ID A0A3B1IZS6_ASTMX Unreviewed; 1081 AA.
AC A0A3B1IZS6;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-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};
OS Astyanax mexicanus (Blind cave fish) (Astyanax fasciatus mexicanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Characidae; Astyanax.
OX NCBI_TaxID=7994 {ECO:0000313|Ensembl:ENSAMXP00000035572.1, ECO:0000313|Proteomes:UP000018467};
RN [1] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RA Jeffery W., Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RX PubMed=25329095; DOI=10.1038/ncomms6307;
RA McGaugh S.E., Gross J.B., Aken B., Blin M., Borowsky R., Chalopin D.,
RA Hinaux H., Jeffery W.R., Keene A., Ma L., Minx P., Murphy D., O'Quin K.E.,
RA Retaux S., Rohner N., Searle S.M., Stahl B.A., Tabin C., Volff J.N.,
RA Yoshizawa M., Warren W.C.;
RT "The cavefish genome reveals candidate genes for eye loss.";
RL Nat. Commun. 5:5307-5307(2014).
RN [3] {ECO:0000313|Ensembl:ENSAMXP00000035572.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR AlphaFoldDB; A0A3B1IZS6; -.
DR Ensembl; ENSAMXT00000048801.1; ENSAMXP00000035572.1; ENSAMXG00000018473.2.
DR GeneTree; ENSGT00940000156215; -.
DR Proteomes; UP000018467; Unassembled WGS sequence.
DR Bgee; ENSAMXG00000018473; Expressed in liver and 14 other cell types or tissues.
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; 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; IPR013087; Znf_C2H2_type.
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; 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.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 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:UP000018467};
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 490..520
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REGION 157..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 242..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 399..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 655..689
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 944..969
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..201
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..229
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..279
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..385
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..414
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 655..670
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 671..685
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1081 AA; 122315 MW; D24E92071EDE52F0 CRC64;
MSKKPPNRPG IAFEVGARVE AQDYLQKWYP SRIEKIDYEE GKMLVHFDRW SHRYDEWILW
DSSRLRPLER PALRKEGLKE EEEVSELRDG EEVLARWTDC RYYPAKIESV NKEGTYTVQF
YDGVVRCVKR IHIKSMPDDA KGQDWIALVK AATAAAKTKG GCRPRTSANS NKDREDRTDL
RFDELEEEEE EEDEADSDGL ASSDEDDCKP SPDELEMTKT KRRRSRQDSF CNVKRARVNK
VAGCVKSEND CKEELPMSVQ QPSSHRDPAA SNSPGEERTL SVVAQRHPLP LSTNSPGTSR
SRRLKHDSGE STISSTSTAA EPSPSPSSIH TLPDMNTAPS SSPQRRRRSQ RLATTSDPTC
PPSPHNQDSN QSSPRTDNTQ KADCDSGCVV KTEPCVNKPS TAASSIHTSS VPPPGTAQSP
VPEKERMTDM LLINHAAEKS SPAVTAAGIK TASRTPKANK HTREPLINIK RSDDPTSPNE
PLIDLDHNKF KCQIPGCTKA FRKAKLLDYH LKYYHNTDKE LESEVCSPER SGRTRATSAS
VPNSTLVEIP DNKRRRTVST SSSLSPQGHM LQLDCAGSCP KPPKFCKKKR SSASVSSDST
EVSLPPLTKE KTFDNFHDKM LKKVTDKDKH LETGLCIKTE RKFKIEEKCQ LIAGKKRDKE
RRDRKDKDPF KIKQKKKKKK KKKSKQHCYS DMDEVSVSYL ERSSFSPFRS STNSFSKHSA
FQYPRAILSV DLTGENLSDI DFLEDSTTES LLFSGDEYNQ DLDSITMEDF QDEEEVTANE
IVRCICEMDE ENGFMIQCEE CMCWQHSVCM GLLEDSIPEQ YICYICRDPP GQRWSAKYRH
DKDWLYKGHM YGLSFLAENY SHQNAKKIVS THQLLADVYS VKKVLHGLQL KMDVLQNKHN
PSLHLWASSW VNSDEDQPMG GVPDCIMFQE HFNQNSNPET YITSEHSYQK PSSTGHPHTQ
EQASQTTPQT VLLVPKEEEV SSAISLSGCM KESSSGQVEQ ARNCLQWQMN LLTHIEDVQN
NLAGRMDLIE KELDVLESWL DFTGELEPPD PLARLPQLKC RIKQLLTDLG KVQQMSTLCS
V
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