GenomeNet

Database: UniProt
Entry: B7ZDA6_DANRE
LinkDB: B7ZDA6_DANRE
Original site: B7ZDA6_DANRE 
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
//
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