FBF2_CAEEL
ID FBF2_CAEEL Reviewed; 632 AA.
AC Q09312;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Fem-3 mRNA-binding factor 2;
GN Name=fbf-2 {ECO:0000312|WormBase:F21H12.5};
GN ORFNames=F21H12.5 {ECO:0000312|WormBase:F21H12.5};
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 [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 [2]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=9393998; DOI=10.1038/37297;
RA Zhang B., Gallegos M., Puoti A., Durkin E., Fields S., Kimble J.,
RA Wickens M.P.;
RT "A conserved RNA-binding protein that regulates sexual fates in the C.
RT elegans hermaphrodite germ line.";
RL Nature 390:477-484(1997).
RN [3]
RP INTERACTION WITH GLD-3.
RX PubMed=12431376; DOI=10.1016/s1534-5807(02)00322-2;
RA Eckmann C.R., Kraemer B., Wickens M., Kimble J.;
RT "GLD-3, a bicaudal-C homolog that inhibits FBF to control germline sex
RT determination in C. elegans.";
RL Dev. Cell 3:697-710(2002).
RN [4]
RP FUNCTION.
RX PubMed=15454534; DOI=10.1534/genetics.104.029264;
RA Eckmann C.R., Crittenden S.L., Suh N., Kimble J.;
RT "GLD-3 and control of the mitosis/meiosis decision in the germline of
RT Caenorhabditis elegans.";
RL Genetics 168:147-160(2004).
RN [5]
RP FUNCTION.
RX PubMed=16319922; DOI=10.1038/sj.emboj.7600901;
RA Lee M.H., Hook B., Lamont L.B., Wickens M., Kimble J.;
RT "LIP-1 phosphatase controls the extent of germline proliferation in
RT Caenorhabditis elegans.";
RL EMBO J. 25:88-96(2006).
RN [6]
RP FUNCTION.
RX PubMed=22820175; DOI=10.1016/j.bbamcr.2012.07.006;
RA Cha D.S., Datla U.S., Hollis S.E., Kimble J., Lee M.H.;
RT "The Ras-ERK MAPK regulatory network controls dedifferentiation in
RT Caenorhabditis elegans germline.";
RL Biochim. Biophys. Acta 1823:1847-1855(2012).
RN [7]
RP FUNCTION, INTERACTION WITH DLC-1, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP PRO-28; SER-136; LYS-137; 139-TYR-GLY-140 AND 607-SER--ASP-632.
RX PubMed=27864381; DOI=10.1242/dev.140921;
RA Wang X., Olson J.R., Rasoloson D., Ellenbecker M., Bailey J., Voronina E.;
RT "Dynein light chain DLC-1 promotes localization and function of the PUF
RT protein FBF-2 in germline progenitor cells.";
RL Development 143:4643-4653(2016).
CC -!- FUNCTION: Involved in the control of stem cells and sex determination
CC in the C.elegans hermaphrodite germline (PubMed:9393998). May also play
CC a role in the hermaphrodite germline proliferation and oogenesis
CC (PubMed:15454534, PubMed:27864381). By binding to the 3'-UTR, represses
CC phosphatase lip-1 expression in the distal part of the germline mitotic
CC zone (PubMed:16319922). Binds specifically to the regulatory region of
CC fem-3 3'-UTR and mediates the sperm/oocyte switch (PubMed:9393998).
CC Negatively regulates gld-3 expression possibly by directly binding to
CC two sites within the gld-3 isoform b 3'-UTR (PubMed:15454534).
CC Suppresses germline tumor formation by preventing the dedifferentiation
CC of secondary spermatocytes (PubMed:22820175).
CC {ECO:0000269|PubMed:15454534, ECO:0000269|PubMed:16319922,
CC ECO:0000269|PubMed:22820175, ECO:0000269|PubMed:9393998}.
CC -!- SUBUNIT: Interacts (via C-terminus) with gld-3 isoform A in an RNA-
CC independent manner (PubMed:12431376). Interacts with dlc-1, and is
CC required for the localization of fbf-2 to P granules (PubMed:27864381).
CC {ECO:0000269|PubMed:12431376, ECO:0000269|PubMed:27864381}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9393998}.
CC Cytoplasmic granule {ECO:0000269|PubMed:27864381}. Note=Recruited to P
CC granules by dlc-1. {ECO:0000269|PubMed:27864381}.
CC -!- TISSUE SPECIFICITY: Expressed specifically in the germline (at protein
CC level). {ECO:0000269|PubMed:9393998}.
CC -!- DEVELOPMENTAL STAGE: Expression increases in abundance during
CC postembryonic development and peaks during the fourth larval stage.
CC {ECO:0000269|PubMed:9393998}.
CC -!- MISCELLANEOUS: Fbf-1 and fbf-2 are >90% identical on both nucleotide
CC and protein sequence level. Experimental approaches often do not
CC distinguish between the two genes, which are collectively referred to
CC as fbf and are considered to be functionally redundant.
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DR EMBL; FO080717; CCD66119.1; -; Genomic_DNA.
DR PIR; T16128; T16128.
DR RefSeq; NP_495220.1; NM_062819.4.
DR PDB; 3K5Q; X-ray; 2.20 A; A=164-575.
DR PDB; 3K5Y; X-ray; 2.30 A; A=164-575.
DR PDB; 3K5Z; X-ray; 2.40 A; A=164-575.
DR PDB; 3K61; X-ray; 2.21 A; A=164-575.
DR PDB; 3K62; X-ray; 1.90 A; A=164-575.
DR PDB; 3K64; X-ray; 2.00 A; A=164-575.
DR PDB; 3QG9; X-ray; 2.25 A; A=164-575.
DR PDB; 3QGB; X-ray; 2.40 A; A=164-575.
DR PDB; 3QGC; X-ray; 1.90 A; A=164-575.
DR PDB; 3V6Y; X-ray; 2.50 A; A=164-575.
DR PDB; 3V74; X-ray; 2.30 A; A=164-575.
DR PDB; 6NOC; X-ray; 2.85 A; A=164-575.
DR PDB; 6NOF; X-ray; 2.25 A; A=164-575.
DR PDB; 6NOH; X-ray; 2.25 A; A=164-575.
DR PDB; 6PUN; X-ray; 2.10 A; A/C=164-575.
DR PDB; 7RZZ; X-ray; 2.39 A; A=164-575.
DR PDB; 7S02; X-ray; 2.34 A; A=164-575.
DR PDBsum; 3K5Q; -.
DR PDBsum; 3K5Y; -.
DR PDBsum; 3K5Z; -.
DR PDBsum; 3K61; -.
DR PDBsum; 3K62; -.
DR PDBsum; 3K64; -.
DR PDBsum; 3QG9; -.
DR PDBsum; 3QGB; -.
DR PDBsum; 3QGC; -.
DR PDBsum; 3V6Y; -.
DR PDBsum; 3V74; -.
DR PDBsum; 6NOC; -.
DR PDBsum; 6NOF; -.
DR PDBsum; 6NOH; -.
DR PDBsum; 6PUN; -.
DR PDBsum; 7RZZ; -.
DR PDBsum; 7S02; -.
DR AlphaFoldDB; Q09312; -.
DR SMR; Q09312; -.
DR BioGRID; 39358; 14.
DR IntAct; Q09312; 2.
DR MINT; Q09312; -.
DR STRING; 6239.F21H12.5; -.
DR EPD; Q09312; -.
DR PaxDb; Q09312; -.
DR PeptideAtlas; Q09312; -.
DR EnsemblMetazoa; F21H12.5.1; F21H12.5.1; WBGene00001402.
DR UCSC; F21H12.5; c. elegans.
DR WormBase; F21H12.5; CE01916; WBGene00001402; fbf-2.
DR eggNOG; KOG1488; Eukaryota.
DR GeneTree; ENSGT00970000196043; -.
DR HOGENOM; CLU_028494_1_0_1; -.
DR InParanoid; Q09312; -.
DR OMA; ICCEAVS; -.
DR OrthoDB; 1320013at2759; -.
DR PhylomeDB; Q09312; -.
DR EvolutionaryTrace; Q09312; -.
DR PRO; PR:Q09312; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00001402; Expressed in germ line (C elegans) and 3 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0043186; C:P granule; IDA:WormBase.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:WormBase.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0017148; P:negative regulation of translation; IGI:WormBase.
DR GO; GO:0010608; P:post-transcriptional regulation of gene expression; IBA:GO_Central.
DR GO; GO:0007548; P:sex differentiation; IEA:UniProtKB-KW.
DR CDD; cd07920; Pumilio; 1.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR033133; PUM-HD.
DR InterPro; IPR033712; Pumilio_RNA-bd.
DR InterPro; IPR001313; Pumilio_RNA-bd_rpt.
DR Pfam; PF00806; PUF; 8.
DR SMART; SM00025; Pumilio; 8.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50302; PUM; 8.
DR PROSITE; PS50303; PUM_HD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Developmental protein; Differentiation;
KW Reference proteome; Repeat; RNA-binding; Sexual differentiation.
FT CHAIN 1..632
FT /note="Fem-3 mRNA-binding factor 2"
FT /id="PRO_0000075933"
FT DOMAIN 162..566
FT /note="PUM-HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00318"
FT REPEAT 187..225
FT /note="Pumilio 1"
FT REPEAT 226..264
FT /note="Pumilio 2"
FT REPEAT 271..307
FT /note="Pumilio 3"
FT REPEAT 308..344
FT /note="Pumilio 4"
FT REPEAT 345..384
FT /note="Pumilio 5"
FT REPEAT 400..436
FT /note="Pumilio 6"
FT REPEAT 438..473
FT /note="Pumilio 7"
FT REPEAT 484..521
FT /note="Pumilio 8"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 609..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 611..632
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 28
FT /note="P->A: Abolishes interaction with dlc-1."
FT /evidence="ECO:0000269|PubMed:27864381"
FT MUTAGEN 136
FT /note="S->A,D: Abolishes interaction with dlc-1."
FT /evidence="ECO:0000269|PubMed:27864381"
FT MUTAGEN 137
FT /note="K->A,D: Abolishes interaction with dlc-1."
FT /evidence="ECO:0000269|PubMed:27864381"
FT MUTAGEN 139..140
FT /note="Missing: Abolishes interaction with dlc-1."
FT /evidence="ECO:0000269|PubMed:27864381"
FT MUTAGEN 607..632
FT /note="Missing: Abolishes interaction with dlc-1."
FT /evidence="ECO:0000269|PubMed:27864381"
FT HELIX 170..172
FT /evidence="ECO:0007829|PDB:3K62"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:3K62"
FT HELIX 185..191
FT /evidence="ECO:0007829|PDB:3K62"
FT HELIX 194..198
FT /evidence="ECO:0007829|PDB:3K62"
FT HELIX 201..210
FT /evidence="ECO:0007829|PDB:3K62"
FT STRAND 211..213
FT /evidence="ECO:0007829|PDB:6NOC"
FT HELIX 217..227
FT /evidence="ECO:0007829|PDB:3K62"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:3K62"
FT HELIX 231..238
FT /evidence="ECO:0007829|PDB:3K62"
FT HELIX 243..256
FT /evidence="ECO:0007829|PDB:3K62"
FT HELIX 262..275
FT /evidence="ECO:0007829|PDB:3K62"
FT HELIX 277..282
FT /evidence="ECO:0007829|PDB:3K62"
FT HELIX 286..296
FT /evidence="ECO:0007829|PDB:3K62"
FT HELIX 299..307
FT /evidence="ECO:0007829|PDB:3K62"
FT HELIX 313..320
FT /evidence="ECO:0007829|PDB:3K62"
FT TURN 322..324
FT /evidence="ECO:0007829|PDB:3K62"
FT HELIX 325..334
FT /evidence="ECO:0007829|PDB:3K62"
FT HELIX 337..348
FT /evidence="ECO:0007829|PDB:3K62"
FT HELIX 350..357
FT /evidence="ECO:0007829|PDB:3K62"
FT HELIX 360..372
FT /evidence="ECO:0007829|PDB:3K62"
FT HELIX 377..379
FT /evidence="ECO:0007829|PDB:3K62"
FT HELIX 384..403
FT /evidence="ECO:0007829|PDB:3K62"
FT HELIX 405..410
FT /evidence="ECO:0007829|PDB:3K62"
FT TURN 412..414
FT /evidence="ECO:0007829|PDB:3K62"
FT HELIX 415..423
FT /evidence="ECO:0007829|PDB:3K62"
FT HELIX 425..427
FT /evidence="ECO:0007829|PDB:3K62"
FT HELIX 428..438
FT /evidence="ECO:0007829|PDB:3K62"
FT TURN 439..441
FT /evidence="ECO:0007829|PDB:3K62"
FT HELIX 443..447
FT /evidence="ECO:0007829|PDB:3K62"
FT HELIX 452..462
FT /evidence="ECO:0007829|PDB:3K62"
FT HELIX 465..477
FT /evidence="ECO:0007829|PDB:3K62"
FT TURN 483..485
FT /evidence="ECO:0007829|PDB:3K62"
FT HELIX 489..495
FT /evidence="ECO:0007829|PDB:3K62"
FT HELIX 499..514
FT /evidence="ECO:0007829|PDB:3K62"
FT STRAND 521..524
FT /evidence="ECO:0007829|PDB:6NOH"
FT HELIX 528..544
FT /evidence="ECO:0007829|PDB:3K62"
FT HELIX 546..549
FT /evidence="ECO:0007829|PDB:3K62"
FT HELIX 553..566
FT /evidence="ECO:0007829|PDB:3K62"
SQ SEQUENCE 632 AA; 71805 MW; 6EDEE8F6791E4386 CRC64;
MDQSKMRRTN QFRKTSQKPP STGIDSYPTP AQSPMAQHET PMWDFNSLNP YFSMLNMNDG
INYARHQQNH IVTSRPPTPL TDLMSLRSFQ SFPNVFMPVS RSRTSSFIQS DTDSSRLESD
DFSQNVRCFS ADIDRSKSYG SSKHYHLKYS RPALSRNSRS FTRSNNVLPT WSLDSNGEMR
SRLSLSEVLD SGDLMKFAVD KTGCQFLEKA VKGSLTSYQK FQLFEQVIGR KDDFLKLSTN
IFGNYLVQSV IGISLATNDD GYTKRQEKLK NFISSQMTDM CLDKFACRVI QSSLQNMDLS
LACKLVQALP RDARLIAICV DQNANHVIQK VVAVIPLKNW EFIVDFVATP EHLRQICSDK
YGCRVVQTII EKLTADSMNV DLTSAAQNLR ERALQRLMTS VTNRCQELAT NEYANYIIQH
IVSNDDLAVY RECIIEKCLM RNLLSLSQEK FASHVVEKAF LHAPLELLAE MMDEIFDGYI
PHPDTGKDAL DIMMFHQFGN YVVQCMLTIC CDAVSGRRQT KEGGYDHAIS FQDWLKKLHS
RVTKERHRLS RFSSGKKMIE TLANLRSTHP IYELQSSGHD SFKTDYFSTA SEHDGPELEK
NGIEEGSLML EPRSNKSSVS VKFSSSGSHG DD
