ID B7ZDA6_DANRE Unreviewed; 1782 AA.
AC B7ZDA6; A0A8M1P2Z5;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 112.
DE SubName: Full=Laminin subunit beta-2 precursor {ECO:0000313|RefSeq:NP_001229974.1};
DE SubName: Full=Laminin, beta 2 (laminin S) {ECO:0000313|Ensembl:ENSDARP00000123269};
GN Name=si:dkey-32e6.2 {ECO:0000313|RefSeq:NP_001229974.1};
GN OrderedLocusNames=lamb2 {ECO:0000313|Ensembl:ENSDARP00000123269,
GN ECO:0000313|RefSeq:NP_001229974.1,
GN ECO:0000313|ZFIN:ZDB-GENE-081030-4};
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 {ECO:0000313|Ensembl:ENSDARP00000123269};
RN [1] {ECO:0000313|RefSeq:NP_001229974.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001229974.1};
RX PubMed=19736328; DOI=10.1242/dev.034561;
RA Jacoby A.S., Busch-Nentwich E., Bryson-Richardson R.J., Hall T.E.,
RA Berger J., Berger S., Sonntag C., Sachs C., Geisler R., Stemple D.L.,
RA Currie P.D.;
RT "The zebrafish dystrophic mutant softy maintains muscle fibre viability
RT despite basement membrane rupture and muscle detachment.";
RL Development 136:3367-3376(2009).
RN [2] {ECO:0000313|RefSeq:NP_001229974.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001229974.1};
RX PubMed=21246659;
RA Sztal T., Berger S., Currie P.D., Hall T.E.;
RT "Characterization of the laminin gene family and evolution in zebrafish.";
RL Dev. Dyn. 240:422-431(2011).
RN [3] {ECO:0000313|RefSeq:NP_001229974.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001229974.1};
RX PubMed=22713473;
RA Berger J., Sztal T., Currie P.D.;
RT "Quantification of birefringence readily measures the level of muscle
RT damage in zebrafish.";
RL Biochem. Biophys. Res. Commun. 423:785-788(2012).
RN [4] {ECO:0000313|RefSeq:NP_001229974.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001229974.1};
RX PubMed=23118857; DOI=10.1371/journal.pone.0046642;
RA Micale L., Loviglio M.N., Manzoni M., Fusco C., Augello B., Migliavacca E.,
RA Cotugno G., Monti E., Borsani G., Reymond A., Merla G.;
RT "A fish-specific transposable element shapes the repertoire of p53 target
RT genes in zebrafish.";
RL PLoS ONE 7:e46642-e46642(2012).
RN [5] {ECO:0000313|Ensembl:ENSDARP00000123269}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000123269};
RG Ensembl;
RL Submitted (FEB-2012) to UniProtKB.
RN [6] {ECO:0000313|Ensembl:ENSDARP00000123269, ECO:0000313|Proteomes:UP000000437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000123269};
RX PubMed=23594743; DOI=10.1038/nature12111;
RG Genome Reference Consortium Zebrafish;
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., Eliott D.,
RA Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B.,
RA Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M.,
RA Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M.,
RA Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J.,
RA Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D.,
RA Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K.,
RA Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R.,
RA Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M.,
RA Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M.,
RA Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M.,
RA Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D.,
RA Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J.,
RA Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I.,
RA Berger A., 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., Lanz C., Raddatz G., Osoegawa K., Zhu B.,
RA Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P.,
RA Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R.,
RA Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I.,
RA Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H.,
RA 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).
RN [7] {ECO:0000313|RefSeq:NP_001229974.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001229974.1};
RX PubMed=24941943; DOI=10.7554/elife.02372;
RA Subramanian A., Schilling T.F.;
RT "Thrombospondin-4 controls matrix assembly during development and repair of
RT myotendinous junctions. .";
RL Elife 3:0-0(2014).
RN [8] {ECO:0000313|RefSeq:NP_001229974.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001229974.1};
RX PubMed=25519245;
RA Nagendran M., Arora P., Gori P., Mulay A., Ray S., Jacob T., Sonawane M.;
RT "Canonical Wnt signalling regulates epithelial patterning by modulating
RT levels of laminins in zebrafish appendages.";
RL Development 142:320-330(2015).
RN [9] {ECO:0000313|RefSeq:NP_001229974.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001229974.1};
RX PubMed=26469318;
RA Elkon R., Milon B., Morrison L., Shah M., Vijayakumar S., Racherla M.,
RA Leitch C.C., Silipino L., Hadi S., Weiss-Gayet M., Barras E., Schmid C.D.,
RA Ait-Lounis A., Barnes A., Song Y., Eisenman D.J., Eliyahu E.,
RA Frolenkov G.I., Strome S.E., Durand B., Zaghloul N.A., Jones S.M.,
RA Reith W., Hertzano R.;
RT "RFX transcription factors are essential for hearing in mice.";
RL Nat. Commun. 6:8549-8549(2015).
RN [10] {ECO:0000313|RefSeq:NP_001229974.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001229974.1};
RX PubMed=27189481;
RA Pasquier J., Cabau C., Nguyen T., Jouanno E., Severac D., Braasch I.,
RA Journot L., Pontarotti P., Klopp C., Postlethwait J.H., Guiguen Y.,
RA Bobe J.;
RT "Gene evolution and gene expression after whole genome duplication in fish:
RT the PhyloFish database.";
RL BMC Genomics 17:368-368(2016).
RN [11] {ECO:0000313|RefSeq:NP_001229974.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001229974.1};
RX PubMed=30924555;
RA Charlton-Perkins M., Almeida A.D., MacDonald R.B., Harris W.A.;
RT "Genetic control of cellular morphogenesis in Muller glia.";
RL Glia 67:1401-1411(2019).
RN [12] {ECO:0000313|RefSeq:NP_001229974.1}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001229974.1};
RG RefSeq;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00460}.
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DR EMBL; AL953864; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001229974.1; NM_001243045.1.
DR STRING; 7955.ENSDARP00000123269; -.
DR PaxDb; 7955-ENSDARP00000005383; -.
DR Ensembl; ENSDART00000147326; ENSDARP00000123269; ENSDARG00000002084.
DR Ensembl; ENSDART00000147326.2; ENSDARP00000123269.1; ENSDARG00000002084.11.
DR GeneID; 337767; -.
DR KEGG; dre:337767; -.
DR CTD; 3913; -.
DR ZFIN; ZDB-GENE-081030-4; lamb2.
DR eggNOG; KOG0994; Eukaryota.
DR HOGENOM; CLU_001560_1_0_1; -.
DR OMA; SCRDHTG; -.
DR OrthoDB; 90222at2759; -.
DR PhylomeDB; B7ZDA6; -.
DR TreeFam; TF312903; -.
DR Proteomes; UP000000437; Chromosome 23.
DR Bgee; ENSDARG00000002084; Expressed in spleen and 32 other cell types or tissues.
DR GO; GO:0043256; C:laminin complex; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR GO; GO:0070831; P:basement membrane assembly; IMP:ZFIN.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0016203; P:muscle attachment; 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; cd22299; cc_LAMB2_C; 1.
DR CDD; cd00055; EGF_Lam; 13.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.10.25.10; Laminin; 9.
DR Gene3D; 2.170.300.10; Tie2 ligand-binding domain superfamily; 2.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR013015; Laminin_IV_B.
DR InterPro; IPR008211; Laminin_N.
DR InterPro; IPR002049; LE_dom.
DR PANTHER; PTHR10574:SF375; LAMININ SUBUNIT BETA-1; 1.
DR PANTHER; PTHR10574; NETRIN/LAMININ-RELATED; 1.
DR Pfam; PF00053; Laminin_EGF; 13.
DR Pfam; PF21199; LAMININ_IV_B; 1.
DR Pfam; PF00055; Laminin_N; 1.
DR PRINTS; PR00011; EGFLAMININ.
DR SMART; SM00181; EGF; 10.
DR SMART; SM00180; EGF_Lam; 13.
DR SMART; SM00136; LamNT; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 13.
DR SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01248; EGF_LAM_1; 6.
DR PROSITE; PS50027; EGF_LAM_2; 12.
DR PROSITE; PS51116; LAMININ_IVB; 1.
DR PROSITE; PS51117; LAMININ_NTER; 1.
PE 1: Evidence at protein level;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00460};
KW Laminin EGF-like domain {ECO:0000256|ARBA:ARBA00023292,
KW ECO:0000256|PROSITE-ProRule:PRU00460};
KW Proteomics identification {ECO:0007829|PeptideAtlas:B7ZDA6};
KW Reference proteome {ECO:0000313|Proteomes:UP000000437};
KW Signal {ECO:0000256|SAM:SignalP, ECO:0000313|RefSeq:NP_001229974.1}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..1782
FT /evidence="ECO:0000256|SAM:SignalP,
FT ECO:0000313|RefSeq:NP_001229974.1"
FT /id="PRO_5035035405"
FT DOMAIN 27..266
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51117"
FT DOMAIN 267..330
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 331..393
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 394..453
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 454..505
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 545..761
FT /note="Laminin IV type B"
FT /evidence="ECO:0000259|PROSITE:PS51116"
FT DOMAIN 767..814
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 815..860
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 861..910
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 911..969
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 970..1021
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1022..1078
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1079..1126
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1127..1173
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT REGION 1324..1369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1274..1308
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1454..1488
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1550..1770
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1347..1369
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 296..305
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 361..370
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 424..433
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 477..486
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 489..503
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 767..779
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 769..786
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 788..797
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 815..827
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 817..834
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 836..845
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 880..889
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 940..949
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 994..1003
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1051..1060
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1079..1091
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1081..1098
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1100..1109
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1127..1139
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1129..1146
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1148..1157
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ SEQUENCE 1782 AA; 196601 MW; F3A9DA9BE0F7B022 CRC64;
MRALLLLSIC VLSAVSAQEP DAAHGCTHGS CYPATGDLLV GREANLKASS TCGLRRREPY
CIVSHLQEEK KCFQCDSRRP YDPQSNPVSH RIENVITTFK PHRKKSWWQS ENGKSDVYLQ
LDLEAEFHFT HLIMTFKTFR PAAMLIERSA DFGRSWQVYR YFANDCESIF PGISQDSLRK
VDDVICESRY SDIEPSTEGE VIFRVLDPAI RIEDPYSPRI QNQLKITNLR LNLTKLHTLG
DNLLDSRPEI KEKYYYAMYE LVVRGNCFCY GHASECAPIE GIRDDIEGMV HGRCVCKHNT
KGLNCEQCDD FYNDLPWRPA EGRNTNACKK CNCNGHSNQC HFDMAVYLAT GNISGGVCDN
CLHNTMGSNC ESCKPFYYQD PTRDIRDPGV CVACDCDPDG SKNGGVCDGH DDPSLGMIAG
QCRCKDNVEG SRCDKCKPGF FGLSASDPRG CQPCKCDPRG TVSGSSQCDP VSGDCFCKRL
VTGHSCNQCL PEHWALSHDT SGCRGCDCDV GGATENQCSM ETGQCQCRSH MIGRQCNQVE
SGYFFMALDH YIYEAETAKL GQGSVFEERE YQPGRPISWT GTGFARAPEG GTLEFAINNI
PYSMEYDVLI RYELQMPRDW EEVRVVVIRP GPIPTSSPCG NTIPADDLLT VSLSSGARFV
VLPQPVCLES GVSYKLRVEL IRYADRNSII TSTNAFVLVD SIALLPRYLS LEMFTAGDPA
SVARKQSFER YRCHETAKSV SRPQMSEVCA KLITSMSALI NDGALACECD PQGSLSSECD
VRGGQCRCRP NISGRRCEKC APGAYGFGPS GCKLCECSLE GSQSRFCDLY SGQCPCRPGA
YGQRCDGCQA GHWGFPNCRP CQCNGHADEC HQRTGACLNC RSNTAGDKCE RCANGYYGNP
VLGLGSQCRP CPCPEGPNSG RHFAASCYQD NRSQQVVCNC NQGYTGPRCD ECAPGYFGDP
SKPGGQCQPC RCSNNIDLSD PESCDKRTGQ CLKCLYNTEG PDCSVCRSGY YGDASRRNCR
KCTCNFLGTE RSQCLSRDDC VCQRATGQCQ CLPNVIGQTC DHCAPNSWNL ASGQGCEPCA
CDPNNAYTSA CNEFTGQCQC RVGFGGKTCT DCQENHWGDP RVLCRACDCD PRGIESSQCN
RMTGHCVCQQ GVSGVRCDQC ARGFSGTFPD CKPCHQCFGD WDRIVQDLAT RTKALTDRAK
ELQTTGLTRA FERRFKELED MLAQARDIVN ARNATAEAVT TLMGMIEVLR AQIGETTDTL
NQQEGDLTAV QDSNYEASNA LSTLEREAKE LNLNADQLNR QLDILKNSNF LGAYDSIRAS
YNKSRDAEHR SNRSTTDTPS TVSQSADTRK KTERLIGQKR DDFNRKNAAN KRTLTDLNAK
VQNLDLKKIN EKVCGAPGDA QCVDSPCGGA GCRDDEGKRR CGGLNCNGAV AVADTALDRS
KHAEKELDKA MGVVEELFKQ VADAKTKAQE AKDRAQAALE KASDTKNKVD HSNNDLRDLI
KQIRQFLMQE GADPDSIEAV ANRVLELSIP ASPKQIRHLA DEIKDRVKSL SNVDAILEQT
QNDVRKAEQL LLDAKKARNK AEGVKNTAES VKKALNDASR AQAAAEKAIQ KAKNDIGLTQ
NQLAQIQSET SASERDLNDA VDRLGDLERQ IEALKTKRAN NSLDAARAEE TATMARDKAN
EAKEILDGEL SDKYRTVQGL MDNKAKTMQD AKHKAEQLRD EAKGLLKDAQ DKLQRLAELE
KDYEENQKVL EGKARQLDGL EDKMKAILNA INRQIQIYNT CQ
//