SPC1_YEAST
ID SPC1_YEAST Reviewed; 94 AA.
AC P46965; D6VWI6;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Signal peptidase complex subunit 1;
DE AltName: Full=Microsomal signal peptidase subunit 1;
GN Name=SPC1; OrderedLocusNames=YJR010C-A; ORFNames=YJR010BW;
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.
RC STRAIN=AB320 / ATCC 37323;
RX PubMed=8663399; DOI=10.1074/jbc.271.28.16460;
RA Fang H., Panzner S., Mullins C., Hartmann E., Green N.;
RT "The homologue of mammalian SPC12 is important for efficient signal
RT peptidase activity in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 271:16460-16465(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
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 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 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 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 [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
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:8663399). Dispensable for SPC enzymatic activity
CC (PubMed:8663399). {ECO:0000269|PubMed:8663399}.
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:9148931). The complex induces a local thinning of the ER
CC membrane which is used to measure the length of the signal peptide (SP)
CC h-region of protein substrates (By similarity). This ensures the
CC selectivity of the complex towards h-regions shorter than 18-20 amino
CC acids (By similarity). SPC associates with the translocon complex
CC (PubMed:10921929). Interacts with SBH1 and SEB2/SBH2 (PubMed:10921929).
CC {ECO:0000250|UniProtKB:P67812, ECO:0000269|PubMed:10921929,
CC ECO:0000269|PubMed:9148931}.
CC -!- INTERACTION:
CC P46965; P15367: SEC11; NbExp=4; IntAct=EBI-17823, EBI-16513;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:8663399}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- MISCELLANEOUS: Present with 5550 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SPCS1 family. {ECO:0000305}.
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DR EMBL; U26257; AAC49366.1; -; Genomic_DNA.
DR EMBL; Z49510; CAA89533.1; -; Genomic_DNA.
DR EMBL; Z49511; CAA89535.1; -; Genomic_DNA.
DR EMBL; AY557861; AAS56187.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08802.1; -; Genomic_DNA.
DR PIR; S61934; S61934.
DR RefSeq; NP_012544.1; NM_001181667.1.
DR AlphaFoldDB; P46965; -.
DR SMR; P46965; -.
DR BioGRID; 33767; 137.
DR ComplexPortal; CPX-1835; Signal peptidase complex.
DR DIP; DIP-2770N; -.
DR IntAct; P46965; 17.
DR MINT; P46965; -.
DR STRING; 4932.YJR010C-A; -.
DR MEROPS; X43.001; -.
DR iPTMnet; P46965; -.
DR MaxQB; P46965; -.
DR PaxDb; P46965; -.
DR PRIDE; P46965; -.
DR EnsemblFungi; YJR010C-A_mRNA; YJR010C-A; YJR010C-A.
DR GeneID; 853467; -.
DR KEGG; sce:YJR010C-A; -.
DR SGD; S000003770; SPC1.
DR VEuPathDB; FungiDB:YJR010C-A; -.
DR eggNOG; KOG4112; Eukaryota.
DR HOGENOM; CLU_134505_2_0_1; -.
DR InParanoid; P46965; -.
DR OMA; PIDFPSQ; -.
DR BioCyc; YEAST:G3O-31655-MON; -.
DR PRO; PR:P46965; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P46965; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IC:ComplexPortal.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0005787; C:signal peptidase complex; IDA:SGD.
DR GO; GO:0045047; P:protein targeting to ER; IGI:SGD.
DR GO; GO:0006465; P:signal peptide processing; IMP:SGD.
DR InterPro; IPR037713; Spc1.
DR InterPro; IPR009542; Spc1/SPCS1.
DR PANTHER; PTHR13202; PTHR13202; 1.
DR PANTHER; PTHR13202:SF0; PTHR13202:SF0; 1.
DR Pfam; PF06645; SPC12; 1.
PE 1: Evidence at protein level;
KW Acetylation; Endoplasmic reticulum; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..94
FT /note="Signal peptidase complex subunit 1"
FT /id="PRO_0000215162"
FT TOPO_DOM 2..28
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 29..49
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 50
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 72..94
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
SQ SEQUENCE 94 AA; 10819 MW; 814D7C7A49F49D6D CRC64;
MSEILQDVQR KLVFPIDFPS QRKTEKFQQL SLMIGALVAC ILGFAQQSLK VLLTAYGISC
VITLICVLPA YPWYNKQKLR WAQPKIEINV DQYD
