ID A0A8I3WQ15_CALJA Unreviewed; 1301 AA.
AC A0A8I3WQ15;
DT 25-MAY-2022, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 1.
DT 10-JUN-2026, entry version 20.
DE RecName: Full=Zinc finger transcription factor Trps1 {ECO:0000256|ARBA:ARBA00073694};
GN Name=TRPS1 {ECO:0000313|Ensembl:ENSCJAP00000094249.1};
OS Callithrix jacchus (White-tufted-ear marmoset) (Simia Jacchus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000094249.1, ECO:0000313|Proteomes:UP000008225};
RN [1] {ECO:0000313|Ensembl:ENSCJAP00000094249.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCJAP00000094249.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JAN-2026) to UniProtKB.
CC -!- FUNCTION: Transcriptional repressor. Binds specifically to GATA
CC sequences and represses expression of GATA-regulated genes at selected
CC sites and stages in vertebrate development. Regulates chondrocyte
CC proliferation and differentiation. Executes multiple functions in
CC proliferating chondrocytes, expanding the region of distal
CC chondrocytes, activating proliferation in columnar cells and supporting
CC the differentiation of columnar into hypertrophic chondrocytes.
CC {ECO:0000256|ARBA:ARBA00058641}.
CC -!- SUBUNIT: Interacts with RNF4; regulates TRPS1 repressor activity.
CC Interacts specifically with the activator form of GLI3 (GLI3A) but not
CC with the repressor form (GLI3R). {ECO:0000256|ARBA:ARBA00066009}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR RefSeq; XP_054102275.1; XM_054246300.1.
DR RefSeq; XP_054102276.1; XM_054246301.1.
DR Ensembl; ENSCJAT00000141951.1; ENSCJAP00000094249.1; ENSCJAG00000005928.6.
DR GeneID; 100406167; -.
DR CTD; 7227; -.
DR GeneTree; ENSGT00940000157893; -.
DR OMA; YESCHSM; -.
DR OrthoDB; 515401at2759; -.
DR Proteomes; UP000008225; Chromosome 16.
DR GO; GO:0000785; C:chromatin; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IEA:Ensembl.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:UniProtKB-KW.
DR GO; GO:0001501; P:skeletal system development; IEA:Ensembl.
DR CDD; cd00202; ZnF_GATA; 1.
DR FunFam; 3.30.160.60:FF:001213; Transcriptional repressor GATA binding 1; 1.
DR FunFam; 3.30.50.10:FF:000020; Zinc finger transcription factor Trps1; 1.
DR FunFam; 3.30.160.60:FF:000674; zinc finger transcription factor Trps1 isoform X2; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 2.
DR Gene3D; 3.30.50.10; Erythroid Transcription Factor GATA-1, subunit A; 1.
DR InterPro; IPR028440; TRPS1.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR InterPro; IPR000679; Znf_GATA.
DR InterPro; IPR013088; Znf_NHR/GATA.
DR PANTHER; PTHR47034; ZINC FINGER TRANSCRIPTION FACTOR TRPS1; 1.
DR PANTHER; PTHR47034:SF1; ZINC FINGER TRANSCRIPTION FACTOR TRPS1; 1.
DR Pfam; PF00320; GATA; 1.
DR Pfam; PF27058; Znf_C2H2_Trps1_1st; 1.
DR Pfam; PF27065; Znf_C2H2_Trps1_2nd; 1.
DR Pfam; PF27047; Znf_C2H2_Trps1_3rd; 1.
DR Pfam; PF27082; Znf_C2H2_Trps1_4th; 1.
DR Pfam; PF27088; Znf_C2H2_Trps1_5th; 1.
DR PRINTS; PR00619; GATAZNFINGER.
DR SMART; SM00355; ZnF_C2H2; 9.
DR SMART; SM00401; ZnF_GATA; 1.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 1.
DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR PROSITE; PS00344; GATA_ZN_FINGER_1; 1.
DR PROSITE; PS50114; GATA_ZN_FINGER_2; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000008225};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Repressor {ECO:0000256|ARBA:ARBA00022491};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00042}.
FT DOMAIN 712..740
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 910..968
FT /note="GATA-type"
FT /evidence="ECO:0000259|PROSITE:PS50114"
FT REGION 19..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 503..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 878..906
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 981..1020
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1059..1098
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1189..1216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..83
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..182
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..209
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..532
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 981..997
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1000..1015
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1060..1069
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1070..1079
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1080..1092
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1301 AA; 143921 MW; CEDCA65F28EC1ACD CRC64;
MIEYSFLSHF GKSRLEFKRD MVRKKNPPLR NVASEGEGQI LEPIGTESKV SGKNKEFSAD
QMSENTDQSD AAEVNHKEEH SLHVQDPSSS SKKDLKSVVL SEKAGFNYES PSKGGSLPSF
PHDEVTDRNM LAFSSPAAGG VCEPLKSPQR AEADDPQDTA CTPSGDSLET KEDQKMSPKA
TEETGQAHSG QANCQGLSPV SVASKNPQVP SDGGVRLNKS KTDLLVNDNP DPAPLSPELQ
DFKCNICGYG YYGNDPTDLI KHFRKYHLGL HNRTRQDAEL DSKILALHNM VQFSHSKDLQ
KVNRSVFSGV LQDINSSRPV LLNGTYDVQV TSGGTFIGIG RKTPDCQGNT KYFRCKFCNF
TYMGNSSTEL EQHFLQTHPN KIKASLPSSE VVKSSEKNSN KSIPALRSSD SGDLGKWQDK
ITVKAGDDTP VGYSVPIKPL DSSRQNGTEA TSYYWCKFCS FSCESSSSLK LLEHYGKQHG
AVQSGGLNPE LNDKLSRGSV INQNDLAKSS EGETMIKADK SSSGAKKKDF SSKGAEDNMV
TSYNCQFCDF RYSKSHGPDV IVVGPLLRHY QQLHNIHKCT IKHCPFCPRG LCSPEKHLGE
ITYPFACRKS NCSHCALLLL HLSPGAAGSS RVKHQCHQCS FTTPDVDILL FHYESVHESQ
ASDVKQEANH LQGSDGQQAV KESKEHSCTK CDFITQVEEE ISRHYRRAHS CYKCRQCSFT
AADTQSLLEH FNTVHCQEQD ITTANGEEDG HAISTIKEEP KIDFKVYNLL TPDSKMGEPV
SESVVKREKL EEKDGLKEKV WTESSSDDLR NVTWRGADIL RGSPSYTQAS LGLLTPVSST
QEQTKTLRDS PNVEAAHLAR PIYGLAVETK GFLQGVPAGG EKSGALPQQY PASGENKSKD
ESQSLLRRRR GSGVFCANCL TTKTSLWRKN ANGGYVCNAC GLYQKLHSTP RPLNIIKQNN
GEQIIRRRTR KRLNPEALQA EQLNKQQRGS SEEQVNGSPL ERRSEDHLTE SHQREIPLPS
LSKYEAQGSL TKSHSAQQPV LVSQTLDIHK RMQPLHIQIK SPQESTGDPG NSSSVSEGKG
SSERGSPIEK YMRPAKHPNY SPPGSPIEKY QYPLFGLPFV HNDFQSEADW LRFWSKYKLS
VPGNPHYLSH VPGLPNPCQN YVPYPTFNLP PHFSAVGSDN DIPLDLAIKH SRPGPTANGA
SKEKTKAPPN VKNEGPLNVV KTEKVDRSTQ DELSTKCVHC GIVFLDEVMY ALHMSCHGDS
GPFQCSICQH LCTDKYDFTT HIQRGLHRNN AQVEKNGKPK E
//
