  • cell morphogenesis involved in differentiation Source: MGI
  • extracellular matrix organization Source: Reactome
  • retina development in camera-type eye Source: MGI
  • visual perception Source: MGI
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Enzyme and pathway databases

ReactomeiR-MMU-3000157. Laminin interactions.
R-MMU-3000171. Non-integrin membrane-ECM interactions.
R-MMU-8874081. MET activates PTK2 signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Laminin subunit gamma-3
Alternative name(s):
Laminin-12 subunit gamma
Laminin-14 subunit gamma
Laminin-15 subunit gamma
Gene namesi
Name:Lamc3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1344394. Lamc3.

Subcellular locationi

GO - Cellular componenti

  • basement membrane Source: MGI
  • extracellular region Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Basement membrane, Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 28Sequence analysisAdd BLAST28
ChainiPRO_000001708029 – 1581Laminin subunit gamma-3Add BLAST1553

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi128N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi280 ↔ 289PROSITE-ProRule annotation
Disulfide bondi282 ↔ 299PROSITE-ProRule annotation
Disulfide bondi301 ↔ 310PROSITE-ProRule annotation
Glycosylationi304N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi313 ↔ 333PROSITE-ProRule annotation
Disulfide bondi336 ↔ 345PROSITE-ProRule annotation
Glycosylationi337N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi338 ↔ 361PROSITE-ProRule annotation
Disulfide bondi364 ↔ 373PROSITE-ProRule annotation
Disulfide bondi376 ↔ 389PROSITE-ProRule annotation
Disulfide bondi392 ↔ 404PROSITE-ProRule annotation
Disulfide bondi394 ↔ 410PROSITE-ProRule annotation
Disulfide bondi412 ↔ 421PROSITE-ProRule annotation
Disulfide bondi424 ↔ 436PROSITE-ProRule annotation
Disulfide bondi439 ↔ 450PROSITE-ProRule annotation
Disulfide bondi441 ↔ 457PROSITE-ProRule annotation
Disulfide bondi459 ↔ 468PROSITE-ProRule annotation
Disulfide bondi471 ↔ 486PROSITE-ProRule annotation
Glycosylationi640N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi719 ↔ 727PROSITE-ProRule annotation
Disulfide bondi721 ↔ 734PROSITE-ProRule annotation
Disulfide bondi736 ↔ 745PROSITE-ProRule annotation
Disulfide bondi748 ↔ 764PROSITE-ProRule annotation
Disulfide bondi767 ↔ 775PROSITE-ProRule annotation
Disulfide bondi769 ↔ 786PROSITE-ProRule annotation
Disulfide bondi789 ↔ 798PROSITE-ProRule annotation
Disulfide bondi801 ↔ 819PROSITE-ProRule annotation
Disulfide bondi822 ↔ 836PROSITE-ProRule annotation
Disulfide bondi824 ↔ 843PROSITE-ProRule annotation
Disulfide bondi846 ↔ 855PROSITE-ProRule annotation
Glycosylationi849N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi858 ↔ 875PROSITE-ProRule annotation
Disulfide bondi878 ↔ 891PROSITE-ProRule annotation
Disulfide bondi880 ↔ 898PROSITE-ProRule annotation
Disulfide bondi900 ↔ 909PROSITE-ProRule annotation
Disulfide bondi912 ↔ 925PROSITE-ProRule annotation
Disulfide bondi928 ↔ 940PROSITE-ProRule annotation
Disulfide bondi930 ↔ 947PROSITE-ProRule annotation
Disulfide bondi949 ↔ 958PROSITE-ProRule annotation
Disulfide bondi961 ↔ 973PROSITE-ProRule annotation
Disulfide bondi976 ↔ 988PROSITE-ProRule annotation
Disulfide bondi978 ↔ 994PROSITE-ProRule annotation
Glycosylationi991N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi996 ↔ 1005PROSITE-ProRule annotation
Disulfide bondi1008 ↔ 1021PROSITE-ProRule annotation
Glycosylationi1162N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1196N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1320N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1514N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ9R0B6.
PaxDbiQ9R0B6.
PRIDEiQ9R0B6.

PTM databases

iPTMnetiQ9R0B6.
PhosphoSitePlusiQ9R0B6.

Expressioni

Tissue specificityi

Strongly expressed in capillaries and arterioles of kidney as well as in interstitial Leydig cells of testis.

Gene expression databases

BgeeiENSMUSG00000026840.
CleanExiMM_LAMC3.
ExpressionAtlasiQ9R0B6. baseline and differential.
GenevisibleiQ9R0B6. MM.

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-3 is a subunit of laminin-12 (laminin-213), laminin-14 (laminin-423) and laminin-15 (laminin-523).

Protein-protein interaction databases

BioGridi204801. 1 interactor.
STRINGi10090.ENSMUSP00000028187.

Structurei

3D structure databases

ProteinModelPortaliQ9R0B6.
SMRiQ9R0B6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini40 – 279Laminin N-terminalPROSITE-ProRule annotationAdd BLAST240
Domaini280 – 335Laminin EGF-like 1PROSITE-ProRule annotationAdd BLAST56
Domaini336 – 391Laminin EGF-like 2PROSITE-ProRule annotationAdd BLAST56
Domaini392 – 438Laminin EGF-like 3PROSITE-ProRule annotationAdd BLAST47
Domaini439 – 488Laminin EGF-like 4PROSITE-ProRule annotationAdd BLAST50
Domaini489 – 498Laminin EGF-like 5; first partPROSITE-ProRule annotation10
Domaini508 – 684Laminin IV type APROSITE-ProRule annotationAdd BLAST177
Domaini685 – 718Laminin EGF-like 5; second partPROSITE-ProRule annotationAdd BLAST34
Domaini719 – 766Laminin EGF-like 6PROSITE-ProRule annotationAdd BLAST48
Domaini767 – 821Laminin EGF-like 7PROSITE-ProRule annotationAdd BLAST55
Domaini822 – 877Laminin EGF-like 8PROSITE-ProRule annotationAdd BLAST56
Domaini878 – 927Laminin EGF-like 9PROSITE-ProRule annotationAdd BLAST50
Domaini928 – 975Laminin EGF-like 10PROSITE-ProRule annotationAdd BLAST48
Domaini976 – 1024Laminin EGF-like 11PROSITE-ProRule annotationAdd BLAST49

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1025 – 1581Domain II and IAdd BLAST557

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili1029 – 1046Sequence analysisAdd BLAST18
Coiled coili1112 – 1153Sequence analysisAdd BLAST42
Coiled coili1208 – 1231Sequence analysisAdd BLAST24
Coiled coili1438 – 1468Sequence analysisAdd BLAST31
Coiled coili1510 – 1575Sequence analysisAdd BLAST66

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 11 laminin EGF-like domains.PROSITE-ProRule annotation
Contains 1 laminin IV type A domain.PROSITE-ProRule annotation
Contains 1 laminin N-terminal domain.PROSITE-ProRule annotation

Keywords - Domaini

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

Phylogenomic databases

eggNOGiKOG1836. Eukaryota.
ENOG410XRDC. LUCA.
GeneTreeiENSGT00780000121851.
HOGENOMiHOG000019301.
HOVERGENiHBG100808.
InParanoidiQ9R0B6.
KOiK06247.
OMAiAGCSSCF.
OrthoDBiEOG091G005L.
TreeFamiTF352481.

Family and domain databases

Gene3Di2.60.120.260. 1 hit.
InterProiIPR000742. EGF-like_dom.
IPR008979. Galactose-bd-like.
IPR002049. Laminin_EGF.
IPR000034. Laminin_IV.
IPR008211. Laminin_N.
[Graphical view]
PfamiPF00052. Laminin_B. 1 hit.
PF00053. Laminin_EGF. 11 hits.
PF00055. Laminin_N. 1 hit.
[Graphical view]
SMARTiSM00181. EGF. 6 hits.
SM00180. EGF_Lam. 11 hits.
SM00281. LamB. 1 hit.
SM00136. LamNT. 1 hit.
[Graphical view]
PROSITEiPS00022. EGF_1. 8 hits.
PS01186. EGF_2. 2 hits.
PS01248. EGF_LAM_1. 11 hits.
PS50027. EGF_LAM_2. 10 hits.
PS51115. LAMININ_IVA. 1 hit.
PS51117. LAMININ_NTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9R0B6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVSRVLSLL ATVASMALVI QETHFAAGAD MGSCYDGVGR AQRCLPEFEN
60 70 80 90 100
AAFGRRAEAS HTCGRPPEDF CPHVGAPGAG LQCQRCDDAD PGRRHDASYL
110 120 130 140 150
TDFHSPDDST WWQSPSMAFG VQYPTSVNLT LSLGKAYEIT YVRLKFHTSR
160 170 180 190 200
PESFAIYKRT YASGPWEPYQ YYSASCQKTY GRPEGHYLRP GEDERVAFCT
210 220 230 240 250
SEFSDISPLN GGNVAFSTLE GRPSAYNFEE SPVLQEWVTS TDILISLDRL
260 270 280 290 300
NTFGDDIFKD PRVLQSYYYA VSDFSVGGRC KCNGHASECE PNAAGQLACR
310 320 330 340 350
CQHNTTGVDC ERCLPFFQDR PWARGTAEDA NECLPCNCSG HSEECTFDRE
360 370 380 390 400
LYRSTGHGGH CQRCRDHTTG PHCERCEKNY YRWSPKTPCQ PCDCHPAGSL
410 420 430 440 450
SLQCDNSGVC PCKPTVTGWK CDRCLPGFHS LSEGGCRPCA CNVAGSLGTC
460 470 480 490 500
DPRSGNCPCK ENVEGSLCDR CRPGTFNLQP HNPVGCSSCF CYGHSKVCSP
510 520 530 540 550
AAGFQEHHIR SDFRHGAGGW QIRSMGVSKR PLQWSQSGLL LGLRGGEELS
560 570 580 590 600
APKKFLGDQR LSYGQPVILT LQVPPGGSPP PIQLRLEGAG LALSLRPSSL
610 620 630 640 650
PSPQDTRQPR RVQLQFLLQE TSEEAESPLP TFHFQRLLSN LTALSIWTSG
660 670 680 690 700
QGPGHSGQVL LCEVQLTSAW PQRELAPPAS WVETCLCPQG YTGQFCEFCA
710 720 730 740 750
LGYKREIPHG GPYANCIPCT CNQHGTCDPN TGICLCGHHT EGPSCERCMP
760 770 780 790 800
GFYGNAFSGR ADDCQPCPCP GQSACATIPE SGDVVCTHCP PGQRGRRCES
810 820 830 840 850
CEDGFFGDPL GLSGAPQPCR RCQCSGNVDL NAVGNCDPHS GHCLRCLYNT
860 870 880 890 900
TGAHCEHCRE GFYGSAVATR PVDKCAPCSC DLRGSVSEKT CNPVTGQCVC
910 920 930 940 950
LPYVSGRDCS RCSPGFYDLQ SGRGCQSCKC HPLGSLENKC HPKTGQCPCR
960 970 980 990 1000
PGVTGQACDR CQLGFFGFSI KGCRDCRCSP LGAASSQCHE NSTCVCRPGF
1010 1020 1030 1040 1050
VGYKCDRCQD NFFLADGDTG CQECPTCYAL VKEEAAKLKA RLMLMEGWLQ
1060 1070 1080 1090 1100
RSDCGSPWGP LDILQGEAPL GDVYQGHHLL QETRGTFLQQ MVGLEDSVKA
1110 1120 1130 1140 1150
TWEQLQVLRG HVHCAQAGAQ KTCIQLAELE ETLQSSEEEV LRAASALSFL
1160 1170 1180 1190 1200
ASLQKGSSTP TNWSHLASEA QILARSHRDT ATKIEATSER ALLASNASYE
1210 1220 1230 1240 1250
LLKLMEGRVA SEAQQELEDR YQEVQAAQTA LGIAVAEALP KAEKALATVK
1260 1270 1280 1290 1300
QVIGDAAPHL GLLVTPEAMN FQARGLSWKV KALEQKLEQK EPEVGQSVGA
1310 1320 1330 1340 1350
LQVEAGRALE KMEPFMQLRN KTTAAFTRAS SAVQAAKVTV IGAETLLADL
1360 1370 1380 1390 1400
EGMKLRSPLP KEQAALKKKA GSIRTRLLED TKRKTKQAER MLGNAASLSS
1410 1420 1430 1440 1450
STKKKSKEAE LMSKDNAKLS RALLREGKQG YRHASRLASQ TQATLRRASR
1460 1470 1480 1490 1500
LLLTSEAHKQ ELEEAKQVTS GLSTVERQIR ESRISLEKDT KVLSELLVKL
1510 1520 1530 1540 1550
GSLGVHQAPA QTLNETQRAL ESLRLQLDSH GALHHKLRQL EEESARQELQ
1560 1570 1580
IQSFEDDLAE IRADKHNLET ILSSLPENCA S
Length:1,581
Mass (Da):172,322
Last modified:July 27, 2011 - v2
Checksum:iA6E83A8F9C678830
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti9L → F in AAD29851 (PubMed:10318827).Curated1
Sequence conflicti190P → T in AAD29851 (PubMed:10318827).Curated1
Sequence conflicti195R → K in AAD29851 (PubMed:10318827).Curated1
Sequence conflicti221G → S in AAD29851 (PubMed:10318827).Curated1
Sequence conflicti394C → R in AAD29851 (PubMed:10318827).Curated1
Sequence conflicti471C → Y in AAD29851 (PubMed:10318827).Curated1
Sequence conflicti1150L → LDEPQLFSLLLK in AAD29851 (PubMed:10318827).Curated1
Sequence conflicti1387Q → H in AAF08983 (Ref. 1) Curated1
Sequence conflicti1438 – 1439AS → TI in AAD29851 (PubMed:10318827).Curated2
Sequence conflicti1479I → V in AAF08983 (Ref. 1) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF083372 mRNA. Translation: AAF08983.1.
AL928893, BX511243 Genomic DNA. Translation: CAM26043.1.
BX511243, AL928893 Genomic DNA. Translation: CAM26482.1.
CH466542 Genomic DNA. Translation: EDL08519.1.
BC096366 mRNA. Translation: AAH96366.1.
AF079520 mRNA. Translation: AAD29851.1.
CCDSiCCDS15903.1.
RefSeqiNP_035966.2. NM_011836.3.
UniGeneiMm.302362.

Genome annotation databases

EnsembliENSMUST00000028187; ENSMUSP00000028187; ENSMUSG00000026840.
GeneIDi23928.
KEGGimmu:23928.
UCSCiuc008jef.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF083372 mRNA. Translation: AAF08983.1.
AL928893, BX511243 Genomic DNA. Translation: CAM26043.1.
BX511243, AL928893 Genomic DNA. Translation: CAM26482.1.
CH466542 Genomic DNA. Translation: EDL08519.1.
BC096366 mRNA. Translation: AAH96366.1.
AF079520 mRNA. Translation: AAD29851.1.
CCDSiCCDS15903.1.
RefSeqiNP_035966.2. NM_011836.3.
UniGeneiMm.302362.

3D structure databases

ProteinModelPortaliQ9R0B6.
SMRiQ9R0B6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204801. 1 interactor.
STRINGi10090.ENSMUSP00000028187.

PTM databases

iPTMnetiQ9R0B6.
PhosphoSitePlusiQ9R0B6.

Proteomic databases

MaxQBiQ9R0B6.
PaxDbiQ9R0B6.
PRIDEiQ9R0B6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000028187; ENSMUSP00000028187; ENSMUSG00000026840.
GeneIDi23928.
KEGGimmu:23928.
UCSCiuc008jef.1. mouse.

Organism-specific databases

CTDi10319.
MGIiMGI:1344394. Lamc3.

Phylogenomic databases

eggNOGiKOG1836. Eukaryota.
ENOG410XRDC. LUCA.
GeneTreeiENSGT00780000121851.
HOGENOMiHOG000019301.
HOVERGENiHBG100808.
InParanoidiQ9R0B6.
KOiK06247.
OMAiAGCSSCF.
OrthoDBiEOG091G005L.
TreeFamiTF352481.

Enzyme and pathway databases

ReactomeiR-MMU-3000157. Laminin interactions.
R-MMU-3000171. Non-integrin membrane-ECM interactions.
R-MMU-8874081. MET activates PTK2 signaling.

Miscellaneous databases

PROiQ9R0B6.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000026840.
CleanExiMM_LAMC3.
ExpressionAtlasiQ9R0B6. baseline and differential.
GenevisibleiQ9R0B6. MM.

Family and domain databases

Gene3Di2.60.120.260. 1 hit.
InterProiIPR000742. EGF-like_dom.
IPR008979. Galactose-bd-like.
IPR002049. Laminin_EGF.
IPR000034. Laminin_IV.
IPR008211. Laminin_N.
[Graphical view]
PfamiPF00052. Laminin_B. 1 hit.
PF00053. Laminin_EGF. 11 hits.
PF00055. Laminin_N. 1 hit.
[Graphical view]
SMARTiSM00181. EGF. 6 hits.
SM00180. EGF_Lam. 11 hits.
SM00281. LamB. 1 hit.
SM00136. LamNT. 1 hit.
[Graphical view]
PROSITEiPS00022. EGF_1. 8 hits.
PS01186. EGF_2. 2 hits.
PS01248. EGF_LAM_1. 11 hits.
PS50027. EGF_LAM_2. 10 hits.
PS51115. LAMININ_IVA. 1 hit.
PS51117. LAMININ_NTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiLAMC3_MOUSE
AccessioniPrimary (citable) accession number: Q9R0B6
Secondary accession number(s): Q4VAI3, Q9WTW6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 13, 2001
Last sequence update: July 27, 2011
Last modified: November 30, 2016
This is version 134 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.