TRA1_CAEEL
ID TRA1_CAEEL Reviewed; 1110 AA.
AC P34708; Q95Q22; Q9U2C0;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Sex-determining transformer protein 1 {ECO:0000312|WormBase:Y47D3A.6a};
DE AltName: Full=Hermaphrodization of XO animals protein 2 {ECO:0000312|WormBase:Y47D3A.6a};
GN Name=tra-1 {ECO:0000312|WormBase:Y47D3A.6a};
GN Synonyms=her-2 {ECO:0000312|WormBase:Y47D3A.6a};
GN ORFNames=Y47D3A.6 {ECO:0000312|WormBase:Y47D3A.6a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B), FUNCTION, AND DEVELOPMENTAL
RP STAGE.
RC STRAIN=Bristol N2;
RX PubMed=1339311; DOI=10.1016/0092-8674(92)90099-x;
RA Zarkower D., Hodgkin J.;
RT "Molecular analysis of the C. elegans sex-determining gene tra-1: a gene
RT encoding two zinc finger proteins.";
RL Cell 70:237-249(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP FUNCTION.
RX PubMed=8367286; DOI=10.1093/nar/21.16.3691;
RA Zarkower D., Hodgkin J.;
RT "Zinc fingers in sex determination: only one of the two C. elegans Tra-1
RT proteins binds DNA in vitro.";
RL Nucleic Acids Res. 21:3691-3698(1993).
RN [4]
RP FUNCTION, AND INTERACTION WITH TRA-2.
RX PubMed=11124807;
RA Lum D.H., Kuwabara P.E., Zarkower D., Spence A.M.;
RT "Direct protein-protein interaction between the intracellular domain of
RT TRA-2 and the transcription factor TRA-1A modulates feminizing activity in
RT C. elegans.";
RL Genes Dev. 14:3153-3165(2000).
RN [5]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11703944; DOI=10.1016/s1534-5807(01)00068-5;
RA Segal S.P., Graves L.E., Verheyden J., Goodwin E.B.;
RT "RNA-Regulated TRA-1 nuclear export controls sexual fate.";
RL Dev. Cell 1:539-551(2001).
RN [6]
RP FUNCTION, AND INTERACTION WITH TRA-2.
RX PubMed=11250902; DOI=10.1093/emboj/20.6.1363;
RA Wang S., Kimble J.;
RT "The TRA-1 transcription factor binds TRA-2 to regulate sexual fates in
RT Caenorhabditis elegans.";
RL EMBO J. 20:1363-1372(2001).
RN [7]
RP FUNCTION.
RX PubMed=18056428; DOI=10.1101/gad.1607007;
RA Schwartz H.T., Horvitz H.R.;
RT "The C. elegans protein CEH-30 protects male-specific neurons from
RT apoptosis independently of the Bcl-2 homolog CED-9.";
RL Genes Dev. 21:3181-3194(2007).
RN [8]
RP FUNCTION.
RX PubMed=18550714; DOI=10.1242/dev.017046;
RA Mason D.A., Rabinowitz J.S., Portman D.S.;
RT "dmd-3, a doublesex-related gene regulated by tra-1, governs sex-specific
RT morphogenesis in C. elegans.";
RL Development 135:2373-2382(2008).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=24682813; DOI=10.1093/nar/gku221;
RA Li T., Kelly W.G.;
RT "A role for WDR5 in TRA-1/Gli mediated transcriptional control of the
RT sperm/oocyte switch in C. elegans.";
RL Nucleic Acids Res. 42:5567-5581(2014).
RN [10]
RP FUNCTION.
RX PubMed=28065609; DOI=10.1016/j.cub.2016.11.045;
RA Serrano-Saiz E., Oren-Suissa M., Bayer E.A., Hobert O.;
RT "Sexually Dimorphic Differentiation of a C. elegans Hub Neuron Is Cell
RT Autonomously Controlled by a Conserved Transcription Factor.";
RL Curr. Biol. 27:199-209(2017).
CC -!- FUNCTION: Plays a major role in controlling sexual phenotype
CC (PubMed:1339311). Terminal global regulator in a well-characterized
CC cascade of sex-determining genes (PubMed:8367286). Promotes female
CC development (PubMed:11124807). Interacts with tra-2 to promote
CC spermatogenesis (PubMed:11250902). Promotes spermatogenesis through the
CC Tip60 HAT complex and by regulating the expression of genes, such as
CC fog-3, required for male development (By similarity). Association with
CC chromatin and at the fog-3 promoter requires wdr-5.1, and may also
CC require wdr-5.2 (PubMed:24682813). With trr-1, activates the fog-3 gene
CC to determine sperm/oocyte cell fate (By similarity). In hermaphrodites,
CC binds to an intronic regulatory site in the ceh-30 gene, preventing
CC ceh-30 transcription and thereby preventing survival of the CEM
CC (cephalic male) sensory neurons (PubMed:18056428). Represses the
CC expression of the transcription factor dmd-3 in hermaphrodites to
CC govern the timing and extent of male tail tip morphogenesis
CC (PubMed:18550714). Plays a role in controlling the sex-specific
CC differentiation of PHC sensory neurons and represses the development of
CC male-specific morphological features (PubMed:28065609).
CC {ECO:0000250|UniProtKB:Q17308, ECO:0000269|PubMed:11124807,
CC ECO:0000269|PubMed:11250902, ECO:0000269|PubMed:1339311,
CC ECO:0000269|PubMed:18056428, ECO:0000269|PubMed:18550714,
CC ECO:0000269|PubMed:24682813, ECO:0000269|PubMed:28065609,
CC ECO:0000269|PubMed:8367286}.
CC -!- SUBUNIT: Interacts with the MX regulatory domain of tra-2.
CC {ECO:0000269|PubMed:11124807, ECO:0000269|PubMed:11250902}.
CC -!- INTERACTION:
CC P34708; P34709: tra-2; NbExp=5; IntAct=EBI-367204, EBI-367223;
CC P34708-1; P17221: fem-1; NbExp=2; IntAct=EBI-367214, EBI-1998155;
CC P34708-1; P49594: fem-2; NbExp=2; IntAct=EBI-367214, EBI-1998402;
CC P34708-1; P34691: fem-3; NbExp=2; IntAct=EBI-367214, EBI-445465;
CC P34708-1; P34709: tra-2; NbExp=5; IntAct=EBI-367214, EBI-367223;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11703944}. Nucleus
CC {ECO:0000269|PubMed:11703944, ECO:0000269|PubMed:24682813}.
CC Note=Localization with chromatin in the nucleus in part depends on
CC normal function of wdr-5.1. {ECO:0000269|PubMed:24682813}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000312|WormBase:Y47D3A.6a}; Synonyms=Tra-1L
CC {ECO:0000303|PubMed:8367286};
CC IsoId=P34708-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:Y47D3A.6b}; Synonyms=Tra-1S
CC {ECO:0000303|PubMed:8367286};
CC IsoId=P34708-2; Sequence=VSP_006821, VSP_006822;
CC -!- TISSUE SPECIFICITY: Expressed in intestine and gonads (at protein
CC level). {ECO:0000269|PubMed:11703944}.
CC -!- DEVELOPMENTAL STAGE: Isoform b is expressed abundantly in second larval
CC (L2) stage. Isoform a is more abundant in embryos.
CC {ECO:0000269|PubMed:1339311}.
CC -!- DOMAIN: Only isoform a (Tra-1L), is thought to bind DNA. Zinc fingers
CC 3, 4 and 5 are the most important for DNA binding; removal of finger 5
CC almost abolishes DNA binding and prevents the selection of binding
CC sites. {ECO:0000269|PubMed:8367286}.
CC -!- SIMILARITY: Belongs to the GLI C2H2-type zinc-finger protein family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB61040.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAC42377.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M93256; AAB59181.1; -; mRNA.
DR EMBL; M94130; AAA91281.1; -; mRNA.
DR EMBL; BX284603; CAB61040.2; ALT_INIT; Genomic_DNA.
DR EMBL; BX284603; CAC42377.1; ALT_INIT; Genomic_DNA.
DR PIR; A43253; A43253.
DR PIR; B43253; B43253.
DR AlphaFoldDB; P34708; -.
DR SMR; P34708; -.
DR BioGRID; 41731; 41.
DR IntAct; P34708; 37.
DR MINT; P34708; -.
DR STRING; 6239.Y47D3A.6a; -.
DR EPD; P34708; -.
DR PaxDb; P34708; -.
DR PeptideAtlas; P34708; -.
DR PRIDE; P34708; -.
DR EnsemblMetazoa; Y47D3A.6a.1; Y47D3A.6a.1; WBGene00006604. [P34708-1]
DR EnsemblMetazoa; Y47D3A.6b.1; Y47D3A.6b.1; WBGene00006604. [P34708-2]
DR UCSC; Y47D3A.6a; c. elegans. [P34708-1]
DR WormBase; Y47D3A.6a; CE52672; WBGene00006604; tra-1. [P34708-1]
DR WormBase; Y47D3A.6b; CE52664; WBGene00006604; tra-1. [P34708-2]
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000169506; -.
DR HOGENOM; CLU_274778_0_0_1; -.
DR InParanoid; P34708; -.
DR OrthoDB; 1318335at2759; -.
DR SignaLink; P34708; -.
DR PRO; PR:P34708; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00006604; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:WormBase.
DR GO; GO:0001162; F:RNA polymerase II intronic transcription regulatory region sequence-specific DNA binding; IDA:WormBase.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:WormBase.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:WormBase.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007417; P:central nervous system development; IBA:GO_Central.
DR GO; GO:0019099; P:female germ-line sex determination; TAS:UniProtKB.
DR GO; GO:0019101; P:female somatic sex determination; IMP:WormBase.
DR GO; GO:0008406; P:gonad development; IGI:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:WormBase.
DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; IMP:WormBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0010468; P:regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; IMP:UniProtKB.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 3.
DR SMART; SM00355; ZnF_C2H2; 5.
DR SUPFAM; SSF57667; SSF57667; 3.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Developmental protein; Differentiation;
KW DNA-binding; Metal-binding; Nucleus; Reference proteome; Repeat;
KW Sexual differentiation; Spermatogenesis; Zinc; Zinc-finger.
FT CHAIN 1..1110
FT /note="Sex-determining transformer protein 1"
FT /id="PRO_0000046895"
FT ZN_FING 208..233
FT /note="C2H2-type 1; low DNA-binding affinity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 244..270
FT /note="C2H2-type 2; low DNA-binding affinity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 276..300
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 306..331
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 337..362
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 170..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 363..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 594..682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 875..896
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1057..1110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..388
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..609
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 647..680
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 878..896
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1073..1088
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1089..1110
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 280..288
FT /note="YPGCGKEYS -> VGFGGDNEI (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_006821"
FT VAR_SEQ 289..1110
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_006822"
SQ SEQUENCE 1110 AA; 122804 MW; EEE72C82841ECD7A CRC64;
MMAPSTEDPD TVVEAQRRGS FSKKKNANGW NKVELVDQCA KQMGSEDKQP GGGDVKTEND
PSKNGLGSAT SNFIQSSVPP SHQTLSNPLQ LSPPAEASVA QQSGASQVFP TFQAALGASS
DELLQPNATS SSTSSSASTS SIVPVVKFTN QTAPNGSTVA TSVGQNVRLT INGKRVGRPP
GTFKRPQNNA ANSSNSGNDS DMMGDHDLTC RWKSCNSSFQ TLKALVDHVQ ESHVQSTEQE
HHAWRCEWEG CDRNETFKAL YMLIVHVRRH TGEKPNKCEY PGCGKEYSRL ENLKTHRRTH
TGEKPYKCEF ADCEKAFSNA SDRAKHQNRT HSNLKPYSCQ IPQCTKSYTD PSSLRKHIKA
VHGDDEYEKA KKSRPANYSN RRRPDHRLAP PTGAMSHPYL ATPNSGASVV AHSSVHQQNF
INMALAQHHH NAQRAQQLMA ATGNVMPMMD PASAAAAAQA QAHHQAQAQM LQTHMMQQAQ
IQAAAQMQAQ VQHQAAMQAH AMQQAQMVLQ NNLLGAQSLL SPFSPLLPPS RAPNVMAMLQ
TPPTPTSVAP MFDIMTSRAP MAPVVSAPTA PAPLVPAPVP ASPVFDELRE QMREVEPLQQ
QQQQEPMDQD LQDIRVDGDS DDEDEEEPRT PSGALLLPRG GNNGDGGFGG SGSSRASSGS
GTMELSAAPI SQNGSRASGS GERGMRSFLI ADILQLAADF QNERLLSDVL DLAIFDTRDV
RSLHNIYQVY IRAHKAIPIT RRPLDWNETH QLHNLYHDPR FNRAEHQDSP AIRDRDTRFW
RTIAEANTMR QRQIEPVPLD DDDEGYFDEM VHRVQNGRLN EQFMEGFESD DDDGFEDEDD
VPGLGIAVYR GRRRVRREAL KQANLDIQEA ETAGRNVGGF GDEEDRNNRG HDQDRSFLDH
YYPPMVVVVE TESPQIVRDQ EMMRQFEEAK KNVETDEIKK RAEAMQFGTS SSHHHTKTLL
IQRALFDKTS SVRRSLLQFI TISVDQEELR QSCHATSAPQ GAHVVHNVVD EFDSIMRAQE
DSNNRILLSL DIPAPSAVTG VSGSITHADN SALQLQQEQP TSSFSSWFPE DDPIYALPPP
PPPPAPPRRR RSADNKDDSE NIPKKPRHQF
