TRA1_CAEBR
ID TRA1_CAEBR Reviewed; 1165 AA.
AC Q17308; A8XH93; C9QPL1; C9QPL2; H8WH38; H8WH39; Q17309;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Sex-determining transformer protein 1 {ECO:0000312|WormBase:CBG13188a};
DE Short=Cbr-tra-1 {ECO:0000303|PubMed:24098152};
GN Name=tra-1 {ECO:0000312|WormBase:CBG13188a};
GN ORFNames=CBG13188 {ECO:0000312|WormBase:CBG13188a};
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B).
RC STRAIN=Gujarat;
RX PubMed=8889522; DOI=10.1093/genetics/144.2.587;
RA de Bono M., Hodgkin J.;
RT "Evolution of sex determination in Caenorhabditis: unusually high
RT divergence of tra-1 and its functional consequences.";
RL Genetics 144:587-595(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
RN [3]
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 [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18245372; DOI=10.1534/genetics.107.073668;
RA Kelleher D.F., de Carvalho C.E., Doty A.V., Layton M., Cheng A.T.,
RA Mathies L.D., Pilgrim D., Haag E.S.;
RT "Comparative genetics of sex determination: masculinizing mutations in
RT Caenorhabditis briggsae.";
RL Genetics 178:1415-1429(2008).
RN [5]
RP FUNCTION.
RX PubMed=24098152; DOI=10.1371/journal.pgen.1003850;
RA Guo Y., Chen X., Ellis R.E.;
RT "Evolutionary change within a bipotential switch shaped the sperm/oocyte
RT decision in hermaphroditic nematodes.";
RL PLoS Genet. 9:E1003850-E1003850(2013).
CC -!- FUNCTION: Plays a major role in controlling sexual phenotype
CC (PubMed:18245372). Terminal global regulator in a well-characterized
CC cascade of sex-determining genes (By similarity). Promotes female
CC development (By similarity). 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 (PubMed:24098152). Association
CC with chromatin and at the fog-3 promoter requires wdr-5.1, and may also
CC require wdr-5.2 (By similarity). With trr-1, activates the fog-3 gene
CC to determine sperm/oocyte cell fate (PubMed:24098152). In
CC hermaphrodites, binds to an intronic regulatory site in the ceh-30
CC gene, preventing ceh-30 transcription and thereby preventing survival
CC of the CEM (cephalic male) sensory neurons (By similarity). Represses
CC the expression of the transcription factor dmd-3 in hermaphrodites to
CC govern the timing and extent of male tail tip morphogenesis (By
CC similarity). Plays a role in controlling the sex-specific
CC differentiation of PHC sensory neurons and represses the development of
CC male-specific morphological features (By similarity).
CC {ECO:0000250|UniProtKB:P34708, ECO:0000269|PubMed:11250902,
CC ECO:0000269|PubMed:18245372, ECO:0000269|PubMed:24098152}.
CC -!- SUBUNIT: Interacts with the MX regulatory domain of tra-2.
CC {ECO:0000269|PubMed:11250902}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P34708}. Cytoplasm
CC {ECO:0000250|UniProtKB:P34708}. Note=Localization with chromatin in the
CC nucleus in part depends on normal function of wdr-5.1.
CC {ECO:0000250|UniProtKB:P34708}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a; Synonyms=Tra-1L;
CC IsoId=Q17308-1; Sequence=Displayed;
CC Name=b; Synonyms=Tra-1S;
CC IsoId=Q17308-2; Sequence=VSP_011646;
CC -!- DOMAIN: Only isoform a is thought to bind DNA. Zinc fingers 3, 4 and 5
CC are the most important for DNA binding; removal of finger 5 almost
CC abolishes DNA binding and prevents the selection of binding sites.
CC {ECO:0000250|UniProtKB:P34708}.
CC -!- DISRUPTION PHENOTYPE: Null mutants exhibit strong masculinization and
CC male mating behavior. XX male mutants are infertile, produce sperm from
CC day one of adulthood, but by day three of adulthood, switch from
CC spermatogenesis to oogenesis and produce irregular oocytes. Mutants
CC display early somatic gonad precursor lineage defects, whereby Z1
CC precursors divide with reverse polarity and Z4 precursors migrate
CC prematurely. Most animals rectify these defects to produce normal male
CC somatic gonad. RNAi-mediated knock-down in XO male animals yields a
CC partially feminized germ line that contains both sperm and oocytes in
CC males, but not hermaphrodites. {ECO:0000269|PubMed:18245372}.
CC -!- SIMILARITY: Belongs to the GLI C2H2-type zinc-finger protein family.
CC {ECO:0000305}.
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DR EMBL; U60649; AAB49336.1; -; mRNA.
DR EMBL; U60649; AAB49337.1; -; mRNA.
DR EMBL; HE601226; CCG58639.1; -; Genomic_DNA.
DR EMBL; HE601226; CCG58640.1; -; Genomic_DNA.
DR PIR; S72248; S72248.
DR RefSeq; XP_002641339.1; XM_002641293.1. [Q17308-2]
DR AlphaFoldDB; Q17308; -.
DR SMR; Q17308; -.
DR STRING; 6238.CBG13188b; -.
DR PRIDE; Q17308; -.
DR GeneID; 8583331; -.
DR KEGG; cbr:CBG_13188; -.
DR CTD; 8583331; -.
DR WormBase; CBG13188a; CBP44731; WBGene00033987; Cbr-tra-1.
DR WormBase; CBG13188b; CBP42626; WBGene00033987; Cbr-tra-1.
DR eggNOG; KOG1721; Eukaryota.
DR HOGENOM; CLU_274778_0_0_1; -.
DR InParanoid; Q17308; -.
DR OMA; DLICRWK; -.
DR OrthoDB; 1318335at2759; -.
DR Proteomes; UP000008549; Chromosome III.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS: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; IBA:GO_Central.
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; TAS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0007548; P:sex differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
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..1165
FT /note="Sex-determining transformer protein 1"
FT /id="PRO_0000046894"
FT ZN_FING 226..251
FT /note="C2H2-type 1; low DNA-binding affinity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 262..288
FT /note="C2H2-type 2; low DNA-binding affinity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 294..318
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 324..349
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 355..380
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 58..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 190..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 378..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 663..741
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1137..1165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..77
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..406
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 702..741
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..42
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000303|PubMed:8889522"
FT /id="VSP_011646"
SQ SEQUENCE 1165 AA; 128954 MW; 6E34AD80CC8CD910 CRC64;
MMAPSTEDPE TVVEAQRRGS FSKKNGNGWT KPGLANGSES KHMEPVTGTN ALMAAIDADD
QETKLKDPLE KEASTYKSAT DRFFQSSHPP SHQTVENPIK LEPPTSSGVT QNGSPVTNSL
VPEAAQPLQT VAESSEPTAA SAEPTDASSA ESSTITVTPV VPVVKFTNQT TPNGSTVATS
VGQNVRLTIN GKRVGRPPGT FKRPPNNPTT NTSHGEETDS EASTDLICRW KDCMLKFANL
KGLVEHVQEK HVQSTEQEHH AWRCEWEGCD RNETFKALYM LIVHVRRHTG EKPNKCEYPG
CGKEYSRLEN LKTHRRTHTG EKPYKCEFSD CEKAFSNASD RAKHQNRTHS NLKPYSCQIG
GCQKSYTDPS SLRKHIKAVH GDEEYEKAKK SRPPNYSNRR RPDHRMPPPT SAMSHPYLAP
PHVLPPVAAP GVHQQNFINL ALAQHHHNQR AQFIANNAAL MDPNGSGAAQ AAAAAQAAQA
QQAQMYQAQA MQQHQFAAQM QQQAVMQVHM QQAALQQAQV AIIQNNLLST QGIMNQFPMM
SPLLTPRAPG NVMSLLQQQQ VTPPTPTMMQ LTPHTPITPI TPITPLTPMG ATTGPMFSMP
NIMMTTPVRM DIPTSVPAAV PVAPVAPVAP VAPAAPVAPP ASSLAEATEP RFRLLRQHME
GAEVAPVLAP QQPLEEDDDM TDDEESGNVA PAVIRNGDGP DDRNSGTGSS SPRSSASSGS
GTLEVAGSVA QNGNRSSSTG ERGMRSFLIA DILQMAHDFQ NGRIITDALH KAIFDTSDVT
AMFHIYRTFE CVCEYLQFTF SAGERLPTWP EVRTIHEYYH SDYDRTRFHA SETVRRRDNL
FWRFVNYCNS DLPIGGRPIL SVSYDEGFEE SIDQGSNFGT IPQQLISRMA AEAFDDEDDG
FDDAFDIPGL RLGGVEVLIQ QQRHRVRRAA LKQAQIDYPT AEEDLGYVGG GFGQEDDDHH
SYAIYEQQKT VAFVDLSEKP KVEVLTDEDF MEQFKAAEAR CQARLAIEPM VKVARTVING
KVVEYTESQL FSPPVSRRTI YSMLKQFPEH QENLLKFITL HVDKCELENV IPSREYMSDM
ESSFFAHHRI VRAALRARGE ITEAEEAEYQ QSSNLMYNQD FAALMFPELD ESHDDFLNDL
PISSRRRSSD SDSKEAPSMK KPRSF
