ID A0A340WPG1_LIPVE Unreviewed; 538 AA.
AC A0A340WPG1;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Zinc finger protein 394 {ECO:0000313|RefSeq:XP_007448954.1};
GN Name=ZNF394 {ECO:0000313|RefSeq:XP_007448954.1};
OS Lipotes vexillifer (Yangtze river dolphin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Lipotidae; Lipotes.
OX NCBI_TaxID=118797 {ECO:0000313|Proteomes:UP000265300, ECO:0000313|RefSeq:XP_007448954.1};
RN [1] {ECO:0000313|RefSeq:XP_007448954.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00187}.
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DR RefSeq; XP_007448954.1; XM_007448892.1.
DR AlphaFoldDB; A0A340WPG1; -.
DR STRING; 118797.A0A340WPG1; -.
DR GeneID; 103079265; -.
DR KEGG; lve:103079265; -.
DR CTD; 84124; -.
DR InParanoid; A0A340WPG1; -.
DR OrthoDB; 5257133at2759; -.
DR Proteomes; UP000265300; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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 CDD; cd07936; SCAN; 1.
DR Gene3D; 6.10.140.140; -; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 6.
DR Gene3D; 1.10.4020.10; DNA breaking-rejoining enzymes; 1.
DR InterPro; IPR001909; KRAB.
DR InterPro; IPR036051; KRAB_dom_sf.
DR InterPro; IPR003309; SCAN_dom.
DR InterPro; IPR038269; SCAN_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR23234:SF10; GENE 10130-RELATED; 1.
DR PANTHER; PTHR23234; ZNF44 PROTEIN; 1.
DR Pfam; PF01352; KRAB; 1.
DR Pfam; PF02023; SCAN; 1.
DR Pfam; PF00096; zf-C2H2; 6.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00431; SCAN; 1.
DR SMART; SM00355; ZnF_C2H2; 7.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 4.
DR SUPFAM; SSF109640; KRAB domain (Kruppel-associated box); 1.
DR SUPFAM; SSF47353; Retrovirus capsid dimerization domain-like; 1.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS50804; SCAN_BOX; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 7.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|PROSITE-ProRule:PRU00187};
KW Reference proteome {ECO:0000313|Proteomes:UP000265300};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00042}.
FT DOMAIN 49..131
FT /note="SCAN box"
FT /evidence="ECO:0000259|PROSITE:PS50804"
FT DOMAIN 140..213
FT /note="KRAB"
FT /evidence="ECO:0000259|PROSITE:PS50805"
FT DOMAIN 337..364
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 370..397
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 398..425
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 426..452
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 453..480
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 481..508
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 509..536
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REGION 26..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 225..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..240
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..282
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 538 AA; 61449 MW; BFD38DD71D5BAB9E CRC64;
MSWIWTASQG RVAALPLSDG PWIVKVEEDS PGGGESDPPG DCPDPETSRR HFRRFRYQEV
AGPEAALSRL RELCRQWLRP EVHSKEQILE LLVLEQFLTI LPQELQAWVR KHCPESGEEA
AALVWALQRE LDGTLRQGLV TVQDVAVSLT WEEWERLGPA QRDLYRESAP KDYGNAVSPS
LETRIENKEL ILKQEILEEV EPQGQLQGPQ EKGPLSSECG VAHEDRIEKP SGDPSLLKLE
KPPEDQGVTS ISDLKSAPRE EGDSKNNELG TSARSSNFVP AQHIQTAERP ITGDEHGNNC
KHRLDTVKPH ESLDSGENCH HSSLLEAQRR FHEERPYTCD TCEKTFKQRS DLFKHQRTHT
GEKPYGCSPY ECQECGKSFS QSATLIKHQR THTGEKPYTC PKCGDSFRQS SHLNRHQRVH
MGQKHYTCHE CGETCRISNH FRHQRTHQGE RPYTCEECAK SFKRCSDLSK HQRIHTGEKP
YECQECGKSF SQSATLVKHQ RTHTGEKPYR CLECGDSFRQ SSHLIRHQRI HRNKAPSF
//
