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SIMR1_CAEEL
ID   SIMR1_CAEEL             Reviewed;         691 AA.
AC   O01477;
DT   07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Protein simr-1 {ECO:0000305};
DE   AltName: Full=siRNA-defective and mortal germline protein 1 {ECO:0000303|PubMed:32338603};
GN   Name=simr-1 {ECO:0000303|PubMed:32338603, ECO:0000312|WormBase:C06A5.6};
GN   ORFNames=C06A5.6 {ECO:0000312|WormBase:C06A5.6};
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, SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF ALA-11 AND
RP   ARG-159.
RX   PubMed=32338603; DOI=10.7554/elife.56731;
RA   Manage K.I., Rogers A.K., Wallis D.C., Uebel C.J., Anderson D.C.,
RA   Nguyen D.A.H., Arca K., Brown K.C., Cordeiro Rodrigues R.J.,
RA   de Albuquerque B.F.M., Ketting R.F., Montgomery T.A., Phillips C.M.;
RT   "A Tudor domain protein, SIMR-1, promotes siRNA production at piRNA-
RT   targeted mRNAs in C. elegans.";
RL   Elife 9:0-0(2020).
CC   -!- FUNCTION: Acts downstream of piRNA production to promote mediator
CC       complex-dependent endogenous siRNA biogenesis from piRNA-target mRNAs
CC       in the RNA interference pathway in germ cells (PubMed:32338603). Not
CC       required to identify target mRNA by the piRNA pathway
CC       (PubMed:32338603). Plays a role in both spermatogenesis and oogenesis
CC       and in maintaining fertility over multiple generations, probably by
CC       directing mutator-dependent silencing to piRNA-targeted genes
CC       (PubMed:32338603). {ECO:0000269|PubMed:32338603}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC       {ECO:0000269|PubMed:32338603}. Note=Localizes to perinuclear foci in
CC       germ cells, called SIMR foci, which are distinct from Mutator foci, P
CC       granules and Z granules (PubMed:32338603). SIMR foci are stacked, with
CC       znfx-1 localizing between simr-1 and pgl-1 (PubMed:32338603). Its
CC       localization at SIMR foci is adjacent to the mutator complex protein
CC       mut-16 (PubMed:32338603). Perinuclear localization is not dependent on
CC       mut-16 (PubMed:32338603). {ECO:0000269|PubMed:32338603}.
CC   -!- DOMAIN: Tudor domain specifically binds peptides with symmetrically
CC       dimethylated arginines (sDMA) and may facilitate protein-protein
CC       interactions (PubMed:32338603). The Tudor domain contains the conserved
CC       arginine and aspartic acid residues, which play a structural role, but
CC       lacks two of the four conserved aromatic residues, so it is unclear
CC       whether it is functional to recognize a methylated substrate
CC       (PubMed:32338603). {ECO:0000303|PubMed:32338603}.
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DR   EMBL; BX284601; CCD61216.1; -; Genomic_DNA.
DR   PIR; T25519; T25519.
DR   RefSeq; NP_491730.1; NM_059329.4.
DR   AlphaFoldDB; O01477; -.
DR   STRING; 6239.C06A5.6; -.
DR   EPD; O01477; -.
DR   PaxDb; O01477; -.
DR   PeptideAtlas; O01477; -.
DR   EnsemblMetazoa; C06A5.6.1; C06A5.6.1; WBGene00015504.
DR   EnsemblMetazoa; C06A5.6.2; C06A5.6.2; WBGene00015504.
DR   EnsemblMetazoa; C06A5.6.3; C06A5.6.3; WBGene00015504.
DR   UCSC; C06A5.6; c. elegans.
DR   WormBase; C06A5.6; CE07953; WBGene00015504; simr-1.
DR   eggNOG; ENOG502RT5V; Eukaryota.
DR   GeneTree; ENSGT00970000196511; -.
DR   HOGENOM; CLU_358340_0_0_1; -.
DR   InParanoid; O01477; -.
DR   OrthoDB; 1788096at2759; -.
DR   Proteomes; UP000001940; Chromosome I.
DR   Bgee; WBGene00015504; Expressed in germ line (C elegans) and 4 other tissues.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR   GO; GO:0090727; P:positive regulation of brood size; IMP:UniProtKB.
DR   GO; GO:1905881; P:positive regulation of oogenesis; IMP:UniProtKB.
DR   GO; GO:0030422; P:siRNA processing; IMP:UniProtKB.
DR   GO; GO:0007283; P:spermatogenesis; IMP:UniProtKB.
PE   1: Evidence at protein level;
KW   Cytoplasm; Reference proteome; RNA-mediated gene silencing.
FT   CHAIN           1..691
FT                   /note="Protein simr-1"
FT                   /id="PRO_0000450823"
FT   DOMAIN          139..204
FT                   /note="Tudor; degenerate"
FT                   /evidence="ECO:0000305|PubMed:32338603"
FT   REGION          547..573
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          588..618
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         11
FT                   /note="A->V: Inhibits piRNA-mediated gene silencing."
FT                   /evidence="ECO:0000269|PubMed:32338603"
FT   MUTAGEN         159
FT                   /note="R->C: Progressive fertility defects at 25 degrees
FT                   Celsius, with animals becoming sterile after 10 to 11
FT                   generations. Expressed in the cytoplasm of germ cells, but
FT                   does not form germline foci. Inhibits piRNA-mediated gene
FT                   silencing."
FT                   /evidence="ECO:0000269|PubMed:32338603"
SQ   SEQUENCE   691 AA;  76791 MW;  2C8A20C97C69FD49 CRC64;
     MSNEKQQWDD AYCLAEEMHD AGRPFKREEL NIADQFICSR FSTIFEYDPY KDTYGFRNQE
     LTHAIPVKSK CRHISDVDIL ELKKNTANAD IRFPSYLNIC PVYAMHPFTV LAFDLSKPVP
     MGMNASMENA APNMKSPTEA EITPGTIYIF KHRDNKCYRC VILFEDGDNN VSDADRKYMV
     AFLDTPQVVS VKLKTLFHLG KFTIESYPCA LYCCRAVGIL EIRKDFGADL NGQINEFYKD
     KVKRKSGVHA LIYKKDDRGD KLIFDCPSIL GTSMTMALEI KDVIGHRSVA ENDPTALSYD
     ELVSKQLPTV DIDDHNSSVV LDLEESVIAQ ELGSTNGADC PCNNDNIDDF MQSQRQNPLD
     NNRDNWDRIN ESRSSMQSFA INQSQAITAN PTPQPTFDES SGEVQTIPES INNLALNGRY
     LEDGRGTEEI REERSVESRQ IGNQVVSQAS CNYLEARQNS TQTANAESVC AIISESHAAL
     PTDIQVIPSQ HVLNENNHTV LPSVAPIIRN ATGHSHIFGR QIPSPAFRRE SLSSGNSIQV
     ATFAATTGPC GSNTSRPTAQ NTANSSINQD MSISNSSTNA RLITIAQDNL NDTENWPNSE
     REQSATEMES GAEATTNSAV DEFAQVSDDM KGLADSMINF LRLTANSNNQ DAFKANIFAM
     ELISTKIPNQ LTKRFFTLKI AEAKSLAEGF N
 
 
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