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Database: UniProt
Entry: A0A2K6PGV0_RHIRO
LinkDB: A0A2K6PGV0_RHIRO
Original site: A0A2K6PGV0_RHIRO 
ID   A0A2K6PGV0_RHIRO        Unreviewed;       747 AA.
AC   A0A2K6PGV0;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Zinc finger protein 184 {ECO:0000313|Ensembl:ENSRROP00000015776.1};
GN   Name=ZNF184 {ECO:0000313|Ensembl:ENSRROP00000015776.1};
OS   Rhinopithecus roxellana (Golden snub-nosed monkey) (Pygathrix roxellana).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Colobinae; Rhinopithecus.
OX   NCBI_TaxID=61622 {ECO:0000313|Ensembl:ENSRROP00000015776.1, ECO:0000313|Proteomes:UP000233200};
RN   [1] {ECO:0000313|Ensembl:ENSRROP00000015776.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. {ECO:0000256|ARBA:ARBA00006991}.
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DR   AlphaFoldDB; A0A2K6PGV0; -.
DR   Ensembl; ENSRROT00000039918.1; ENSRROP00000015776.1; ENSRROG00000032055.1.
DR   GeneTree; ENSGT00940000162941; -.
DR   OMA; TIPTWER; -.
DR   Proteomes; UP000233200; Unplaced.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd07765; KRAB_A-box; 1.
DR   Gene3D; 6.10.140.140; -; 1.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 19.
DR   InterPro; IPR001909; KRAB.
DR   InterPro; IPR036051; KRAB_dom_sf.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR24399:SF54; GASTRULA ZINC FINGER PROTEIN XLCGF26.1-LIKE-RELATED; 1.
DR   PANTHER; PTHR24399; ZINC FINGER AND BTB DOMAIN-CONTAINING; 1.
DR   Pfam; PF01352; KRAB; 1.
DR   Pfam; PF00096; zf-C2H2; 19.
DR   SMART; SM00349; KRAB; 1.
DR   SMART; SM00355; ZnF_C2H2; 19.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 10.
DR   SUPFAM; SSF109640; KRAB domain (Kruppel-associated box); 1.
DR   PROSITE; PS50805; KRAB; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 19.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 19.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233200};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00042}.
FT   DOMAIN          24..95
FT                   /note="KRAB"
FT                   /evidence="ECO:0000259|PROSITE:PS50805"
FT   DOMAIN          218..245
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          246..273
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          274..301
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          302..329
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          330..357
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          358..385
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          386..413
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          414..441
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          442..469
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          470..497
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          498..525
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          526..553
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          554..581
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          582..609
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          610..637
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          638..665
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          666..693
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          694..721
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          722..747
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   REGION          187..208
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        187..207
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   747 AA;  86032 MW;  24EF277FA827E271 CRC64;
     MSQPDLLLML FPHTEICLVF QESVTFKDVI VDFTQEEWKQ LDPGQRDLFR DVTLENYTHL
     VSIGLQVSKP DVISQLEQGT EPWIMEPSIP VGTCADWETR LEDSMSAPEP DISEEELSPE
     VIVEKHKRDD SWSSNLLESW ECEGSLERQQ ANQQTLPKEI KLTEKTIPSW EKGPVNNEFG
     KSINVSSNLV TQEPSPEETS TKRSIKQNSN PVKKEKSCKC NECGKAFSYC SALIRHQRTH
     TGEKPYKCNE CEKAFSRSEN LINHQRIHTG DKPYKCDQCG KGFIEGPSLT QHQRIHTGEK
     PYKCDECGKA FSQRTHLVQH QRIHTGEKPY TCNECGKAFS QRGHFMEHQK IHTGEKPFKC
     DECDKTFTRS THLTQHQKIH TGEKTYKCNE CGKAFNGPST FIRHHMIHTG EKPYECNECG
     KAFSQHSNLT QHQKTHTGEK PYDCAECGKS FSYWSSLAQH LKIHTGEKPY KCNECGKAFS
     YCSSLTQHRR IHTREKPFEC SECGKAFSYL SNLNQHQKTH TQEKAYECKE CGKAFIRSSS
     LAKHERIHTG EKPYQCHECG KTFSYGSSLI QHRKIHTGER PYKCNECGRA FNQNIHLTQH
     KRIHTGAKPY ECAECGKAFR HCSSLAQHQK THTEEKPYQC NKCEKTFSQS SHLTQHQRIH
     TGEKPYKCNE CDKAFSRSTH LTEHQNTHTG EKPYNCNECR KTFSQSTYLI QHQRIHSGEK
     PFGCNDCGKS FRYRSALNKH QRLHPGI
//
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