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Signal peptidase complex subunit SPC1 (Microsomal signal peptidase subunit 1)

 SPC1_YEAST              Reviewed;          94 AA.
P46965; D6VWI6;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 1.
18-JUL-2018, entry version 149.
RecName: Full=Signal peptidase complex subunit SPC1;
AltName: Full=Microsomal signal peptidase subunit 1;
Name=SPC1; OrderedLocusNames=YJR010C-A; ORFNames=YJR010BW;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
STRAIN=AB320 / ATCC 37323;
PubMed=8663399; DOI=10.1074/jbc.271.28.16460;
Fang H., Panzner S., Mullins C., Hartmann E., Green N.;
"The homologue of mammalian SPC12 is important for efficient signal
peptidase activity in Saccharomyces cerevisiae.";
J. Biol. Chem. 271:16460-16465(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=8641269;
Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N.,
Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H.,
Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A.,
Hennemann A., Herbert C.J., Heumann K., Hilger F., Hollenberg C.P.,
Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L.,
Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V.,
Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M.,
Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W.,
Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M.,
Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A.,
Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M.,
Zollner A., Karpfinger-Hartl L.;
"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
X.";
EMBO J. 15:2031-2049(1996).
[3]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=17322287; DOI=10.1101/gr.6037607;
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A.,
Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
Kolodner R.D., LaBaer J.;
"Approaching a complete repository of sequence-verified protein-
encoding clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[5]
IDENTIFICATION IN THE SIGNAL PEPTIDASE COMPLEX.
PubMed=9148931; DOI=10.1074/jbc.272.20.13159;
Meyer H.A., Hartmann E.;
"The yeast SPC22/23 homolog Spc3p is essential for signal peptidase
activity.";
J. Biol. Chem. 272:13159-13164(1997).
[6]
INTERACTION WITH SBH1 AND SEB2.
PubMed=10921929; DOI=10.1074/jbc.M006126200;
Antonin W., Meyer H.A., Hartmann E.;
"Interactions between Spc2p and other components of the endoplasmic
reticulum translocation sites of the yeast Saccharomyces cerevisiae.";
J. Biol. Chem. 275:34068-34072(2000).
[7]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[8]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
-!- FUNCTION: Nonessential component of the signal peptidase complex
(SPC), which catalyzes the cleavage of N-terminal signal sequences
of proteins targeted to the endoplasmic reticulum. Signal peptide
cleavage occurs during the translocation (cotranslationally or
post-translationally) through the translocon pore into the
endoplasmic reticulum. SPC3 is not required for signal peptidase
activity. {ECO:0000269|PubMed:8663399}.
-!- SUBUNIT: Component of the signal peptidase complex (SPC), which
consists of SPC1, SPC2, SPC3 and SEC11. SPC associates with the
translocon complex. SPC1 interacts with SBH1 and SEB2.
{ECO:0000269|PubMed:10921929, ECO:0000269|PubMed:9148931}.
-!- INTERACTION:
Q8N6L0:CCDC155 (xeno); NbExp=3; IntAct=EBI-17823, EBI-749265;
P04912:HTA2; NbExp=2; IntAct=EBI-17823, EBI-8076;
P02294:HTB2; NbExp=2; IntAct=EBI-17823, EBI-8094;
P25339:PUF4; NbExp=2; IntAct=EBI-17823, EBI-23703;
P32445:RIM1; NbExp=2; IntAct=EBI-17823, EBI-15206;
P05755:RPS9B; NbExp=2; IntAct=EBI-17823, EBI-16181;
P15367:SEC11; NbExp=5; IntAct=EBI-17823, EBI-16513;
Q04969:SPC2; NbExp=3; IntAct=EBI-17823, EBI-27827;
Q12133:SPC3; NbExp=2; IntAct=EBI-17823, EBI-17829;
O13528:TY1A-PR1; NbExp=2; IntAct=EBI-17823, EBI-37069;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
membrane protein.
-!- MISCELLANEOUS: Present with 5550 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the SPCS1 family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; U26257; AAC49366.1; -; Genomic_DNA.
EMBL; Z49510; CAA89533.1; -; Genomic_DNA.
EMBL; Z49511; CAA89535.1; -; Genomic_DNA.
EMBL; AY557861; AAS56187.1; -; Genomic_DNA.
EMBL; BK006943; DAA08802.1; -; Genomic_DNA.
PIR; S61934; S61934.
RefSeq; NP_012544.1; NM_001181667.1.
ProteinModelPortal; P46965; -.
BioGrid; 33767; 136.
ComplexPortal; CPX-1835; Signal peptidase complex.
DIP; DIP-2770N; -.
IntAct; P46965; 51.
MINT; P46965; -.
STRING; 4932.YJR010C-A; -.
iPTMnet; P46965; -.
MaxQB; P46965; -.
PaxDb; P46965; -.
PRIDE; P46965; -.
EnsemblFungi; YJR010C-A; YJR010C-A; YJR010C-A.
GeneID; 853467; -.
KEGG; sce:YJR010C-A; -.
EuPathDB; FungiDB:YJR010C-A; -.
SGD; S000003770; SPC1.
HOGENOM; HOG000000815; -.
InParanoid; P46965; -.
KO; K12946; -.
OMA; TAYGISC; -.
OrthoDB; EOG092C5P2Z; -.
BioCyc; YEAST:G3O-31655-MONOMER; -.
PRO; PR:P46965; -.
Proteomes; UP000002311; Chromosome X.
GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
GO; GO:0005787; C:signal peptidase complex; IDA:SGD.
GO; GO:0008233; F:peptidase activity; IEA:InterPro.
GO; GO:0045047; P:protein targeting to ER; IGI:SGD.
GO; GO:0006465; P:signal peptide processing; IMP:SGD.
InterPro; IPR037713; Spc1.
InterPro; IPR009542; SPC12.
PANTHER; PTHR13202; PTHR13202; 1.
PANTHER; PTHR13202:SF0; PTHR13202:SF0; 1.
Pfam; PF06645; SPC12; 1.
1: Evidence at protein level;
Acetylation; Complete proteome; Endoplasmic reticulum; Membrane;
Reference proteome; Transmembrane; Transmembrane helix.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22814378}.
CHAIN 2 94 Signal peptidase complex subunit SPC1.
/FTId=PRO_0000215162.
TOPO_DOM 2 28 Cytoplasmic. {ECO:0000255}.
TRANSMEM 29 49 Helical. {ECO:0000255}.
TOPO_DOM 50 50 Lumenal. {ECO:0000255}.
TRANSMEM 51 71 Helical. {ECO:0000255}.
TOPO_DOM 72 94 Cytoplasmic. {ECO:0000255}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:22814378}.
SEQUENCE 94 AA; 10819 MW; 814D7C7A49F49D6D CRC64;
MSEILQDVQR KLVFPIDFPS QRKTEKFQQL SLMIGALVAC ILGFAQQSLK VLLTAYGISC
VITLICVLPA YPWYNKQKLR WAQPKIEINV DQYD


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