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SRPB_YEAST
ID   SRPB_YEAST              Reviewed;         244 AA.
AC   P36057; D6VX44;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 187.
DE   RecName: Full=Signal recognition particle receptor subunit beta;
DE            Short=SR-beta;
GN   Name=SRP102; OrderedLocusNames=YKL154W; ORFNames=YKL609;
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].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8091859; DOI=10.1002/yea.320100005;
RA   Vandenbol M., Bolle P.-A., Dion C., Portetelle D., Hilger F.;
RT   "DNA sequencing of a 36.2 kb fragment located between the FAS1 and LAP loci
RT   of chromosome XI of Saccharomyces cerevisiae.";
RL   Yeast 10:S35-S40(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8196765; DOI=10.1038/369371a0;
RA   Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA   Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA   Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA   Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA   Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA   Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA   Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA   Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA   Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA   Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA   Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA   Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA   Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA   Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA   Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA   Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA   Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA   Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA   Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA   van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA   von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA   Becker I., Mewes H.-W.;
RT   "Complete DNA sequence of yeast chromosome XI.";
RL   Nature 369:371-378(1994).
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   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   [5]
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 27-244 IN COMPLEX WITH GTP AND
RP   SRP101, AND SUBUNIT.
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 signal recognition particle (SRP) complex
CC       receptor (SR) (By similarity). Ensures, in conjunction with the SRP
CC       complex, the correct targeting of the nascent secretory proteins to the
CC       endoplasmic reticulum membrane system (By similarity). May mediate the
CC       membrane association of SR (By similarity).
CC       {ECO:0000250|UniProtKB:P47758}.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta chain.
CC       {ECO:0000269|PubMed:12654246}.
CC   -!- INTERACTION:
CC       P36057; P32916: SRP101; NbExp=5; IntAct=EBI-18091, EBI-18098;
CC       P36057; P36057: SRP102; NbExp=2; IntAct=EBI-18091, EBI-18091;
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:O13950}; Single-pass membrane protein
CC       {ECO:0000255}.
CC   -!- MISCELLANEOUS: Present with 8250 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the SRP receptor beta subunit family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA81499.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; Z26877; CAA81499.1; ALT_INIT; Genomic_DNA.
DR   EMBL; Z28154; CAA81995.1; -; Genomic_DNA.
DR   EMBL; BK006944; DAA09010.1; -; Genomic_DNA.
DR   PIR; S37984; S37984.
DR   RefSeq; NP_012768.1; NM_001179720.1.
DR   PDB; 1NRJ; X-ray; 1.70 A; B=31-244.
DR   PDB; 2GED; X-ray; 2.20 A; A/B=36-183.
DR   PDBsum; 1NRJ; -.
DR   PDBsum; 2GED; -.
DR   AlphaFoldDB; P36057; -.
DR   SMR; P36057; -.
DR   BioGRID; 33983; 426.
DR   ComplexPortal; CPX-780; Signal recognition particle receptor complex.
DR   DIP; DIP-4753N; -.
DR   IntAct; P36057; 15.
DR   MINT; P36057; -.
DR   STRING; 4932.YKL154W; -.
DR   TCDB; 3.A.5.8.1; the general secretory pathway (sec) family.
DR   iPTMnet; P36057; -.
DR   MaxQB; P36057; -.
DR   PaxDb; P36057; -.
DR   PRIDE; P36057; -.
DR   EnsemblFungi; YKL154W_mRNA; YKL154W; YKL154W.
DR   GeneID; 853702; -.
DR   KEGG; sce:YKL154W; -.
DR   SGD; S000001637; SRP102.
DR   VEuPathDB; FungiDB:YKL154W; -.
DR   eggNOG; KOG0090; Eukaryota.
DR   GeneTree; ENSGT00940000167928; -.
DR   HOGENOM; CLU_091084_1_0_1; -.
DR   InParanoid; P36057; -.
DR   OMA; NKQDVAM; -.
DR   BioCyc; YEAST:G3O-31924-MON; -.
DR   EvolutionaryTrace; P36057; -.
DR   PRO; PR:P36057; -.
DR   Proteomes; UP000002311; Chromosome XI.
DR   RNAct; P36057; protein.
DR   GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:SGD.
DR   GO; GO:0016020; C:membrane; IC:ComplexPortal.
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; ISS:SGD.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0005047; F:signal recognition particle binding; IMP:SGD.
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   CDD; cd04105; SR_beta; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR019009; SRP_receptor_beta_su.
DR   PANTHER; PTHR11485:SF34; PTHR11485:SF34; 1.
DR   Pfam; PF09439; SRPRB; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Endoplasmic reticulum; GTP-binding; Membrane;
KW   Nucleotide-binding; Receptor; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..244
FT                   /note="Signal recognition particle receptor subunit beta"
FT                   /id="PRO_0000101230"
FT   TRANSMEM        7..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         45..53
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000269|PubMed:12654246"
FT   BINDING         66..69
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000269|PubMed:12654246"
FT   BINDING         90
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000269|PubMed:12654246"
FT   BINDING         154..157
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000269|PubMed:12654246"
FT   STRAND          40..44
FT                   /evidence="ECO:0007829|PDB:1NRJ"
FT   HELIX           51..60
FT                   /evidence="ECO:0007829|PDB:1NRJ"
FT   STRAND          73..75
FT                   /evidence="ECO:0007829|PDB:1NRJ"
FT   HELIX           78..80
FT                   /evidence="ECO:0007829|PDB:1NRJ"
FT   STRAND          84..87
FT                   /evidence="ECO:0007829|PDB:1NRJ"
FT   HELIX           92..95
FT                   /evidence="ECO:0007829|PDB:1NRJ"
FT   HELIX           96..105
FT                   /evidence="ECO:0007829|PDB:1NRJ"
FT   HELIX           106..108
FT                   /evidence="ECO:0007829|PDB:1NRJ"
FT   STRAND          109..117
FT                   /evidence="ECO:0007829|PDB:1NRJ"
FT   HELIX           126..142
FT                   /evidence="ECO:0007829|PDB:1NRJ"
FT   STRAND          149..154
FT                   /evidence="ECO:0007829|PDB:1NRJ"
FT   HELIX           164..187
FT                   /evidence="ECO:0007829|PDB:1NRJ"
FT   HELIX           214..216
FT                   /evidence="ECO:0007829|PDB:1NRJ"
FT   STRAND          217..219
FT                   /evidence="ECO:0007829|PDB:1NRJ"
FT   STRAND          221..225
FT                   /evidence="ECO:0007829|PDB:1NRJ"
FT   TURN            228..231
FT                   /evidence="ECO:0007829|PDB:1NRJ"
FT   HELIX           234..243
FT                   /evidence="ECO:0007829|PDB:1NRJ"
SQ   SEQUENCE   244 AA;  26974 MW;  EA4AE9126B2A04B5 CRC64;
     MLSNTLIIAC LLVIGTTIAL IAVQKASSKT GIKQKSYQPS IIIAGPQNSG KTSLLTLLTT
     DSVRPTVVSQ EPLSAADYDG SGVTLVDFPG HVKLRYKLSD YLKTRAKFVK GLIFMVDSTV
     DPKKLTTTAE FLVDILSITE SSCENGIDIL IACNKSELFT ARPPSKIKDA LESEIQKVIE
     RRKKSLNEVE RKINEEDYAE NTLDVLQSTD GFKFANLEAS VVAFEGSINK RKISQWREWI
     DEKL
 
 
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