ID A0A2Y9IFK3_ENHLU Unreviewed; 1476 AA.
AC A0A2Y9IFK3;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=LOW QUALITY PROTEIN: zinc finger protein 287 {ECO:0000313|RefSeq:XP_022347452.1};
GN Name=LOC111139477 {ECO:0000313|RefSeq:XP_022347452.1};
OS Enhydra lutris kenyoni (northern sea otter).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Lutrinae; Enhydra.
OX NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022347452.1};
RN [1] {ECO:0000313|RefSeq:XP_022347452.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022347452.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00187}.
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DR RefSeq; XP_022347452.1; XM_022491744.1.
DR KEGG; elk:111139477; -.
DR OrthoDB; 4625041at2759; -.
DR Proteomes; UP000248482; 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; 2.
DR CDD; cd07936; SCAN; 1.
DR Gene3D; 6.10.140.140; -; 2.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 30.
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; PTHR23226; ZINC FINGER AND SCAN DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR23226:SF406; ZINC FINGER PROTEIN 684; 1.
DR Pfam; PF01352; KRAB; 2.
DR Pfam; PF02023; SCAN; 1.
DR Pfam; PF00096; zf-C2H2; 27.
DR SMART; SM00349; KRAB; 2.
DR SMART; SM00431; SCAN; 1.
DR SMART; SM00355; ZnF_C2H2; 29.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 16.
DR SUPFAM; SSF109640; KRAB domain (Kruppel-associated box); 2.
DR SUPFAM; SSF47353; Retrovirus capsid dimerization domain-like; 1.
DR PROSITE; PS50805; KRAB; 2.
DR PROSITE; PS50804; SCAN_BOX; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 27.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 30.
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:UP000248482};
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 1..73
FT /note="KRAB"
FT /evidence="ECO:0000259|PROSITE:PS50805"
FT DOMAIN 225..252
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 253..280
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 281..308
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 309..336
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 337..364
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 365..392
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 393..420
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 421..448
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 449..476
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 477..504
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 505..532
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 533..560
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 561..576
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 682..760
FT /note="SCAN box"
FT /evidence="ECO:0000259|PROSITE:PS50804"
FT DOMAIN 804..872
FT /note="KRAB"
FT /evidence="ECO:0000259|PROSITE:PS50805"
FT DOMAIN 1001..1028
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1029..1056
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1057..1084
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1085..1112
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1113..1140
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1141..1168
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1169..1196
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1197..1224
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1225..1252
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1253..1280
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1281..1308
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1309..1336
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1337..1364
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1365..1387
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1388..1415
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1416..1443
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1444..1474
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REGION 768..787
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1476 AA; 170061 MW; EA8ECD337AA364D3 CRC64;
MFKDVAIDFT LEEWRLMDPS QRKRKLHKDV ILENYRNLFS LGLAVSKPDM ISHLEAGKGP
WVVVREIART PYPELETKPA TTNAVSTEDV SEDVSQETVI DKLTENGLWN SRMGGLWKRN
ERIFRLQNSQ ENHLNQKIDG VTHKKIPSGQ RRFRFGSFLF PEAGIITEEP QSKCQTHENF
TGNLDLITDT HLEKKLCKDT EGGKAIRPTS ELTLGQKXNN KEKPYKCSTC EKSFHCRSLL
IQHQRTHTKE KPYECNECGK MFSQPSYLSQ HKKIHTGEKP YKCNECGKAF IKYSYLTVHH
RMHTGEKPYK CNECGKAFMR SSSLIVHQRI HTREKPYKCT DCERAFAKMV NLKEHQKIHT
GVKPYKCCDC EKSFRTKSYL TVHQRTHTGE KPYKCNECGK VFRRNSGFKT HQRTHTGVKP
FKCNDCGKAF SHMVHVTEHQ KIHSREKPYK CDVCGKAFRS SSYLTVHRLT HTGEKPYTCK
ECGKGCITPW RLTRHQRIHT GERPYKCEEC GKAFRTNSDL TVHLRVHTGE KPYKCNECGK
AFRTNSDLTV HLRKHTGEKP YKCNECGKAF RSSSSLTECE SGARAPAAIV APGLSGRSGC
ASARPPRQHE TSSIWLTTGD IKNIARLTLP PVAMLASCKR MTSSSRAQVL LMWKPDKAQS
GPHNIAKETL ASRILRDTET CRQNFRNFPY PDLAGPRKAL NQLRELCLKW LRPEIHSKEQ
ILELLVLEQF LTILPGEVRT WVKSQYPESS EEVVTLVEDL TQILEEEAVP QNTALPQETP
EEDSKGRPAF QAGWLNDLVT KESMTFKDVA VDITQEDWEI MRPVQKELYK TVTLQNYWNM
VSLGLTVYRP TVIPLLEEPW MVIKEILEGP SPEWKTEAQE CTPVTNTSTL VKTGTQTVKL
EEPYDYDEKF ERHASDTYRK IPTNGRNFTL KSVISKEDDP MEECLSKYDI YRNTFEKHSN
LIIQFGTQSD NKTMYDEGRA TFNHVSYGIV HRKIYPGEKP YKCNVCGKKF RKNPSFVKHQ
STHTKEKSHE CEECGKEFRH ISSLIAHQRM HTGEKPYECH QCGKAFSQRA HLTIHQRIHT
GEKPYKCDDC GKDFSQRAHL TIHQRTHTGE KPYRCLECGK TFSHSSSLIN HQRVHTGEKP
YICNECGKTF SQSTHLLQHQ KIHTGKKPYK CNECWKVFSQ STYLIRHQRI HSGEKCYKCN
ECGKAFAHSS TLIQHQTTHT GEKSYICKIC GKAFSQSANL TQHHRTHTGE KPYKCSVCGK
AFSQSVHLTQ HQRIHNGEKP FKCNICGKAY RQGANLTQHQ RIHTGEKPYK CNECGKAFIY
SSSLNQHQRT HTGERPYKCN ECDKDFSQRT CLIQHQRIHT GEKPYACRIC GKANLTQHQR
IHTGEKPYKC NECGKAFIYS SSLNQHQRTH TGERPYKCNE CDKDFSQRTC LIQHQRIHTG
EKPYACRICG KXXXTFTQST NLIQHQRVHT GAKHHN
//
