FEM3_CAEEL
ID FEM3_CAEEL Reviewed; 388 AA.
AC P34691;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Sex-determination protein fem-3;
DE AltName: Full=Ce-FEM-3;
DE AltName: Full=Feminization of XX and XO animals protein 3;
GN Name=fem-3; ORFNames=C01F6.4;
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 [GENOMIC DNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RC STRAIN=Bristol N2;
RX PubMed=1376249; DOI=10.1002/j.1460-2075.1992.tb05289.x;
RA Ahringer J., Rosenquist T.A., Lawson D.N., Kimble J.;
RT "The Caenorhabditis elegans sex determining gene fem-3 is regulated post-
RT transcriptionally.";
RL EMBO J. 11:2303-2310(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, AND INTERACTION WITH TRA-2.
RC STRAIN=Bristol N2;
RX PubMed=10364161; DOI=10.1101/gad.13.11.1453;
RA Mehra A., Gaudet J., Heck L., Kuwabara P.E., Spence A.M.;
RT "Negative regulation of male development in Caenorhabditis elegans by a
RT protein-protein interaction between TRA-2A and FEM-3.";
RL Genes Dev. 13:1453-1463(1999).
RN [4]
RP FUNCTION, AND INTERACTION WITH TRA-2.
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 [5]
RP INTERACTION WITH SEL-10.
RX PubMed=15306688; DOI=10.1073/pnas.0405087101;
RA Jaeger S., Schwartz H.T., Horvitz H.R., Conradt B.;
RT "The Caenorhabditis elegans F-box protein SEL-10 promotes female
RT development and may target FEM-1 and FEM-3 for degradation by the
RT proteasome.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:12549-12554(2004).
RN [6]
RP FUNCTION, IDENTIFICATION IN THE CBC(FEM-1) COMPLEX, AND INTERACTION WITH
RP TRA-1; FEM-1 AND FEM-2.
RX PubMed=17609115; DOI=10.1016/j.devcel.2007.05.008;
RA Starostina N.G., Lim J.M., Schvarzstein M., Wells L., Spence A.M.,
RA Kipreos E.T.;
RT "A CUL-2 ubiquitin ligase containing three FEM proteins degrades TRA-1 to
RT regulate C. elegans sex determination.";
RL Dev. Cell 13:127-139(2007).
RN [7]
RP IDENTIFICATION IN A COMPLEX WITH FEM-1 AND FEM-2, AND INTERACTION WITH
RP FEM-2.
RX PubMed=23760267; DOI=10.1074/jbc.m113.464339;
RA Zhang Y., Zhao H., Wang J., Ge J., Li Y., Gu J., Li P., Feng Y., Yang M.;
RT "Structural insight into Caenorhabditis elegans sex-determining protein
RT FEM-2.";
RL J. Biol. Chem. 288:22058-22066(2013).
CC -!- FUNCTION: Required for male development. In XO (male) animals, fem-3
CC directs male differentiation in all tissues. In XX (hermaphrodite)
CC animals, it specifies the first 80 or so germ cells to be sperm.
CC Negatively regulates male development when bound to tra-2. Together
CC with fem-2 associates with the CBC(fem-1) E3 ubiquitin-protein ligase
CC complex which mediates the ubiquitination and subsequent proteasomal
CC degradation of tra-1. {ECO:0000269|PubMed:10364161,
CC ECO:0000269|PubMed:12477393, ECO:0000269|PubMed:1376249,
CC ECO:0000269|PubMed:17609115}.
CC -!- SUBUNIT: Component of a complex containing fem-1, fem-2 and fem-3
CC (PubMed:23760267). Interacts with fem-1 and fem-2 (via N-terminus)
CC (PubMed:23760267, PubMed:17609115). Part of a E3 ubiquitin-protein
CC ligase complex, at least composed of cul-2, elc-1, tra-1, fem-1, fem-2
CC and fem-3; mediates the ubiquitination and subsequent proteasomal
CC degradation of tra-1 (PubMed:17609115). Interacts with tra-1
CC (PubMed:17609115). Interacts with sel-10 (PubMed:15306688). Interacts
CC with tra-2 (PubMed:10364161, PubMed:12477393).
CC {ECO:0000269|PubMed:10364161, ECO:0000269|PubMed:12477393,
CC ECO:0000269|PubMed:15306688, ECO:0000269|PubMed:17609115,
CC ECO:0000269|PubMed:23760267}.
CC -!- INTERACTION:
CC P34691; P17221: fem-1; NbExp=3; IntAct=EBI-445465, EBI-1998155;
CC P34691; Q93794: sel-10; NbExp=2; IntAct=EBI-445465, EBI-323098;
CC P34691; P34708-1: tra-1; NbExp=2; IntAct=EBI-445465, EBI-367214;
CC P34691; P34709: tra-2; NbExp=4; IntAct=EBI-445465, EBI-367223;
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC {ECO:0000269|PubMed:1376249}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X64963; CAA46126.1; -; Genomic_DNA.
DR EMBL; X64962; CAA46125.1; -; mRNA.
DR EMBL; Z68213; CAA92437.1; -; Genomic_DNA.
DR PIR; S22692; S22692.
DR RefSeq; NP_001255365.1; NM_001268436.1.
DR AlphaFoldDB; P34691; -.
DR BioGRID; 42840; 8.
DR ComplexPortal; CPX-3385; Fem-2 phosphatase complex.
DR IntAct; P34691; 6.
DR MINT; P34691; -.
DR STRING; 6239.C01F6.4a; -.
DR PaxDb; P34691; -.
DR EnsemblMetazoa; C01F6.4a.1; C01F6.4a.1; WBGene00001413.
DR GeneID; 177734; -.
DR KEGG; cel:CELE_C01F6.4; -.
DR UCSC; C01F6.4; c. elegans.
DR CTD; 177734; -.
DR WormBase; C01F6.4a; CE02953; WBGene00001413; fem-3.
DR eggNOG; ENOG502TI3W; Eukaryota.
DR HOGENOM; CLU_636523_0_0_1; -.
DR InParanoid; P34691; -.
DR OMA; FVFQRTM; -.
DR OrthoDB; 1759382at2759; -.
DR SignaLink; P34691; -.
DR PRO; PR:P34691; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00001413; Expressed in germ line (C elegans) and 4 other tissues.
DR ExpressionAtlas; P34691; baseline and differential.
DR GO; GO:0031462; C:Cul2-RING ubiquitin ligase complex; IDA:ComplexPortal.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0008287; C:protein serine/threonine phosphatase complex; IDA:ComplexPortal.
DR GO; GO:0032991; C:protein-containing complex; IMP:UniProtKB.
DR GO; GO:0019903; F:protein phosphatase binding; IPI:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0030238; P:male sex determination; IMP:WormBase.
DR GO; GO:0019102; P:male somatic sex determination; IMP:UniProtKB.
DR GO; GO:0042006; P:masculinization of hermaphroditic germ-line; IMP:WormBase.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; IMP:UniProtKB.
DR GO; GO:1904146; P:positive regulation of meiotic cell cycle process involved in oocyte maturation; IMP:UniProtKB.
DR GO; GO:0060282; P:positive regulation of oocyte development; IMP:UniProtKB.
DR GO; GO:0071168; P:protein localization to chromatin; IMP:UniProtKB.
DR GO; GO:1905936; P:regulation of germ cell proliferation; IGI:UniProtKB.
DR GO; GO:0007530; P:sex determination; IMP:ComplexPortal.
DR GO; GO:0007548; P:sex differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR InterPro; IPR030804; BBS5/fem-3.
DR PIRSF; PIRSF010072; DUF1448; 1.
PE 1: Evidence at protein level;
KW Developmental protein; Differentiation; Reference proteome; Repeat;
KW Sexual differentiation; Spermatogenesis; Ubl conjugation pathway.
FT CHAIN 1..388
FT /note="Sex-determination protein fem-3"
FT /id="PRO_0000087220"
FT REPEAT 7..10
FT /note="1-1"
FT REPEAT 110..113
FT /note="2-1"
FT REPEAT 141..144
FT /note="2-2"
FT REPEAT 234..237
FT /note="3-1"
FT REPEAT 284..287
FT /note="3-2"
FT REPEAT 371..374
FT /note="1-2"
FT VARIANT 142
FT /note="T -> I (in allele E2063)"
FT VARIANT 159
FT /note="M -> I (in allele E2006)"
FT VARIANT 299
FT /note="P -> S (in allele Q77)"
FT VARIANT 360
FT /note="E -> K (in allele E2143)"
SQ SEQUENCE 388 AA; 46230 MW; 5366B23BBCF0CA28 CRC64;
MEVDPGSDDV EADRETRAQK LKLKRNVKFR AQMRRFDEYC GVTNLTVDDL NWPLISGIPL
QRQRLTGATY YDDSLLDQNP WDEFSIDRFL EITSIQLITA GAGYERNDEI TRFVFQRTMK
TIVTYCNFMY DLARRNGKVQ ITRFELQDLI HRDEFRFYMY FRQFLPNPDP NCTAFSNHYT
SLLHTLYFNI PGMPQFWNNS QMYNYAATRG QRLVQNIAAF YPPEYFWNED ESKYHTTFVV
PRGTEFSKFY ARRFHEALGM PPLENEIITV LDWLAKLCIL EIVYHTTIWC DITGFGGLPR
IEHYRLAMEN VEDIIFDLAI DDFSISRLQL QISPFEISRY SPLDVSGYYE TIKRKKDIEE
YQNRFYEVHY SDDVRIMNVY ATDCSRKR
