ID   W5MBY1_LEPOC            Unreviewed;       649 AA.
AC   W5MBY1;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   RecName: Full=RING finger protein 207 {ECO:0000256|ARBA:ARBA00021526};
OS   Lepisosteus oculatus (Spotted gar).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC   Lepisosteus.
OX   NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000005890.1, ECO:0000313|Proteomes:UP000018468};
RN   [1] {ECO:0000313|Proteomes:UP000018468}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT   "The Draft Genome of Lepisosteus oculatus.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLOCP00000005890.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   EMBL; AHAT01009785; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_015192464.1; XM_015336978.1.
DR   AlphaFoldDB; W5MBY1; -.
DR   STRING; 7918.ENSLOCP00000005890; -.
DR   Ensembl; ENSLOCT00000005898.1; ENSLOCP00000005890.1; ENSLOCG00000004882.1.
DR   GeneID; 102685979; -.
DR   KEGG; loc:102685979; -.
DR   CTD; 568322; -.
DR   eggNOG; KOG2177; Eukaryota.
DR   GeneTree; ENSGT00510000048612; -.
DR   HOGENOM; CLU_034912_0_0_1; -.
DR   InParanoid; W5MBY1; -.
DR   OMA; ELDTMYF; -.
DR   OrthoDB; 2878026at2759; -.
DR   Proteomes; UP000018468; Linkage group LG25.
DR   Bgee; ENSLOCG00000004882; Expressed in heart and 6 other cell types or tissues.
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   CDD; cd16558; RING-HC_RNF207; 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; SM00336; BBOX; 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   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00024}.
FT   DOMAIN          25..64
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          93..145
FT                   /note="B box-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50119"
FT   REGION          629..649
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          430..457
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   649 AA;  74177 MW;  7189E49DC119FE68 CRC64;
     MSGGIFTPLD NLYDLDSANC HPLVCHLCHE QYEQPCLLDC YHTFCASCLR GRAIESRLTC
     PLCRQQSIVK GINGLPPEDR LLRFLVDNSA DCEETVQCAN CDFECKKQDV DAMYYCNTCN
     QPLCSTCREV THKAKMFSRH EIVSLAKRTK EAHKKCSLHE EPYIMFSTEK KSMLCINCFR
     DMQVESRAHC IDIETAYMQG CEKLDQAVLA VKELQTSARE AIVLLKAMIG EVRANVDEEE
     SAISTLFSSM QEKLAERKKI LLKAAQSQHE EKEKAFKEQL AHLAALLPTL QVHLVTCSAF
     LSSANKFEFL DLGYQLMERL KKIVKLPHRL RPAQSSKINT EYRSEFARCL EPLLMLNQRR
     SVSVTSVGGV SGMANSNGLL QSSLSVPCHS PSSSDMALTS SVVRKPTSHR YISTKVLLAE
     GGESPFTEHC RNYENMYRTL QTDIQKLKDQ VQEMHRDLTK HHSLIKTDTM GEILEKSLEM
     DVQIASEYSS VEMMRAMFEE IWEETFQRVA NEQEIYEAQL HDLLQLKQEN SYLTTIAKQI
     GPYIRSIAKV KERLEPRLKE PKELKDDRTE TMLKIYEDST MANEAQHRNE LSCTTDDDQE
     KLVDNRNKIL DNRALNILSE EPALKSKDYY WPGKQKNGVE ASSRKELTL
//