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Database: UniProt
Entry: Q1LVF0
LinkDB: Q1LVF0
Original site: Q1LVF0 
ID   LAMC1_DANRE             Reviewed;        1593 AA.
AC   Q1LVF0; Q8JHV8;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 2.
DT   01-OCT-2014, entry version 69.
DE   RecName: Full=Laminin subunit gamma-1;
DE   Flags: Precursor;
GN   Name=lamc1;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=12070089;
RA   Parsons M.J., Pollard S.M., Saude L., Feldman B., Coutinho P.,
RA   Hirst E.M.A., Stemple D.L.;
RT   "Zebrafish mutants identify an essential role for laminins in
RT   notochord formation.";
RL   Development 129:3137-3146(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen;
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C.,
RA   Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L.,
RA   McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C.,
RA   Koch R., Rauch G.J., White S., Chow W., Kilian B., Quintais L.T.,
RA   Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T.,
RA   Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F.,
RA   Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H.,
RA   Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Eliott D., Threadgold G.,
RA   Harden G., Ware D., Mortimer B., Kerry G., Heath P., Phillimore B.,
RA   Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., Pelan S.,
RA   Griffiths G., Smith M., Glithero R., Howden P., Barker N., Stevens C.,
RA   Harley J., Holt K., Panagiotidis G., Lovell J., Beasley H.,
RA   Henderson C., Gordon D., Auger K., Wright D., Collins J., Raisen C.,
RA   Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J.,
RA   Babbage A., Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S.,
RA   Wray P., Ellington A., Matthews N., Ellwood M., Woodmansey R.,
RA   Clark G., Cooper J., Tromans A., Grafham D., Skuce C., Pandian R.,
RA   Andrews R., Harrison E., Kimberley A., Garnett J., Fosker N., Hall R.,
RA   Garner P., Kelly D., Bird C., Palmer S., Gehring I., Berger A.,
RA   Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA   Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA   Rudolph-Geiger S., Teucke M., Osoegawa K., Zhu B., Rapp A., Widaa S.,
RA   Langford C., Yang F., Carter N.P., Harrow J., Ning Z., Herrero J.,
RA   Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C.,
RA   Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H.,
RA   Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J.,
RA   Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the
RT   human genome.";
RL   Nature 496:498-503(2013).
CC   -!- FUNCTION: Binding to cells via a high affinity receptor, laminin
CC       is thought to mediate the attachment, migration and organization
CC       of cells into tissues during embryonic development by interacting
CC       with other extracellular matrix components. {ECO:0000250}.
CC   -!- SUBUNIT: Laminin is a complex glycoprotein, consisting of three
CC       different polypeptide chains (alpha, beta, gamma), which are bound
CC       to each other by disulfide bonds into a cross-shaped molecule
CC       comprising one long and three short arms with globules at each
CC       end. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix, basement membrane {ECO:0000250}.
CC   -!- SIMILARITY: Contains 10 laminin EGF-like domains.
CC       {ECO:0000255|PROSITE-ProRule:PRU00460}.
CC   -!- SIMILARITY: Contains 1 laminin IV type A domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00458}.
CC   -!- SIMILARITY: Contains 1 laminin N-terminal domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00466}.
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DR   EMBL; AF468048; AAM61766.1; -; mRNA.
DR   EMBL; BX681417; CAK05288.2; -; Genomic_DNA.
DR   EMBL; BX571812; CAK05288.2; JOINED; Genomic_DNA.
DR   EMBL; BX571812; CAQ13276.1; -; Genomic_DNA.
DR   EMBL; BX681417; CAQ13276.1; JOINED; Genomic_DNA.
DR   RefSeq; NP_775384.1; NM_173277.1.
DR   UniGene; Dr.132970; -.
DR   ProteinModelPortal; Q1LVF0; -.
DR   SMR; Q1LVF0; 755-918.
DR   Ensembl; ENSDART00000004277; ENSDARP00000024860; ENSDARG00000036279.
DR   GeneID; 286832; -.
DR   KEGG; dre:286832; -.
DR   CTD; 3915; -.
DR   ZFIN; ZDB-GENE-021226-3; lamc1.
DR   eggNOG; NOG235720; -.
DR   GeneTree; ENSGT00750000117374; -.
DR   HOGENOM; HOG000019301; -.
DR   HOVERGEN; HBG100808; -.
DR   InParanoid; Q8JHV8; -.
DR   KO; K05635; -.
DR   OMA; EATDYPW; -.
DR   OrthoDB; EOG7SR4KJ; -.
DR   PhylomeDB; Q1LVF0; -.
DR   TreeFam; TF352481; -.
DR   Reactome; REACT_174890; Laminin interactions.
DR   Reactome; REACT_203359; Degradation of the extracellular matrix.
DR   Reactome; REACT_217702; Non-integrin membrane-ECM interactions.
DR   Reactome; REACT_223985; ECM proteoglycans.
DR   NextBio; 20806483; -.
DR   PRO; PR:Q1LVF0; -.
DR   Bgee; Q1LVF0; -.
DR   GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0050908; P:detection of light stimulus involved in visual perception; IMP:ZFIN.
DR   GO; GO:0007517; P:muscle organ development; IMP:ZFIN.
DR   GO; GO:0048570; P:notochord morphogenesis; IMP:ZFIN.
DR   GO; GO:0007634; P:optokinetic behavior; IMP:ZFIN.
DR   GO; GO:0031290; P:retinal ganglion cell axon guidance; IMP:ZFIN.
DR   GO; GO:0007519; P:skeletal muscle tissue development; IMP:ZFIN.
DR   InterPro; IPR002049; EGF_laminin.
DR   InterPro; IPR018031; Laminin_B_subgr.
DR   InterPro; IPR000034; Laminin_B_type_IV.
DR   InterPro; IPR008211; Laminin_N.
DR   Pfam; PF00052; Laminin_B; 1.
DR   Pfam; PF00053; Laminin_EGF; 11.
DR   Pfam; PF00055; Laminin_N; 1.
DR   SMART; SM00180; EGF_Lam; 10.
DR   SMART; SM00281; LamB; 1.
DR   SMART; SM00136; LamNT; 1.
DR   PROSITE; PS00022; EGF_1; 7.
DR   PROSITE; PS01186; EGF_2; 2.
DR   PROSITE; PS01248; EGF_LAM_1; 10.
DR   PROSITE; PS50027; EGF_LAM_2; 10.
DR   PROSITE; PS51115; LAMININ_IVA; 1.
DR   PROSITE; PS51117; LAMININ_NTER; 1.
PE   2: Evidence at transcript level;
KW   Basement membrane; Cell adhesion; Coiled coil; Complete proteome;
KW   Disulfide bond; Extracellular matrix; Glycoprotein;
KW   Laminin EGF-like domain; Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL        1     19       {ECO:0000255}.
FT   CHAIN        20   1593       Laminin subunit gamma-1.
FT                                /FTId=PRO_0000364201.
FT   DOMAIN       30    269       Laminin N-terminal. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00466}.
FT   DOMAIN      270    325       Laminin EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      326    381       Laminin EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      382    428       Laminin EGF-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      429    478       Laminin EGF-like 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      505    673       Laminin IV type A. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00458}.
FT   DOMAIN      708    756       Laminin EGF-like 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      757    811       Laminin EGF-like 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      812    867       Laminin EGF-like 7. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      868    918       Laminin EGF-like 8. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      919    966       Laminin EGF-like 9. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      967   1014       Laminin EGF-like 10.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   REGION     1014   1593       Domain II and I. {ECO:0000250}.
FT   COILED     1021   1580       {ECO:0000255}.
FT   CARBOHYD     44     44       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    118    118       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    560    560       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    634    634       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    654    654       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD   1006   1006       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD   1091   1091       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD   1159   1159       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD   1189   1189       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD   1207   1207       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD   1254   1254       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD   1364   1364       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD   1379   1379       N-linked (GlcNAc...). {ECO:0000255}.
FT   DISULFID    270    279       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    272    289       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    291    300       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    303    323       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    326    335       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    328    351       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    354    363       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    366    379       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    382    394       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    384    400       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    402    411       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    414    426       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    429    440       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    431    447       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    449    458       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    461    476       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    708    717       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    710    724       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    726    735       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    738    754       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    757    765       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    759    776       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    779    788       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    791    809       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    812    826       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    814    833       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    836    845       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    848    865       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    868    882       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    870    889       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    891    900       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    903    916       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    919    931       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    921    938       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    940    949       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    952    964       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    967    979       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    969    985       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    987    996       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    999   1012       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   CONFLICT    819    819       D -> E (in Ref. 1; AAM61766).
FT                                {ECO:0000305}.
SQ   SEQUENCE   1593 AA;  176206 MW;  3A7982905896D403 CRC64;
     MSLFSCLLLW TLWAACSHGA MDECIDEDDR PQRCMPEFVN AAFNATVVAT NTCGSPPEEF
     CVQTGVTGVT KSCHICNAAD PRLHHGAVYL TDYNQPVQPT WWQSQTMLAG IQYPNSINLT
     LHLGKSFDIT YVRLKFHTSR PESFAIYKRS SEDGPWTPYQ YYSGSCEKTY SKNNRGFIRT
     GEDEQQALCT DEFSDISPLY GGNVAFSTLE GRPSAYNFDN SPVLQDWVTA TDIRVTLNRL
     NTFGDEVFND PKVLKSYYYA ISDFAVGGRC KCNGHASECV KNEYSKLVCN CKHNTEGADC
     NVCKPFYNDR PWRRATAENP NECLPCNCNG KSAECYFDPE LYRATGHGGH CRNCADNTDG
     PKCERCLANY YREASGQRCL SCGCNPVGSL STQCDNTGRC SCKPGVMGDK CDRCQPGYHS
     LSEAGCRPCS CNPAGSTQEC DVQTGRCQCK ENVDGFNCDR CKLGYFNLDP QNPQGCTPCF
     CFQHSTVCES ADGYSVHKIT STFDRDDEGW KGKQRDDSSV PVQWSPSSGE ISLISEDYFP
     IYFVAPDKFL HNQLLSYGQN LTLNFRIQRH DARLSAEDVV LEGSGLRVAV PLIAQGNSYP
     GEETQTFVFR LHDTTDYPWR PTIKHADFQK LLYNLTSIMI RGTYSAQSAG YLDNVSLVTA
     RRGPGTPARW VEKCTCPQGY LGQHCEQCDQ GFRRSRPELR RFSTCERCNC NGHSDTCDPE
     TGMCNCQHNT AGLSCERCKD GFYGDSTVGS SSDCKACPCP AGATCAVVPK TNEVVCTNCP
     TGTTGKRCEL CDDGFFGDPL GEKGPVRACR ACSCNNNIDP NAVGNCNRES GECLKCIYNT
     AGVFCDRCKQ GFYGDARAAN VADKCKPCKC SPYGTVDRQT ACSQVTGQCP CLPHVINRDC
     GACELGFYNL QSGKGCERCN CNPIGSTNGQ CDIVSGQCEC QPGVTGQHCE RCEVNFFGFS
     SSGCKPCDCD PEGSESAQCK EDGRCHCRPG FVGSRCDMCE ENYFYNRSTP GCQQCPNCYS
     LVRDKVNQQR QKLLDLQNLI DSLDNTETTV SDKAFEDRLK EAEKTIMDLL EEAQASKEVD
     KGLLDRLNNI NKTLNNQWNR LQNIKNTVDN TGAQADRARN RVRDAENLIN TAREELDKAK
     EAISKVDIKI PTTSGDPNNM TLLAEEARKL SEKHKADADQ IEKIAKDAND TSTKAYNMLK
     KALDGENKTS SDIDELNRKY LEAKDLAKNL EKQAAKVHAE AEEAGNKALK IYANLTSLPP
     INTKTLEDDA NKIKKEASDL DKLIDKTEKE YNDLREDLRG KETEVRKLLD KGKTEQQTAD
     QLLARADAAK ALAEEAAKKG KSTFQEAQDI LNNLRDFDKR VNDNKTAAED AMRRIPQINA
     TINEANDKTR RAEAALGNAA ADAKDAKAKA EEAEKIANDV QKGSAKTKAD AEKAFEDTMK
     LDKDVDKMMD QLTAAEKELE KKKAEADTDM MMASMASDNA KDAEGNARKA KSAVREVLNT
     INALLGQLGN IDKVDLSKLN QIDNALKDAK DKMAGSELDR KLKELNDIAK SQEDMISDYD
     RQIQEIRADI ANLNDIKNTL PEGCFNTPSL ERP
//
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