ID   SPC3_YARLI              Reviewed;         185 AA.
AC   Q6C4R5;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Signal peptidase complex subunit 3;
DE   AltName: Full=Microsomal signal peptidase subunit 3;
GN   Name=SPC3; OrderedLocusNames=YALI0E24321g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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. Essential for the SPC catalytic activity,
CC       possibly by stabilizing and positioning the active center of the
CC       complex close to the lumenal surface. Essential for viability.
CC       {ECO:0000250|UniProtKB:Q12133}.
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:P67812,
CC       ECO:0000250|UniProtKB:Q12133}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q12133}; Single-pass type II membrane protein
CC       {ECO:0000250|UniProtKB:Q12133}.
CC   -!- SIMILARITY: Belongs to the SPCS3 family. {ECO:0000305}.
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DR   EMBL; CR382131; CAG79946.1; -; Genomic_DNA.
DR   RefSeq; XP_504347.1; XM_504347.1.
DR   AlphaFoldDB; Q6C4R5; -.
DR   SMR; Q6C4R5; -.
DR   STRING; 4952.CAG79946; -.
DR   EnsemblFungi; CAG79946; CAG79946; YALI0_E24321g.
DR   GeneID; 2912544; -.
DR   KEGG; yli:YALI0E24321g; -.
DR   VEuPathDB; FungiDB:YALI0_E24321g; -.
DR   HOGENOM; CLU_068714_2_1_1; -.
DR   InParanoid; Q6C4R5; -.
DR   OMA; LHWNIQP; -.
DR   Proteomes; UP000001300; Chromosome E.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; IPR007653; SPC3.
DR   PANTHER; PTHR12804; PTHR12804; 1.
DR   Pfam; PF04573; SPC22; 1.
DR   PIRSF; PIRSF016089; SPC22; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; Glycoprotein; Membrane; Reference proteome;
KW   Signal-anchor; Transmembrane; Transmembrane helix.
FT   CHAIN           1..185
FT                   /note="Signal peptidase complex subunit 3"
FT                   /id="PRO_0000218950"
FT   TOPO_DOM        1..16
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        17..37
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        38..185
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        151
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   185 AA;  20925 MW;  D32178D0B75532ED CRC64;
     MHTSIQRIQQ TFSQASTVLS IIAAIVFVVS YIQLVVANVW SLPEANFNLR GSKAARRFSR
     QYGANDPKKG KENVALKFDL DADLSPLFNW NTKLVFAYLT ATYDGKRDDI VNEITIWDQI
     ITDKDDSHIK LKGANSKYSL YDVEESFRNR NATVKLHWNI QPHVGAKIYG SLDATKGSIK
     FPQLV