位置:首页 > 蛋白库 > SR543_ARATH
SR543_ARATH
ID   SR543_ARATH             Reviewed;         495 AA.
AC   P49967; Q93W49; Q9FVP9;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   20-JUN-2002, sequence version 2.
DT   03-AUG-2022, entry version 153.
DE   RecName: Full=Signal recognition particle 54 kDa protein 3;
DE            Short=SRP54;
GN   Name=SRP-54C; OrderedLocusNames=At1g48900; ORFNames=F27K7.8;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7824644; DOI=10.1104/pp.106.3.1157;
RA   Chu B., Lindstrom J.T., Belanger F.C.;
RT   "Arabidopsis thaliana expresses three divergent Srp54 genes.";
RL   Plant Physiol. 106:1157-1162(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
CC   -!- FUNCTION: Binds to the signal sequence of presecretory protein when
CC       they emerge from the ribosomes and transfers them to TRAM
CC       (translocating chain-associating membrane protein).
CC   -!- SUBUNIT: Signal recognition particle consists of a 7S RNA molecule of
CC       300 nucleotides and six protein subunits: SRP72, SRP68, SRP54, SRP19,
CC       SRP14 and SRP9.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=P49967-1; Sequence=Displayed;
CC   -!- DOMAIN: Has a two domain structure: the G-domain binds GTP; the M-
CC       domain binds the 7S RNA in presence of SRP19 and also binds the signal
CC       sequence.
CC   -!- SIMILARITY: Belongs to the GTP-binding SRP family. SRP54 subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG29734.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U12127; AAA66200.1; -; Genomic_DNA.
DR   EMBL; AC084414; AAG29734.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE32363.1; -; Genomic_DNA.
DR   EMBL; AY054273; AAL06932.1; -; mRNA.
DR   EMBL; AY052331; AAK96524.1; -; mRNA.
DR   EMBL; AF446864; AAL38597.1; -; mRNA.
DR   PIR; G96526; G96526.
DR   RefSeq; NP_564535.1; NM_103783.2. [P49967-1]
DR   AlphaFoldDB; P49967; -.
DR   SMR; P49967; -.
DR   BioGRID; 26537; 2.
DR   STRING; 3702.AT1G48900.1; -.
DR   iPTMnet; P49967; -.
DR   PaxDb; P49967; -.
DR   PRIDE; P49967; -.
DR   ProteomicsDB; 226861; -. [P49967-1]
DR   EnsemblPlants; AT1G48900.1; AT1G48900.1; AT1G48900. [P49967-1]
DR   GeneID; 841312; -.
DR   Gramene; AT1G48900.1; AT1G48900.1; AT1G48900. [P49967-1]
DR   KEGG; ath:AT1G48900; -.
DR   Araport; AT1G48900; -.
DR   TAIR; locus:2028563; AT1G48900.
DR   eggNOG; KOG0780; Eukaryota.
DR   HOGENOM; CLU_009301_6_1_1; -.
DR   InParanoid; P49967; -.
DR   PhylomeDB; P49967; -.
DR   PRO; PR:P49967; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; P49967; baseline and differential.
DR   Genevisible; P49967; AT.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005786; C:signal recognition particle, endoplasmic reticulum targeting; IBA:GO_Central.
DR   GO; GO:0008312; F:7S RNA binding; IBA:GO_Central.
DR   GO; GO:0030942; F:endoplasmic reticulum signal peptide binding; IBA:GO_Central.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0006616; P:SRP-dependent cotranslational protein targeting to membrane, translocation; IBA:GO_Central.
DR   Gene3D; 1.10.260.30; -; 1.
DR   Gene3D; 1.20.120.140; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00306; SRP54; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR036891; Signal_recog_part_SRP54_M_sf.
DR   InterPro; IPR013822; Signal_recog_particl_SRP54_hlx.
DR   InterPro; IPR004125; Signal_recog_particle_SRP54_M.
DR   InterPro; IPR036225; SRP/SRP_N.
DR   InterPro; IPR022941; SRP54.
DR   InterPro; IPR006325; SRP54_euk.
DR   InterPro; IPR000897; SRP54_GTPase_dom.
DR   InterPro; IPR042101; SRP54_N_sf.
DR   PANTHER; PTHR11564; PTHR11564; 1.
DR   Pfam; PF00448; SRP54; 1.
DR   Pfam; PF02881; SRP54_N; 1.
DR   Pfam; PF02978; SRP_SPB; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00962; SRP54; 1.
DR   SMART; SM00963; SRP54_N; 1.
DR   SUPFAM; SSF47364; SSF47364; 1.
DR   SUPFAM; SSF47446; SSF47446; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR01425; SRP54_euk; 1.
DR   PROSITE; PS00300; SRP54; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cytoplasm; GTP-binding; Nucleotide-binding;
KW   Reference proteome; Ribonucleoprotein; RNA-binding;
KW   Signal recognition particle.
FT   CHAIN           1..495
FT                   /note="Signal recognition particle 54 kDa protein 3"
FT                   /id="PRO_0000101206"
FT   REGION          1..295
FT                   /note="G-domain"
FT   REGION          296..495
FT                   /note="M-domain"
FT   BINDING         108..115
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         190..194
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         248..251
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        9
FT                   /note="R -> G (in Ref. 1; AAA66200)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        99
FT                   /note="A -> R (in Ref. 1; AAA66200)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        392
FT                   /note="N -> G (in Ref. 1; AAA66200)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   495 AA;  54782 MW;  5B03EE98CE8483BF CRC64;
     MVLAELGGRI TRAIQQMSNV TIIDEKALNE CLNEITRALL QSDVSFPLVK EMQSNIKKIV
     NLEDLAAGHN KRRIIEQAIF SELCKMLDPG KPAFAPKKAK ASVVMFVGLQ GAGKTTTCTK
     YAYYHQKKGY KPALVCADTF RAGAFDQLKQ NATKAKIPFY GSYTESDPVK IAVEGVDTFK
     KENCDLIIVD TSGRHKQEAS LFEEMRQVAE ATKPDLVIFV MDSSIGQAAF DQAQAFKQSV
     AVGAVIITKM DGHAKGGGAL SAVAATKSPV IFIGTGEHMD EFEVFDVKPF VSRLLGMGDW
     SGFVDKLQEV VPKDQQPELL EKLSQGNFTL RIMYDQFQNI LNMGPLKEVF SMLPGISAEM
     MPKGHEKESQ AKIKRYMTMM DSMTNDELDS SNPKVFNESR MMRIARGSGR QVREVMEMLE
     EYKRLAKIWS KMKGLKIPKN GDMSALSRNM NAQHMSKVLP PQMLKQIGGM GGLQSLMKQM
     GSGKDMMGMF GGGDK
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024