ID G3RE15_GORGO Unreviewed; 674 AA.
AC G3RE15;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 87.
DE RecName: Full=DNA-binding protein SATB {ECO:0000256|RuleBase:RU361129};
DE AltName: Full=Special AT-rich sequence-binding protein {ECO:0000256|RuleBase:RU361129};
GN Name=SATB2 {ECO:0000313|Ensembl:ENSGGOP00000013785.3};
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:ENSGGOP00000013785.3, ECO:0000313|Proteomes:UP000001519};
RN [1] {ECO:0000313|Ensembl:ENSGGOP00000013785.3, 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:ENSGGOP00000013785.3, 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:ENSGGOP00000013785.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00108,
CC ECO:0000256|RuleBase:RU000682}.
CC -!- SIMILARITY: Belongs to the CUT homeobox family.
CC {ECO:0000256|ARBA:ARBA00008190, ECO:0000256|RuleBase:RU361129}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CABD030017950; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030017951; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030017952; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030017953; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G3RE15; -.
DR SMR; G3RE15; -.
DR Ensembl; ENSGGOT00000014179.3; ENSGGOP00000013785.3; ENSGGOG00000014123.3.
DR eggNOG; KOG3755; Eukaryota.
DR GeneTree; ENSGT00390000008096; -.
DR HOGENOM; CLU_012559_1_0_1; -.
DR TreeFam; TF332714; -.
DR Proteomes; UP000001519; Chromosome 2B.
DR Bgee; ENSGGOG00000014123; Expressed in prefrontal cortex and 3 other cell types or tissues.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:UniProt.
DR GO; GO:0006338; P:chromatin remodeling; IEA:InterPro.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:UniProt.
DR CDD; cd00086; homeodomain; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR Gene3D; 1.10.260.40; lambda repressor-like DNA-binding domains; 2.
DR Gene3D; 1.10.260.70; SATB, CULT domain; 1.
DR Gene3D; 3.10.20.710; SATB, ubiquitin-like oligomerisation domain; 1.
DR InterPro; IPR003350; CUT_dom.
DR InterPro; IPR032355; CUTL.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR InterPro; IPR039673; SATB1/SATB2.
DR InterPro; IPR038216; SATB_CUTL_sf.
DR InterPro; IPR038224; SATB_ULD_sf.
DR InterPro; IPR032392; ULD.
DR PANTHER; PTHR15116; DNA-BINDING PROTEIN SATB FAMILY MEMBER; 1.
DR PANTHER; PTHR15116:SF15; DNA-BINDING PROTEIN SATB2; 1.
DR Pfam; PF02376; CUT; 2.
DR Pfam; PF16557; CUTL; 1.
DR Pfam; PF00046; Homeodomain; 1.
DR Pfam; PF16534; ULD; 1.
DR SMART; SM01109; CUT; 2.
DR SMART; SM00389; HOX; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 1.
DR SUPFAM; SSF47413; lambda repressor-like DNA-binding domains; 2.
DR PROSITE; PS51042; CUT; 2.
DR PROSITE; PS51983; CUTL; 1.
DR PROSITE; PS50071; HOMEOBOX_2; 1.
DR PROSITE; PS51982; ULD; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PROSITE-
KW ProRule:PRU00108};
KW Homeobox {ECO:0000256|ARBA:ARBA00023155, ECO:0000256|PROSITE-
KW ProRule:PRU00108};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW ProRule:PRU00108}; Reference proteome {ECO:0000313|Proteomes:UP000001519};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transcription {ECO:0000256|RuleBase:RU361129};
KW Transcription regulation {ECO:0000256|RuleBase:RU361129};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT DOMAIN 1..99
FT /note="ULD"
FT /evidence="ECO:0000259|PROSITE:PS51982"
FT DOMAIN 102..175
FT /note="CUTL"
FT /evidence="ECO:0000259|PROSITE:PS51983"
FT DOMAIN 291..378
FT /note="CUT"
FT /evidence="ECO:0000259|PROSITE:PS51042"
FT DOMAIN 414..501
FT /note="CUT"
FT /evidence="ECO:0000259|PROSITE:PS51042"
FT DOMAIN 553..614
FT /note="Homeobox"
FT /evidence="ECO:0000259|PROSITE:PS50071"
FT DNA_BIND 555..615
FT /note="Homeobox"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00108"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 376..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 521..558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 635..674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..414
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..551
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 635..653
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 654..674
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 674 AA; 76035 MW; 13400506610AFACC CRC64;
MERRSESPCL RDSPDRRSGS PDVKGPPPVK VARLEQNGSP MGARGRPNGA VAKAVGGIIK
LGRWNPLPLS YVTDAPDATV ADMLQDVYHV VTLKIQLQSC SKLEDLPAEQ WNHATVRNAL
KELLKEMNQS TLAKECPLSQ SMISSIVNST YYANVSATKC QEFGRWYKKY KKIKVERVER
ENLSDYCVLG QRPMHLPNMN QLASLGKTNE QSPHSQIHHS TPIRNQVPAL QPIMSPGLLS
PQLSPQLVRQ QIAMAHLINQ QIAVSRLLAH QHPQAINQQF LNHPPIPRAV KPEPTNSSVE
VSPDIYQQVR DELKRASVSQ AVFARVAFNR TQGLLSEILR KEEDPRTASQ SLLVNLRAMQ
NFLNLPEVER DRIYQDERER SMNPNVSMVS SASSSPSSSR TPQAKTSTPT TDLPIKVDGA
NINITAAIYD EIQQEMKRAK VSQALFAKVA ANKSQGWLCE LLRWKENPSP ENRTLWENLC
TIRRFLNLPQ HERDVIYEEE SRHHHSERMQ HVVQLPPEPV QVLHRQQSQP AKESSPPREE
APPPPPPTED SCAKKPRSRT KISLEALGIL QSFIHDVGLY PDQEAIHTLS AQLDLPKHTI
IKFFQNQRYH VKHHGKLKEH LGSAVDVAEY KDEELLTESE ENDSEEGSEE MYKVEAEEEN
ADKSKAAPAE IDQR
//
