TRPS1_XENLA
ID TRPS1_XENLA Reviewed; 1271 AA.
AC Q90ZS6; Q90ZS7;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Zinc finger transcription factor Trps1;
GN Name=trps1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS XTRPS1 AND MTRPS1), FUNCTION,
RP REPRESSOR DOMAIN, AND MUTAGENESIS OF 886-CYS--CYS-889.
RX PubMed=11285235; DOI=10.1093/emboj/20.7.1715;
RA Malik T.H., Shoichet S.A., Latham P., Kroll T.G., Peters L.L.,
RA Shivdasani R.A.;
RT "Transcriptional repression and developmental functions of the atypical
RT vertebrate GATA protein TRPS1.";
RL EMBO J. 20:1715-1725(2001).
CC -!- FUNCTION: Transcriptional repressor. Represses expression of GATA-
CC regulated genes at selected sites and stages in vertebrate development.
CC {ECO:0000269|PubMed:11285235}.
CC -!- SUBUNIT: Binds specifically to GATA sequences.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=xTRPS1; Synonyms=Zygotic;
CC IsoId=Q90ZS6-1; Sequence=Displayed;
CC Name=mTRPS1; Synonyms=Maternal;
CC IsoId=Q90ZS6-2; Sequence=VSP_001607;
CC -!- PTM: Sumoylated. Sumoylation in the repressor domain inhibits the
CC transcription repression activity. Sumoylation on Lys-1191 is the major
CC site. Appears to be sumoylated on multiple sites (By similarity).
CC {ECO:0000250}.
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DR EMBL; AF346838; AAK39510.1; -; mRNA.
DR EMBL; AF346837; AAK39509.1; -; mRNA.
DR RefSeq; NP_001083884.1; NM_001090415.1. [Q90ZS6-1]
DR AlphaFoldDB; Q90ZS6; -.
DR PRIDE; Q90ZS6; -.
DR DNASU; 399173; -.
DR GeneID; 399173; -.
DR KEGG; xla:399173; -.
DR CTD; 399173; -.
DR Xenbase; XB-GENE-1013668; trps1.S.
DR Proteomes; UP000186698; Chromosome 6S.
DR Bgee; 399173; Expressed in zone of skin and 12 other tissues.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd00202; ZnF_GATA; 1.
DR Gene3D; 3.30.50.10; -; 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; PTHR47034; 1.
DR Pfam; PF00320; GATA; 1.
DR PRINTS; PR00619; GATAZNFINGER.
DR SMART; SM00355; ZnF_C2H2; 9.
DR SMART; SM00401; ZnF_GATA; 1.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS00344; GATA_ZN_FINGER_1; 1.
DR PROSITE; PS50114; GATA_ZN_FINGER_2; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..1271
FT /note="Zinc finger transcription factor Trps1"
FT /id="PRO_0000083510"
FT ZN_FING 217..242
FT /note="C2H2-type 1; atypical"
FT ZN_FING 328..353
FT /note="C2H2-type 2; atypical"
FT ZN_FING 426..451
FT /note="C2H2-type 3; atypical"
FT ZN_FING 513..543
FT /note="C2H2-type 4; atypical"
FT ZN_FING 604..627
FT /note="C2H2-type 5"
FT ZN_FING 656..679
FT /note="C2H2-type 6"
FT ZN_FING 682..705
FT /note="C2H2-type 7"
FT ZN_FING 886..910
FT /note="GATA-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00094"
FT ZN_FING 1205..1227
FT /note="C2H2-type 8"
FT ZN_FING 1233..1257
FT /note="C2H2-type 9"
FT REGION 1..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 124..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 353..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 843..877
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 938..987
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1031..1064
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1153..1271
FT /note="Transcriptional repressor domain"
FT REGION 1154..1196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..66
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..378
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 848..869
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 950..968
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 969..983
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1031..1051
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 1182
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CROSSLNK 1191
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT VAR_SEQ 364..616
FT /note="Missing (in isoform mTRPS1)"
FT /evidence="ECO:0000303|PubMed:11285235"
FT /id="VSP_001607"
FT MUTAGEN 886..889
FT /note="CANC->GANA: Abolishes transcriptional repressive
FT activity towards GATA."
FT /evidence="ECO:0000269|PubMed:11285235"
FT CONFLICT 848
FT /note="A -> S (in Ref. 1; AAK39509)"
FT /evidence="ECO:0000305"
FT CONFLICT 852
FT /note="K -> R (in Ref. 1; AAK39509)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1271 AA; 141437 MW; BFA6841A939E1DCA CRC64;
MVRKKNPPLR NIASEGEAQI TESAASKRED TISSKEISTD PMQENSEQSG LVEHNSDDHS
FHDQEPSSSI NKDSASLSLS ERAVVNYSHL KGRNVYFSPM EVTDRNMLAL VTTDTRSACD
PLKSPIKSEA DDTQELASSA SVDSLEAKEE NDMSPRATDF TVQCGKVDCQ SSSPASVASD
NLHVPSDGIA GLNKSQAVLL VNDNSDSAPL SPELQDFKCN ICGYGYYGND PTDLIKHFRK
YHLGLHNRTR QDVELDTKIL ALHNMVQFSQ SKDFQKMNRS VLSGVLQDFN SPRPVLLNGT
YDVQVTFGET FIGIGRKTPD CQGNTKYFRC KFCNFTYLAK SATELEQHFL KTHPNKMKMS
SDSGKPSEKS TNKSSPIPRS CEPGDLGKWQ DKITVKAADD IPVGYSVPIK PVDSCRQNGT
DDTNYYWCKF CSFSCESSSN SKLLEHHSKQ HGGGKSESPN SDLNDEIFRG SVINQNEITK
SSDEQLPTKI DKGLAKKKDV SSVPTEDIIV TNYNCQFCDF RYSKSHGPEV ILVGPLLRHY
QQHHNIHKCT IKHCPFCPRG LCTPEKHLGE ITYPFACKKS NCSHCALLLL HLSSGGTEST
RVKHQCDQCS FSSPDVDVLL LHYENAHEAQ ACEIKQELNH QHGADGQPSI KEIKEHSCTK
CDFIVQVEED LPRHYRRVHN CYKCRQCNFT AADTQSLLDH FNSAHCQEFE ITTSNGGEHH
GTSSIKEEPK TDLKVYNLVT PDSKMGEAIF DSTVKKEKLE DKETLREKAW SDGSVDDLRG
VAWRAPDILR TSPSYSQMGL GLLTTVSVNQ DQQKSSRDSP NVEAAHLARP VYGLSIEPKG
FQGVTAGASG EKSGQHTPQY PTAGDSKSKD ESQSLLRRRR GSGVFCANCL TTKTSLWRKN
ANGGYVCNAC GLYQKLHSTP RPLNIIKQNN GEQIIRRRTR KRLNPEALQP EQLTKHQRAS
SEEQANGSPL DIRSEDHSME GHQRENQQLS MNKYGSQASL TKSHSAQQTM IVSQTMDIHK
RMQPLHIQIK SPQESSGEPG NSSSVSDGKG SSERGSPIEK YMRPIKHPNY SPPGSPIEKY
QYPLFGLPFV HNDFQSEADW LRFWSKYKLS VPGNPHYLSH VPGLPNPCPN YVPYPTFNLP
AQYSSVGSDN DIPLDLAMKH SRPGSGTNGD SKEKSKSPVS VKDDGPLNVT KIEKSDKSTQ
DELSTKCVHC GIVFLDEVMY ALHMSCHGES GPFQCSICQH LCTDKYDFTT HIQRGLHRNI
AQAEKNGKNK D
