LAMC1_DANRE
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-AUG-2022, entry version 111.
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 Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=12070089; DOI=10.1242/dev.129.13.3137;
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 notochord
RT 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., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., 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., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., 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., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
CC -!- FUNCTION: Binding to cells via a high affinity receptor, laminin is
CC thought to mediate the attachment, migration and organization of cells
CC into tissues during embryonic development by interacting with other
CC 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 to
CC each other by disulfide bonds into a cross-shaped molecule comprising
CC one long and three short arms with globules at each end. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix, basement membrane {ECO:0000250}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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 AlphaFoldDB; Q1LVF0; -.
DR SMR; Q1LVF0; -.
DR STRING; 7955.ENSDARP00000024860; -.
DR PaxDb; Q1LVF0; -.
DR PeptideAtlas; Q1LVF0; -.
DR PRIDE; Q1LVF0; -.
DR Ensembl; ENSDART00000004277; ENSDARP00000024860; ENSDARG00000036279.
DR GeneID; 286832; -.
DR KEGG; dre:286832; -.
DR CTD; 3915; -.
DR ZFIN; ZDB-GENE-021226-3; lamc1.
DR eggNOG; KOG1836; Eukaryota.
DR GeneTree; ENSGT00940000166185; -.
DR HOGENOM; CLU_002471_1_0_1; -.
DR InParanoid; Q1LVF0; -.
DR OMA; ACLPCHC; -.
DR OrthoDB; 156553at2759; -.
DR PhylomeDB; Q1LVF0; -.
DR TreeFam; TF352481; -.
DR Reactome; R-DRE-3000157; Laminin interactions.
DR Reactome; R-DRE-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-DRE-8874081; MET activates PTK2 signaling.
DR Reactome; R-DRE-8957275; Post-translational protein phosphorylation.
DR PRO; PR:Q1LVF0; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 2.
DR Bgee; ENSDARG00000036279; Expressed in paraxial mesoderm and 59 other tissues.
DR GO; GO:0005604; C:basement membrane; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
DR GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR GO; GO:0007411; P:axon guidance; IMP:ZFIN.
DR GO; GO:0007420; P:brain development; IMP:ZFIN.
DR GO; GO:0048854; P:brain morphogenesis; IMP:ZFIN.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0050908; P:detection of light stimulus involved in visual perception; IMP:ZFIN.
DR GO; GO:0001654; P:eye development; IMP:ZFIN.
DR GO; GO:0007517; P:muscle organ development; IMP:ZFIN.
DR GO; GO:0030903; P:notochord 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 GO; GO:0061053; P:somite development; IMP:ZFIN.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IBA:GO_Central.
DR GO; GO:0009888; P:tissue development; IBA:GO_Central.
DR CDD; cd00055; EGF_Lam; 9.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000034; Laminin_IV.
DR InterPro; IPR008211; Laminin_N.
DR InterPro; IPR002049; LE_dom.
DR Pfam; PF00052; Laminin_B; 1.
DR Pfam; PF00053; Laminin_EGF; 11.
DR Pfam; PF00055; Laminin_N; 1.
DR SMART; SM00181; EGF; 5.
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; Disulfide bond;
KW Extracellular matrix; Glycoprotein; Laminin EGF-like domain;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..1593
FT /note="Laminin subunit gamma-1"
FT /id="PRO_0000364201"
FT DOMAIN 30..269
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00466"
FT DOMAIN 270..325
FT /note="Laminin EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 326..381
FT /note="Laminin EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 382..428
FT /note="Laminin EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 429..478
FT /note="Laminin EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 505..673
FT /note="Laminin IV type A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00458"
FT DOMAIN 708..756
FT /note="Laminin EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 757..811
FT /note="Laminin EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 812..867
FT /note="Laminin EGF-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 868..918
FT /note="Laminin EGF-like 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 919..966
FT /note="Laminin EGF-like 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 967..1014
FT /note="Laminin EGF-like 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT REGION 1014..1593
FT /note="Domain II and I"
FT /evidence="ECO:0000250"
FT COILED 1021..1580
FT /evidence="ECO:0000255"
FT CARBOHYD 44
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 560
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 634
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 654
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1006
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1091
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1159
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1189
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1207
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1254
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1364
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1379
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 270..279
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 272..289
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 291..300
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 303..323
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 326..335
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 328..351
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 354..363
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 366..379
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 382..394
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 384..400
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 402..411
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 414..426
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 429..440
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 431..447
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 449..458
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 461..476
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 708..717
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 710..724
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 726..735
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 738..754
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 757..765
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 759..776
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 779..788
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 791..809
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 812..826
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 814..833
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 836..845
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 848..865
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 868..882
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 870..889
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 891..900
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 903..916
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 919..931
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 921..938
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 940..949
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 952..964
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 967..979
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 969..985
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 987..996
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 999..1012
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT CONFLICT 819
FT /note="D -> E (in Ref. 1; AAM61766)"
FT /evidence="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
