RN207_MOUSE
ID RN207_MOUSE Reviewed; 635 AA.
AC Q3V3A7; A6PW94;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=RING finger protein 207;
GN Name=Rnf207; Synonyms=Gm143;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
CC -!- FUNCTION: Plays a role in cardiac repolarization possibly by
CC stabilizing membrane expression of the potassium channel KCNH2/HERG, or
CC 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 -!- SUBUNIT: Interacts with the core-glycosylated, but not the fully
CC glycosylated form of KCNH2/HERG. Interacts with DNAJA1 and HSPA8.
CC Interacts (via the C-terminus) with HSPA1A; this interaction additively
CC increases KCNH2 expression. {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 -!- SEQUENCE CAUTION:
CC Sequence=BAE20631.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK042379; BAE20631.1; ALT_SEQ; mRNA.
DR EMBL; AL611985; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS51393.1; -.
DR RefSeq; NP_001028661.2; NM_001033489.2.
DR AlphaFoldDB; Q3V3A7; -.
DR STRING; 10090.ENSMUSP00000075540; -.
DR iPTMnet; Q3V3A7; -.
DR PhosphoSitePlus; Q3V3A7; -.
DR PaxDb; Q3V3A7; -.
DR PRIDE; Q3V3A7; -.
DR ProteomicsDB; 299844; -.
DR Antibodypedia; 27241; 112 antibodies from 17 providers.
DR Ensembl; ENSMUST00000076183; ENSMUSP00000075540; ENSMUSG00000058498.
DR GeneID; 433809; -.
DR KEGG; mmu:433809; -.
DR UCSC; uc008waf.2; mouse.
DR CTD; 388591; -.
DR MGI; MGI:2684989; Rnf207.
DR VEuPathDB; HostDB:ENSMUSG00000058498; -.
DR eggNOG; KOG4367; Eukaryota.
DR GeneTree; ENSGT00510000048612; -.
DR InParanoid; Q3V3A7; -.
DR OMA; YEDSYRH; -.
DR OrthoDB; 489543at2759; -.
DR PhylomeDB; Q3V3A7; -.
DR TreeFam; TF318184; -.
DR BioGRID-ORCS; 433809; 1 hit in 73 CRISPR screens.
DR PRO; PR:Q3V3A7; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q3V3A7; protein.
DR Bgee; ENSMUSG00000058498; Expressed in retinal neural layer and 117 other tissues.
DR ExpressionAtlas; Q3V3A7; baseline and differential.
DR Genevisible; Q3V3A7; MM.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0051087; F:chaperone binding; ISO:MGI.
DR GO; GO:0030544; F:Hsp70 protein binding; ISO:MGI.
DR GO; GO:0044325; F:transmembrane transporter binding; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:1902261; P:positive regulation of delayed rectifier potassium channel activity; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
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; IBA:GO_Central.
DR GO; GO:1903762; P:positive regulation of voltage-gated potassium channel activity involved in ventricular cardiac muscle cell action potential repolarization; ISO:MGI.
DR GO; GO:0055117; P:regulation of cardiac muscle contraction; IBA:GO_Central.
DR GO; GO:1901207; P:regulation of heart looping; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR021978; DUF3583.
DR InterPro; IPR039320; RNF207.
DR InterPro; IPR000315; Znf_B-box.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
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; PF12126; DUF3583; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00336; BBOX; 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 2: Evidence at transcript level;
KW Coiled coil; Cytoplasm; Metal-binding; Reference proteome; Zinc;
KW Zinc-finger.
FT CHAIN 1..635
FT /note="RING finger protein 207"
FT /id="PRO_0000300810"
FT ZN_FING 25..64
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 553..635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 422..460
FT /evidence="ECO:0000255"
FT COMPBIAS 553..568
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 589..604
FT /note="Polar 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 635 AA; 70759 MW; EE4E051F6B9060AC CRC64;
MSGAIFAPLE GLSALDAASG HPLVCPLCHG QYERPCLLDC FHDFCTGCLR GRATDGRLSC
PLCQHQTLVK GPSGLPPVDR LLQFLVDSSG DGSEAVRCAN CDLECSQQDA ETTYFCNTCG
QPLCARCREE THRARMFARH DIVALGQRSR DVIQKCTLHS EPYIMFSTDK KSLLCIRCFR
DMQGESRAHC VDLESAYVQG CERLEQAVLA VKALQTATKE AIALLQSMVE EVRHSAAEEE
AAIHALFGSM QDRMAERKAL LLQTVQSQYE EKDKAFKEQL THLASLLPTL QVHLVICSSF
LSLASKAEFL DLGYELMERL QGIVTRPHRL RPAQSSKIAS DHRAEFARCL EPLLLLGPRR
EVSTVGGANT LSGGSSPMVL KTPSCPSPVG KMSGSPVQKP SPHRFISTKV LLAEGEDTPF
TEHCRHYEDS YRGLQVEVQN LKDQVQELHR DLTKHHSLIK AEIMGDILRR SLLLDTQIAS
EYASLEGRRA IFQEIWEDSY QRVATQQEIY EAQLRDLLQL RQENAYLTIV TKQITPYIRS
IARVKERLEP RFQVPVDEHA EHGQNMYDET PGRTDPGCTT EKRDKASEPN GSSWSLSSLP
EGPSLKNQDH LRPKLEAGDE GWRAGSGSKG ACYQA
