ID A0A2Y9JC57_ENHLU Unreviewed; 1019 AA.
AC A0A2Y9JC57;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=PHD finger protein 20-like protein 1 {ECO:0000256|ARBA:ARBA00014842};
GN Name=LOC111146781 {ECO:0000313|RefSeq:XP_022358171.1};
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_022358171.1};
RN [1] {ECO:0000313|RefSeq:XP_022358171.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022358171.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR RefSeq; XP_022358171.1; XM_022502463.1.
DR AlphaFoldDB; A0A2Y9JC57; -.
DR STRING; 391180.A0A2Y9JC57; -.
DR KEGG; elk:111146781; -.
DR OrthoDB; 5491784at2759; -.
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:0140034; F:methylation-dependent protein binding; IEA:UniProt.
DR CDD; cd20104; MBT_PHF20L1-like; 1.
DR CDD; cd15633; PHD_PHF20L1; 1.
DR CDD; cd20454; Tudor_PHF20L1; 1.
DR Gene3D; 2.30.30.140; -; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR014002; Agenet_dom_plant.
DR InterPro; IPR040477; KDM4-like_Tudor.
DR InterPro; IPR043449; PHF20-like.
DR InterPro; IPR002999; Tudor.
DR InterPro; IPR047405; Tudor_PHF20L1.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR15856:SF26; PHD FINGER PROTEIN 20-LIKE PROTEIN 1; 1.
DR PANTHER; PTHR15856; PHD FINGER PROTEIN 20-RELATED; 1.
DR Pfam; PF16660; PHD20L1_u1; 1.
DR Pfam; PF20826; PHD_5; 1.
DR Pfam; PF18104; Tudor_2; 1.
DR SMART; SM00743; Agenet; 2.
DR SMART; SM00249; PHD; 1.
DR SMART; SM00333; TUDOR; 2.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 2.
DR PROSITE; PS01359; ZF_PHD_1; 1.
PE 4: Predicted;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW 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}.
FT DOMAIN 11..73
FT /note="Agenet"
FT /evidence="ECO:0000259|SMART:SM00743"
FT DOMAIN 11..71
FT /note="Tudor"
FT /evidence="ECO:0000259|SMART:SM00333"
FT DOMAIN 85..141
FT /note="Agenet"
FT /evidence="ECO:0000259|SMART:SM00743"
FT DOMAIN 85..141
FT /note="Tudor"
FT /evidence="ECO:0000259|SMART:SM00333"
FT DOMAIN 683..727
FT /note="Zinc finger PHD-type"
FT /evidence="ECO:0000259|SMART:SM00249"
FT REGION 183..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 308..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 388..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 482..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 865..923
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..214
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..236
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..346
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..455
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..561
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..579
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 894..919
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1019 AA; 115258 MW; AE2482E5DEA78A5C CRC64;
MSKKPPNRPG ITFEIGARLE ALDYLQKWYP SRIEKIDYEE GKMLVHFERW SHRYDEWIYW
DSNRLRPLER PALRKEGLKD EEDFFDFKAG EEVLARWTDC RYYPAKIEAI NKEGTFTVQF
YDGVIRCLKR MHIKAMPEDA KGQVKSQHPL SWCCPIDPAG SCNQSMGSED WIALVKAAAA
AAAKNKTGSK PRASANSNKE KEKDDRKWFK VPSKKEETST SIASAEVEKK EDLPTSSETF
GLHVENVPKM VFPQPESTLS NKRKNNQGNS FQAKRARLNK ITGLLASKAV GVDGADRKED
CTETAPMLEQ AISPKPQSQK KNEADISSSA NTQKPALLSS TLSSGKARSK KCKHESGDSS
GCIKPPKSPL SPELIQVEDL TLVSQLSSSV INKTSSPQPV NPPRPFKHSE RRRRSQRLAT
LPMPDDSVEK VSPPSPATDG KVFSISSQNP QESSVPEVPD VAHLSLEKLG PCLPLDLSRG
SEVSAPLAPD PAYHNECPRA EKEDTQMLTN PASRAIADGR GAPTASGISK TEKKVKLEEK
SSTAFGKRKE KDKERKEKKD KDHYKPKQKK KKKKKKKSKQ HDYSDYEDSS LEFLERCSSP
LTRSSGSSLA LRSMFTEKNT TYQYPRAILS VDLSGENLSD VEFLDDSSTE SLLLSGDEYN
QDFDSTNFEE SQDEDDALNE IVRCICEMDE ENGFMIQCEE CLCWQHSVCM GLLEESIPEQ
YICYVCRDPP GQRWSAKYRY DKDWLDNGRM CGLSFLKENY SHLNAKKIVS THHLLADVYG
VTEVLHGLQL KIGILKNKHH PDLHLWACSG KRKDQDQGIA GIEKKVAVQD TVNIEEKKYH
IQNHKEPPRL PLKMEGTYIT SEHSYQKPQH FGQDCKSLVD PGSSDDDDVS SFEEEQEFHT
KDKNRSHYSV KEDGMPEKNP AERNTVFIYN DKKGTEDPGD SHLQWQLNLL THIENMQNEV
TSRMDLIEKE VDVLESWLDF TGELEPPDPL ARLPQLKRHI KQLLIDMGKV QQIATLCSV
//