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Database: UniProt
Entry: A0A8B9WLD0_BOSMU
LinkDB: A0A8B9WLD0_BOSMU
Original site: A0A8B9WLD0_BOSMU 
ID   A0A8B9WLD0_BOSGR        Unreviewed;      1293 AA.
AC   A0A8B9WLD0;
DT   19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2022, sequence version 1.
DT   10-JUN-2026, entry version 21.
DE   RecName: Full=Zinc finger transcription factor Trps1 {ECO:0000256|ARBA:ARBA00073694};
GN   Name=TRPS1 {ECO:0000313|Ensembl:ENSBGRP00000007160.1};
OS   Bos grunniens (Wild yak) (Bos mutus grunniens).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=30521 {ECO:0000313|Ensembl:ENSBGRP00000007160.1, ECO:0000313|Proteomes:UP000694520};
RN   [1] {ECO:0000313|Ensembl:ENSBGRP00000007160.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Zhang S., Liu J.;
RL   Submitted (MAY-2019) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSBGRP00000007160.1}
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   Ensembl; ENSBGRT00000008217.1; ENSBGRP00000007160.1; ENSBGRG00000004435.1.
DR   GeneTree; ENSGT00940000157893; -.
DR   Proteomes; UP000694520; Chromosome 18.
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:UP000694520};
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          704..732
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          902..960
FT                   /note="GATA-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50114"
FT   REGION          1..210
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          376..407
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          495..523
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          654..674
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          870..898
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          974..1012
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1051..1087
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1181..1207
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        53..67
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        161..175
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        176..202
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        500..523
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        974..989
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        992..1007
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1052..1061
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1062..1071
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1072..1084
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1293 AA;  142300 MW;  3197CCE0E9444ABE CRC64;
     MPYEVNAGYD FTNMVRKKNP PLRNIASEGE GQTLEPVGTE SKGPGKNKEF SADQMSENTD
     QSDATELNNK EEHSLHVQDP SSSSKKDLKS SVLSEKAGFN YENSSKGGNL PSYSHDEVTE
     RNMLAFSSPA AGGVCEPLKS PQRAEADDPQ DMACTPSGDS LEMKEDQKMS PKATEETGQV
     QSGQANCQGS SPVSVASKNP QVPSDGGVRL NKSKTDVLVN DNPDPAPLSP ELQDFKCNIC
     GYGYYGNDPT DLIKHFRKYH LGLHNRTRQD AELDSKILAL HNMVQFSHSK DFQKVNRSVL
     SGVLQDISSS RPVLLNGTYD VQVTSGGTFI GIGRKTPDCQ GNTKYFRCKF CNFTYMGNSS
     TELEQHFLQT HPNKIKASLP SSEGAKPSEK NSNKSIPAVR SGDAGDLGKW QDKITVKAGD
     DSPVGYSVPI KPLDSRQNGT EATSYYWCKF CSFSCESSSS LKLLEHYGKQ HGGVQSGGLN
     PELNDKLSRG SVINQNDLTK SAEGEPMTKA DKGSSGVKKK DFSSKGAEDN MVTSYNCQFC
     DFRYSKSHGP DVIVVGPLLR HYQQLHNIHK CTIKHCPFCP RGLCSPEKHL GEITYPFACR
     KSNCSHCALL LLHLSPGAAG SSRVKHQCHQ CSFSTPDVDV LLFHYESAHE SQASDVKQEG
     SHLQGPDGQP AVKESKEHSC TKCDFITQVE EEISRHYRRA HSCYKCRQCS FTAAETQSLL
     EHFNTVHCQE QDSTTANGEE DGHAVSTIKE EPKIDLKVYS LLNPDSKMGE PVAESVVKRE
     KLEDKDGLKE KAWAESSSDD LRSVTWRGAD ILRGSPSYTQ ASLGLLTPVS GPQEQTKTLR
     DSPNVEAAHL ARPIYGLAVD TKGFLQGAPA GGEKAGALPQ QYPASGESKS KDESQSLLRR
     RRGSGVFCAN CLTTKTSLWR KNANGGYVCN ACGLYQKLHS TPRPLNIIKQ NNGEQIIRRR
     TRKRLNPEAL QAEQLNKQQR ASSEEQVNGS PLERRSEDHL TEGHQREIPL PSLSKYEAQG
     SLTKSHSAQQ PVLVSQTLDI HKRMQPLHIQ IKSPQESTGD PGNSSSVSEG KGSSERGSPI
     EKYMRPAKHP NYSPPGSPIE KYQYPLFGLP FVHNDFQSEA DWLRFWSKYK LSVPGNPHYL
     SHVPGLPNPC QNYVPYPTFN LPPHFSAVGS DNDIPLDLAI KHSRPGPTAN GASKEKTKAP
     SNVKNEGPLN VVKTEKVDRS TQDELSTKCV HCGIVFLDEV MYALHMSCHG DSGPFQCSIC
     QHLCTDKYDF TTHIQRGLHR NNAQVEKNGK PKE
//
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