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Database: UniProt
Entry: A0A8C7AHE0_NEOVI
LinkDB: A0A8C7AHE0_NEOVI
Original site: A0A8C7AHE0_NEOVI 
ID   A0A8C7AHE0_NEOVI        Unreviewed;      1285 AA.
AC   A0A8C7AHE0;
DT   19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2022, sequence version 1.
DT   10-JUN-2026, entry version 20.
DE   RecName: Full=Zinc finger transcription factor Trps1 {ECO:0000256|ARBA:ARBA00073694};
OS   Neogale vison (American mink) (Mustela vison).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC   Mustelinae; Neogale.
OX   NCBI_TaxID=452646 {ECO:0000313|Ensembl:ENSNVIP00000008768.1, ECO:0000313|Proteomes:UP000694425};
RN   [1] {ECO:0000313|Ensembl:ENSNVIP00000008768.1}
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; ENSNVIT00000010260.1; ENSNVIP00000008768.1; ENSNVIG00000006947.1.
DR   GeneTree; ENSGT00940000157893; -.
DR   Proteomes; UP000694425; 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:UP000694425};
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          696..724
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          894..952
FT                   /note="GATA-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50114"
FT   REGION          1..202
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          367..398
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          489..516
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          860..891
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          965..1004
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1043..1085
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1173..1198
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..11
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        44..53
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        68..87
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        152..166
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        167..193
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        492..516
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        965..981
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        984..999
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1044..1053
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1054..1063
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1064..1076
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1285 AA;  141345 MW;  14C84225F11508E2 CRC64;
     MQSNMVRKKN PPLRNVASEG EGQSLEPIGT ESKVSGKNKE FSADQMSENT DQSDAAELNN
     KEEHSSHGQD PSSSSKKGLK SSVLSEKAGF NYESPSKGGN LPSHPHDEVT DRNMLAFSSP
     AAGGVCEPLK SPQRAEADDP QDMACTPSGD SLETKEDHKM SPKATEETGQ AQSGQANCQG
     SSPVSVASKN PQVPSDGGVR LNKSKTDLLV NDIPDPAPLS PELQDFKCNI CGYGYYGNDP
     TDLIKHFRKY HLGLHNRTRQ DAELDSKILA LHNMVQFSHS KDFQKVNRSV LSGVLQDINS
     SRPVLLNGTY DVQVTSGGTF IGIGRKTPDC QGNTKYFRCK FCNFTYMGNS STELEQHFLQ
     THPNKIKASL PSSEGAKPSE KNSNKSIPAL RSSDSGDLGK WQDKITVKTG DDTPVGYSVP
     IKPLDSSRQN GTEATSYYWC KFCSFSCESS SSLKLLEHYG KQHGGAQSGG LNPELNDKLS
     RGSVINQNDL AKSAEGEPMA KADKGSSGAK KKDFSSKGAE DNMVTSYNCQ FCDFRYSKSH
     GPDVIVVGPL LRHYQQLHNI HKCTIKHCPF CPRGLCSPEK HLGEITYPFA CRKSNCSHCA
     LLLLHLSPGA AGSSRVKHQC HQCSFSTPDV DVLLFHYESS HESQASEVKQ EANHLQGSDG
     QPAVKESKEH SCTKCDFITQ VEEEISRHYR RAHSCYKCRQ CSFTAADTQS LLEHFNTVHC
     HEQDITTANG EEDGHAVSTI KEEPKIDLKV YSLLNPDSKM GEPVSESVVK REKVEDKDGL
     KDKVWTESSS DDLRNMTWRG ADILRGSPSY TQASLGLLTP VSGPQEQTKT LRDSPNVEAA
     HLARPIYGLA VETKGFLQGV PAGGEKSGTL TQQYPASGEN KSKDESQSLL RRRRGSGVFC
     ANCLTTKTSL WRKNANGGYV CNACGLYQKL HSTPRPLNII KQNNGEQIIR RRTRKRLNPE
     ALQAEQLNKQ QRGGSEEQVN GSPLERRSED HLTEGHQREI PLPSLSKYEA QGSLTKSHSA
     QQPVLVSQTL DIHKRMQPLH IQIKSPQEST GDPGNSSSVS EGKGSSERGS PIEKYMRPAK
     HPNYSPPGSP IEKYQYPLFG LPFVHNDFQS EADWLRFWSK YKLSVPGNPH YLSHVPGLPN
     PCQNYVPYPT FNLPPHFSAV GSDNDIPLDL AIKHSRPGPT ANGASKEKTK APSNVKSEGP
     LNVVKTEKVD RSTQDELSTK CVHCGIVFLD EVMYALHMSC HGDSGPFQCS ICQHLCTDKY
     DFTTHIQRGL HRNNAQAEKN GKPKE
//
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