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 03-APR-2013, entry version 60.
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=AB;
RG The Danio rerio sequencing project at the Sanger Institute;
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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 (By similarity).
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 end
CC (By similarity).
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix, basement membrane (By similarity).
CC -!- SIMILARITY: Contains 10 laminin EGF-like domains.
CC -!- SIMILARITY: Contains 1 laminin IV type A domain.
CC -!- SIMILARITY: Contains 1 laminin N-terminal domain.
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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 IPI; IPI00496826; -.
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; ENSGT00690000102103; -.
DR HOGENOM; HOG000019301; -.
DR HOVERGEN; HBG100808; -.
DR InParanoid; Q8JHV8; -.
DR KO; K05635; -.
DR OMA; EATDYPW; -.
DR OrthoDB; EOG49GKFS; -.
DR NextBio; 20806483; -.
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: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 Potential.
FT CHAIN 20 1593 Laminin subunit gamma-1.
FT /FTId=PRO_0000364201.
FT DOMAIN 30 269 Laminin N-terminal.
FT DOMAIN 270 325 Laminin EGF-like 1.
FT DOMAIN 326 381 Laminin EGF-like 2.
FT DOMAIN 382 428 Laminin EGF-like 3.
FT DOMAIN 429 478 Laminin EGF-like 4.
FT DOMAIN 505 673 Laminin IV type A.
FT DOMAIN 708 756 Laminin EGF-like 5.
FT DOMAIN 757 811 Laminin EGF-like 6.
FT DOMAIN 812 867 Laminin EGF-like 7.
FT DOMAIN 868 918 Laminin EGF-like 8.
FT DOMAIN 919 966 Laminin EGF-like 9.
FT DOMAIN 967 1014 Laminin EGF-like 10.
FT REGION 1014 1593 Domain II and I (By similarity).
FT COILED 1021 1580 Potential.
FT CARBOHYD 44 44 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 118 118 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 560 560 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 634 634 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 654 654 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 1006 1006 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 1091 1091 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 1159 1159 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 1189 1189 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 1207 1207 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 1254 1254 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 1364 1364 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 1379 1379 N-linked (GlcNAc...) (Potential).
FT DISULFID 270 279 By similarity.
FT DISULFID 272 289 By similarity.
FT DISULFID 291 300 By similarity.
FT DISULFID 303 323 By similarity.
FT DISULFID 326 335 By similarity.
FT DISULFID 328 351 By similarity.
FT DISULFID 354 363 By similarity.
FT DISULFID 366 379 By similarity.
FT DISULFID 382 394 By similarity.
FT DISULFID 384 400 By similarity.
FT DISULFID 402 411 By similarity.
FT DISULFID 414 426 By similarity.
FT DISULFID 429 440 By similarity.
FT DISULFID 431 447 By similarity.
FT DISULFID 449 458 By similarity.
FT DISULFID 461 476 By similarity.
FT DISULFID 708 717 By similarity.
FT DISULFID 710 724 By similarity.
FT DISULFID 726 735 By similarity.
FT DISULFID 738 754 By similarity.
FT DISULFID 757 765 By similarity.
FT DISULFID 759 776 By similarity.
FT DISULFID 779 788 By similarity.
FT DISULFID 791 809 By similarity.
FT DISULFID 812 826 By similarity.
FT DISULFID 814 833 By similarity.
FT DISULFID 836 845 By similarity.
FT DISULFID 848 865 By similarity.
FT DISULFID 868 882 By similarity.
FT DISULFID 870 889 By similarity.
FT DISULFID 891 900 By similarity.
FT DISULFID 903 916 By similarity.
FT DISULFID 919 931 By similarity.
FT DISULFID 921 938 By similarity.
FT DISULFID 940 949 By similarity.
FT DISULFID 952 964 By similarity.
FT DISULFID 967 979 By similarity.
FT DISULFID 969 985 By similarity.
FT DISULFID 987 996 By similarity.
FT DISULFID 999 1012 By similarity.
FT CONFLICT 819 819 D -> E (in Ref. 1; AAM61766).
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
//
