ID A0A493TVP7_ANAPP Unreviewed; 1265 AA.
AC A0A493TVP7;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Zinc finger protein 532 {ECO:0000313|Ensembl:ENSAPLP00000029630.1};
GN Name=ZNF532 {ECO:0000313|Ensembl:ENSAPLP00000029630.1};
OS Anas platyrhynchos platyrhynchos (Northern mallard).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC Anatinae; Anas.
OX NCBI_TaxID=8840 {ECO:0000313|Ensembl:ENSAPLP00000029630.1, ECO:0000313|Proteomes:UP000016666};
RN [1] {ECO:0000313|Ensembl:ENSAPLP00000029630.1, ECO:0000313|Proteomes:UP000016666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Hou Z.-C., Zhou Z.-K., Zhu F., Hou S.-S.;
RT "A new Pekin duck reference genome.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSAPLP00000029630.1}
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 AlphaFoldDB; A0A493TVP7; -.
DR Ensembl; ENSAPLT00000033848.1; ENSAPLP00000029630.1; ENSAPLG00000010349.2.
DR GeneTree; ENSGT00940000154437; -.
DR Proteomes; UP000016666; Chromosome Z.
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; 5.
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:SF3; ZINC FINGER PROTEIN 532; 1.
DR PANTHER; PTHR47222; ZINC FINGER PROTEIN 532-RELATED; 1.
DR Pfam; PF00096; zf-C2H2; 1.
DR Pfam; PF16622; zf-C2H2_11; 1.
DR Pfam; PF13912; zf-C2H2_6; 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; 9.
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:UP000016666};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00042}.
FT DOMAIN 642..660
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 778..808
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 807..834
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 870..897
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 901..929
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 989..1017
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1019..1047
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1167..1195
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1228..1250
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REGION 99..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 131..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 310..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 931..983
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1087..1106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1193..1224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..145
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..161
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..329
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..382
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 940..958
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 959..983
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1210..1224
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1265 AA; 138644 MW; 2BADEA6C43D2374D CRC64;
MKSWMGKSVC QEGKLVQFFT DLLTIKYMTM GDMKTPDFDD LLAAFDIPDM VDPKAAIESG
HDDHESHIKQ NAHTDEDSHA PSSSDVGVSV IVKNVRTIDS SEGVDKDGHH STGNGLHNGF
LTSSALDSYS KDEGKSFKDD GSTSESTLKD SAFNQFSPIS SAEEFDDDEK IEVDDPPDKE
EMRANFRANV LTGSVSQQEY DKLKALGGEN LIKSGIPVSS SIDKNKVAKR ETETNSVNLS
VYEPFKARKA EDKLLKDNSE KLLENRVLDG KLSTEKSETS LASISQSKAK SSAKLSSCIA
AIAALSAKKA ATDTSKDLQS NSGESSPLPK DMSESPRAME KSPESQSLID GAKKPSVKPP
DSPRSVSSEN SSKGSPSSPA GSTPAIPKVR IKTIKTSSGE IKRTVTRVLP EVDLDSGKKT
EQSASMVTSM TSLLSSPTSA VLSSPPRAPL QSAVVTNAVA SAELAPKQVT IKPVATAFLP
VSAVKTAGSQ VINLKLANNT TVKATVISAA SVQSASSAII KAANAIQQQT VVVPASSLAS
AKLVPKTVHL ANLNLLPQGA QTTSELRQVL TKPQQQIKQA IISAAASQPS KKVSRVQVVS
SLQSSVVEAF NKVLSSVNPV PVYIPNLSPP ANAGITLPTR GYKCLECGDS FALEKSLTQH
YDRRSVRIEV TCNHCTKNLV FYNKCSLLSH ARGHKEKGVV MQCSHLILKP VPADQMIASP
SSNTATSMLQ SPVGVGTHTV TKIQSGITGT VISAPASTPI IPAMPLDEDP SKLCRHGLKC
LECNEVFQDE TSLATHFQQA ADTSGQKTCN ICQMLLPNQC SFASHQRIHQ HKSPYTCPEC
GAICRSVHFQ THVTKNCLHY TRRVGFRIIY KCSMCDTVFT LQPLLYRHFD QHIENQKVSV
FKCPDCSLLY AQKQLMMDHI KSMHGTLKSV EGPPNLGINL PLSTKPTNQN STSHNKEDTK
SVNGTEKLEK KSPSPIKKGE PKKVTSRGWT CWECDRFFTQ RDVYISHMRK EHGKQMKKHP
CRQCDKSFSS SHSLCRHNRI KHKGIRKVYT CSHCPDSRRT FTKRLMLEKH IQLMHGIKDP
DVKEMTESTN MEEREVKEDT KVPSPKRKLE EPILEFRPPR GAITQPLKKL KINVFKVHKC
AVCGFTTENL LQFHEHIPQH KSDGSSYQCR ECGLCYTSHV SLSRHLFIVH KLKEPQPVSK
QNGSGEDNQQ ENKPNHEDES SDNTVSDRRC KVCAKTFETE AALNTHMRTH GMAFIKSKRM
SSAEK
//
