TRA2_CAERE
ID TRA2_CAERE Reviewed; 1485 AA.
AC Q9NIW4;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 52.
DE RecName: Full=Sex-determining transformer protein 2;
DE AltName: Full=Cr-tra-2;
DE Flags: Precursor;
GN Name=tra-2 {ECO:0000312|EMBL:AAF71402.1};
OS Caenorhabditis remanei (Caenorhabditis vulgaris).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=31234;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAF71402.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=SB146 {ECO:0000312|EMBL:AAF71402.1};
RX PubMed=10790387; DOI=10.1093/genetics/155.1.105;
RA Haag E.S., Kimble J.;
RT "Regulatory elements required for development of Caenorhabditis elegans
RT hermaphrodites are conserved in the tra-2 homologue of C. remanei, a
RT male/female sister species.";
RL Genetics 155:105-116(2000).
RN [2] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH FEM-3.
RC STRAIN=SB146 {ECO:0000269|PubMed:12477393};
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).
CC -!- FUNCTION: Plays a major role in controlling sexual cell fates. Promotes
CC female development in XX animals where it sequesters one or more of the
CC FEM proteins to the membrane thereby freeing the tra-1 protein (a
CC putative transcription factor) to enter the nucleus and promote female
CC development. In XO animals it acts as a receptor for her-1 which
CC prevents it from binding to FEM proteins thereby repressing the
CC activity of tra-1. Negatively regulates male development when bound to
CC fem-3 and is required together with tra-1 for promoting
CC spermatogenesis. {ECO:0000250|UniProtKB:P34709,
CC ECO:0000269|PubMed:10790387, ECO:0000269|PubMed:12477393}.
CC -!- SUBUNIT: Interacts with tra-1 and fem-3. {ECO:0000250|UniProtKB:P34709,
CC ECO:0000269|PubMed:12477393}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Somatic and germline tissues.
CC {ECO:0000269|PubMed:10790387}.
CC -!- MISCELLANEOUS: The MX region mediates a post-translational regulation,
CC essential for the onset of hermaphrodite spermatogenesis.
CC {ECO:0000250}.
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DR EMBL; AF187965; AAF71402.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9NIW4; -.
DR SMR; Q9NIW4; -.
DR IntAct; Q9NIW4; 1.
DR STRING; 31234.CRE26197; -.
DR PRIDE; Q9NIW4; -.
DR eggNOG; ENOG502R9RT; Eukaryota.
DR HOGENOM; CLU_005001_0_0_1; -.
DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
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 Developmental protein; Differentiation; Membrane; Receptor;
KW Sexual differentiation; Signal; Spermatogenesis; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..1485
FT /note="Sex-determining transformer protein 2"
FT /evidence="ECO:0000255"
FT /id="PRO_0000022576"
FT TRANSMEM 438..458
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 490..510
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 584..604
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 732..752
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 923..943
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 950..970
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 980..1000
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1033..1053
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1063..1083
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1181..1201
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1131..1271
FT /note="Interaction with fem-3"
FT /evidence="ECO:0000250"
FT REGION 1143..1175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1228..1252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1275..1306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1348..1384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1401..1422
FT /note="MX regulatory domain; required for tra-1 binding"
FT /evidence="ECO:0000250"
FT REGION 1442..1485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1153..1169
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1232..1250
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1456..1472
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1485 AA; 170558 MW; 6AAF14B775F705EF CRC64;
MSLRSNKLLV AAVIFTVVTF GLLLTSSIFN NKTTTSLTYG GILPKFGQRI IEKKSNEEYI
IEKIEHTQKD GEDVRSTRYL THHSYLLRNL AKMEVKHHGK DFSINDICYK PHNAIFETTF
APENIDKLPN YLQRLILEAQ RLSPCLIVTP LNCYHDSYRI HSEMSKWNTS NVTNFLNRKL
RNSYIDAIGE SEERPYIKST YGPDLIKEWA HLMFKLPSKQ TSSFSKKDLS SKIELWLSSI
ESKTNLTELG RPSEVDNYFD ICTSMQQVHD FDERKRKFGL YDDDDEFLIG LDCVENKTKF
IEWIQERELR GVSKPFNPNQ QCDGIFKNSE GLEFFYGTRS FGNNTAPFDK MKTEIGLMTP
EQILTTMLHS DFVNGFESIW TIERAQELLD DFRLAIRQEV KRFNENRSSL KIGIDTRVVQ
REESNETELE ISSNLDSVVY FILFIRCVLL IFFAFFAWSV NPLRSAVMFL VRDALTSLLF
SILCKSDGQI ELNSELLGYI ILLTIVNTYL TTRVSWYKDR NETCIQRAKD FPSRSNFSLL
FSIDSLRENC DSRQLQYALA KLSKYLTALD TYSTETFMQL PNYWPFISIL FVPITGCYWY
FVDINLPKIS VVLLPSFIVA TIEQRQVEKS LLKERKAKKE FQKVQKKKME KFLSDGAVDR
LLSGNSESVE DKKLYKSKDC VIHKESAGRL YELSRSSYDV SKIMAYPNQR VRDFRFDALG
CYFWLMKLKS AGILLYGSAV LFVLLSVAVM LIPIQRTSLQ KDMNNEVYFG FSINNMSSDW
ANINKNLHAF NSEIDSIQSL QTISNWKKGF DRFEGRFYKN SSRISDANDY VEWMNQEPIN
WSVMAPLTRI SPKFGIPSPF KFRFRYQIEV NNNESEVIDT VQRIDTLLTK YKGTLSSPIV
DGVLYEYYHG NAAVWNSFVF NELLASGILS AFFALIVVIF SITPSISSVL IFSFFVIGSR
LEIAAVISLF SLDNQQLYTD SAVLVGFLVA WAPFYELSLF RRRLLYKLKT RCTPELSSGK
RIRPPFTKAV DTAQVFAIVL AASLIIAVVA GVVPEFQKFF WPTVILIVVQ LVAFGNSIAV
LVATNQMFER EVRNFLDNEF ELGNGTTAGQ VCHMAQKLIP PKYDIPIPMN DFHIRPTNMS
KFYAPPPAKK RAKQTNNETD PEKKEDEPGT SNANNVSQEE AAHRLAILPW HFVLGGIPVD
LTTRSDQIIN GPFIGISSDA MRTHEINSEL EDQDDYSSES SVEDVESDPA PEEEIKYHEE
NMLHMIEKVQ KDAAEKEAKE KVHQVESAQR RAPNFDDPNV AGPSHRYQRN EERISTDIVP
ADPPREIPAN PVPPPTHVLV QRAPRPHEMP PVIDRTIPRD PRTEPPNLQE CIQQNDDPSL
PPHPRRHQYP DHYGRAMISY CEDVYWTYND GRLPPNVAMP PRPFDWHYRR VAPPEDFNYV
PPPGQPSIPI PAEAMALREE RARAHREQEQ RDNSQSPSPS PEPGL
