SPC3_YEAST
ID SPC3_YEAST Reviewed; 184 AA.
AC Q12133; D6VY67;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Signal peptidase complex subunit 3;
DE AltName: Full=Microsomal signal peptidase subunit 3;
GN Name=SPC3; OrderedLocusNames=YLR066W; ORFNames=L2186;
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 IDENTIFICATION IN THE
RP 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(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 FUNCTION.
RX PubMed=9148930; DOI=10.1074/jbc.272.20.13152;
RA Fang H., Mullins C., Green N.;
RT "In addition to SEC11, a newly identified gene, SPC3, is essential for
RT signal peptidase activity in the yeast endoplasmic reticulum.";
RL J. Biol. Chem. 272:13152-13158(1997).
RN [6]
RP INTERACTION WITH SEC11.
RX PubMed=10206957; DOI=10.1074/jbc.274.17.11519;
RA VanValkenburgh C., Chen X., Mullins C., Fang H., Green N.;
RT "The catalytic mechanism of endoplasmic reticulum signal peptidase appears
RT to be distinct from most eubacterial signal peptidases.";
RL J. Biol. Chem. 274:11519-11525(1999).
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 IDENTIFICATION BY MASS SPECTROMETRY [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: Essential component of the signal peptidase complex (SPC)
CC which catalyzes the cleavage of N-terminal signal sequences from
CC nascent proteins as they are translocated into the lumen of the
CC endoplasmic reticulum (PubMed:9148931, PubMed:9148930). Essential for
CC the SPC catalytic activity, possibly by stabilizing and positioning the
CC active center of the complex close to the lumenal surface
CC (PubMed:9148931, PubMed:9148930). Essential for viability
CC (PubMed:9148931, PubMed:9148930). {ECO:0000269|PubMed:9148930,
CC ECO:0000269|PubMed:9148931}.
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). Interacts with SEC11 (PubMed:10206957). SPC
CC associates with the translocon complex (PubMed:9148931).
CC {ECO:0000250|UniProtKB:P67812, ECO:0000269|PubMed:10206957,
CC ECO:0000269|PubMed:9148931}.
CC -!- INTERACTION:
CC Q12133; P15367: SEC11; NbExp=3; IntAct=EBI-17829, EBI-16513;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:14562095}; Single-pass type II membrane protein
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: Present with 6840 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SPCS3 family. {ECO:0000305}.
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DR EMBL; U92975; AAB51390.1; -; Genomic_DNA.
DR EMBL; X94607; CAA64312.1; -; Genomic_DNA.
DR EMBL; Z73238; CAA97622.1; -; Genomic_DNA.
DR EMBL; AY558205; AAS56531.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09383.1; -; Genomic_DNA.
DR PIR; S61639; S61639.
DR RefSeq; NP_013167.1; NM_001181953.1.
DR AlphaFoldDB; Q12133; -.
DR SMR; Q12133; -.
DR BioGRID; 31340; 122.
DR ComplexPortal; CPX-1835; Signal peptidase complex.
DR DIP; DIP-5083N; -.
DR IntAct; Q12133; 4.
DR MINT; Q12133; -.
DR STRING; 4932.YLR066W; -.
DR MEROPS; X45.001; -.
DR MaxQB; Q12133; -.
DR PaxDb; Q12133; -.
DR PRIDE; Q12133; -.
DR EnsemblFungi; YLR066W_mRNA; YLR066W; YLR066W.
DR GeneID; 850755; -.
DR KEGG; sce:YLR066W; -.
DR SGD; S000004056; SPC3.
DR VEuPathDB; FungiDB:YLR066W; -.
DR eggNOG; KOG3372; Eukaryota.
DR GeneTree; ENSGT00940000169388; -.
DR HOGENOM; CLU_068714_2_1_1; -.
DR InParanoid; Q12133; -.
DR OMA; LHWNIQP; -.
DR BioCyc; YEAST:G3O-32219-MON; -.
DR ChiTaRS; SPC3; yeast.
DR PRO; PR:Q12133; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q12133; 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:0045047; P:protein targeting to ER; IMP:SGD.
DR GO; GO:0006465; P:signal peptide processing; IDA:SGD.
DR InterPro; IPR007653; SPC3.
DR PANTHER; PTHR12804; PTHR12804; 1.
DR Pfam; PF04573; SPC22; 1.
DR PIRSF; PIRSF016089; SPC22; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycoprotein; Membrane; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..184
FT /note="Signal peptidase complex subunit 3"
FT /id="PRO_0000218951"
FT TOPO_DOM 1..14
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 15..35
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 36..184
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 184 AA; 21349 MW; C6F30CC6C21C8C20 CRC64;
MFSFVQRFQN VSNQAFSMGI VMVVFIMASS YYQLINNNAF SVPSNIDNVK TLINVRTSRY
FGSQRGKAKE NMKIKFDLNT DLTPLFNWNT KQVFVYLTAE YNSTEKITSE VTFWDKIIKS
KDDAVIDVND LRSKYSIWDI EDGKFEGKDL VFKLHWNVQP WVGLLTYGET VGNYTLTVEN
KNKV
