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 01-MAY-2013, entry version 111.
DE RecName: Full=Sex-determining transformer protein 1;
DE AltName: Full=Hermaphrodization of XO animals protein 2;
GN Name=tra-1; Synonyms=her-2; ORFNames=Y47D3A.6;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B), FUNCTION, AND
RP DEVELOPMENTAL 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
RT gene encoding two zinc finger proteins.";
RL Cell 70:237-249(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE
RP SPLICING.
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
RT investigating 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
RT Tra-1 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
RT of TRA-2 and the transcription factor TRA-1A modulates feminizing
RT activity in 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
RT in 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).
CC -!- FUNCTION: Plays a major role in controlling sexual phenotype.
CC Terminal global regulator in a well-characterized cascade of sex-
CC determining genes. Promotes female development. Required together
CC with tra-2 for promoting spermatogenesis. In hermaphrodites, binds
CC to an intronic regulatory site in the ceh-30 gene, preventing ceh-
CC 30 transcription and thereby preventing survival of the CEM
CC (cephalic male) sensory neurons.
CC -!- SUBUNIT: Interacts with the MX regulatory domain of tra-2.
CC -!- INTERACTION:
CC P17221:fem-1; NbExp=2; IntAct=EBI-367214, EBI-1998155;
CC P49594:fem-2; NbExp=2; IntAct=EBI-367214, EBI-1998402;
CC P34691:fem-3; NbExp=2; IntAct=EBI-367214, EBI-445465;
CC P34709:tra-2; NbExp=5; IntAct=EBI-367214, EBI-367223;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a; Synonyms=Tra-1L;
CC IsoId=P34708-1; Sequence=Displayed;
CC Name=b; Synonyms=Tra-1S;
CC IsoId=P34708-2; Sequence=VSP_006821, VSP_006822;
CC -!- TISSUE SPECIFICITY: Expressed in intestine and gonads (at protein
CC level).
CC -!- DEVELOPMENTAL STAGE: Isoform b is expressed abundantly in second
CC larval (L2) stage. Isoform a is more abundant in embryos.
CC -!- DOMAIN: Only isoform a (Tra-1L), is thought to bind DNA. Zinc
CC fingers 3, 4 and 5 are the most important for DNA binding; removal
CC of finger 5 almost abolishes DNA binding and prevents the
CC selection of binding sites.
CC -!- SIMILARITY: Belongs to the GLI C2H2-type zinc-finger protein
CC family.
CC -!- SIMILARITY: Contains 5 C2H2-type zinc fingers.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB61040.2; Type=Erroneous initiation;
CC Sequence=CAC42377.1; Type=Erroneous initiation;
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DR EMBL; M93256; AAB59181.1; -; mRNA.
DR EMBL; M94130; AAA91281.1; -; mRNA.
DR EMBL; AL117202; CAB61040.2; ALT_INIT; Genomic_DNA.
DR EMBL; AL117202; CAC42377.1; ALT_INIT; Genomic_DNA.
DR PIR; A43253; A43253.
DR PIR; B43253; B43253.
DR RefSeq; NP_001022880.1; NM_001027709.1.
DR RefSeq; NP_001022881.1; NM_001027710.2.
DR UniGene; Cel.9756; -.
DR ProteinModelPortal; P34708; -.
DR SMR; P34708; 210-418.
DR IntAct; P34708; 6.
DR MINT; MINT-154380; -.
DR PaxDb; P34708; -.
DR PRIDE; P34708; -.
DR GeneID; 176548; -.
DR KEGG; cel:CELE_Y47D3A.6; -.
DR UCSC; Y47D3A.6a; c. elegans.
DR CTD; 176548; -.
DR WormBase; Y47D3A.6a; CE28129; WBGene00006604; tra-1.
DR WormBase; Y47D3A.6b; CE28130; WBGene00006604; tra-1.
DR eggNOG; COG5048; -.
DR HOGENOM; HOG000154672; -.
DR InParanoid; P34708; -.
DR KO; K06230; -.
DR NextBio; 893034; -.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000980; F:RNA polymerase II distal enhancer 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:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0019099; P:female germ-line sex determination; TAS:UniProtKB.
DR GO; GO:0019101; P:female somatic sex determination; TAS:UniProtKB.
DR GO; GO:0008406; P:gonad development; IGI:WormBase.
DR GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:WormBase.
DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; IMP:WormBase.
DR GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:WormBase.
DR GO; GO:0007283; P:spermatogenesis; IMP:UniProtKB.
DR Gene3D; 3.30.160.60; -; 5.
DR InterPro; IPR007087; Znf_C2H2.
DR InterPro; IPR015880; Znf_C2H2-like.
DR InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd.
DR Pfam; PF00096; zf-C2H2; 3.
DR SMART; SM00355; ZnF_C2H2; 5.
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; Complete proteome; Cytoplasm;
KW Developmental protein; Differentiation; DNA-binding; Metal-binding;
KW Nucleus; Reference proteome; Repeat; Sexual differentiation;
KW Spermatogenesis; Zinc; Zinc-finger.
FT CHAIN 1 1110 Sex-determining transformer protein 1.
FT /FTId=PRO_0000046895.
FT ZN_FING 208 233 C2H2-type 1; low DNA-binding affinity.
FT ZN_FING 244 270 C2H2-type 2; low DNA-binding affinity.
FT ZN_FING 276 300 C2H2-type 3.
FT ZN_FING 306 331 C2H2-type 4.
FT ZN_FING 337 362 C2H2-type 5.
FT COMPBIAS 129 141 Ser/Thr-rich.
FT COMPBIAS 454 458 Poly-Ala.
FT COMPBIAS 599 604 Poly-Gln.
FT COMPBIAS 1073 1087 Pro-rich.
FT VAR_SEQ 280 288 YPGCGKEYS -> VGFGGDNEI (in isoform b).
FT /FTId=VSP_006821.
FT VAR_SEQ 289 1110 Missing (in isoform b).
FT /FTId=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
//
