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Q9R0B6

- LAMC3_MOUSE

UniProt

Q9R0B6 - LAMC3_MOUSE

Protein

Laminin subunit gamma-3

Gene

Lamc3

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 119 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    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

    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

    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

    ArrayExpressiQ9R0B6.
    BgeeiQ9R0B6.
    CleanExiMM_LAMC3.
    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.
    GeneTreeiENSGT00750000117374.
    HOGENOMiHOG000019301.
    HOVERGENiHBG100808.
    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

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    MAVSRVLSLL ATVASMALVI QETHFAAGAD MGSCYDGVGR AQRCLPEFEN     50
    AAFGRRAEAS HTCGRPPEDF CPHVGAPGAG LQCQRCDDAD PGRRHDASYL 100
    TDFHSPDDST WWQSPSMAFG VQYPTSVNLT LSLGKAYEIT YVRLKFHTSR 150
    PESFAIYKRT YASGPWEPYQ YYSASCQKTY GRPEGHYLRP GEDERVAFCT 200
    SEFSDISPLN GGNVAFSTLE GRPSAYNFEE SPVLQEWVTS TDILISLDRL 250
    NTFGDDIFKD PRVLQSYYYA VSDFSVGGRC KCNGHASECE PNAAGQLACR 300
    CQHNTTGVDC ERCLPFFQDR PWARGTAEDA NECLPCNCSG HSEECTFDRE 350
    LYRSTGHGGH CQRCRDHTTG PHCERCEKNY YRWSPKTPCQ PCDCHPAGSL 400
    SLQCDNSGVC PCKPTVTGWK CDRCLPGFHS LSEGGCRPCA CNVAGSLGTC 450
    DPRSGNCPCK ENVEGSLCDR CRPGTFNLQP HNPVGCSSCF CYGHSKVCSP 500
    AAGFQEHHIR SDFRHGAGGW QIRSMGVSKR PLQWSQSGLL LGLRGGEELS 550
    APKKFLGDQR LSYGQPVILT LQVPPGGSPP PIQLRLEGAG LALSLRPSSL 600
    PSPQDTRQPR RVQLQFLLQE TSEEAESPLP TFHFQRLLSN LTALSIWTSG 650
    QGPGHSGQVL LCEVQLTSAW PQRELAPPAS WVETCLCPQG YTGQFCEFCA 700
    LGYKREIPHG GPYANCIPCT CNQHGTCDPN TGICLCGHHT EGPSCERCMP 750
    GFYGNAFSGR ADDCQPCPCP GQSACATIPE SGDVVCTHCP PGQRGRRCES 800
    CEDGFFGDPL GLSGAPQPCR RCQCSGNVDL NAVGNCDPHS GHCLRCLYNT 850
    TGAHCEHCRE GFYGSAVATR PVDKCAPCSC DLRGSVSEKT CNPVTGQCVC 900
    LPYVSGRDCS RCSPGFYDLQ SGRGCQSCKC HPLGSLENKC HPKTGQCPCR 950
    PGVTGQACDR CQLGFFGFSI KGCRDCRCSP LGAASSQCHE NSTCVCRPGF 1000
    VGYKCDRCQD NFFLADGDTG CQECPTCYAL VKEEAAKLKA RLMLMEGWLQ 1050
    RSDCGSPWGP LDILQGEAPL GDVYQGHHLL QETRGTFLQQ MVGLEDSVKA 1100
    TWEQLQVLRG HVHCAQAGAQ KTCIQLAELE ETLQSSEEEV LRAASALSFL 1150
    ASLQKGSSTP TNWSHLASEA QILARSHRDT ATKIEATSER ALLASNASYE 1200
    LLKLMEGRVA SEAQQELEDR YQEVQAAQTA LGIAVAEALP KAEKALATVK 1250
    QVIGDAAPHL GLLVTPEAMN FQARGLSWKV KALEQKLEQK EPEVGQSVGA 1300
    LQVEAGRALE KMEPFMQLRN KTTAAFTRAS SAVQAAKVTV IGAETLLADL 1350
    EGMKLRSPLP KEQAALKKKA GSIRTRLLED TKRKTKQAER MLGNAASLSS 1400
    STKKKSKEAE LMSKDNAKLS RALLREGKQG YRHASRLASQ TQATLRRASR 1450
    LLLTSEAHKQ ELEEAKQVTS GLSTVERQIR ESRISLEKDT KVLSELLVKL 1500
    GSLGVHQAPA QTLNETQRAL ESLRLQLDSH GALHHKLRQL EEESARQELQ 1550
    IQSFEDDLAE IRADKHNLET ILSSLPENCA S 1581
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 ENSGT00750000117374.
    HOGENOMi HOG000019301.
    HOVERGENi HBG100808.
    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

    ArrayExpressi Q9R0B6.
    Bgeei Q9R0B6.
    CleanExi MM_LAMC3.
    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

    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 1, 2014
    This is version 119 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