ID   SEC65_YEAST             Reviewed;         273 AA.
AC   P29478; D6W0H9;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   27-MAR-2024, entry version 172.
DE   RecName: Full=Signal recognition particle subunit SEC65;
GN   Name=SEC65; OrderedLocusNames=YML105C; ORFNames=YM8339.14C;
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].
RX   PubMed=1313948; DOI=10.1038/356534a0;
RA   Stirling C.J., Hewitt E.W.;
RT   "The S. cerevisiae SEC65 gene encodes a component of yeast signal
RT   recognition particle with homology to human SRP19.";
RL   Nature 356:534-537(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169872;
RA   Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA   Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA   Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA   Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL   Nature 387:90-93(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   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [5]
RP   CHARACTERIZATION.
RX   PubMed=1313947; DOI=10.1038/356532a0;
RA   Hann B.C., Stirling C.J., Walter P.;
RT   "SEC65 gene product is a subunit of the yeast signal recognition particle
RT   required for its integrity.";
RL   Nature 356:532-533(1992).
RN   [6]
RP   IDENTIFICATION IN THE SRP COMPLEX.
RX   PubMed=7925282; DOI=10.1002/j.1460-2075.1994.tb06759.x;
RA   Brown J.D., Hann B.C., Medzihradszky K.F., Niwa M., Burlingame A.L.,
RA   Walter P.;
RT   "Subunits of the Saccharomyces cerevisiae signal recognition particle
RT   required for its functional expression.";
RL   EMBO J. 13:4390-4400(1994).
CC   -!- FUNCTION: Signal-recognition-particle (SRP) assembly has a crucial role
CC       in targeting secretory proteins to the rough endoplasmic reticulum (ER)
CC       membrane. SRP is required for the cotranslational protein translocation
CC       for ER import and preferentially recognizes strongly hydrophobic signal
CC       sequences. It is involved in targeting the nascent chain-ribosome (RNC)
CC       complex to the ER and is proposed to participate in the arrest of
CC       nascent chain elongation during membrane targeting. SEC65 is required
CC       for SRP integrity.
CC   -!- SUBUNIT: Fungal signal recognition particle (SRP) complex consists of a
CC       7S RNA molecule (scR1) and at least six protein subunits: SRP72, SRP68,
CC       SRP54, SEC65, SRP21 and SRP14. {ECO:0000269|PubMed:7925282}.
CC   -!- INTERACTION:
CC       P29478; P38985: SRP14; NbExp=7; IntAct=EBI-16641, EBI-17977;
CC       P29478; P32342: SRP21; NbExp=5; IntAct=EBI-16641, EBI-17984;
CC       P29478; P38688: SRP72; NbExp=8; IntAct=EBI-16641, EBI-18011;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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DR   EMBL; X65783; CAA46666.1; -; Genomic_DNA.
DR   EMBL; Z49210; CAA89113.1; -; Genomic_DNA.
DR   EMBL; AY693145; AAT93164.1; -; Genomic_DNA.
DR   EMBL; BK006946; DAA09793.1; -; Genomic_DNA.
DR   PIR; S21731; S21731.
DR   RefSeq; NP_013602.1; NM_001182467.1.
DR   AlphaFoldDB; P29478; -.
DR   SMR; P29478; -.
DR   BioGRID; 35038; 396.
DR   ComplexPortal; CPX-609; Signal recognition particle.
DR   DIP; DIP-3850N; -.
DR   IntAct; P29478; 6.
DR   MINT; P29478; -.
DR   STRING; 4932.YML105C; -.
DR   iPTMnet; P29478; -.
DR   MaxQB; P29478; -.
DR   PaxDb; 4932-YML105C; -.
DR   PeptideAtlas; P29478; -.
DR   EnsemblFungi; YML105C_mRNA; YML105C; YML105C.
DR   GeneID; 854866; -.
DR   KEGG; sce:YML105C; -.
DR   AGR; SGD:S000004573; -.
DR   SGD; S000004573; SEC65.
DR   VEuPathDB; FungiDB:YML105C; -.
DR   eggNOG; KOG3198; Eukaryota.
DR   GeneTree; ENSGT00390000004950; -.
DR   HOGENOM; CLU_065433_1_1_1; -.
DR   InParanoid; P29478; -.
DR   OMA; IPKVKGF; -.
DR   OrthoDB; 1468133at2759; -.
DR   BioCyc; YEAST:G3O-32689-MONOMER; -.
DR   Reactome; R-SCE-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR   BioGRID-ORCS; 854866; 8 hits in 10 CRISPR screens.
DR   PRO; PR:P29478; -.
DR   Proteomes; UP000002311; Chromosome XIII.
DR   RNAct; P29478; Protein.
DR   GO; GO:0005786; C:signal recognition particle, endoplasmic reticulum targeting; IDA:SGD.
DR   GO; GO:0008312; F:7S RNA binding; IDA:SGD.
DR   GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; IDA:SGD.
DR   GO; GO:0006617; P:SRP-dependent cotranslational protein targeting to membrane, signal sequence recognition; IMP:SGD.
DR   Gene3D; 3.30.56.30; Signal recognition particle, SRP19-like subunit; 1.
DR   HAMAP; MF_00305; SRP19; 1.
DR   InterPro; IPR002778; Signal_recog_particle_SRP19.
DR   InterPro; IPR036521; SRP19-like_sf.
DR   InterPro; IPR022938; SRP19_arc-type.
DR   PANTHER; PTHR17453; SIGNAL RECOGNITION PARTICLE 19 KD PROTEIN; 1.
DR   PANTHER; PTHR17453:SF0; SIGNAL RECOGNITION PARTICLE 19 KDA PROTEIN; 1.
DR   Pfam; PF01922; SRP19; 1.
DR   SUPFAM; SSF69695; SRP19; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Reference proteome; Ribonucleoprotein;
KW   Signal recognition particle.
FT   CHAIN           1..273
FT                   /note="Signal recognition particle subunit SEC65"
FT                   /id="PRO_0000135212"
FT   REGION          25..71
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        40..71
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   273 AA;  31170 MW;  4F4A6CBB9225E385 CRC64;
     MPRLEEIDDF NDIDDLDMEL AELDPSLRTP IAPKITPKVV RSQDQENPAF LPGTNNNSNS
     NNNSSNEKEQ LSFINPKTGK VERSEAISKK DLEEVKRFQV LYPCYFDINR SHKEGRRVPK
     ELAVENPLAK TMADAVRELG ILCIFEGEKC HPQDFGNPGR IRVLFKENGQ LIGAATKFKG
     GKRQLMKAVG EYMKRHPTTI ESLREIPYGP DFDNIEFKKI PRVKGFKMNE IVPLHSPFLM
     GHPMTKSVYE TPKITAAEKS FKPPKNKYKV VRR
//