PIWL3_HUMAN
ID PIWL3_HUMAN Reviewed; 882 AA.
AC Q7Z3Z3;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Piwi-like protein 3;
GN Name=PIWIL3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND VARIANT MET-418.
RX PubMed=12906857; DOI=10.1016/s0888-7543(03)00129-0;
RA Sasaki T., Shiohama A., Minoshima S., Shimizu N.;
RT "Identification of eight members of the Argonaute family in the human
RT genome.";
RL Genomics 82:323-330(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
CC -!- FUNCTION: May play a role during spermatogenesis by repressing
CC transposable elements and preventing their mobilization, which is
CC essential for the germline integrity. Acts via the piRNA metabolic
CC process, which mediates the repression of transposable elements during
CC meiosis by forming complexes composed of piRNAs and Piwi proteins and
CC govern the methylation and subsequent repression of transposons.
CC Directly binds piRNAs, a class of 24 to 30 nucleotide RNAs that are
CC generated by a Dicer-independent mechanism and are primarily derived
CC from transposons and other repeated sequence elements. Besides their
CC function in transposable elements repression, piRNAs are probably
CC involved in other processes during meiosis such as translation
CC regulation (By similarity). {ECO:0000250|UniProtKB:Q9JMB7}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Note=Probable component
CC of the meiotic nuage, also named P granule, a germ-cell-specific
CC organelle required to repress transposon activity during meiosis.
CC {ECO:0000250|UniProtKB:Q9JMB7}.
CC -!- TISSUE SPECIFICITY: Expressed in testis. {ECO:0000269|PubMed:12906857}.
CC -!- SIMILARITY: Belongs to the argonaute family. Piwi subfamily.
CC {ECO:0000305}.
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DR EMBL; AB079368; BAC81343.1; -; mRNA.
DR EMBL; AP000358; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP000359; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS33623.1; -.
DR RefSeq; NP_001008496.2; NM_001008496.3.
DR AlphaFoldDB; Q7Z3Z3; -.
DR SMR; Q7Z3Z3; -.
DR BioGRID; 136921; 3.
DR STRING; 9606.ENSP00000330031; -.
DR iPTMnet; Q7Z3Z3; -.
DR PhosphoSitePlus; Q7Z3Z3; -.
DR BioMuta; PIWIL3; -.
DR DMDM; 229485673; -.
DR EPD; Q7Z3Z3; -.
DR jPOST; Q7Z3Z3; -.
DR MassIVE; Q7Z3Z3; -.
DR PaxDb; Q7Z3Z3; -.
DR PeptideAtlas; Q7Z3Z3; -.
DR PRIDE; Q7Z3Z3; -.
DR Antibodypedia; 24076; 93 antibodies from 25 providers.
DR DNASU; 440822; -.
DR Ensembl; ENST00000332271.9; ENSP00000330031.5; ENSG00000184571.14.
DR GeneID; 440822; -.
DR KEGG; hsa:440822; -.
DR UCSC; uc003abd.3; human.
DR CTD; 440822; -.
DR DisGeNET; 440822; -.
DR GeneCards; PIWIL3; -.
DR HGNC; HGNC:18443; PIWIL3.
DR HPA; ENSG00000184571; Not detected.
DR MIM; 610314; gene.
DR neXtProt; NX_Q7Z3Z3; -.
DR OpenTargets; ENSG00000184571; -.
DR PharmGKB; PA38332; -.
DR VEuPathDB; HostDB:ENSG00000184571; -.
DR eggNOG; KOG1042; Eukaryota.
DR GeneTree; ENSGT00950000183200; -.
DR InParanoid; Q7Z3Z3; -.
DR OMA; NTRRYMM; -.
DR OrthoDB; 220258at2759; -.
DR PhylomeDB; Q7Z3Z3; -.
DR TreeFam; TF354206; -.
DR PathwayCommons; Q7Z3Z3; -.
DR SignaLink; Q7Z3Z3; -.
DR BioGRID-ORCS; 440822; 16 hits in 1068 CRISPR screens.
DR ChiTaRS; PIWIL3; human.
DR GenomeRNAi; 440822; -.
DR Pharos; Q7Z3Z3; Tbio.
DR PRO; PR:Q7Z3Z3; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q7Z3Z3; protein.
DR Bgee; ENSG00000184571; Expressed in testis and 4 other tissues.
DR ExpressionAtlas; Q7Z3Z3; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0043186; C:P granule; IBA:GO_Central.
DR GO; GO:0004521; F:endoribonuclease activity; IBA:GO_Central.
DR GO; GO:0034584; F:piRNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0031047; P:gene silencing by RNA; IBA:GO_Central.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR Gene3D; 3.30.420.10; -; 1.
DR InterPro; IPR014811; ArgoL1.
DR InterPro; IPR003100; PAZ_dom.
DR InterPro; IPR036085; PAZ_dom_sf.
DR InterPro; IPR003165; Piwi.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR Pfam; PF08699; ArgoL1; 1.
DR Pfam; PF02170; PAZ; 1.
DR Pfam; PF02171; Piwi; 1.
DR SMART; SM00949; PAZ; 1.
DR SMART; SM00950; Piwi; 1.
DR SUPFAM; SSF101690; SSF101690; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR PROSITE; PS50821; PAZ; 1.
DR PROSITE; PS50822; PIWI; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Developmental protein; Differentiation; Meiosis;
KW Reference proteome; RNA-binding; RNA-mediated gene silencing;
KW Spermatogenesis; Translation regulation.
FT CHAIN 1..882
FT /note="Piwi-like protein 3"
FT /id="PRO_0000234571"
FT DOMAIN 289..406
FT /note="PAZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00142"
FT DOMAIN 578..868
FT /note="Piwi"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00150"
FT REGION 1..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 186
FT /note="P -> L (in dbSNP:rs61083377)"
FT /id="VAR_061024"
FT VARIANT 375
FT /note="P -> S (in dbSNP:rs1475853)"
FT /id="VAR_034383"
FT VARIANT 412
FT /note="C -> R (in dbSNP:rs1892722)"
FT /id="VAR_034384"
FT VARIANT 418
FT /note="V -> M (in dbSNP:rs1892723)"
FT /evidence="ECO:0000269|PubMed:12906857"
FT /id="VAR_034385"
FT VARIANT 471
FT /note="V -> I (in dbSNP:rs11703684)"
FT /id="VAR_054774"
FT VARIANT 589
FT /note="R -> C (in dbSNP:rs738826)"
FT /id="VAR_059130"
SQ SEQUENCE 882 AA; 101089 MW; 5646695FE070469B CRC64;
MPGRARTRAR GRARRRESYQ QEAPGGPRAP GSATTQEPPQ LQSTPRPLQE EVPVVRPLQP
RAARGGAGGG AQSQGVKEPG PEAGLHTAPL QERRIGGVFQ DLVVNTRQDM KHVKDSKTGS
EGTVVQLLAN HFRVISRPQW VAYKYNVDYK PDIEDGNLRT ILLDQHRRKF GERHIFDGNS
LLLSRPLKER RVEWLSTTKD KNIVKITVEF SKELTPTSPD CLRYYNILFR RTFKLLDFEQ
VGRNYYTKKK AIQLYRHGTS LEIWLGYVTS VLQYENSITL CADVSHKLLR IETAYDFIKR
TSAQAQTGNI REEVTNKLIG SIVLTKYNNK TYRVDDIDWK QNPEDTFNKS DGSKITYIDY
YRQQHKEIVT VKKQPLLVSQ GRWKKGLTGT QREPILLIPQ LCHMTGLTDE ICKDYSIVKE
LAKHTRLSPR RRHHTLKEFI NTLQDNKKVR ELLQLWDLKF DTNFLSVPGR VLKNANIVQG
RRMVKANSQG DWSREIRELP LLNAMPLHSW LILYSRSSHR EAMSLKGHLQ SVTAPMGITM
KPAEMIEVDG DANSYIDTLR KYTRPTLQMG MSCLLVFKVI CILPNDDKRR YDSIKRYLCT
KCPIPSQCVV KKTLEKVQAR TIVTKIAQQM NCKMGGALWK VETDVQRTMF VGIDCFHDIV
NRQKSIAGFV ASTNAELTKW YSQCVIQKTG EELVKELEIC LKAALDVWCK NESSMPHSVI
VYRDGVGDGQ LQALLDHEAK KMSTYLKTIS PNNFTLAFIV VKKRINTRFF LKHGSNFQNP
PPGTVIDVEL TRNEWYDFFI VSQSVQDGTV TPTHYNVIYD TIGLSPDTVQ RLTYCLCHMY
YNLPGIIRVP APCHYAHKLA YLVGQSIHQE PNRSLSTRLF YL
