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Q9R0B6

- LAMC3_MOUSE

UniProt

Q9R0B6 - LAMC3_MOUSE

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Protein

Laminin subunit gamma-3

Gene

Lamc3

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

  1. astrocyte development Source: MGI
  2. cell adhesion Source: UniProtKB-KW
  3. cell morphogenesis involved in differentiation Source: MGI
  4. retina development in camera-type eye Source: MGI
  5. visual perception Source: MGI
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Enzyme and pathway databases

ReactomeiREACT_196607. Non-integrin membrane-ECM interactions.
REACT_202342. Laminin interactions.

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
ProteomesiUP000000589: Chromosome 2

Organism-specific databases

MGIiMGI:1344394. Lamc3.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Basement membrane, Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2828Sequence AnalysisAdd
BLAST
Chaini29 – 15811553Laminin subunit gamma-3PRO_0000017080Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi128 – 1281N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi280 ↔ 289PROSITE-ProRule annotation
Disulfide bondi282 ↔ 299PROSITE-ProRule annotation
Disulfide bondi301 ↔ 310PROSITE-ProRule annotation
Glycosylationi304 – 3041N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi313 ↔ 333PROSITE-ProRule annotation
Disulfide bondi336 ↔ 345PROSITE-ProRule annotation
Glycosylationi337 – 3371N-linked (GlcNAc...)Sequence Analysis
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
Glycosylationi640 – 6401N-linked (GlcNAc...)Sequence Analysis
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
Glycosylationi849 – 8491N-linked (GlcNAc...)Sequence Analysis
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
Glycosylationi991 – 9911N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi996 ↔ 1005PROSITE-ProRule annotation
Disulfide bondi1008 ↔ 1021PROSITE-ProRule annotation
Glycosylationi1162 – 11621N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1196 – 11961N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1320 – 13201N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1514 – 15141N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ9R0B6.
PRIDEiQ9R0B6.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiQ9R0B6.
CleanExiMM_LAMC3.
ExpressionAtlasiQ9R0B6. baseline and differential.
GenevestigatoriQ9R0B6.

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 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ9R0B6.
SMRiQ9R0B6. Positions 34-391.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini40 – 279240Laminin N-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini280 – 33556Laminin EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini336 – 39156Laminin EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini392 – 43847Laminin EGF-like 3PROSITE-ProRule annotationAdd
BLAST
Domaini439 – 48850Laminin EGF-like 4PROSITE-ProRule annotationAdd
BLAST
Domaini489 – 49810Laminin EGF-like 5; first partPROSITE-ProRule annotation
Domaini508 – 684177Laminin IV type APROSITE-ProRule annotationAdd
BLAST
Domaini685 – 71834Laminin EGF-like 5; second partPROSITE-ProRule annotationAdd
BLAST
Domaini719 – 76648Laminin EGF-like 6PROSITE-ProRule annotationAdd
BLAST
Domaini767 – 82155Laminin EGF-like 7PROSITE-ProRule annotationAdd
BLAST
Domaini822 – 87756Laminin EGF-like 8PROSITE-ProRule annotationAdd
BLAST
Domaini878 – 92750Laminin EGF-like 9PROSITE-ProRule annotationAdd
BLAST
Domaini928 – 97548Laminin EGF-like 10PROSITE-ProRule annotationAdd
BLAST
Domaini976 – 102449Laminin EGF-like 11PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1025 – 1581557Domain II and IAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1029 – 104618Sequence AnalysisAdd
BLAST
Coiled coili1112 – 115342Sequence AnalysisAdd
BLAST
Coiled coili1208 – 123124Sequence AnalysisAdd
BLAST
Coiled coili1438 – 146831Sequence AnalysisAdd
BLAST
Coiled coili1510 – 157566Sequence AnalysisAdd
BLAST

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

eggNOGiNOG235720.
GeneTreeiENSGT00760000118860.
HOGENOMiHOG000019301.
HOVERGENiHBG100808.
InParanoidiQ9R0B6.
KOiK06247.
OMAiQRGRRCE.
TreeFamiTF352481.

Family and domain databases

Gene3Di2.60.120.260. 1 hit.
InterProiIPR002049. EGF_laminin.
IPR008979. Galactose-bd-like.
IPR000034. Laminin_B_type_IV.
IPR008211. Laminin_N.
[Graphical view]
PfamiPF00052. Laminin_B. 1 hit.
PF00053. Laminin_EGF. 10 hits.
PF00055. Laminin_N. 1 hit.
[Graphical view]
SMARTiSM00180. EGF_Lam. 10 hits.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti9 – 91L → F in AAD29851. (PubMed:10318827)Curated
Sequence conflicti190 – 1901P → T in AAD29851. (PubMed:10318827)Curated
Sequence conflicti195 – 1951R → K in AAD29851. (PubMed:10318827)Curated
Sequence conflicti221 – 2211G → S in AAD29851. (PubMed:10318827)Curated
Sequence conflicti394 – 3941C → R in AAD29851. (PubMed:10318827)Curated
Sequence conflicti471 – 4711C → Y in AAD29851. (PubMed:10318827)Curated
Sequence conflicti1150 – 11501L → LDEPQLFSLLLK in AAD29851. (PubMed:10318827)Curated
Sequence conflicti1387 – 13871Q → H in AAF08983. 1 PublicationCurated
Sequence conflicti1438 – 14392AS → TI in AAD29851. (PubMed:10318827)Curated
Sequence conflicti1479 – 14791I → V in AAF08983. 1 PublicationCurated

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 .
CCDSi CCDS15903.1.
RefSeqi NP_035966.2. NM_011836.3.
UniGenei Mm.302362.

3D structure databases

ProteinModelPortali Q9R0B6.
SMRi Q9R0B6. Positions 34-391.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 204801. 1 interaction.

Proteomic databases

PaxDbi Q9R0B6.
PRIDEi Q9R0B6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000028187 ; ENSMUSP00000028187 ; ENSMUSG00000026840 .
GeneIDi 23928.
KEGGi mmu:23928.
UCSCi uc008jef.1. mouse.

Organism-specific databases

CTDi 10319.
MGIi MGI:1344394. Lamc3.

Phylogenomic databases

eggNOGi NOG235720.
GeneTreei ENSGT00760000118860.
HOGENOMi HOG000019301.
HOVERGENi HBG100808.
InParanoidi Q9R0B6.
KOi K06247.
OMAi QRGRRCE.
TreeFami TF352481.

Enzyme and pathway databases

Reactomei REACT_196607. Non-integrin membrane-ECM interactions.
REACT_202342. Laminin interactions.

Miscellaneous databases

NextBioi 303725.
PROi Q9R0B6.
SOURCEi Search...

Gene expression databases

Bgeei Q9R0B6.
CleanExi MM_LAMC3.
ExpressionAtlasi Q9R0B6. baseline and differential.
Genevestigatori Q9R0B6.

Family and domain databases

Gene3Di 2.60.120.260. 1 hit.
InterProi IPR002049. EGF_laminin.
IPR008979. Galactose-bd-like.
IPR000034. Laminin_B_type_IV.
IPR008211. Laminin_N.
[Graphical view ]
Pfami PF00052. Laminin_B. 1 hit.
PF00053. Laminin_EGF. 10 hits.
PF00055. Laminin_N. 1 hit.
[Graphical view ]
SMARTi SM00180. EGF_Lam. 10 hits.
SM00136. LamNT. 1 hit.
[Graphical view ]
PROSITEi PS00022. 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Mouse laminin 12 gamma 3 chain."
    Albus A.M., Burgeson B., Champliaud M.-F., Koch M., Olson P.
    Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Mammary tumor.
  5. "Molecular cloning and tissue-specific expression of a novel murine laminin gamma3 chain."
    Iivanainen A., Morita T., Tryggvason K.
    J. Biol. Chem. 274:14107-14111(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-1526.

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: October 29, 2014
This is version 120 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

External Data

Dasty 3