ID G3RCS2_GORGO Unreviewed; 1300 AA.
AC G3RCS2;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 69.
DE SubName: Full=Zinc finger protein 536 {ECO:0000313|Ensembl:ENSGGOP00000013306.3};
GN Name=ZNF536 {ECO:0000313|Ensembl:ENSGGOP00000013306.3};
OS Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000013306.3, ECO:0000313|Proteomes:UP000001519};
RN [1] {ECO:0000313|Ensembl:ENSGGOP00000013306.3, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Scally A.;
RT "Insights into the evolution of the great apes provided by the gorilla
RT genome.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGGOP00000013306.3, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22398555; DOI=10.1038/nature10842;
RA Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT "Insights into hominid evolution from the gorilla genome sequence.";
RL Nature 483:169-175(2012).
RN [3] {ECO:0000313|Ensembl:ENSGGOP00000013306.3}
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 EMBL; CABD030113004; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030113005; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030113006; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030113007; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004060491.2; XM_004060443.2.
DR STRING; 9593.ENSGGOP00000013306; -.
DR Ensembl; ENSGGOT00000013687.3; ENSGGOP00000013306.3; ENSGGOG00000013640.3.
DR GeneID; 101136636; -.
DR KEGG; ggo:101136636; -.
DR CTD; 9745; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000156397; -.
DR HOGENOM; CLU_008125_0_0_1; -.
DR InParanoid; G3RCS2; -.
DR OMA; EKMTQGH; -.
DR OrthoDB; 3849084at2759; -.
DR TreeFam; TF332241; -.
DR Proteomes; UP000001519; Chromosome 19.
DR Bgee; ENSGGOG00000013640; Expressed in cerebellum and 3 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; 6.
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; 10.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 5.
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:UP000001519};
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 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 47..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 584..604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 650..739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 802..826
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 856..893
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 938..985
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1124..1260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..65
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..676
FT /note="Basic and acidic 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 856..877
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 938..976
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1191..1239
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1300 AA; 141334 MW; 927BD840C5CCDB6B CRC64;
MEEASLCLGV SSAEPEAEPH LSGPVLNGQY AMSQKLHQIT SQLSHAFPEL HPRPNPEEKP
PASLEEKAHV PMSGQPMGSQ MALLANQLGR EVDTSLNGRV DLQQFLNGQN LGIMSQMSDI
EDDARKNRKY PCPLCGKRFR FNSILSLHMR THTGEKPFKC PYCDHRAAQK GNLKIHLRTH
KLGNLGKGRG RVREENRLLH ELEERAILRD KQLKGSLLQP RPDLKPPPHA QQAPLAACTL
ALQANHSVPD VAHPVPSPKP ASVQEDAVAP AVGFRCTFCK GKFKKREELD RHIRILHKPY
KCTLCDFAAS QEEELISHVE KAHITAESAQ GQGPNGGGEQ SANEFRCEVC GQVFSQAWFL
KGHMRKHKDS FEHCCQICGR RFKEPWFLKN HMKVHLNKLS VKNKSPSDPE VPVPMGGMSQ
EAHANLYSRY LSCLQSGFMA PDKAGLSEPS QLYGKGELPM KEKEALGKLL SPISSMAHGV
PEGDKHSLLG CLNLVPPLKS SCIERLQAAA KAAEMDPVNS YQAWQLMARG MAMEHGFLSK
EHPLQRNHED TLANAGVLFD KEKREYVLVG ADGSKQKMPA DLVHSTKVGS QRDLPSKLDP
LESSRDFLSH GLNQTLEYNL QGPGNMKEKP TECPDCGRVF RTYHQVVVHS RVHKRDRKGE
EDGLHVGLDE RRGSGSDQES QSVSRSTTPG SSNVTEESGV GGGLSQTGSA QEDSPHPSSP
SSSDIGEEAG RSAGVQQPAL LRDRSLGSAM KDCPYCGKTF RTSHHLKVHL RIHTGEKPYK
CPHCDYAGTQ SASLKYHLER HHRERQNGAG PLSGQPPNQD HKDEMSSKAS LFIRPDILRG
AFKGLPGIDF RGGPASQQWT SGVLSSGDHS GQAAGMSSEV PSDALKGTDL PSKSTHFSEI
GRAYQSIVSN GVNFQGSLQA FMDSFVLSSL KKEKDIKDKA LADPPSMKVH GVDGGEEKPS
GKSSQRKSEK SQYEPLDLSV RPDAASLPGS SVTVQDSIAW HGCLFCAFTT SSMELMALHL
QANHLGKAKR KDNTIGVTVN CKDQAREASK MALLPSLQSN KDLGLSNMIS SLDSASEKMA
QGQLKETLGE QKSGAWTGHV DPAFCNFPSD FYKQFGVYPG MVGSGASSSC PNKEPDGKAH
SEEDAPILIP ENTSKNTTDD LSDIASSEDM DSSKGENNDE EDVETEPEMT TKPLSALSKD
SSSDGGDSLQ PTGTSQPIQG LVSPLSQAPE KQWHSQGLLQ AQEPLAGPPK PERGPQSLDK
PMNMLSVLRA YSSDGLAAFN GLASSTANSG CIKRPDLCGK
//
