ID A0A2Y9IKG3_ENHLU Unreviewed; 617 AA.
AC A0A2Y9IKG3;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Zinc finger imprinted 2 {ECO:0000313|RefSeq:XP_022347779.1};
GN Name=LOC111139715 {ECO:0000313|RefSeq:XP_022347779.1};
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_022347779.1};
RN [1] {ECO:0000313|RefSeq:XP_022347779.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022347779.1};
RG RefSeq;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|PROSITE-ProRule:PRU00187}.
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DR RefSeq; XP_022347779.1; XM_022492071.1.
DR AlphaFoldDB; A0A2Y9IKG3; -.
DR STRING; 391180.A0A2Y9IKG3; -.
DR KEGG; elk:111139715; -.
DR OrthoDB; 5265736at2759; -.
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; 1.
DR CDD; cd07936; SCAN; 1.
DR Gene3D; 6.10.140.140; -; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 5.
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; PTHR24381; ZINC FINGER PROTEIN; 1.
DR PANTHER; PTHR24381:SF413; ZINC FINGER PROTEIN 436; 1.
DR Pfam; PF01352; KRAB; 1.
DR Pfam; PF02023; SCAN; 1.
DR Pfam; PF00096; zf-C2H2; 4.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00431; SCAN; 1.
DR SMART; SM00355; ZnF_C2H2; 5.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 3.
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; 5.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW ProRule:PRU00187}; Reference proteome {ECO:0000313|Proteomes:UP000248482};
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 102..180
FT /note="SCAN box"
FT /evidence="ECO:0000259|PROSITE:PS50804"
FT DOMAIN 224..295
FT /note="KRAB"
FT /evidence="ECO:0000259|PROSITE:PS50805"
FT DOMAIN 418..445
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 446..473
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 502..529
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 554..583
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 584..611
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REGION 278..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..305
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..364
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..381
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 617 AA; 70765 MW; AF527604A597B252 CRC64;
MRRGLGAKSD RELFSQARRR AGEVLGFRIF FSYDTALPII FHKVCSGATC LFEYLCPEAV
KMLHMTDVLD ILKNPQLFRL HDQEENPETI PIRNPGVLKV SHQKFRDFQY LSVTGPHQAV
SQIQELCRQW LQPETHTKEQ MMEQLVLEQF LNTLPEGVRS WVRSRKPKNS KEAGSLVASL
IQACGEKGFS PQDFVLAEER NTKEHQKDTE MSDSLSSAGS QELVTFQDVV VDFSPEELTY
LSAAQRNLYR EVMLENYRNL VSLGYRFSKP DIISQLEEEE SRVREEDSNT ELCQDGEERP
KTKDLTPEQS LPMEKSSSEA GMEDRMGGNF CSVSVGEPSD DPSDSCQVNQ EKPLSPVTMG
ESKSPAQERS HDSDDSESSS DLTKQSEGPP GKDPQERATP GVCTSSQPVD DEPFLQENRC
GFCERTFLTQ TARERHEQIH TGKKPFECKQ CGEAFYLMPH LTRHQRTHSS EKSFGCDEGR
KPFIQHADIC GRVRIRSQED YYECFQCGKA FIQDVHLFQH LKAHEAAKAL PPVLPRIKTY
LIRYQRKHDY VGERACQCCD CGKAFSRSSH LMQHYRIHAQ ERPYQCQLCG RCFSRPSYLT
QHYQLHSQMK PDECSYY
//