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Database: UniProt
Entry: H9GIQ1_ANOCA
LinkDB: H9GIQ1_ANOCA
Original site: H9GIQ1_ANOCA 
ID   H9GIQ1_ANOCA            Unreviewed;      1375 AA.
AC   H9GIQ1;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   29-SEP-2021, sequence version 3.
DT   27-MAR-2024, entry version 62.
DE   SubName: Full=Zinc finger protein 536 {ECO:0000313|Ensembl:ENSACAP00000012010.3};
GN   Name=ZNF536 {ECO:0000313|Ensembl:ENSACAP00000012010.3};
OS   Anolis carolinensis (Green anole) (American chameleon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Iguania; Dactyloidae; Anolis.
OX   NCBI_TaxID=28377 {ECO:0000313|Ensembl:ENSACAP00000012010.3, ECO:0000313|Proteomes:UP000001646};
RN   [1] {ECO:0000313|Ensembl:ENSACAP00000012010.3}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JBL SC #1 {ECO:0000313|Ensembl:ENSACAP00000012010.3};
RG   The Genome Sequencing Platform;
RA   Di Palma F., Alfoldi J., Heiman D., Young S., Grabherr M., Johnson J.,
RA   Lander E.S., Lindblad-Toh K.;
RT   "The Genome Sequence of Anolis carolinensis (Green Anole Lizard).";
RL   Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSACAP00000012010.3}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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   RefSeq; XP_003225480.1; XM_003225432.3.
DR   STRING; 28377.ENSACAP00000012010; -.
DR   Ensembl; ENSACAT00000012255.3; ENSACAP00000012010.3; ENSACAG00000012257.3.
DR   GeneID; 100553330; -.
DR   KEGG; acs:100553330; -.
DR   CTD; 9745; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000156397; -.
DR   HOGENOM; CLU_008125_0_0_1; -.
DR   InParanoid; H9GIQ1; -.
DR   TreeFam; TF332241; -.
DR   Proteomes; UP000001646; Unplaced.
DR   Bgee; ENSACAG00000012257; Expressed in testis and 6 other cell types or tissues.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IEA:Ensembl.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0044323; F:retinoic acid-responsive element binding; IEA:Ensembl.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0045665; P:negative regulation of neuron differentiation; IEA:Ensembl.
DR   GO; GO:0048387; P:negative regulation of retinoic acid receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IBA:GO_Central.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 7.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR45925; ZINC FINGER PROTEIN; 1.
DR   PANTHER; PTHR45925:SF2; ZINC FINGER PROTEIN 536; 1.
DR   Pfam; PF00096; zf-C2H2; 5.
DR   Pfam; PF16606; zf-C2H2_assoc; 1.
DR   Pfam; PF13909; zf-H2C2_5; 1.
DR   SMART; SM00355; ZnF_C2H2; 11.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 6.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 8.
PE   3: Inferred from homology;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001646};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00042}.
FT   DOMAIN          130..157
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          158..180
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          274..302
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          345..372
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          373..400
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          631..658
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          751..778
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          779..806
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   REGION          210..260
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          667..730
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          802..830
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          854..893
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          943..973
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1075..1099
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1153..1217
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1334..1375
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        215..252
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        677..726
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        877..893
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        955..973
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1076..1099
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1189..1203
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1334..1348
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1375 AA;  151359 MW;  92FBC7AD06F0465D CRC64;
     MEEASLCLGV SSAVPEADVH LNSSILNGQY SMSQKLHQIT SQLSHAFPEL QNRQNPEEKA
     STLLEDKSLA SIANQPISSQ MALLANQLNR EVDTTLNGRV DLQQFLNGQN LGIMSQMSDI
     EDDARKNRKY PCPLCGKRFR FNSILSLHMR THTGEKPFKC PYCDHRAAQK GNLKIHLRTH
     KLGNLGKGRG RVREENRLLH ELEERAILRD KQMKSSLLQP RSDNKSHPHS QPMPLANCNL
     PVPTNHSTPD ISNPVPSPKP ASVQEEVVAT AAGFRCTFCK GKFKKREELD RHIRILHKPY
     KCTLCDFAAS QEEELISHVE KAHITAESAQ GQGSNGNGEQ AANEFRCEVC GQVFSQAWFL
     KGHMRKHKDS FEHCCQICGR RFKEPWFLKN HMKVHLNKLS VKNKSPNDSE VPVSIGSMSQ
     EAHANLYSRY LSCLQSGFLP PDKASLSEQN QTYSKGDLPM KEREVLGKLL SPIAGIGHGL
     TEGDKHSLLG CLNLVPPLKS SCIERLQAAA KAAEMDPVNS YQAWQLMARG MAMEHGFLTK
     EHQIQRSHED TLANAGVMFD KEKREYVLVG ADGSKQKMPA DLVHSTKMGN QRDLSNKLDP
     LEGSRDFLSH GMNHGLDFNM QSHSNVKEKP TECPDCGRVF RTYHQVVVHS RVHKRDRKAE
     DEIIQASIEE RRGSGSDQES QSVSRSTTPG SSNITEESGM GGGLSQTGSA QEDSPHPSSP
     SSSDVGDEVG RSAGIQQPAL LRDRSLGSAM KDCPYCGKTF RTSHHLKVHL RIHTGEKPYK
     CPHCDYAGTQ SASLKYHLER HHRERQNGAG PLSGQSQSQD HKEETLNKGS MFIRPEVLRG
     AFKSLPGIDF RSGMGSQQWS PGMLSSGEHP GHSVGMSSDV SPDNMKSSDL SSKGTRFSEL
     GRAYHSMVGN GVNFQGSLQA FMDNFVLSSL KKEKEMKDKA LSDCLPTKPL GSESGEEKVS
     GKARKTEKSQ YEPLDLSVRP DATSLPGSSV TVQDNIAWHG CLFCSFTTSS MELMALHLQA
     NHLGKAKRKD GVLGLIRNGK DQSREAIASA NKASLLPTSI QSNKDAAVTN LIGQIDPASE
     RMNQGSKESP GEQKNTSWSG HMDSTFYNFA ADFYKQFGVY SGVVGAHNSF TTSETEIKTP
     SEDDSTMLLS DSVNKSATDD LSDIASSEDM ESSKEETIDD EDIETESDLM NKPLSSLNKD
     SAERGDSIQG AASKASQGLI SPLPLSEKQW HSQSLLPPHE AAQSEMKPEQ AQSPHVLEKQ
     VNMLSVLRAY SSDGLAAFNG LASSTGSSGC IKRPDLCGHR PFQCRYCPYS ASQKGNLKTH
     VLCVHRMPFD NSQYPDRRFK RSRVDSEASG NFEEPAAVKP GSSAELTEEG SKAQE
//
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