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TRA2_CAEBR
ID   TRA2_CAEBR              Reviewed;        1489 AA.
AC   Q17307; A8XCP0; Q8ST82; Q8STA3;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2009, sequence version 3.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=Sex-determining transformer protein 2 {ECO:0000312|WormBase:CBG11194a};
DE            Short=Cbr-Tra-2A {ECO:0000312|WormBase:CBG11194a};
DE            Short=Cbr-tra-2 {ECO:0000303|PubMed:24098152};
DE   Flags: Precursor;
GN   Name=tra-2 {ECO:0000312|WormBase:CBG11194a};
GN   ORFNames=CBG11194 {ECO:0000312|WormBase:CBG11194a};
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].
RX   PubMed=7971272; DOI=10.1093/nar/22.21.4414;
RA   Kuwabara P.E., Shah S.;
RT   "Cloning by synteny: identifying C. briggsae homologues of C. elegans
RT   genes.";
RL   Nucleic Acids Res. 22:4414-4418(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND ALTERNATIVE SPLICING.
RC   STRAIN=Gujarat;
RX   PubMed=8889523; DOI=10.1093/genetics/144.2.597;
RA   Kuwabara P.E.;
RT   "Interspecies comparison reveals evolution of control regions in the
RT   nematode sex-determining gene tra-2.";
RL   Genetics 144:597-607(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-137, AND VARIANTS ASN-30; SER-40;
RP   GLU-57 AND THR-120.
RC   STRAIN=AF16, HK104, HK105, PB800, PB826, and VT847;
RX   PubMed=12019226; DOI=10.1093/genetics/161.1.99;
RA   Graustein A., Gaspar J.M., Walters J.R., Palopoli M.F.;
RT   "Levels of DNA polymorphism vary with mating system in the nematode genus
RT   Caenorhabditis.";
RL   Genetics 161:99-107(2002).
RN   [5]
RP   FUNCTION, AND INTERACTION WITH TRA-1.
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   [6]
RP   FUNCTION, AND INTERACTION WITH FEM-3.
RX   PubMed=12477393; DOI=10.1016/s0960-9822(02)01333-7;
RA   Haag E.S., Wang S., Kimble J.;
RT   "Rapid coevolution of the nematode sex-determining genes fem-3 and tra-2.";
RL   Curr. Biol. 12:2035-2041(2002).
RN   [7]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
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 cell fates
CC       (PubMed:8889523, PubMed:11250902, PubMed:24098152). Promotes female
CC       development in XX animals where it sequesters one or more of the FEM
CC       proteins to the membrane thereby freeing the tra-1 protein (a putative
CC       transcription factor) to enter the nucleus and promote female
CC       development (By similarity). In XO animals it acts as a receptor for
CC       her-1 which prevents it from binding to FEM proteins thereby repressing
CC       the activity of tra-1 (By similarity). Negatively regulates male
CC       development when bound to fem-3 and is required together with tra-1 for
CC       promoting spermatogenesis (PubMed:12477393). Also required for
CC       feminizing tra-3 activity (By similarity).
CC       {ECO:0000250|UniProtKB:P34709, ECO:0000269|PubMed:11250902,
CC       ECO:0000269|PubMed:12477393, ECO:0000269|PubMed:24098152,
CC       ECO:0000269|PubMed:8889523}.
CC   -!- SUBUNIT: Interacts with tra-1 and fem-3. {ECO:0000269|PubMed:11250902,
CC       ECO:0000269|PubMed:12477393}.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced.;
CC       Name=a;
CC         IsoId=Q17307-1; Sequence=Displayed;
CC   -!- DISRUPTION PHENOTYPE: Null hermaphrodite mutants have masculinized germ
CC       lines, producing only sperm. Animals make incomplete male tails,
CC       producing shorter stubby tails that lack sensory structures called
CC       rays. {ECO:0000269|PubMed:24098152}.
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DR   EMBL; U59879; AAB49333.1; -; mRNA.
DR   EMBL; HE601002; CAP30389.1; -; Genomic_DNA.
DR   EMBL; AF491464; AAM09704.1; -; Genomic_DNA.
DR   EMBL; AF491465; AAM09705.1; -; Genomic_DNA.
DR   EMBL; AF491466; AAM09706.1; -; Genomic_DNA.
DR   EMBL; AF491467; AAM09707.1; -; Genomic_DNA.
DR   EMBL; AF491468; AAM09708.1; -; Genomic_DNA.
DR   EMBL; AF491469; AAM09709.1; -; Genomic_DNA.
DR   PIR; S72250; S72250.
DR   AlphaFoldDB; Q17307; -.
DR   IntAct; Q17307; 1.
DR   STRING; 6238.CBG11194; -.
DR   PRIDE; Q17307; -.
DR   WormBase; CBG11194a; CBP38209; WBGene00032357; Cbr-tra-2.
DR   eggNOG; ENOG502R9RT; Eukaryota.
DR   HOGENOM; CLU_005001_0_0_1; -.
DR   InParanoid; Q17307; -.
DR   OMA; SIWTIER; -.
DR   OrthoDB; 1388750at2759; -.
DR   Proteomes; UP000008549; Chromosome II.
DR   GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; IBA:GO_Central.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0018992; P:germ-line sex determination; IMP:UniProtKB.
DR   GO; GO:0040021; P:hermaphrodite germ-line sex determination; IEA:InterPro.
DR   GO; GO:0042001; P:hermaphrodite somatic sex determination; IEA:InterPro.
DR   GO; GO:0007548; P:sex differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR   InterPro; IPR032848; Ce-Tra-2.
DR   PANTHER; PTHR39365; PTHR39365; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Developmental protein; Differentiation; Membrane;
KW   Receptor; Reference proteome; Sexual differentiation; Signal;
KW   Spermatogenesis; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..33
FT                   /evidence="ECO:0000255"
FT   CHAIN           34..1489
FT                   /note="Sex-determining transformer protein 2"
FT                   /id="PRO_0000022573"
FT   TRANSMEM        454..474
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        489..509
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        513..533
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        600..620
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        622..642
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        749..769
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        931..951
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        958..978
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        986..1006
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1041..1061
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1066..1086
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1138..1288
FT                   /note="Interaction with fem-3"
FT                   /evidence="ECO:0000250"
FT   REGION          1143..1176
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1233..1393
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1402..1423
FT                   /note="MX regulatory domain; required for tra-1 binding"
FT   REGION          1412..1489
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1275..1302
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1423..1438
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1439..1453
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1459..1483
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VARIANT         30
FT                   /note="T -> N (in strain: HK104, HK105, PB800 and PB826)"
FT                   /evidence="ECO:0000269|PubMed:12019226"
FT   VARIANT         40
FT                   /note="I -> S (in strain: HK104, HK105, PB800 and PB826)"
FT                   /evidence="ECO:0000269|PubMed:12019226"
FT   VARIANT         57
FT                   /note="Q -> E (in strain: HK104, HK105, PB800 and PB826)"
FT                   /evidence="ECO:0000269|PubMed:12019226"
FT   VARIANT         120
FT                   /note="A -> T (in strain: HK104, HK105, PB800 and PB826)"
FT                   /evidence="ECO:0000269|PubMed:12019226"
FT   CONFLICT        55
FT                   /note="T -> M (in Ref. 1; AAB49333)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        825..830
FT                   /note="GRRVLI -> WKKSFDRYERRIYQ (in Ref. 1; AAB49333)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1489 AA;  171114 MW;  979CABEAADCE5949 CRC64;
     MKLAFNKLLV ASVVFTVLSF GLLLASLFTT TATTPSEWTI LLPEFRFPVN KKQTTEQFLV
     EKIVHEHEEG EDVRSALYLT HHGYFMNAIA NMKVTYRQKS YTVNDVCFKP HSAIFENVPA
     PENIDKLPAY FQRLLLEMQR LSPCLIVTPL NCFYDSYHIH SEISNWNAST DYLNRRLRNS
     YLEAIEEKDS RPYVKSTYGP ELIKEWARHM FAIPSKPLSN FSKSDLYSRV KTWLSSIAAR
     KKICADPMRS CDETLDAENY FNVCTVMQQI NDYDERRKQR LKFQLEYGDE EFTTRLDCVE
     DREKFIEWMQ ERNLRDMLKL FASSVEIPDH KEIPNQVCDG IYHDLDTSSG LELFRGARSF
     SNNTSAYDTI NVELGFMTPE NLLTTMRHSD FVNGFESIWT IERARELLNE FRLALKVEVT
     KFSESRSSRR VKVTTRIVNQ IEEEGSDEEM EYHMIYFILG ACALMVALFA AFAFSEAFLT
     SLSMFLLRGF ITGLLFIFLC KSGGLILIDS NFLCYITMHL AFNLVMTARV TFICYRIGGC
     VQSEKDFVKS NFSSLGSVPV DSLKEDSCKR HVQYVLAKYT KFQVAQDAYS EEPFEKLPKY
     WFLIAIVLVP VIGVYWFFID SDVQKICIVL LPAFLIAAFE EMRVKNQLLR ERRIKKAIQR
     LQKEENTRIM SRGEIDNLLS GNAELSGEKS HYESKQGVLH HGSAGGLFEL SRSTYDVSLI
     MAYPNQMIRN LRLCALGAYF RLFKMKYCAV VVSSVAALLI LLSIGLLFIP VQRSSVPKEL
     QQDELSIDFA IPNVSSSSWE SINEYLEEFN SEIDSITNLQ TITNGRRVLI NSTSKINNFL
     KWVDDEPISW YLTAPLTRPY RKTHLPNPFR FQFRYGFDSI QKSTIIDVVE RIDTLLTKYT
     ETLSFPKAIG FLYEHYHQKA VVWNSFAYHE IFAAAVLAGF FSIIVVFFSI GPVVLPTLAF
     AFFVVGNRLE IAAIVSLFSL EYHQCYTNVA VFVGFLAAWT PFCDLARFRG RLLYKDQTRR
     TPELATQRRI RVPHVAAVDT VQIFAIFLTA TILLIVITAI IPQFRAFFIP TVILLITLLL
     AVFNSLAVSL AAYQMFEHEV RHCYHDQLQS LTTTGKVCDM TRKKLLPREE DLSIPMEEFS
     IRPTENTKHY APRPIDNSDP PEQAADEEVV NQDPSMEAAR RQYVEFTHRT TGMPIELINQ
     FVDNFPVFNV PANFLPNYFA LGGAPLDANN GVLLRQPGIA PPPRPNREED EEERFGLGGG
     EDDDSYPSSG DDIGDPAKEQ QEVTDDVATR YKEEEVRKKV QPAVPNYDDP NVPGPSNPVP
     RQVEQVSREA PEDSPNREPR ILVYQRPPRL HEIPQISHGR NPLHDPPSME EYVQKYDDPN
     QPPSRRADQY PPSFTPAMVG YCEDVYWKYN ERNLPDNVPM PPRPRDWDQR RLVELPPPED
     FDEVPPPGRS AIPIPPGAIR LRERRREQHL REQEARRNRP ESPDDTPGL
 
 
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