ID A0A096MFZ6_POEFO Unreviewed; 1164 AA.
AC A0A096MFZ6;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Zinc finger protein 592 {ECO:0000313|Ensembl:ENSPFOP00000030337.1};
OS Poecilia formosa (Amazon molly) (Limia formosa).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000030337.1, ECO:0000313|Proteomes:UP000028760};
RN [1] {ECO:0000313|Proteomes:UP000028760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA Schartl M., Warren W.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPFOP00000030337.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: May be involved in transcriptional regulation.
CC {ECO:0000256|ARBA:ARBA00003767}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000256|ARBA:ARBA00006991}.
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DR EMBL; AYCK01011353; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A096MFZ6; -.
DR Ensembl; ENSPFOT00000031726.1; ENSPFOP00000030337.1; ENSPFOG00000003802.2.
DR GeneTree; ENSGT00940000158357; -.
DR Proteomes; UP000028760; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 4.
DR InterPro; IPR045914; Zn532-like.
DR InterPro; IPR041697; Znf-C2H2_11.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR47222; ZINC FINGER PROTEIN 532-RELATED; 1.
DR PANTHER; PTHR47222:SF1; ZINC FINGER PROTEIN 592; 1.
DR Pfam; PF00096; zf-C2H2; 2.
DR Pfam; PF16622; zf-C2H2_11; 1.
DR SMART; SM00355; ZnF_C2H2; 13.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 4.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 7.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 7.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000028760};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00042}.
FT DOMAIN 727..754
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 814..842
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 881..909
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 963..991
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 993..1021
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1104..1131
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1133..1161
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REGION 199..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 249..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 382..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 910..960
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..280
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..319
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..355
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..434
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1164 AA; 129344 MW; 1F60764AEB7B5CFC CRC64;
MGDMKTPDFD DLLAAFDIPD ATGLDSKEAI QESHEEIDNQ LKHSVICLDD SLLSNPDATT
ADIPLVSVIV KNTSRQESLE GFSDQLHSVT ALQNGFKGQE ACVKPVEPSN TSFSNSFQAD
LNGEGSRELP GEIPLQQKPD ETAVFSPSLS HFSPPYSPQT EALYSNNQKV SKQEGPCCLE
ARILAEPLVP GREQKSDIFL FDASPKNTKE STPENGRSND HLSDSYIRGE TENTTRACCP
FTSLSSEQNF KEAESQNTED VTNSYSSAKF QTSKLPLSNE APIAPNTKKD PTETTDPTES
SASNSDCVKA NNMAAISPRS PRSPNVVKRL MKPSDSPVSL CSDSSGKTSP AVASVSSPAI
PRVRIKTIKT TSGQIKRTVT SVLPDSETDE IHSAYESSPS QSMISEDSYC NVSPRQSQAV
DCSPGSNPAA CTSSPKMPRR SEEKSRGFRT GFHRSSRAVQ RSVAHDAQKP KRASSTTGLT
SNTNFLPKAM HLASLNLVPH SVAASVAARP SSHQQSQNIL PSSVCSTVPL VHQVKTATPF
PRSSAPNTAA GTLNRLLTSA NPVPVYVPNL SPPPECNIKL PPRGYCCLEC GDSFGVERSL
AFHYNRRSVQ IEVGCTHCAK TLVFFNRCAL LAHAREHKSN GSVMQCTQLH LKPISEEQMF
VPLSSESANT GPYPSTFVSP VSEPVMPLYP DGVIRNRFRC LECNKQLPDY KALAGHYQKM
SEDVEGLICK VCSMLLPNKC SFRTHQRLHA HKSPYCCPEC GAPSRSADIQ KHVKENCLHY
ARKAWYKCLH CDMVFRTLLG QKTHVEEKHC EVLYKCSVCP VAFKTSDGCE VHLKNKHKSS
RQTPHFCRLV FKCSCKALFN KKHNFFQHFH ENANKRVTCV FKCPECNSVF PQKRLLMQHF
KTVHVGNMTA DTEKDSKEKE GLDWFPESHP VQREKSHITR KNTDSPRKKS EQDPKSRVKP
RGWTCGECLQ CFAERESYVS HMKINHGKSM KKYPCRHCEL SFNAATSLRR HIRSEHDGKR
RIYSCWYCTD PKTTFTTSVM LKNHISLMHG IKNPDLRQMP KSSIKEFKSP SGIILASPVR
RRQADTPDRS DLDAPSAKRL KAQFRCSKCG FTTDDSTEFQ QHIPQHKTDE NTPQCLHCGL
CFTSVVSLNR HLFIVHKVKD PSEG
//
