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Database: UniProt
Entry: A0A6P6HS10_PUMCO
LinkDB: A0A6P6HS10_PUMCO
Original site: A0A6P6HS10_PUMCO 
ID   A0A6P6HS10_PUMCO        Unreviewed;      1287 AA.
AC   A0A6P6HS10;
DT   02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT   02-DEC-2020, sequence version 1.
DT   10-JUN-2026, entry version 24.
DE   RecName: Full=Zinc finger transcription factor Trps1 {ECO:0000256|ARBA:ARBA00073694};
GN   Name=TRPS1 {ECO:0000313|RefSeq:XP_025778590.1};
OS   Puma concolor (Mountain lion) (Felis concolor).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Puma.
OX   NCBI_TaxID=9696 {ECO:0000313|Proteomes:UP000515131, ECO:0000313|RefSeq:XP_025778590.1};
RN   [1] {ECO:0000313|RefSeq:XP_025778590.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_025778590.1};
RG   RefSeq;
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_025778590.1; XM_025922805.1.
DR   GeneID; 112859537; -.
DR   CTD; 7227; -.
DR   Proteomes; UP000515131; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IEA:TreeGrafter.
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:0045892; P:negative regulation of DNA-templated transcription; IEA:UniProtKB-ARBA.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:TreeGrafter.
DR   GO; GO:0001501; P:skeletal system development; IEA:UniProtKB-ARBA.
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:UP000515131};
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          698..726
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          896..954
FT                   /note="GATA-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50114"
FT   REGION          1..216
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          369..400
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          491..518
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          862..893
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          967..1006
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1045..1085
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1175..1202
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        46..55
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        61..70
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        73..89
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        154..168
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        169..195
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        494..518
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        986..1001
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1046..1055
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1056..1065
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1066..1078
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1287 AA;  141661 MW;  5D23D83168C54DBA CRC64;
     MKSMLDMVRK KNPPLRNVVS EGEGQTLEPI GTESKVSGKN KEFSADQMSE NTDQSDAAEL
     NNKEEHRLHG QDSSSSSKKG PKSSSLSEKA GFNYESPSKG GNLPSHPHDE VTDRNMLAFS
     SPAVGGVCEP LKSPQRAEAD DPQDTACTPA GDSLETKEDH KMSPKATEET GQAQSSQANC
     QGSSPVSVAS KNPQVPSDGG VRLNKSKTDL LVNDNPDPAP LSPELQDFKC NICGYGYYGN
     DPTDLIKHFR KYHLGLHNRT RQDAELDSKI LALHNMVQFS HSKDFQKVNR SVLSGVLQDI
     NSSRPVLLNG TYDVQVTSGG TFIGIGRKTP DCQGNTKYFR CKFCNFTYMG NSSTELEQHF
     LQTHPNKIKA SLPSSEGAKP SEKNSNKSIP ALRSGDSGDL GKWQDKITVK AGDDTPVGYS
     VPIKPLDSSR QNGTEATSYY WCKFCSFSCE SSSSLKLLEH YGKQHGGAQS GCLNPELNDK
     LSRGSVINQN DLAKSAEGEP MTKADKGSSG AKKKDFSSKG AEDNMVTSYN CQFCDFRYSK
     SHGPDVIIVG PLLRHYQQLH NIHKCTIKHC PFCPRGLCSP EKHLGEITYP FACRKSSCSH
     CALLLLHLSP GAAGSSRVKH QCHQCSFSTP DVDVLLFHYE SVHESQASDV KQEANHLQGS
     DGQPAVKESK EHSCTKCDFI TQVEEEISRH YRRAHSCYKC RQCSFTAADT QSLLEHFNTV
     HCQEQDITTA NGEEDGHAVS AIKEEPKIDL KVYSLLNPDS KMGEPVSESV VKREKVEDKD
     GLKEKVWTES SSDDLRNMTW RGADILRGSP SYTQASLGLL TPVSGTQEQT KTLRDSPNVE
     AAHLARPIYG LAVETKGFLQ GVPAGGEKSG PLTQQYPASG ENKSKDESQS LLRRRRGSGV
     FCANCLTTKT SLWRKNANGG YVCNACGLYQ KLHSTPRPLN IIKQNNGEQI IRRRTRKRLN
     PEALQAEQLN KHQRGGSEEQ VNGSPLERRS EDHLTEGHQR EIPLPSLSKY EAQGSLTKSH
     SAQQPVLVSQ TLDIHKRMQP LHIQIKSPQE STGDPGNSSS VSEGKGSSER GSPIEKYMRP
     AKHPNYSPPG SPIEKYQYPL FGLPFVHNDF QSEADWLRFW SKYKLSVPGN PHYLSHVPGL
     PNPCQNYVPY PTFNLPPHFS AVGSDNDIPL DLAIKHSRPG PTANGASKEK TKAPSSVKSE
     GPLNVVKTEK VDRSTQDELS TKCVHCGIVF LDEVMYALHM SCHGDSGPFQ CSICQHLCTD
     KYDFTTHIQR GLHRNNAQAE KNGKPKE
//
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