ID A0A2Y9J1S3_ENHLU Unreviewed; 593 AA.
AC A0A2Y9J1S3;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Metal-response element-binding transcription factor 2 isoform X1 {ECO:0000313|RefSeq:XP_022352030.1};
GN Name=LOC111142966 {ECO:0000313|RefSeq:XP_022352030.1};
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_022352030.1};
RN [1] {ECO:0000313|RefSeq:XP_022352030.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022352030.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the Polycomblike family.
CC {ECO:0000256|ARBA:ARBA00008084}.
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DR RefSeq; XP_022352030.1; XM_022496322.1.
DR AlphaFoldDB; A0A2Y9J1S3; -.
DR STRING; 391180.A0A2Y9J1S3; -.
DR KEGG; elk:111142966; -.
DR OrthoDB; 5483634at2759; -.
DR Proteomes; UP000248482; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035064; F:methylated histone binding; IEA:UniProt.
DR CDD; cd15578; PHD1_MTF2; 1.
DR CDD; cd15580; PHD2_MTF2; 1.
DR CDD; cd20450; Tudor_MTF2; 1.
DR Gene3D; 2.30.30.140; -; 1.
DR Gene3D; 3.90.980.20; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR040477; KDM4-like_Tudor.
DR InterPro; IPR025894; Mtf2_C_dom.
DR InterPro; IPR042014; MTF2_PHD1.
DR InterPro; IPR042015; MTF2_PHD2.
DR InterPro; IPR002999; Tudor.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR12628:SF12; METAL-RESPONSE ELEMENT-BINDING TRANSCRIPTION FACTOR 2; 1.
DR PANTHER; PTHR12628; POLYCOMB-LIKE TRANSCRIPTION FACTOR; 1.
DR Pfam; PF14061; Mtf2_C; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF18104; Tudor_2; 1.
DR SMART; SM00249; PHD; 2.
DR SMART; SM00333; TUDOR; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 2.
DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000248482};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 102..157
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 357..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..401
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..474
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 593 AA; 67110 MW; 62757029743EA13A CRC64;
MRDSTGAGNS LVHKRSPLRR NQKTPTSLTK LSLQDGHKVK KPACKFEEGQ DVLARWSDGL
FYLGTIKKIN ILKQSCFIIF EDSSKSWVLW KDIQTGATGS GEMVCTICQE EYSEAPNEMV
ICDKCGQGYH QLCHTPHIDS SVIDSDEKWL CRQCVFATTT KRGGALKKGP NAKALQVMKQ
TLPYSVADLE WDAGHKTNVQ QCYCYCGGPG DWYLKMLQCC KCKQWFHEAC VQCLQKPMLF
GDRFYTFICS VCSSGPEYLK RLPLQWVDIA HLCLYNLSVI HKKKYFDSEL ELMTYINENW
DRLHPGELAD TPKSERYEHV LEALNDYKTM FMSGKEIKKK KHLFGLRIRV PPVPPNVAFK
AEKEPEGTSH EFKIKGRKAS KPISDSREVS NGIEKKGKKK SVGRPPGPYT RKMIQKTAEP
PLDKESISEN PTLDLPSPIG RTEGTAHTSN TSDVDFTGAS SAKETTSSSI SRHYGLSDSR
KRTRTGRSWP AAIPHLRRRR GRLPRRALQT QNSEIVKDDE GKEDYQFDEL NTEILNNLAD
QELQLNHLKN SITSYFGAAG RIACGEKYRV LARRVTLDGK VQYLVEWEGA TAS
//
