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Database: UniProt
Entry: Q4KLV6
LinkDB: Q4KLV6
Original site: Q4KLV6 
ID   AGO4_XENLA              Reviewed;         884 AA.
AC   Q4KLV6;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   31-JUL-2019, entry version 61.
DE   RecName: Full=Protein argonaute-4 {ECO:0000255|HAMAP-Rule:MF_03033};
DE            Short=Argonaute4 {ECO:0000255|HAMAP-Rule:MF_03033};
DE   AltName: Full=Argonaute RISC catalytic component 4;
DE   AltName: Full=Eukaryotic translation initiation factor 2C 4 {ECO:0000255|HAMAP-Rule:MF_03033};
DE            Short=eIF-2C 4 {ECO:0000255|HAMAP-Rule:MF_03033};
DE            Short=eIF2C 4 {ECO:0000255|HAMAP-Rule:MF_03033};
GN   Name=ago4; Synonyms=eif2c4;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus;
OC   Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Required for RNA-mediated gene silencing (RNAi). Binds
CC       to short RNAs such as microRNAs (miRNAs) and represses the
CC       translation of mRNAs which are complementary to them. Lacks
CC       endonuclease activity and does not appear to cleave target mRNAs.
CC       {ECO:0000255|HAMAP-Rule:MF_03033}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000255|HAMAP-
CC       Rule:MF_03033}.
CC   -!- SIMILARITY: Belongs to the argonaute family. Ago subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_03033}.
DR   EMBL; BC098982; AAH98982.1; -; mRNA.
DR   RefSeq; NP_001089574.1; NM_001096105.1.
DR   SMR; Q4KLV6; -.
DR   IntAct; Q4KLV6; 1.
DR   PRIDE; Q4KLV6; -.
DR   GeneID; 734630; -.
DR   KEGG; xla:734630; -.
DR   CTD; 734630; -.
DR   Xenbase; XB-GENE-1006885; ago4.
DR   KO; K11593; -.
DR   OrthoDB; 159407at2759; -.
DR   GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
DR   GO; GO:0016442; C:RISC complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0035198; F:miRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0035278; P:miRNA mediated inhibition of translation; ISS:UniProtKB.
DR   GO; GO:0006402; P:mRNA catabolic process; ISS:UniProtKB.
DR   Gene3D; 3.30.420.10; -; 1.
DR   HAMAP; MF_03033; AGO4; 1.
DR   InterPro; IPR028604; AGO4.
DR   InterPro; IPR014811; ArgoL1.
DR   InterPro; IPR032472; ArgoL2.
DR   InterPro; IPR032473; Argonaute_Mid_dom.
DR   InterPro; IPR032474; Argonaute_N.
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; PF16488; ArgoL2; 1.
DR   Pfam; PF16487; ArgoMid; 1.
DR   Pfam; PF16486; ArgoN; 1.
DR   Pfam; PF02170; PAZ; 1.
DR   Pfam; PF02171; Piwi; 1.
DR   SMART; SM01163; DUF1785; 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; Ribonucleoprotein; RNA-binding;
KW   RNA-mediated gene silencing; Translation regulation.
FT   CHAIN         1    884       Protein argonaute-4.
FT                                /FTId=PRO_0000371226.
FT   DOMAIN      248    361       PAZ. {ECO:0000255|HAMAP-Rule:MF_03033}.
FT   DOMAIN      532    843       Piwi. {ECO:0000255|HAMAP-Rule:MF_03033}.
SQ   SEQUENCE   884 AA;  99538 MW;  6416DEB78E4DB2A6 CRC64;
     MGRKTLCESE TVCRDVTING SAGCLQNVGP PPTNLFQPPR RPGLGTLGKP IRLLANHFQV
     QIPKIDVYHY DVDIKPEKRP RRVNREVVDT MVRHFKMPIF GDNQPGYDGK RNMYTAHPLP
     IGRDRVDLEV TLPGEGKDQT FKVTIQWVSV VSLQLLLEAL SGHLSEVPDD SVQALDVITR
     HLPSMRYTPV GRSFFSPPEG YYHPLGGGRE VWFGFHQSVR PAMWNMMLNI DVSATAFYRA
     QPVIEFMCEV LDVQNINEQT KPLTDSQRVK FTKEIRGLKV EVTHCGQMKR KYRVCNVTRR
     PASHQTFPLQ LENGQAMECT VAQYFKQKYS LQLKYPHLPC LQVGQEQKHT YLPLEVCNIV
     AGQRCIKKLT DNQTSTMIKA TARSAPDRQE EISRLVKSNS MVGGPDPYLK EFGIVVHNEM
     TELTGRVLPA PMLQYGGRNK TVATPNQGVW DMRGKQFYAG IEIKVWAVAC FAPQKQCRED
     LLKSFTDQLR KISKDAGMPI QGQPCFCKYA QGADSVEPMF KHLKLTYVGL QLIVVILPGK
     TPVYAEVKRV GDTLLGMATQ CVQVKNVVKT SPQTLSNLCL KINAKLGGIN NVLVPHQRPS
     VFQQPVIFLG ADVTHPPAGD GKKPSIAAVV GSMDGHPSRY CATVRVQTSR QETTQELLYS
     QEVIQDLCNM VRELLIQFYK STRFKPTRII YYRGGVSEGQ MKQVAWPELM AIRKACISLE
     EDYRPGITYI VVQKRHHTRL FCSDKTERVG KSGNVPAGTT VDSTITHPSE FDFYLCSHAG
     IQGTSRPSHY QVLWDDNCFT ADELQLLTYQ LCHTYVRCTR SVSIPAPAYY ARLVAFRARY
     HLVDKDHDSA EGSHVSGQSN GRDPQALAKA VQIHHDTQHS MYFA
//
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