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SRP68_CAEEL
ID   SRP68_CAEEL             Reviewed;         622 AA.
AC   Q20822;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 2.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=Signal recognition particle subunit SRP68 {ECO:0000305};
DE            Short=SRP68;
DE   AltName: Full=Probable signal recognition particle 68 kDa protein;
GN   Name=srpa-68 {ECO:0000312|WormBase:F55C5.8};
GN   ORFNames=F55C5.8 {ECO:0000312|WormBase:F55C5.8};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
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).
CC   -!- FUNCTION: Component of the signal recognition particle (SRP) complex, a
CC       ribonucleoprotein complex that mediates the cotranslational targeting
CC       of secretory and membrane proteins to the endoplasmic reticulum (ER)
CC       (By similarity). The SRP complex interacts with the signal sequence in
CC       nascent secretory and membrane proteins and directs them to the
CC       membrane of the ER (By similarity). The SRP complex targets the
CC       ribosome-nascent chain complex to the SRP receptor (SR), which is
CC       anchored in the ER, where SR compaction and GTPase rearrangement drive
CC       cotranslational protein translocation into the ER (By similarity).
CC       Binds the signal recognition particle RNA (7SL RNA), srpa-72 binds to
CC       this complex subsequently (By similarity). The SRP complex possibly
CC       participates in the elongation arrest function (By similarity).
CC       {ECO:0000250|UniProtKB:P38687, ECO:0000250|UniProtKB:Q9UHB9}.
CC   -!- SUBUNIT: Heterodimer with srpa-72 (By similarity). Srpa-68/srpa-72
CC       heterodimer formation is stabilized by the presence of 7SL RNA (By
CC       similarity). Component of a signal recognition particle (SRP) complex
CC       that consists of a 7SL RNA molecule of 300 nucleotides and six protein
CC       subunits: srpa-72, srpa-68, SRP54, F37F2.2/SRP19, F25G6.8/SRP14 and
CC       ZK512.4/SRP9 (By similarity). Within the SRP complex, interacts (via C-
CC       terminus) with srpa-72 (via N-terminus) (By similarity).
CC       {ECO:0000250|UniProtKB:Q00004, ECO:0000250|UniProtKB:Q9UHB9}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UHB9}.
CC       Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9UHB9}. Endoplasmic
CC       reticulum {ECO:0000250|UniProtKB:Q9UHB9}.
CC   -!- DOMAIN: The N-terminus is required for RNA-binding.
CC       {ECO:0000250|UniProtKB:Q9UHB9}.
CC   -!- SIMILARITY: Belongs to the SRP68 family. {ECO:0000305}.
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DR   EMBL; Z78198; CAB01573.1; -; Genomic_DNA.
DR   PIR; T22716; T22716.
DR   RefSeq; NP_506083.1; NM_073682.4.
DR   AlphaFoldDB; Q20822; -.
DR   SMR; Q20822; -.
DR   BioGRID; 44709; 5.
DR   STRING; 6239.F55C5.8; -.
DR   EPD; Q20822; -.
DR   PaxDb; Q20822; -.
DR   PeptideAtlas; Q20822; -.
DR   EnsemblMetazoa; F55C5.8.1; F55C5.8.1; WBGene00010097.
DR   GeneID; 179686; -.
DR   KEGG; cel:CELE_F55C5.8; -.
DR   UCSC; F55C5.8; c. elegans.
DR   CTD; 179686; -.
DR   WormBase; F55C5.8; CE20875; WBGene00010097; srpa-68.
DR   eggNOG; KOG2460; Eukaryota.
DR   GeneTree; ENSGT00390000011856; -.
DR   HOGENOM; CLU_018649_0_1_1; -.
DR   InParanoid; Q20822; -.
DR   OMA; DERFIHI; -.
DR   OrthoDB; 1019762at2759; -.
DR   PhylomeDB; Q20822; -.
DR   Reactome; R-CEL-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR   PRO; PR:Q20822; -.
DR   Proteomes; UP000001940; Chromosome V.
DR   Bgee; WBGene00010097; Expressed in adult organism and 4 other tissues.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005786; C:signal recognition particle, endoplasmic reticulum targeting; IBA:GO_Central.
DR   GO; GO:0008312; F:7S RNA binding; IEA:InterPro.
DR   GO; GO:0030942; F:endoplasmic reticulum signal peptide binding; IEA:InterPro.
DR   GO; GO:0005047; F:signal recognition particle binding; IBA:GO_Central.
DR   GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; IEA:InterPro.
DR   CDD; cd15481; SRP68-RBD; 1.
DR   Gene3D; 1.10.3450.40; -; 1.
DR   InterPro; IPR026258; SRP68.
DR   InterPro; IPR034652; SRP68-RBD.
DR   InterPro; IPR038253; SRP68_N_sf.
DR   PANTHER; PTHR12860; PTHR12860; 1.
DR   Pfam; PF16969; SRP68; 1.
DR   PIRSF; PIRSF038995; SRP68; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Endoplasmic reticulum; Nucleus; Reference proteome;
KW   Ribonucleoprotein; RNA-binding; Signal recognition particle.
FT   CHAIN           1..622
FT                   /note="Signal recognition particle subunit SRP68"
FT                   /id="PRO_0000135229"
FT   REGION          576..622
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        589..606
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   622 AA;  70574 MW;  A7B8808E46169636 CRC64;
     MTNDVEMKSE TEELPPFPTV HILQVVKDAQ QQHGLRHGDY ARYRKYCAAK LERMRKALKF
     TNSHNCQKKR KAKFVKKWLS VESVQNVQFL NFGIFESERR YAEAMIDKIT LEDNPEKSRK
     KFSMINSLRK AVLHATNLEK IVQESERFDA PTKLEAQAYA AWMRGMCSFE SRNWQKASES
     LKLAKTVYEK LAEATNNTTL SSIFKGRCRE IQPQLRLCEF NIAESPGAVG TMTELMELRM
     QMGEGGDSSV DKLISEMRAS ATSAEVVTIE WGGAKSTVDD EKAKQVVQEW KQTEVELAQC
     QTPKEKMALF EKATADTRDA IDRISDIIRR KSSENADTTV LQSIKAYLEF LKMNGTASRY
     LAIIDNTKSE KKSKPQDLLR LYDSVIEIYK EVAEIPGADH DKNLIQAFEV KVEYYRAFRC
     FYMASSYSAL HKYSEAAALF DRTVSRVQDA EGKLKKLKSS SFITNETQSS LNELRSEVES
     AKVTVRAARL ASAAGDVKTD SELAKIIDKR PLLETVNEWR QWDVRNSLKD KKTIPVASLP
     PAFIPMPNKP IFFDLANFHL TMPNVDDRLE KLQKDRDATP KKAAKGSSAA AASSKTSNQE
     EEEQQGLTGM LSGWKKSFWG NK
 
 
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