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WAGO1_CAEEL
ID   WAGO1_CAEEL             Reviewed;         945 AA.
AC   Q21770;
DT   19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Argonaute protein wago-1 {ECO:0000305};
DE   AltName: Full=Worm-specific argonaute protein 1 {ECO:0000312|WormBase:R06C7.1};
GN   Name=wago-1 {ECO:0000312|WormBase:R06C7.1};
GN   ORFNames=R06C7.1 {ECO:0000312|WormBase:R06C7.1};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239 {ECO:0000312|EMBL:CAA95839.1};
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] {ECO:0000305}
RP   TISSUE SPECIFICITY.
RX   PubMed=11030340; DOI=10.1016/s1097-2765(00)00059-9;
RA   Reinke V., Smith H.E., Nance J., Wang J., Van Doren C., Begley R.,
RA   Jones S.J.M., Davis E.B., Scherer S., Ward S., Kim S.K.;
RT   "A global profile of germline gene expression in C. elegans.";
RL   Mol. Cell 6:605-616(2000).
RN   [3]
RP   GENE FAMILY.
RX   PubMed=17110334; DOI=10.1016/j.cell.2006.09.033;
RA   Yigit E., Batista P.J., Bei Y., Pang K.M., Chen C.C., Tolia N.H.,
RA   Joshua-Tor L., Mitani S., Simard M.J., Mello C.C.;
RT   "Analysis of the C. elegans Argonaute family reveals that distinct
RT   Argonautes act sequentially during RNAi.";
RL   Cell 127:747-757(2006).
RN   [4]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=19800275; DOI=10.1016/j.molcel.2009.09.020;
RA   Gu W., Shirayama M., Conte D. Jr., Vasale J., Batista P.J., Claycomb J.M.,
RA   Moresco J.J., Youngman E.M., Keys J., Stoltz M.J., Chen C.C., Chaves D.A.,
RA   Duan S., Kasschau K.D., Fahlgren N., Yates J.R., Mitani S.,
RA   Carrington J.C., Mello C.C.;
RT   "Distinct argonaute-mediated 22G-RNA pathways direct genome surveillance in
RT   the C. elegans germline.";
RL   Mol. Cell 36:231-244(2009).
RN   [5]
RP   INTERACTION WITH RDE-12, AND SUBCELLULAR LOCATION.
RX   PubMed=24684931; DOI=10.1016/j.cub.2014.03.008;
RA   Shirayama M., Stanney W., Gu W., Seth M., Mello C.C.;
RT   "The vasa homolog rde-12 engages target mRNA and multiple argonaute
RT   proteins to promote RNAi in C. elegans.";
RL   Curr. Biol. 24:845-851(2014).
RN   [6]
RP   INTERACTION WITH ZNFX-1.
RX   PubMed=29775580; DOI=10.1016/j.molcel.2018.04.009;
RA   Ishidate T., Ozturk A.R., Durning D.J., Sharma R., Shen E.Z., Chen H.,
RA   Seth M., Shirayama M., Mello C.C.;
RT   "ZNFX-1 Functions within Perinuclear Nuage to Balance Epigenetic Signals.";
RL   Mol. Cell 70:639-649(2018).
CC   -!- FUNCTION: Argonaute protein which is involved in the endogenous small
CC       interfering RNA (endo-siRNA) pathway. Interacts with secondary 22G-
CC       RNAs, which are RNA-dependent RNA polymerase-derived endo-siRNAs,
CC       typically 22 nucleotides in length with a 5'guanosine residue. In the
CC       germline, functions in a genome surveillance system to silence
CC       transposons and aberrant transcripts. {ECO:0000269|PubMed:19800275}.
CC   -!- SUBUNIT: Interacts with rde-12 (PubMed:24684931). Interacts with znfx-1
CC       (PubMed:29775580). {ECO:0000269|PubMed:24684931,
CC       ECO:0000269|PubMed:29775580}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic granule {ECO:0000269|PubMed:19800275,
CC       ECO:0000269|PubMed:24684931}.
CC   -!- TISSUE SPECIFICITY: Enriched in sperm and oocytes.
CC       {ECO:0000269|PubMed:11030340}.
CC   -!- MISCELLANEOUS: Members of the WAGO (worm-specific argonaute) subfamily
CC       lack conserved metal-binding residues found in other argonaute proteins
CC       and probably do not cleave target mRNAs directly.
CC       {ECO:0000303|PubMed:17110334}.
CC   -!- SIMILARITY: Belongs to the Argonaute family. WAGO subfamily.
CC       {ECO:0000305}.
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DR   EMBL; BX284601; CAA95839.1; -; Genomic_DNA.
DR   PIR; T23965; T23965.
DR   RefSeq; NP_492045.1; NM_059644.5.
DR   AlphaFoldDB; Q21770; -.
DR   SMR; Q21770; -.
DR   BioGRID; 37906; 25.
DR   STRING; 6239.R06C7.1; -.
DR   EPD; Q21770; -.
DR   PaxDb; Q21770; -.
DR   PeptideAtlas; Q21770; -.
DR   EnsemblMetazoa; R06C7.1.1; R06C7.1.1; WBGene00011061.
DR   GeneID; 172463; -.
DR   KEGG; cel:CELE_R06C7.1; -.
DR   UCSC; R06C7.1; c. elegans.
DR   CTD; 172463; -.
DR   WormBase; R06C7.1; CE06244; WBGene00011061; wago-1.
DR   eggNOG; KOG1041; Eukaryota.
DR   GeneTree; ENSGT00940000173649; -.
DR   HOGENOM; CLU_310185_0_0_1; -.
DR   InParanoid; Q21770; -.
DR   OMA; KCCNIFF; -.
DR   OrthoDB; 220258at2759; -.
DR   PhylomeDB; Q21770; -.
DR   Reactome; R-CEL-203927; MicroRNA (miRNA) biogenesis.
DR   Reactome; R-CEL-426486; Small interfering RNA (siRNA) biogenesis.
DR   Reactome; R-CEL-5578749; Transcriptional regulation by small RNAs.
DR   PRO; PR:Q21770; -.
DR   Proteomes; UP000001940; Chromosome I.
DR   Bgee; WBGene00011061; Expressed in germ line (C elegans) and 4 other tissues.
DR   GO; GO:0043186; C:P granule; IDA:WormBase.
DR   GO; GO:0017151; F:DEAD/H-box RNA helicase binding; IPI:WormBase.
DR   GO; GO:0004521; F:endoribonuclease activity; IBA:GO_Central.
DR   GO; GO:0035198; F:miRNA binding; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0003727; F:single-stranded RNA binding; IBA:GO_Central.
DR   GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.420.10; -; 1.
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; 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   1: Evidence at protein level;
KW   Developmental protein; Reference proteome; RNA-mediated gene silencing.
FT   CHAIN           1..945
FT                   /note="Argonaute protein wago-1"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000087436"
FT   DOMAIN          321..432
FT                   /note="PAZ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00142,
FT                   ECO:0000305"
FT   DOMAIN          636..899
FT                   /note="Piwi"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00150"
FT   REGION          1..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..29
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   945 AA;  105437 MW;  6751A5184FD54BF7 CRC64;
     MSPHPPQPHP PMPPMPPVTA PPGAMTPMPP VPADAQKLHQ STGNDACIKR LQQLNVEDGA
     KMYMKPTEPG KMGRPVDIQT NVFGIEVTKE TTVHRFMVHA KADLTSTKEV TFTKKGKEDF
     VVQDRRDKCC NIFFLAVEKN PEFFKMKDGN QIVYDGQSTL YTTVNLFSEL DANGTKSKVF
     QINGADTGND DLKTLPCISL EIYAPRDNSI TLSSENLGKR TADQNIEVNN REYTQFLELA
     LNQHCVRETN RFGCFEHGKV YFLNATEEGF DQRDCVDVGD GKQLYPGLKK TIQFIEGPYG
     RGQNNPSLVI DGMKAAFHKE QTVIQKLFDI TGQDPSNGLN NMTREKAAAV IKGLDCYSTY
     TNRKRHLRIE GIFHESATKT RFELPDGKTC SIAEYYADKY KISLQYPNAN LVVCKDRGNN
     NYFPAELMTV SRNQRVTIPQ QTGNQSQKTT KECAVLPDVR QRMIITGKNA VNITLENELL
     VALGIKVYSE PLMVQARELD GKELVYQRSV MSDMGKWRAP PGWFVKPATV PDLWAAYAVG
     NPGCRFSIGD VNQLVGMFID SCKKKGMVIK PPCETGLYST EKIMTQLEKV AASKCKYVLM
     ITDDAIVHLH KQYKALEQRT MMIVQDMKIS KANAVVKDGK RLTLENIINK TNVKLGGLNY
     TVSDAKKSMT DEQLIIGVGV SAPPAGTKYM MDNKGHLNPQ IIGFASNAVA NHEFVGDFVL
     APSGQDTMAS IEDVLQNSID LFEKNRKALP KRIIIYRSGA SEGSHASILA YEIPLARAII
     HGYSKEIKLI FIVVTKEHSY RFFRDQLRSG GKATEMNIPP GIVLDNAVTN PACKQFFLNG
     HTTLQGTAKT PLYTVLADDC KAPMDRLEEL TFTLCHHHQI VSLSTSIPTP LYVANEYAKR
     GRDLWGELTT KGPIEAKESQ GERLKELTKE IGYKQTDLNQ KRVNA
 
 
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