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Q9Y6N6

- LAMC3_HUMAN

UniProt

Q9Y6N6 - LAMC3_HUMAN

Protein

Laminin subunit gamma-3

Gene

LAMC3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 3 (05 Oct 2010)
      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 - Molecular functioni

    1. structural molecule activity Source: ProtInc

    GO - Biological processi

    1. astrocyte development Source: Ensembl
    2. cell adhesion Source: UniProtKB-KW
    3. cell morphogenesis involved in differentiation Source: Ensembl
    4. extracellular matrix organization Source: Reactome
    5. retina development in camera-type eye Source: Ensembl
    6. visual perception Source: Ensembl

    Keywords - Biological processi

    Cell adhesion

    Enzyme and pathway databases

    ReactomeiREACT_163874. Non-integrin membrane-ECM interactions.
    REACT_169262. 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
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:6494. LAMC3.

    Subcellular locationi

    GO - Cellular componenti

    1. basement membrane Source: UniProtKB-SubCell
    2. extracellular region Source: Reactome
    3. membrane Source: ProtInc
    4. proteinaceous extracellular matrix Source: ProtInc

    Keywords - Cellular componenti

    Basement membrane, Extracellular matrix, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Cortical malformations occipital (OCCM) [MIM:614115]: A disease in which affected individuals develop seizures, sometimes associated with transient visual changes. Brain MRI shows both pachygyria and polymicrogyria restricted to the lateral occipital lobes.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti350 – 3501G → R in OCCM. 1 Publication
    VAR_066404

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi614115. phenotype.
    Orphaneti280640. Occipital pachygyria and polymicrogyria.
    PharmGKBiPA30282.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1919Sequence AnalysisAdd
    BLAST
    Chaini20 – 15751556Laminin subunit gamma-3PRO_0000017079Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi87 – 871N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi119 – 1191N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi271 ↔ 280PROSITE-ProRule annotation
    Disulfide bondi273 ↔ 290PROSITE-ProRule annotation
    Disulfide bondi292 ↔ 301PROSITE-ProRule annotation
    Glycosylationi295 – 2951N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi304 ↔ 324PROSITE-ProRule annotation
    Disulfide bondi327 ↔ 336PROSITE-ProRule annotation
    Glycosylationi328 – 3281N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi329 ↔ 352PROSITE-ProRule annotation
    Disulfide bondi355 ↔ 364PROSITE-ProRule annotation
    Disulfide bondi367 ↔ 380PROSITE-ProRule annotation
    Disulfide bondi383 ↔ 395PROSITE-ProRule annotation
    Disulfide bondi385 ↔ 401PROSITE-ProRule annotation
    Disulfide bondi403 ↔ 412PROSITE-ProRule annotation
    Disulfide bondi415 ↔ 427PROSITE-ProRule annotation
    Disulfide bondi430 ↔ 441PROSITE-ProRule annotation
    Disulfide bondi432 ↔ 448PROSITE-ProRule annotation
    Disulfide bondi450 ↔ 459PROSITE-ProRule annotation
    Disulfide bondi462 ↔ 477PROSITE-ProRule annotation
    Glycosylationi631 – 6311N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi707 ↔ 715PROSITE-ProRule annotation
    Disulfide bondi709 ↔ 722PROSITE-ProRule annotation
    Disulfide bondi724 ↔ 733PROSITE-ProRule annotation
    Disulfide bondi736 ↔ 752PROSITE-ProRule annotation
    Disulfide bondi755 ↔ 763PROSITE-ProRule annotation
    Disulfide bondi757 ↔ 774PROSITE-ProRule annotation
    Disulfide bondi777 ↔ 786PROSITE-ProRule annotation
    Disulfide bondi789 ↔ 807PROSITE-ProRule annotation
    Disulfide bondi810 ↔ 824PROSITE-ProRule annotation
    Disulfide bondi812 ↔ 831PROSITE-ProRule annotation
    Disulfide bondi834 ↔ 843PROSITE-ProRule annotation
    Glycosylationi837 – 8371N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi846 ↔ 863PROSITE-ProRule annotation
    Disulfide bondi866 ↔ 880PROSITE-ProRule annotation
    Disulfide bondi868 ↔ 887PROSITE-ProRule annotation
    Disulfide bondi889 ↔ 898PROSITE-ProRule annotation
    Disulfide bondi901 ↔ 914PROSITE-ProRule annotation
    Disulfide bondi917 ↔ 929PROSITE-ProRule annotation
    Disulfide bondi919 ↔ 936PROSITE-ProRule annotation
    Disulfide bondi938 ↔ 947PROSITE-ProRule annotation
    Disulfide bondi950 ↔ 962PROSITE-ProRule annotation
    Disulfide bondi965 ↔ 977PROSITE-ProRule annotation
    Disulfide bondi967 ↔ 983PROSITE-ProRule annotation
    Glycosylationi980 – 9801N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi985 ↔ 994PROSITE-ProRule annotation
    Disulfide bondi997 ↔ 1010PROSITE-ProRule annotation
    Glycosylationi1185 – 11851N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiQ9Y6N6.
    PaxDbiQ9Y6N6.
    PRIDEiQ9Y6N6.

    Expressioni

    Tissue specificityi

    Broadly expressed in: skin, heart, lung, and the reproductive tracts.

    Gene expression databases

    ArrayExpressiQ9Y6N6.
    BgeeiQ9Y6N6.
    CleanExiHS_LAMC3.
    GenevestigatoriQ9Y6N6.

    Organism-specific databases

    HPAiHPA022814.

    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

    BioGridi115603. 21 interactions.
    IntActiQ9Y6N6. 21 interactions.
    MINTiMINT-7034525.
    STRINGi9606.ENSP00000354360.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9Y6N6.
    SMRiQ9Y6N6. Positions 25-482, 662-1016.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini31 – 270240Laminin N-terminalPROSITE-ProRule annotationAdd
    BLAST
    Domaini271 – 32656Laminin EGF-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini327 – 38256Laminin EGF-like 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini383 – 42947Laminin EGF-like 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini430 – 47950Laminin EGF-like 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini480 – 48910Laminin EGF-like 5; first partPROSITE-ProRule annotation
    Domaini499 – 672174Laminin IV type APROSITE-ProRule annotationAdd
    BLAST
    Domaini673 – 70634Laminin EGF-like 5; second partPROSITE-ProRule annotationAdd
    BLAST
    Domaini707 – 75448Laminin EGF-like 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini755 – 80955Laminin EGF-like 7PROSITE-ProRule annotationAdd
    BLAST
    Domaini810 – 86556Laminin EGF-like 8PROSITE-ProRule annotationAdd
    BLAST
    Domaini866 – 91651Laminin EGF-like 9PROSITE-ProRule annotationAdd
    BLAST
    Domaini917 – 96448Laminin EGF-like 10PROSITE-ProRule annotationAdd
    BLAST
    Domaini965 – 101349Laminin EGF-like 11PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1014 – 1575562Domain II and IAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili1073 – 113462Sequence AnalysisAdd
    BLAST
    Coiled coili1201 – 122828Sequence AnalysisAdd
    BLAST
    Coiled coili1410 – 149283Sequence AnalysisAdd
    BLAST
    Coiled coili1523 – 156745Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi1059 – 10613Cell 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 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.
    HOGENOMiHOG000019301.
    HOVERGENiHBG100808.
    KOiK06247.
    OMAiQRGRRCE.
    OrthoDBiEOG7SR4KJ.
    PhylomeDBiQ9Y6N6.
    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. 11 hits.
    PF00055. Laminin_N. 1 hit.
    [Graphical view]
    SMARTiSM00180. EGF_Lam. 10 hits.
    SM00136. LamNT. 1 hit.
    [Graphical view]
    PROSITEiPS00022. EGF_1. 7 hits.
    PS01186. EGF_2. 2 hits.
    PS01248. EGF_LAM_1. 10 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.

    Q9Y6N6-1 [UniParc]FASTAAdd to Basket

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    MAAAALLLGL ALLAPRAAGA GMGACYDGAG RPQRCLPVFE NAAFGRLAQA     50
    SHTCGSPPED FCPHVGAAGA GAHCQRCDAA DPQRHHNASY LTDFHSQDES 100
    TWWQSPSMAF GVQYPTSVNI TLRLGKAYEI TYVRLKFHTS RPESFAIYKR 150
    SRADGPWEPY QFYSASCQKT YGRPEGQYLR PGEDERVAFC TSEFSDISPL 200
    SGGNVAFSTL EGRPSAYNFE ESPGLQEWVT STELLISLDR LNTFGDDIFK 250
    DPKVLQSYYY AVSDFSVGGR CKCNGHASEC GPDVAGQLAC RCQHNTTGTD 300
    CERCLPFFQD RPWARGTAEA AHECLPCNCS GRSEECTFDR ELFRSTGHGG 350
    RCHHCRDHTA GPHCERCQEN FYHWDPRMPC QPCDCQSAGS LHLQCDDTGT 400
    CACKPTVTGW KCDRCLPGFH SLSEGGCRPC TCNPAGSLDT CDPRSGRCPC 450
    KENVEGNLCD RCRPGTFNLQ PHNPAGCSSC FCYGHSKVCA STAQFQVHHI 500
    LSDFHQGAEG WWARSVGGSE HPPQWSPNGV LLSPEDEEEL TAPEKFLGDQ 550
    RFSYGQPLIL TFRVPPGDSP LPVQLRLEGT GLALSLRHSS LSGPQDAGHP 600
    REVELRFHLQ ETSEDVAPPL PPFHFQRLLA NLTSLRLRVS PGPSPAGPVF 650
    LTEVRLTSAR PGLSPPASWV EICSCPTGYT GQFCESCAPG YKREMPQGGP 700
    YASCVPCTCN QHGTCDPNTG ICVCSHHTEG PSCERCLPGF YGNPFAGQAD 750
    DCQPCPCPGQ SACTTIPESR EVVCTHCPPG QRGRRCEVCD DGFFGDPLGL 800
    FGHPQPCHQC QCSGNVDPNA VGNCDPLSGH CLRCLHNTTG DHCEHCQEGF 850
    YGSALAPRPA DKCMPCSCHP QGSVSEQMPC DPVTGQCSCL PHVTARDCSR 900
    CYPGFFDLQP GRGCRSCKCH PLGSQEDQCH PKTGQCTCRP GVTGQACDRC 950
    QLGFFGFSIK GCRACRCSPL GAASAQCHEN GTCVCRPGFE GYKCDRCHDN 1000
    FFLTADGTHC QQCPSCYALV KEEAAKLKAR LTLTEGWLQG SDCGSPWGPL 1050
    DILLGEAPRG DVYQGHHLLP GAREAFLEQM MSLEGAVKAA REQLQRLNKG 1100
    ARCAQAGSQK TCTQLADLEA VLESSEEEIL HAAAILASLE IPQEGPSQPT 1150
    KWSHLATEAR ALARSHRDTA TKIAATAWRA LLASNTSYAL LWNLLEGRVA 1200
    LETQRDLEDR YQEVQAAQKA LRTAVAEVLP EAESVLATVQ QVGADTAPYL 1250
    ALLASPGALP QKSRAEDLGL KAKALEKTVA SWQHMATEAA RTLQTAAQAT 1300
    LRQTEPLTKL HQEARAALTQ ASSSVQAATV TVMGARTLLA DLEGMKLQFP 1350
    RPKDQAALQR KADSVSDRLL ADTRKKTKQA ERMLGNAAPL SSSAKKKGRE 1400
    AEVLAKDSAK LAKALLRERK QAHRRASRLT SQTQATLQQA SQQVLASEAR 1450
    RQELEEAERV GAGLSEMEQQ IRESRISLEK DIETLSELLA RLGSLDTHQA 1500
    PAQALNETQW ALERLRLQLG SPGSLQRKLS LLEQESQQQE LQIQGFESDL 1550
    AEIRADKQNL EAILHSLPEN CASWQ 1575
    Length:1,575
    Mass (Da):171,227
    Last modified:October 5, 2010 - v3
    Checksum:iD09DAFB3A900E1BD
    GO

    Sequence cautioni

    The sequence AAD36991.1 differs from that shown. Reason: Frameshift at positions 598 and 609.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti957 – 9571F → S in AAD36991. (PubMed:10225960)Curated
    Sequence conflicti979 – 9791E → Y in AAD36991. (PubMed:10225960)Curated
    Sequence conflicti999 – 9991D → Y in AAD36991. (PubMed:10225960)Curated
    Sequence conflicti1024 – 10241A → T in AAD36991. (PubMed:10225960)Curated
    Sequence conflicti1157 – 11571T → I in AAD36991. (PubMed:10225960)Curated
    Sequence conflicti1309 – 13091K → KARSRLTATSASQ in CAH69983. (PubMed:15164053)Curated
    Sequence conflicti1309 – 13091K → MARSRLTATFASQ in AAD36991. (PubMed:10225960)Curated
    Sequence conflicti1313 – 13131E → G in AAD36991. (PubMed:10225960)Curated
    Sequence conflicti1433 – 14331T → M in BAD92124. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti350 – 3501G → R in OCCM. 1 Publication
    VAR_066404
    Natural varianti522 – 5221P → S.1 Publication
    Corresponds to variant rs869457 [ dbSNP | Ensembl ].
    VAR_056145
    Natural varianti544 – 5441E → G.2 Publications
    Corresponds to variant rs10901333 [ dbSNP | Ensembl ].
    VAR_056146
    Natural varianti770 – 7701R → G.2 Publications
    Corresponds to variant rs3739510 [ dbSNP | Ensembl ].
    VAR_056147
    Natural varianti1082 – 10821S → G.2 Publications
    Corresponds to variant rs2275140 [ dbSNP | Ensembl ].
    VAR_056148
    Natural varianti1264 – 12641R → W.
    Corresponds to variant rs11244275 [ dbSNP | Ensembl ].
    VAR_056149

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF041835 mRNA. Translation: AAD36991.1. Frameshift.
    AL583807, AL355872 Genomic DNA. Translation: CAH69983.1.
    AL583807, AL355872 Genomic DNA. Translation: CAH69984.3.
    AL355872, AL583807 Genomic DNA. Translation: CAX14981.1.
    AB208887 mRNA. Translation: BAD92124.1.
    CCDSiCCDS6938.1.
    RefSeqiNP_006050.3. NM_006059.3.
    UniGeneiHs.201805.

    Genome annotation databases

    EnsembliENST00000361069; ENSP00000354360; ENSG00000050555.
    GeneIDi10319.
    KEGGihsa:10319.
    UCSCiuc004caa.1. human.

    Polymorphism databases

    DMDMi308153586.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF041835 mRNA. Translation: AAD36991.1 . Frameshift.
    AL583807 , AL355872 Genomic DNA. Translation: CAH69983.1 .
    AL583807 , AL355872 Genomic DNA. Translation: CAH69984.3 .
    AL355872 , AL583807 Genomic DNA. Translation: CAX14981.1 .
    AB208887 mRNA. Translation: BAD92124.1 .
    CCDSi CCDS6938.1.
    RefSeqi NP_006050.3. NM_006059.3.
    UniGenei Hs.201805.

    3D structure databases

    ProteinModelPortali Q9Y6N6.
    SMRi Q9Y6N6. Positions 25-482, 662-1016.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115603. 21 interactions.
    IntActi Q9Y6N6. 21 interactions.
    MINTi MINT-7034525.
    STRINGi 9606.ENSP00000354360.

    Chemistry

    ChEMBLi CHEMBL2364187.

    Polymorphism databases

    DMDMi 308153586.

    Proteomic databases

    MaxQBi Q9Y6N6.
    PaxDbi Q9Y6N6.
    PRIDEi Q9Y6N6.

    Protocols and materials databases

    DNASUi 10319.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000361069 ; ENSP00000354360 ; ENSG00000050555 .
    GeneIDi 10319.
    KEGGi hsa:10319.
    UCSCi uc004caa.1. human.

    Organism-specific databases

    CTDi 10319.
    GeneCardsi GC09P133884.
    H-InvDB HIX0008477.
    HGNCi HGNC:6494. LAMC3.
    HPAi HPA022814.
    MIMi 604349. gene.
    614115. phenotype.
    neXtProti NX_Q9Y6N6.
    Orphaneti 280640. Occipital pachygyria and polymicrogyria.
    PharmGKBi PA30282.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG235720.
    HOGENOMi HOG000019301.
    HOVERGENi HBG100808.
    KOi K06247.
    OMAi QRGRRCE.
    OrthoDBi EOG7SR4KJ.
    PhylomeDBi Q9Y6N6.
    TreeFami TF352481.

    Enzyme and pathway databases

    Reactomei REACT_163874. Non-integrin membrane-ECM interactions.
    REACT_169262. Laminin interactions.

    Miscellaneous databases

    ChiTaRSi LAMC3. human.
    GeneWikii LAMC3.
    GenomeRNAii 10319.
    NextBioi 39119.
    PROi Q9Y6N6.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Y6N6.
    Bgeei Q9Y6N6.
    CleanExi HS_LAMC3.
    Genevestigatori Q9Y6N6.

    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. 11 hits.
    PF00055. Laminin_N. 1 hit.
    [Graphical view ]
    SMARTi SM00180. EGF_Lam. 10 hits.
    SM00136. LamNT. 1 hit.
    [Graphical view ]
    PROSITEi PS00022. EGF_1. 7 hits.
    PS01186. EGF_2. 2 hits.
    PS01248. EGF_LAM_1. 10 hits.
    PS50027. EGF_LAM_2. 10 hits.
    PS51115. LAMININ_IVA. 1 hit.
    PS51117. LAMININ_NTER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization and expression of the laminin gamma3 chain: a novel, non-basement membrane-associated, laminin chain."
      Koch M., Olson P.F., Albus A., Jin W., Hunter D.D., Brunken W.J., Burgeson R.E., Champliaud M.-F.
      J. Cell Biol. 145:605-618(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS SER-522; GLY-544; GLY-770 AND GLY-1082.
      Tissue: Placenta.
    2. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "Homo sapiens protein coding cDNA."
      Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 197-1575, VARIANTS GLY-544; GLY-770 AND GLY-1082.
      Tissue: Spleen.
    4. Cited for: VARIANT OCCM ARG-350.

    Entry informationi

    Entry nameiLAMC3_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y6N6
    Secondary accession number(s): B1APX9, B1APY0, Q59H72
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 13, 2001
    Last sequence update: October 5, 2010
    Last modified: October 1, 2014
    This is version 131 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 9
      Human chromosome 9: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3