ID   RN207_RABIT             Reviewed;         594 AA.
AC   I1VZH0;
DT   06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2012, sequence version 1.
DT   03-AUG-2022, entry version 42.
DE   RecName: Full=RING finger protein 207;
GN   Name=RNF207;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986 {ECO:0000312|EMBL:AFI56569.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC   STRAIN=New Zealand white; TISSUE=Heart;
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 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:0000269|PubMed:25281747}.
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}.
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DR   EMBL; JQ754141; AFI56569.1; -; mRNA.
DR   RefSeq; NP_001287860.1; NM_001300931.1.
DR   AlphaFoldDB; I1VZH0; -.
DR   SMR; I1VZH0; -.
DR   STRING; 9986.ENSOCUP00000022153; -.
DR   GeneID; 100351676; -.
DR   KEGG; ocu:100351676; -.
DR   CTD; 388591; -.
DR   eggNOG; KOG4367; Eukaryota.
DR   OrthoDB; 489543at2759; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030544; F:Hsp70 protein binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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   2: Evidence at transcript level;
KW   Coiled coil; Cytoplasm; Metal-binding; Reference proteome; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..594
FT                   /note="RING finger protein 207"
FT                   /id="PRO_0000436856"
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          369..400
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          552..594
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          424..458
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        557..572
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   594 AA;  65682 MW;  166D061B6999378D CRC64;
     MSGAIFAPLE GPGALDAASG HPLVCPLCHA QYERPCLLDC FHDFCAGCLR GRTADGRVAC
     PLCQHQTVVK GPSGLPPVDR LLQFLVDSSG DGVEAVHCAN CDLDCSKQDA ETACFCNTCG
     QPLCARCRDE THRARMFARH DIVALGQRSR DVLQKCPLHA EPYLMFSTDK KSLLCIRCFR
     DLQGESRAHC VDLESAYVQG CERLEQAVLA VKALQAATRE AIALLQAMVE EVRRSAEEEA
     AAIHALFDSV QEKLAERKAL LLQAVQSQYE EKDQAFKEQL SHLATLLPTL QIHLVICSSF
     LSLANKAEFL DLGYELMERL QGVVTRPHRL RPAQSSKIAS DYRAEFARCL EPLLLLGPRR
     ATGAQGGANT LAGGSGPKVL MGPSCPSPVR KVSRSPVQKP TLPRSISTKV LLADGEDTPF
     AEHCRHYEDS YRGLQAEVQN LKDQVQELHR DLTKHHSLIR AEIMADILHR SLRLDAQIDS
     EYASVEGMRA VFQEIWEESY QRLAGEQEIY EAQLRDLFQL KQENAHLTTI TKHITPYVRS
     IAKVKERLEP RFQASADDES ENPQTAYDAS RNGETPASLL LPGSVASAEP PFVN