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SPC3_DEBHA
ID   SPC3_DEBHA              Reviewed;         190 AA.
AC   Q6BPD6;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Signal peptidase complex subunit 3;
DE   AltName: Full=Microsomal signal peptidase subunit 3;
GN   Name=SPC3; OrderedLocusNames=DEHA2E14454g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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; CR382137; CAG88178.2; -; Genomic_DNA.
DR   RefSeq; XP_459934.2; XM_459934.1.
DR   AlphaFoldDB; Q6BPD6; -.
DR   SMR; Q6BPD6; -.
DR   STRING; 4959.XP_459934.2; -.
DR   EnsemblFungi; CAG88178; CAG88178; DEHA2E14454g.
DR   GeneID; 2902208; -.
DR   KEGG; dha:DEHA2E14454g; -.
DR   VEuPathDB; FungiDB:DEHA2E14454g; -.
DR   eggNOG; KOG3372; Eukaryota.
DR   HOGENOM; CLU_068714_2_1_1; -.
DR   InParanoid; Q6BPD6; -.
DR   OMA; LHWNIQP; -.
DR   OrthoDB; 1514162at2759; -.
DR   Proteomes; UP000000599; Chromosome E.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005787; C:signal peptidase complex; IEA:InterPro.
DR   GO; GO:0006465; P:signal peptide processing; IEA:InterPro.
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; Membrane; Reference proteome; Signal-anchor;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..190
FT                   /note="Signal peptidase complex subunit 3"
FT                   /id="PRO_0000218947"
FT   TOPO_DOM        1..9
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        10..32
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        33..190
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   190 AA;  21768 MW;  A3A32FC7DA1970E4 CRC64;
     MFNIVTRFQY AANQALTSSI IIAGIVIVSS LLQLYSNNAW SLGTTSISNI KPQVSLKHSF
     NYGSVNRKPK ENSRIQFDLE TDLSPLFNWN TKQLFVYLTA EYPGKSDGSS NKITYWDKII
     TSKEDAVLSL KNQKSKYSVW DIEPSFRQRD AVVKLEWNLQ PHIGPLIFGE TDEIADFKFA
     EYVDKKKEQK
 
 
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