SPC2_YEAST
ID SPC2_YEAST Reviewed; 178 AA.
AC Q04969; D6VZB9;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Signal peptidase complex subunit 2;
DE AltName: Full=Microsomal signal peptidase subunit 2;
GN Name=SPC2; Synonyms=SPY1; OrderedLocusNames=YML055W; ORFNames=YM9958.07;
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 [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 [2]
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 [3]
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 [4]
RP IDENTIFICATION IN THE SIGNAL PEPTIDASE COMPLEX, AND FUNCTION.
RX PubMed=8910564; DOI=10.1074/jbc.271.46.29094;
RA Mullins C., Meyer H.A., Hartmann E., Green N., Fang H.;
RT "Structurally related Spc1p and Spc2p of yeast signal peptidase complex are
RT functionally distinct.";
RL J. Biol. Chem. 271:29094-29099(1996).
RN [5]
RP IDENTIFICATION IN THE SIGNAL PEPTIDASE COMPLEX.
RX PubMed=9148931; DOI=10.1074/jbc.272.20.13159;
RA Meyer H.A., Hartmann E.;
RT "The yeast SPC22/23 homolog Spc3p is essential for signal peptidase
RT activity.";
RL J. Biol. Chem. 272:13159-13164(1997).
RN [6]
RP FUNCTION, AND INTERACTION WITH SBH1 AND SEB2.
RX PubMed=10921929; DOI=10.1074/jbc.m006126200;
RA Antonin W., Meyer H.A., Hartmann E.;
RT "Interactions between Spc2p and other components of the endoplasmic
RT reticulum translocation sites of the yeast Saccharomyces cerevisiae.";
RL J. Biol. Chem. 275:34068-34072(2000).
RN [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [8]
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 [9]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
CC -!- FUNCTION: Component of the signal peptidase complex (SPC) which
CC catalyzes the cleavage of N-terminal signal sequences from nascent
CC proteins as they are translocated into the lumen of the endoplasmic
CC reticulum (PubMed:8910564, PubMed:10921929). Enhances the enzymatic
CC activity of SPC and facilitates the interactions between different
CC components of the translocation site (PubMed:8910564, PubMed:10921929).
CC {ECO:0000269|PubMed:10921929, ECO:0000269|PubMed:8910564}.
CC -!- SUBUNIT: Component of the signal peptidase complex (SPC) composed of a
CC catalytic subunit SEC11 and three accessory subunits SPC1, SPC2 and
CC SPC3 (PubMed:8910564, PubMed:9148931). The complex induces a local
CC thinning of the ER membrane which is used to measure the length of the
CC signal peptide (SP) h-region of protein substrates (By similarity).
CC This ensures the selectivity of the complex towards h-regions shorter
CC than 18-20 amino acids (By similarity). SPC associates with the
CC translocon complex (PubMed:10921929). Interacts with SBH1 and SEB2/SBH2
CC (PubMed:10921929). {ECO:0000250|UniProtKB:P67812,
CC ECO:0000269|PubMed:10921929, ECO:0000269|PubMed:8910564,
CC ECO:0000269|PubMed:9148931}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:14562095}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- MISCELLANEOUS: Present with 4890 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: Important for signal peptidase activity and cell
CC viability at high temperatures.
CC -!- SIMILARITY: Belongs to the SPCS2 family. {ECO:0000305}.
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DR EMBL; Z46729; CAA86720.1; -; Genomic_DNA.
DR EMBL; AY557966; AAS56292.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09843.1; -; Genomic_DNA.
DR PIR; S49805; S49805.
DR RefSeq; NP_013657.1; NM_001182413.1.
DR AlphaFoldDB; Q04969; -.
DR SMR; Q04969; -.
DR BioGRID; 35112; 117.
DR ComplexPortal; CPX-1835; Signal peptidase complex.
DR DIP; DIP-4540N; -.
DR IntAct; Q04969; 20.
DR MINT; Q04969; -.
DR STRING; 4932.YML055W; -.
DR MEROPS; X45.001; -.
DR MaxQB; Q04969; -.
DR PaxDb; Q04969; -.
DR PRIDE; Q04969; -.
DR TopDownProteomics; Q04969; -.
DR DNASU; 854949; -.
DR EnsemblFungi; YML055W_mRNA; YML055W; YML055W.
DR GeneID; 854949; -.
DR KEGG; sce:YML055W; -.
DR SGD; S000004519; SPC2.
DR VEuPathDB; FungiDB:YML055W; -.
DR eggNOG; ENOG502S2C7; Eukaryota.
DR GeneTree; ENSGT00440000038181; -.
DR HOGENOM; CLU_131066_0_0_1; -.
DR InParanoid; Q04969; -.
DR OMA; WIWAVEA; -.
DR BioCyc; YEAST:G3O-32651-MON; -.
DR PRO; PR:Q04969; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q04969; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IC:ComplexPortal.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005787; C:signal peptidase complex; IDA:SGD.
DR GO; GO:0120236; P:negative regulation of post-translational protein targeting to membrane, translocation; IMP:SGD.
DR GO; GO:0045047; P:protein targeting to ER; IMP:SGD.
DR GO; GO:0006465; P:signal peptide processing; IMP:SGD.
DR InterPro; IPR009582; Spc2/SPCS2.
DR PANTHER; PTHR13085; PTHR13085; 1.
DR Pfam; PF06703; SPC25; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..178
FT /note="Signal peptidase complex subunit 2"
FT /id="PRO_0000203253"
FT TOPO_DOM 1..37
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 59..67
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 89..178
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 178 AA; 20802 MW; 432742B2E1E5382C CRC64;
MSSAKPINVY SIPELNQALD EALPSVFARL NYERSYALLD AKLYIGYSIA VVAGLSFFLD
KKFERDQIVT YQKLLVGAYF VLSLLFWYFS RFIEKGTVYV GKRRGTKEEI YVKTKFEKNE
PLYLVELVQK KKGENSKKEL KAKLEVNKVF NESGYLQNDA YFKWFSEQHN VLDTKKNE
