PUF7_CAEEL
ID PUF7_CAEEL Reviewed; 485 AA.
AC O44169;
DT 13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Pumilio domain-containing protein 7 {ECO:0000303|PubMed:17234175};
GN Name=puf-7 {ECO:0000312|EMBL:CCD61586.1, ECO:0000312|WormBase:B0273.2};
GN ORFNames=B0273.2;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1] {ECO:0000312|EMBL:CCD61586.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:CCD61586.1};
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] {ECO:0000305}
RP DISRUPTION PHENOTYPE.
RX PubMed=10518502; DOI=10.1242/dev.126.21.4861;
RA Subramaniam K., Seydoux G.;
RT "nos-1 and nos-2, two genes related to Drosophila nanos, regulate
RT primordial germ cell development and survival in Caenorhabditis elegans.";
RL Development 126:4861-4871(1999).
RN [3] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17234175; DOI=10.1016/j.ydbio.2006.12.004;
RA Lublin A.L., Evans T.C.;
RT "The RNA-binding proteins PUF-5, PUF-6, and PUF-7 reveal multiple systems
RT for maternal mRNA regulation during C. elegans oogenesis.";
RL Dev. Biol. 303:635-649(2007).
RN [4] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22542599; DOI=10.1016/j.ydbio.2012.03.019;
RA Hubstenberger A., Cameron C., Shtofman R., Gutman S., Evans T.C.;
RT "A network of PUF proteins and Ras signaling promote mRNA repression and
RT oogenesis in C. elegans.";
RL Dev. Biol. 366:218-231(2012).
RN [5] {ECO:0000305, ECO:0000312|PDB:3V71}
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 76-453 IN COMPLEX WITH RNA,
RP FUNCTION, AND MUTAGENESIS OF SER-441.
RX PubMed=22205700; DOI=10.1074/jbc.m111.326264;
RA Qiu C., Kershner A., Wang Y., Holley C.P., Wilinski D., Keles S.,
RA Kimble J., Wickens M., Hall T.M.;
RT "Divergence of Pumilio/fem-3 mRNA binding factor (PUF) protein specificity
RT through variations in an RNA-binding pocket.";
RL J. Biol. Chem. 287:6949-6957(2012).
CC -!- FUNCTION: RNA-binding protein that binds to the consensus sequence 5'-
CC CUCUGUAUCUUGU-3' in mRNA 3'-UTRs and modulates mRNA expression and
CC stability. Functions redundantly with puf-5 and puf-6 in oocyte
CC formation and organization, early embryonic cell divisions, and
CC repression of expression of glp-1 and other maternal mRNAs in late
CC oogenesis. {ECO:0000269|PubMed:17234175, ECO:0000269|PubMed:22205700,
CC ECO:0000269|PubMed:22542599}.
CC -!- DISRUPTION PHENOTYPE: Simultaneous knockdown of puf-6 and puf-7 results
CC in ectopic primordial germ cells (PGCs) outside the somatic gonads,
CC premature PGC proliferation in L1 larvae and germ cell death. Does not
CC affect germline development in adult hermaphrodites. Disruption with
CC puf-5 and puf-6 results in abnormally small oocytes, disorganization of
CC oocyte nuclei and cells, inefficient yolk uptake by oocytes, embryonic
CC arrest with impaired eggshell formation and cytokinesis defects,
CC impaired repression of glp-1 in late oogenesis, and mislocalization of
CC rme-2 to the cytoplasm instead of the plasma membrane.
CC {ECO:0000269|PubMed:10518502, ECO:0000269|PubMed:17234175,
CC ECO:0000269|PubMed:22542599}.
CC -!- MISCELLANEOUS: Puf-6 and puf-7 are >98% 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 puf6/7 and are considered to be functionally redundant.
CC {ECO:0000305}.
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DR EMBL; FO080145; CCD61586.1; -; Genomic_DNA.
DR PIR; T32538; T32538.
DR RefSeq; NP_500820.1; NM_068419.4.
DR PDB; 3V71; X-ray; 2.90 A; A=76-453.
DR PDBsum; 3V71; -.
DR AlphaFoldDB; O44169; -.
DR SMR; O44169; -.
DR STRING; 6239.B0273.2.2; -.
DR PaxDb; O44169; -.
DR EnsemblMetazoa; B0273.2.1; B0273.2.1; WBGene00004243.
DR GeneID; 177332; -.
DR KEGG; cel:CELE_B0273.2; -.
DR UCSC; B0273.2.1; c. elegans.
DR CTD; 177332; -.
DR WormBase; B0273.2; CE16788; WBGene00004243; puf-7.
DR eggNOG; KOG1488; Eukaryota.
DR GeneTree; ENSGT00970000196107; -.
DR HOGENOM; CLU_028494_0_0_1; -.
DR InParanoid; O44169; -.
DR OMA; SDSYIFN; -.
DR OrthoDB; 238378at2759; -.
DR PhylomeDB; O44169; -.
DR PRO; PR:O44169; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00004243; Expressed in adult organism 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:0003730; F:mRNA 3'-UTR binding; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; ISS:WormBase.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007281; P:germ cell development; IGI:WormBase.
DR GO; GO:0048477; P:oogenesis; IEA:UniProtKB-KW.
DR GO; GO:0010608; P:post-transcriptional regulation of gene expression; IBA:GO_Central.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
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; IPR001313; Pumilio_RNA-bd_rpt.
DR Pfam; PF00806; PUF; 7.
DR SMART; SM00025; Pumilio; 7.
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; Cell cycle; Cell division; Developmental protein;
KW Differentiation; Oogenesis; Reference proteome; Repeat; RNA-binding;
KW Translation regulation.
FT CHAIN 1..485
FT /note="Pumilio domain-containing protein 7"
FT /id="PRO_0000424282"
FT REPEAT 86..124
FT /note="Pumilio 1"
FT /evidence="ECO:0000255"
FT REPEAT 128..163
FT /note="Pumilio 2"
FT /evidence="ECO:0000255"
FT REPEAT 164..200
FT /note="Pumilio 3"
FT /evidence="ECO:0000255"
FT REPEAT 201..236
FT /note="Pumilio 4"
FT /evidence="ECO:0000255"
FT REPEAT 237..279
FT /note="Pumilio 5"
FT /evidence="ECO:0000255"
FT REPEAT 287..324
FT /note="Pumilio 6"
FT /evidence="ECO:0000255"
FT REPEAT 326..361
FT /note="Pumilio 7"
FT /evidence="ECO:0000255"
FT REPEAT 370..411
FT /note="Pumilio 8"
FT /evidence="ECO:0000255"
FT REGION 29..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 439..454
FT /note="RNA-binding"
FT /evidence="ECO:0000269|PubMed:22205700"
FT COMPBIAS 47..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 441
FT /note="S->A: Reduced RNA-binding activity."
FT /evidence="ECO:0000269|PubMed:22205700"
FT HELIX 84..89
FT /evidence="ECO:0007829|PDB:3V71"
FT HELIX 93..98
FT /evidence="ECO:0007829|PDB:3V71"
FT HELIX 100..108
FT /evidence="ECO:0007829|PDB:3V71"
FT HELIX 117..127
FT /evidence="ECO:0007829|PDB:3V71"
FT HELIX 130..137
FT /evidence="ECO:0007829|PDB:3V71"
FT HELIX 142..151
FT /evidence="ECO:0007829|PDB:3V71"
FT HELIX 155..167
FT /evidence="ECO:0007829|PDB:3V71"
FT HELIX 170..174
FT /evidence="ECO:0007829|PDB:3V71"
FT HELIX 179..189
FT /evidence="ECO:0007829|PDB:3V71"
FT HELIX 192..203
FT /evidence="ECO:0007829|PDB:3V71"
FT HELIX 207..212
FT /evidence="ECO:0007829|PDB:3V71"
FT TURN 214..216
FT /evidence="ECO:0007829|PDB:3V71"
FT HELIX 217..224
FT /evidence="ECO:0007829|PDB:3V71"
FT TURN 229..231
FT /evidence="ECO:0007829|PDB:3V71"
FT HELIX 233..240
FT /evidence="ECO:0007829|PDB:3V71"
FT HELIX 244..250
FT /evidence="ECO:0007829|PDB:3V71"
FT HELIX 254..265
FT /evidence="ECO:0007829|PDB:3V71"
FT STRAND 269..271
FT /evidence="ECO:0007829|PDB:3V71"
FT HELIX 274..289
FT /evidence="ECO:0007829|PDB:3V71"
FT HELIX 292..296
FT /evidence="ECO:0007829|PDB:3V71"
FT TURN 299..301
FT /evidence="ECO:0007829|PDB:3V71"
FT HELIX 302..309
FT /evidence="ECO:0007829|PDB:3V71"
FT HELIX 315..325
FT /evidence="ECO:0007829|PDB:3V71"
FT TURN 326..329
FT /evidence="ECO:0007829|PDB:3V71"
FT HELIX 331..334
FT /evidence="ECO:0007829|PDB:3V71"
FT HELIX 340..350
FT /evidence="ECO:0007829|PDB:3V71"
FT HELIX 353..363
FT /evidence="ECO:0007829|PDB:3V71"
FT STRAND 371..373
FT /evidence="ECO:0007829|PDB:3V71"
FT HELIX 377..382
FT /evidence="ECO:0007829|PDB:3V71"
FT HELIX 387..401
FT /evidence="ECO:0007829|PDB:3V71"
FT TURN 412..414
FT /evidence="ECO:0007829|PDB:3V71"
FT HELIX 415..436
FT /evidence="ECO:0007829|PDB:3V71"
FT HELIX 440..451
FT /evidence="ECO:0007829|PDB:3V71"
SQ SEQUENCE 485 AA; 54761 MW; 5E6E9569D014BE24 CRC64;
MTPNRRSTDS YNMLGASFDF DPDFSLLSNK THKNKNPKPP VKLLPYRHGS NTTSSDSDSY
IFNSGSGSSD AETPAPVAPI FISLEDVLLN GQLIDFAIDP SGVKFLEANY PLDSEDQIRK
AVFEKFTEST TLFVGLCHSR NGNFIVQKLV ELATPAEQRE LLRQMIDGGL LAMCKDKFAC
RVVQLALQKF DHSNVFQLIQ ELSTFDLAAM CTDQISIHVI QRVVKQLPVD MWTFFVHFLS
SGDSLMAVCQ DKYGCRLVQQ VIDRLAENPK LPCFKFRIQL LHSLMTCIVR NCYRLSSNEF
ANYVIQYVIK SSGIMEMYRD TIIDKCLLRN LLSMSQDKYA SHVIEGAFLF APPALLHEMM
EEIFSGYVKD VESNRDALDI LLFHQYGNYV VQQMISICTA ALIGKEEREL PPAILLLYSG
WYEKMKQRVL QHASRLERFS SGKKIIDSVM RHGVPTAAAV NAQAAPSLME LTAQFDAMFP
SFLAR
