ID   PID5_CAEEL              Reviewed;        1061 AA.
AC   Q9GUI6; A0A163VU95; A0A168HAZ2;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 3.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=Protein pid-5 {ECO:0000305};
DE   AltName: Full=piRNA-induced silencing defective protein 5 {ECO:0000312|WormBase:Y45G5AM.2a};
GN   Name=pid-5 {ECO:0000312|WormBase:Y45G5AM.2a};
GN   ORFNames=Y45G5AM.2 {ECO:0000312|WormBase:Y45G5AM.2a};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN   [1] {ECO:0000312|Proteomes:UP000001940}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
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   FUNCTION, INTERACTION WITH PID-2; APP-1 AND PRMT-5, SUBCELLULAR LOCATION,
RP   AND DEVELOPMENTAL STAGE.
RX   PubMed=33231880; DOI=10.15252/embj.2020105280;
RA   Placentino M., de Jesus Domingues A.M., Schreier J., Dietz S., Hellmann S.,
RA   de Albuquerque B.F., Butter F., Ketting R.F.;
RT   "Intrinsically disordered protein PID-2 modulates Z granules and is
RT   required for heritable piRNA-induced silencing in the Caenorhabditis
RT   elegans embryo.";
RL   EMBO J. 40:e105280-e105280(2021).
CC   -!- FUNCTION: Together with pid-4, it is involved in gene silencing
CC       mediated by a class of 21 nucleotide PIWI-interacting RNAs (piRNAs)
CC       that possess a uracil residue at the 5'-end (also called 21U-RNAs) and
CC       guide the Piwi protein prg-1 to its DNA targets for silencing
CC       (PubMed:33231880). Together with pid-4, it is required for the
CC       biogenesis of secondary and tertiary 22G-siRNAs (PubMed:33231880).
CC       Specifically, promotes the production of 22G-siRNAs from the 5' end of
CC       target mRNAs (PubMed:33231880). Together with pid-4, plays a role in
CC       small RNA-directed transgenerational epigenetic inheritance (also
CC       called RNAe) over several generations and germline immortality
CC       (PubMed:33231880). Together with pid-4, plays a role in the formation
CC       of liquid-like condensates in the cytoplasm called Z granules
CC       (PubMed:33231880). {ECO:0000269|PubMed:33231880}.
CC   -!- SUBUNIT: May interact with pid-2, app-1 and prmt-5.
CC       {ECO:0000269|PubMed:33231880}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC       {ECO:0000269|PubMed:33231880}. Cytoplasm, P-body
CC       {ECO:0000269|PubMed:33231880}. Note=Co-localizes with pid-4 at P
CC       granules in germ cells. {ECO:0000269|PubMed:33231880}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=a {ECO:0000312|WormBase:Y45G5AM.2a};
CC         IsoId=Q9GUI6-1; Sequence=Displayed;
CC       Name=c {ECO:0000312|WormBase:Y45G5AM.2c};
CC         IsoId=Q9GUI6-2; Sequence=VSP_061047;
CC       Name=d {ECO:0000312|WormBase:Y45G5AM.2d};
CC         IsoId=Q9GUI6-3; Sequence=VSP_061046;
CC   -!- DEVELOPMENTAL STAGE: Expressed in germ cells of L4 larvae
CC       (PubMed:33231880). Expressed at low levels in the pachytene stage of
CC       the meiotic region of L4 larvae (PubMed:33231880).
CC       {ECO:0000269|PubMed:33231880}.
CC   -!- SIMILARITY: Belongs to the peptidase M24B family. {ECO:0000305}.
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DR   EMBL; BX284605; CCD74321.1; -; Genomic_DNA.
DR   EMBL; BX284605; SAP35608.1; -; Genomic_DNA.
DR   EMBL; BX284605; SAP35609.1; -; Genomic_DNA.
DR   RefSeq; NP_001317846.1; NM_001330835.1. [Q9GUI6-2]
DR   RefSeq; NP_001317847.1; NM_001330836.1. [Q9GUI6-3]
DR   RefSeq; NP_504162.2; NM_071761.5. [Q9GUI6-1]
DR   AlphaFoldDB; Q9GUI6; -.
DR   SMR; Q9GUI6; -.
DR   STRING; 6239.Y45G5AM.2; -.
DR   EPD; Q9GUI6; -.
DR   PaxDb; Q9GUI6; -.
DR   PeptideAtlas; Q9GUI6; -.
DR   EnsemblMetazoa; Y45G5AM.2a.1; Y45G5AM.2a.1; WBGene00021555. [Q9GUI6-1]
DR   EnsemblMetazoa; Y45G5AM.2c.1; Y45G5AM.2c.1; WBGene00021555. [Q9GUI6-2]
DR   EnsemblMetazoa; Y45G5AM.2d.1; Y45G5AM.2d.1; WBGene00021555. [Q9GUI6-3]
DR   GeneID; 178819; -.
DR   KEGG; cel:CELE_Y45G5AM.2; -.
DR   UCSC; Y45G5AM.2; c. elegans. [Q9GUI6-1]
DR   CTD; 178819; -.
DR   WormBase; Y45G5AM.2a; CE31111; WBGene00021555; pid-5. [Q9GUI6-1]
DR   WormBase; Y45G5AM.2c; CE51642; WBGene00021555; pid-5. [Q9GUI6-2]
DR   WormBase; Y45G5AM.2d; CE51609; WBGene00021555; pid-5. [Q9GUI6-3]
DR   eggNOG; KOG2413; Eukaryota.
DR   GeneTree; ENSGT00970000196568; -.
DR   HOGENOM; CLU_311745_0_0_1; -.
DR   InParanoid; Q9GUI6; -.
DR   OMA; IGNCYET; -.
DR   OrthoDB; 417805at2759; -.
DR   PhylomeDB; Q9GUI6; -.
DR   Proteomes; UP000001940; Chromosome V.
DR   Bgee; WBGene00021555; Expressed in germ line (C elegans) and 3 other tissues.
DR   ExpressionAtlas; Q9GUI6; baseline and differential.
DR   GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR   GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
DR   CDD; cd01085; APP; 1.
DR   Gene3D; 3.40.350.10; -; 2.
DR   Gene3D; 3.90.230.10; -; 1.
DR   InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR   InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR   InterPro; IPR000587; Creatinase_N.
DR   InterPro; IPR000994; Pept_M24.
DR   InterPro; IPR033740; Pept_M24B.
DR   InterPro; IPR032416; Peptidase_M24_C.
DR   Pfam; PF01321; Creatinase_N; 1.
DR   Pfam; PF00557; Peptidase_M24; 1.
DR   Pfam; PF16188; Peptidase_M24_C; 1.
DR   SUPFAM; SSF55920; SSF55920; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Reference proteome;
KW   RNA-mediated gene silencing.
FT   CHAIN           1..1061
FT                   /note="Protein pid-5"
FT                   /id="PRO_0000452726"
FT   VAR_SEQ         1..376
FT                   /note="Missing (in isoform d)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_061046"
FT   VAR_SEQ         1..58
FT                   /note="Missing (in isoform c)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_061047"
SQ   SEQUENCE   1061 AA;  122664 MW;  0C5C08877EE82BB9 CRC64;
     MPTSADDSLP LEDSEECDAY IAKFLRPRTH LFSTVKQEKQ RRESHDNKYE TAVRSKAIMP
     SQASKVYRKE MFYSTSKCDS RFINNLHTFN TFDGGSGYSE ASPHYAMDFV KNKGFADDEM
     AGHLKSLEVS RKMTENVKWL NDNRNDLKTA LRRSNSCPEF PIDRDREKIT TLRRNEKRNE
     NAKISNFDAS FVPELCCSDD YPSILCSIAT AFKTVVSRVN AQSIGSGELK IAKVLCSTED
     LFAYVIPKRF NTRDALFAFS NQFRAWLEYK PNVQLYTHYR FINVILYLEE FKHERTEFRR
     ARHVCNLKSR RNHGLFLELD TGMLRVVEIT PEKVRFLANS WAHNPSAIVE VRFDGVKNEK
     DISEEIQAIR NTGRATMISF DREHREHMNG KWPNPRTWSS LGTVVLRREC THHKDHSKPP
     LTRLFCEDRD CIGLCSTGDY FKVPIPEEPN PSHDKLVELR ARFASERTLG YTDRTPIAAY
     ILPNTDAHQN ELIPDFFSRV QFLNGYSGPS GLAIITLNEA MFWVDNGLLK SAESQVDDRS
     WTVKEYQSVE EVINWLAKIL PPKSKVGFDP TLVSYTWHQQ ALQSMTSDRF ELVAIPGNIV
     DEIWRMRPFQ RGDVVKMLDK NTPEIPVHVK IDRLRKSLKP NKCLAAVITS LEDIMWLLNI
     RGNDLPYNPV TYSYLFITMS DVRLFIDAKR LNDVSKAYFA RQSIDVDDYK AASPYIYDWI
     SATKSSFADK KILISPETNY LIGRLIGEDH SMIDPSIMER IKKIKNTDQL KGMRASNLRD
     SIAIVEFLCK FEKERRDGYT FTEYELAADI EEVKTRNREY IGLKQPTIFS AGEHSSVHAH
     RPDAQKIVFH YQQFMFQTGS HYTDGATNCA RTIWDSYPTE EFMNQYTLVL KGHIRLASAS
     FPKTLTYGSR LDIFARIALW DAGLDYDHET GHSVGHFLNI RDTQIVIGRE PYSSNSIIEA
     GQVMTIEPGY YSEGMYGIRI GNCYETVDVT LSQNDQYFLR FEPLTLIPIQ TSIVNKDLLT
     SEEINWLNKY HFKVFSKIGY ILRKENRMEE YDWLFNACQP I