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DRL_DANRE
ID   DRL_DANRE               Reviewed;         411 AA.
AC   Q9W747; B0R153; Q504H6;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 2.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=Zinc finger protein draculin;
GN   Name=drl {ECO:0000312|ZFIN:ZDB-GENE-991213-3}; Synonyms=dra;
GN   ORFNames=si:dkey-261j4.2;
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] {ECO:0000305, ECO:0000312|EMBL:AAD40679.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Blood, and Embryo;
RX   PubMed=10433904; DOI=10.1242/dev.126.17.3735;
RA   Herbomel P., Thisse B., Thisse C.;
RT   "Ontogeny and behaviour of early macrophages in the zebrafish embryo.";
RL   Development 126:3735-3745(1999).
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   -!- TISSUE SPECIFICITY: Specifically expressed in the hematopoietic lineage
CC       during embryogenesis; first expressed at the late blastula stage around
CC       the blastoderm margin. During gastrulation, restricted to the ventral
CC       mesoderm, the presumptive prechordal plate and the dorso-marginal cells
CC       of the organizer. At the 3-somite stage, strongly expressed in a caudal
CC       domain (marking the erythroid lineage) and a cephalic domain of the
CC       lateral mesoderm. At the 8- to 10-somite stage, caudal expression is in
CC       two bands of lateral mesoderm which later converge at the midline.
CC       Anterior expression is also in two bands of lateral mesoderm which
CC       converge as two patches at the midline by the 15-somite stage, with
CC       increased scattering of single cells (macrophage precursors) away from
CC       the midline to the yolksac. Once at the yolksac, expression is lost. By
CC       20-24 hours post-fertilization (hpf), expressed in proerythroblasts in
CC       the erythroid blood island centered above the uro-genital opening.
CC       Expression persists in circulating erythroblasts but is lost in mature
CC       erythrocytes. {ECO:0000269|PubMed:10433904}.
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DR   EMBL; AF157109; AAD40679.1; -; mRNA.
DR   EMBL; AL935280; CAQ13760.1; -; Genomic_DNA.
DR   RefSeq; NP_571052.1; NM_130977.1.
DR   AlphaFoldDB; Q9W747; -.
DR   SMR; Q9W747; -.
DR   STRING; 7955.ENSDARP00000088134; -.
DR   PaxDb; Q9W747; -.
DR   Ensembl; ENSDART00000097364; ENSDARP00000088134; ENSDARG00000078004.
DR   GeneID; 30167; -.
DR   KEGG; dre:30167; -.
DR   CTD; 30167; -.
DR   ZFIN; ZDB-GENE-991213-3; drl.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00950000182774; -.
DR   HOGENOM; CLU_002678_44_0_1; -.
DR   InParanoid; Q9W747; -.
DR   OrthoDB; 1318335at2759; -.
DR   PhylomeDB; Q9W747; -.
DR   TreeFam; TF334420; -.
DR   PRO; PR:Q9W747; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 5.
DR   Bgee; ENSDARG00000078004; Expressed in ventral mesoderm and 28 other tissues.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; NAS:ZFIN.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0001702; P:gastrulation with mouth forming second; IEP:ZFIN.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   Pfam; PF00096; zf-C2H2; 10.
DR   SMART; SM00355; ZnF_C2H2; 13.
DR   SUPFAM; SSF57667; SSF57667; 7.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 13.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 13.
PE   2: Evidence at transcript level;
KW   Developmental protein; Metal-binding; Reference proteome; Repeat; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..411
FT                   /note="Zinc finger protein draculin"
FT                   /id="PRO_0000046936"
FT   ZN_FING         36..58
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         64..86
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         92..114
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         120..142
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         148..170
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         176..198
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         204..226
FT                   /note="C2H2-type 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         232..254
FT                   /note="C2H2-type 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         260..282
FT                   /note="C2H2-type 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         288..310
FT                   /note="C2H2-type 10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         316..338
FT                   /note="C2H2-type 11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         344..366
FT                   /note="C2H2-type 12"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         372..394
FT                   /note="C2H2-type 13"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        46
FT                   /note="S -> T (in Ref. 1; AAD40679)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        49
FT                   /note="A -> V (in Ref. 1; AAD40679)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   411 AA;  48030 MW;  465B63D7934EC802 CRC64;
     MKNTTKPCRT EHHNAEGQRD RMEGNKKGET KAKKSVACSH CKKRFSHKAH LQIHMRVHTG
     EKPYRCDQCG KCFPYKQSLK LHLDIHAKGN PYTCDECGES FKTRLQLRSH MTLHPKYKPY
     KCDQCEKSYG REDHLQRHMK LHTGEKPHKC EHCGKSFPMR DLLRSHLMVH SEVKPYTCDQ
     CGKGFTLKKS YNEHMNIHTG ERPYTCDQCG KGFPYEQSLN LHMRFHREEK PFTCDQCGQS
     FSQKGAYNIH MKIHTGEKPY TCDQCGMSFR HGYSLKLHMT HHTGEKPFHC DQCDKCYSTA
     LFLKNHIKTH DKAQIYSCLT CGKTFNQLRG LRLHEKRHSL TKPFMCFDCG KCYFTDTELK
     QHLPVHSNER PYMCSLCFKS FPRMGSLIVH EKTHNGEKPD CRTGSKKSQD E
 
 
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