SRPR_YEAST
ID SRPR_YEAST Reviewed; 621 AA.
AC P32916; D6VSS1; Q05553;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=Signal recognition particle receptor subunit alpha homolog;
DE Short=SR-alpha;
DE AltName: Full=Docking protein alpha;
DE Short=DP-alpha;
GN Name=SRP101; OrderedLocusNames=YDR292C; ORFNames=D9819.3;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=1327299; DOI=10.1091/mbc.3.8.895;
RA Ogg S.C., Poritz M.A., Walter P.;
RT "Signal recognition particle receptor is important for cell growth and
RT protein secretion in Saccharomyces cerevisiae.";
RL Mol. Biol. Cell 3:895-911(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP INTERACTION WITH SRP102.
RX PubMed=9679135; DOI=10.1083/jcb.142.2.341;
RA Ogg S.C., Barz W.P., Walter P.;
RT "A functional GTPase domain, but not its transmembrane domain, is required
RT for function of the SRP receptor beta-subunit.";
RL J. Cell Biol. 142:341-354(1998).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-523, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-239 AND SER-523, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1-158 IN COMPLEX WITH SRP102 AND
RP GTP.
RX PubMed=12654246; DOI=10.1016/s0092-8674(03)00161-2;
RA Schwartz T., Blobel G.;
RT "Structural basis for the function of the beta subunit of the eukaryotic
RT signal recognition particle receptor.";
RL Cell 112:793-803(2003).
CC -!- FUNCTION: Component of the SRP (signal recognition particle) receptor
CC (SR). Ensures, in conjunction with the signal recognition particle, the
CC correct targeting of the nascent secretory proteins to the endoplasmic
CC reticulum membrane system. GTP hydrolysis may enhance the fidelity of
CC and provide unidirectionality to the targeting reaction. It is
CC important but not essential for cell growth. May be directly involved
CC in mitochondrial protein import. {ECO:0000269|PubMed:1327299}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta chain.
CC {ECO:0000269|PubMed:12654246}.
CC -!- INTERACTION:
CC P32916; P36057: SRP102; NbExp=5; IntAct=EBI-18098, EBI-18091;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:1327299}; Peripheral membrane protein
CC {ECO:0000269|PubMed:1327299}; Cytoplasmic side
CC {ECO:0000269|PubMed:1327299}. Note=Thought to be anchored in the
CC membrane through an interaction with SRP102/SR-beta, which contains a
CC bona fide transmembrane domain. {ECO:0000269|PubMed:1327299}.
CC -!- DOMAIN: The SRX domain is sufficient for interaction with GTP-bound
CC SRP102/SR-beta.
CC -!- DOMAIN: The NG domain, also named G domain, is a special guanosine
CC triphosphatase (GTPase) domain, which forms a guanosine 5'-triphosphate
CC (GTP)-dependent complex with a homologous NG domain in the signal
CC recognition particle (SRP) complex subunit SRP54 (By similarity). The
CC two NG domains undergo cooperative rearrangements upon their assembly,
CC which culminate in the reciprocal activation of the GTPase activity of
CC one another (By similarity). GTPase induced rearrangement of SR drives
CC SRP-mediated cotranslational protein translocation into the ER (By
CC similarity). {ECO:0000250|UniProtKB:P08240}.
CC -!- MISCELLANEOUS: Present with 2000 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the GTP-binding SRP family. {ECO:0000305}.
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DR EMBL; M77274; AAA35093.1; -; Genomic_DNA.
DR EMBL; U51031; AAB64468.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12131.1; -; Genomic_DNA.
DR PIR; S70121; S70121.
DR RefSeq; NP_010578.3; NM_001180600.3.
DR PDB; 1NRJ; X-ray; 1.70 A; A=1-158.
DR PDBsum; 1NRJ; -.
DR AlphaFoldDB; P32916; -.
DR SMR; P32916; -.
DR BioGRID; 32344; 338.
DR ComplexPortal; CPX-780; Signal recognition particle receptor complex.
DR DIP; DIP-1672N; -.
DR IntAct; P32916; 3.
DR MINT; P32916; -.
DR STRING; 4932.YDR292C; -.
DR TCDB; 3.A.5.8.1; the general secretory pathway (sec) family.
DR iPTMnet; P32916; -.
DR MaxQB; P32916; -.
DR PaxDb; P32916; -.
DR PRIDE; P32916; -.
DR EnsemblFungi; YDR292C_mRNA; YDR292C; YDR292C.
DR GeneID; 851886; -.
DR KEGG; sce:YDR292C; -.
DR SGD; S000002700; SRP101.
DR VEuPathDB; FungiDB:YDR292C; -.
DR eggNOG; KOG0781; Eukaryota.
DR GeneTree; ENSGT00550000074936; -.
DR HOGENOM; CLU_009301_8_1_1; -.
DR InParanoid; P32916; -.
DR OMA; RRHNDAT; -.
DR BioCyc; YEAST:G3O-29855-MON; -.
DR EvolutionaryTrace; P32916; -.
DR PRO; PR:P32916; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P32916; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:SGD.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005785; C:signal recognition particle receptor complex; IPI:SGD.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0005047; F:signal recognition particle binding; IMP:SGD.
DR GO; GO:0006605; P:protein targeting; IBA:GO_Central.
DR GO; GO:0045047; P:protein targeting to ER; IMP:SGD.
DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; IC:SGD.
DR GO; GO:0006617; P:SRP-dependent cotranslational protein targeting to membrane, signal sequence recognition; IC:ComplexPortal.
DR Gene3D; 1.20.120.140; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011012; Longin-like_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR013822; Signal_recog_particl_SRP54_hlx.
DR InterPro; IPR036225; SRP/SRP_N.
DR InterPro; IPR000897; SRP54_GTPase_dom.
DR InterPro; IPR042101; SRP54_N_sf.
DR InterPro; IPR015284; SRX_dom.
DR Pfam; PF00448; SRP54; 2.
DR Pfam; PF02881; SRP54_N; 1.
DR Pfam; PF09201; SRX; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00962; SRP54; 1.
DR SMART; SM00963; SRP54_N; 1.
DR SUPFAM; SSF47364; SSF47364; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF64356; SSF64356; 1.
DR PROSITE; PS00300; SRP54; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Endoplasmic reticulum; GTP-binding; Membrane;
KW Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome.
FT CHAIN 1..621
FT /note="Signal recognition particle receptor subunit alpha
FT homolog"
FT /id="PRO_0000101216"
FT REGION 1..158
FT /note="SRX"
FT REGION 167..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 398..620
FT /note="NG domain"
FT /evidence="ECO:0000250|UniProtKB:P08240"
FT COMPBIAS 169..184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 404..411
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 510..514
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 572..575
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 239
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 523
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT CONFLICT 499
FT /note="S -> A (in Ref. 1; AAA35093)"
FT /evidence="ECO:0000305"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:1NRJ"
FT STRAND 13..19
FT /evidence="ECO:0007829|PDB:1NRJ"
FT HELIX 27..39
FT /evidence="ECO:0007829|PDB:1NRJ"
FT HELIX 44..46
FT /evidence="ECO:0007829|PDB:1NRJ"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:1NRJ"
FT STRAND 58..62
FT /evidence="ECO:0007829|PDB:1NRJ"
FT STRAND 74..80
FT /evidence="ECO:0007829|PDB:1NRJ"
FT TURN 81..84
FT /evidence="ECO:0007829|PDB:1NRJ"
FT STRAND 85..93
FT /evidence="ECO:0007829|PDB:1NRJ"
FT HELIX 96..115
FT /evidence="ECO:0007829|PDB:1NRJ"
FT HELIX 118..125
FT /evidence="ECO:0007829|PDB:1NRJ"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:1NRJ"
FT TURN 140..144
FT /evidence="ECO:0007829|PDB:1NRJ"
FT HELIX 145..152
FT /evidence="ECO:0007829|PDB:1NRJ"
SQ SEQUENCE 621 AA; 69278 MW; 032400E5B3310C91 CRC64;
MFDQLAVFTP QGQVLYQYNC LGKKFSEIQI NSFISQLITS PVTRKESVAN ANTDGFDFNL
LTINSEHKNS PSFNALFYLN KQPELYFVVT FAEQTLELNQ ETQQTLALVL KLWNSLHLSE
SILKNRQGQN EKNKHNYVDI LQGIEDDLKK FEQYFRIKYE ESIKQDHINP DNFTKNGSVP
QSHNKNTKKK LRDTKGKKQS TGNVGSGRKW GRDGGMLDEM NHEDAAKLDF SSSNSHNSSQ
VALDSTINKD SFGDRTEGGD FLIKEIDDLL SSHKDEITSG NEAKNSGYVS TAFGFLQKHV
LGNKTINESD LKSVLEKLTQ QLITKNVAPE AADYLTQQVS HDLVGSKTAN WTSVENTARE
SLTKALTQIL TPGVSVDLLR EIQSKRSKKD EEGKCDPYVF SIVGVNGVGK STNLSKLAFW
LLQNNFKVLI VACDTFRSGA VEQLRVHVEN LAQLMDDSHV RGSKNKRGKT GNDYVELFEA
GYGGSDLVTK IAKQAIKYSR DQNFDIVLMD TAGRRHNDPT LMSPLKSFAD QAKPDKIIMV
GEALVGTDSV QQAKNFNDAF GKGRNLDFFI ISKCDTVGEM LGTMVNMVYA TGIPILFVGV
GQTYTDLRTL SVKWAVNTLM S
