ID   SPC1_ASHGO              Reviewed;          91 AA.
AC   Q74Z81;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Signal peptidase complex subunit 1;
GN   Name=SPC1; OrderedLocusNames=AGR325C;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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. Dispensable for SPC enzymatic activity.
CC       {ECO:0000250|UniProtKB:P46965}.
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 (By similarity). 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. This ensures the selectivity of the
CC       complex towards h-regions shorter than 18-20 amino acids (By
CC       similarity). SPC associates with the translocon complex (By
CC       similarity). {ECO:0000250|UniProtKB:P46965,
CC       ECO:0000250|UniProtKB:P67812}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:P46965}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the SPCS1 family. {ECO:0000305}.
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DR   EMBL; AE016820; AAS54815.1; -; Genomic_DNA.
DR   RefSeq; NP_986991.1; NM_212053.1.
DR   AlphaFoldDB; Q74Z81; -.
DR   SMR; Q74Z81; -.
DR   STRING; 33169.AAS54815; -.
DR   EnsemblFungi; AAS54815; AAS54815; AGOS_AGR325C.
DR   GeneID; 4623294; -.
DR   KEGG; ago:AGOS_AGR325C; -.
DR   eggNOG; KOG4112; Eukaryota.
DR   HOGENOM; CLU_134505_2_0_1; -.
DR   InParanoid; Q74Z81; -.
DR   OMA; PIDFPSQ; -.
DR   Proteomes; UP000000591; Chromosome VII.
DR   GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR   GO; GO:0005787; C:signal peptidase complex; IBA:GO_Central.
DR   GO; GO:0045047; P:protein targeting to ER; IBA:GO_Central.
DR   GO; GO:0006465; P:signal peptide processing; IBA:GO_Central.
DR   InterPro; IPR009542; Spc1/SPCS1.
DR   PANTHER; PTHR13202; PTHR13202; 1.
DR   Pfam; PF06645; SPC12; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..91
FT                   /note="Signal peptidase complex subunit 1"
FT                   /id="PRO_0000215161"
FT   TOPO_DOM        1..28
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        29..48
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        49..51
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        52..71
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        72..91
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   91 AA;  9877 MW;  8BF18F48553A5525 CRC64;
     MEIFNDLSRK LVFPIDYPSQ RRVAKLTDII LGSGTLVSCL LGFYAGSLSL TLYAFAAAYG
     LALLLVVPAY GKYRQQKLAW VGSAAATTKD L