ID RN207_BOVIN Reviewed; 556 AA.
AC A0JNG4; Q08D80;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 24-JAN-2024, entry version 95.
DE RecName: Full=RING finger protein 207;
GN Name=RNF207;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=Hereford; TISSUE=Basal ganglia, and Heart ventricle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A0JNG4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A0JNG4-2; Sequence=VSP_028438;
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DR EMBL; BC123895; AAI23896.1; -; mRNA.
DR EMBL; BC126674; AAI26675.1; -; mRNA.
DR RefSeq; NP_001071525.1; NM_001078057.1. [A0JNG4-1]
DR AlphaFoldDB; A0JNG4; -.
DR SMR; A0JNG4; -.
DR STRING; 9913.ENSBTAP00000066184; -.
DR PaxDb; 9913-ENSBTAP00000034008; -.
DR Ensembl; ENSBTAT00000034107.5; ENSBTAP00000034008.5; ENSBTAG00000009075.6. [A0JNG4-1]
DR GeneID; 616057; -.
DR KEGG; bta:616057; -.
DR CTD; 388591; -.
DR VEuPathDB; HostDB:ENSBTAG00000009075; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00510000048612; -.
DR InParanoid; A0JNG4; -.
DR Proteomes; UP000009136; Chromosome 16.
DR Bgee; ENSBTAG00000009075; Expressed in cardiac atrium and 105 other cell types or tissues.
DR ExpressionAtlas; A0JNG4; baseline and differential.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; 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:0055117; P:regulation of cardiac muscle contraction; IBA:GO_Central.
DR GO; GO:1901207; P:regulation of heart looping; IBA:GO_Central.
DR CDD; cd19814; Bbox1_RNF207-like; 1.
DR Gene3D; 1.20.58.1540; Actin interacting protein 3, C-terminal domain; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
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:SF0; RING FINGER PROTEIN 207; 1.
DR PANTHER; PTHR22635; UNCHARACTERIZED; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 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 Alternative splicing; Coiled coil; Cytoplasm; Metal-binding;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..556
FT /note="RING finger protein 207"
FT /id="PRO_0000300808"
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 517..556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 218..273
FT /evidence="ECO:0000255"
FT COILED 385..425
FT /evidence="ECO:0000255"
FT COMPBIAS 517..533
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"
FT VAR_SEQ 1..356
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_028438"
SQ SEQUENCE 556 AA; 61668 MW; B77FB618A35EDB6E CRC64;
MSGAIFTSLE GPGALDGTSG HPLVCPLCHA QYERPCLLDC FHEFCAGCLR GRAADGRLAC
PLCQHQTVVK GPSGLPPVDR LLQFLVDSSG DGTEVVRCAN CDLECGKQDA ETTYFCNTCG
QPLCARCRDE THRARMFARH DIVALGQRSR DVLQKCTLHA EPYVLFSTDK KSLLCIRCFR
DMQGESRVHC VDLESAYVQG CERLQQAVLE VKALQTATRE AIELLQAMVE EVRRSAAEEE
AAIQALFSSM QDKLSERKAL LLQAVQSLAN KAEFLDLGYE LMERLQGIVT RPHRLRPAQS
SKITSDHRAE FARCLEPLLL LGPRRAAGAG GGTSTLTGGL GPKVLRGPGC PSPVGKMLGS
PVQKPTLHRS ISTKVLLAEG DASPFTEHCR HYEDSYRRLQ AEMQNLKDQV QELHRDLTKH
HSLIKAEIMG DILHKALQVD AQIASEYASV EGLRAVFQEI WEDSYQRVAN EQEIYEAQLH
DLLQLKQENA YLTTITKQIT PYIRSIAKVK ERLEPRFQVP VDEPSDHPQN THDDGVNAEA
PARVSTLKPA MEKEVS
//
