RN207_DANRE
ID RN207_DANRE Reviewed; 634 AA.
AC E9QHE3;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=RING finger protein 207;
GN Name=rnf207b; Synonyms=rnf207;
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 [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).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25281747; DOI=10.1074/jbc.m114.592295;
RA Roder K., Werdich A.A., Li W., Liu M., Kim T.Y., Organ-Darling L.E.,
RA Moshal K.S., Hwang J.M., Lu Y., Choi B.R., MacRae C.A., Koren G.;
RT "RING finger protein RNF207, a novel regulator of cardiac excitation.";
RL J. Biol. Chem. 289:33730-33740(2014).
CC -!- FUNCTION: Plays a role in cardiac repolarization possibly by
CC stabilizing membrane expression of the potassium channel kcnh6a/zerg,
CC or by assisting its synthesis, folding or export from the endoplasmic
CC reticulum, in a heat shock protein-dependent manner.
CC {ECO:0000250|UniProtKB:Q6ZRF8}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6ZRF8}.
CC Note=Probably located in the endoplasmic reticulum and/or possibly the
CC cis-Golgi apparatus. {ECO:0000250|UniProtKB:Q6ZRF8}.
CC -!- DISRUPTION PHENOTYPE: Morpholino knockdown of the protein results in
CC abnormal contractility and looping in developing heart. Morphants show
CC prolonged duration of cardiac action potentials, occasional 2:1
CC atrioventricular block and slowed conduction velocity
CC (PubMed:25281747). {ECO:0000269|PubMed:25281747}.
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DR EMBL; CR847529; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001188378.1; NM_001201449.1.
DR AlphaFoldDB; E9QHE3; -.
DR SMR; E9QHE3; -.
DR STRING; 7955.ENSDARP00000122299; -.
DR PaxDb; E9QHE3; -.
DR Ensembl; ENSDART00000142000; ENSDARP00000122299; ENSDARG00000012409.
DR GeneID; 568322; -.
DR KEGG; dre:568322; -.
DR CTD; 568322; -.
DR ZFIN; ZDB-GENE-080227-9; rnf207b.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00510000048612; -.
DR HOGENOM; CLU_034912_0_0_1; -.
DR OMA; ELDTMYF; -.
DR OrthoDB; 489543at2759; -.
DR PhylomeDB; E9QHE3; -.
DR TreeFam; TF318184; -.
DR PRO; PR:E9QHE3; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 23.
DR Bgee; ENSDARG00000012409; Expressed in heart and 10 other tissues.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IBA:GO_Central.
DR GO; GO:0051087; F:chaperone binding; IBA:GO_Central.
DR GO; GO:0030544; F:Hsp70 protein binding; IBA:GO_Central.
DR GO; GO:0044325; F:transmembrane transporter binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0086019; P:cell-cell signaling involved in cardiac conduction; IMP:BHF-UCL.
DR GO; GO:1901018; P:positive regulation of potassium ion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:1903954; P:positive regulation of voltage-gated potassium channel activity involved in atrial cardiac muscle cell action potential repolarization; IMP:BHF-UCL.
DR GO; GO:1903762; P:positive regulation of voltage-gated potassium channel activity involved in ventricular cardiac muscle cell action potential repolarization; IMP:BHF-UCL.
DR GO; GO:0055117; P:regulation of cardiac muscle contraction; IMP:BHF-UCL.
DR GO; GO:1901207; P:regulation of heart looping; IMP:BHF-UCL.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR039320; RNF207.
DR InterPro; IPR000315; Znf_B-box.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR22635; PTHR22635; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS50119; ZF_BBOX; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Metal-binding; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..634
FT /note="RING finger protein 207"
FT /id="PRO_0000436857"
FT ZN_FING 25..63
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 93..145
FT /note="B box-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT REGION 575..634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..608
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 609..634
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 127
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 132
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
SQ SEQUENCE 634 AA; 72647 MW; 5402268D04426CE4 CRC64;
MSGEIFYSVD NLYDLDSANC HPLVCHLCQE QYEHPCLLDC YHTFCASCLR GRVADSRLTC
PVCGHQSVVK GINALPPEDR LLKFLVDSSA DSEETVQCAN CDLECKKQDV DAMYYCNTCC
QPLCRDCRET THKAKMFSRH EIVSLAKRTK EAHKKCALHE EFYIMFSTEK KSMLCINCFR
DMQVESRAHC IDIETAYIQG CEKLDQAVLA VKELQMSARE AIILLKAMIG EVRANVDEEE
SAICTLFSNM QEKLAERKKI LLKAARSQHE EKERTFKEQL SHLAALLPTL QVHLVTCSAF
LSSANKFEFL DMGYQLMERL KKIVKLPHRL RPTQSSKINT EYRSEFARCL EPLLLLGQRR
SMSTTGSVAL ALGNASGLMQ SSLSVQCHSP AMSDMSLCSS VVRRPTSHRY ISTKVLLAKG
GETPFMEHCC NYENSYRTLQ TEIQKLKDQV QEIHRDLTKH HSLTKPDSMS EILEKSVQVD
SQISSEYASV ELMRAMFEEI WEETLQRVAN EQEIYEAQLH DLLQLKQENS YLTTISRQIG
PYIRSIAKVK ERLEPRLKEP KELKDDRTEI MLKLYEDSTS TADTQPSNEL SCNTEDNWTL
NSLSEETNPK NKDYYRTNKQ KNTTDSTNRK EIPM
