SCP3_KLULA
ID SCP3_KLULA Reviewed; 189 AA.
AC Q6CRY8;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Signal peptidase complex subunit 3;
DE AltName: Full=Microsomal signal peptidase subunit 3;
GN Name=SPC3; OrderedLocusNames=KLLA0D05401g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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; CR382124; CAH00397.1; -; Genomic_DNA.
DR RefSeq; XP_453301.1; XM_453301.1.
DR AlphaFoldDB; Q6CRY8; -.
DR SMR; Q6CRY8; -.
DR STRING; 28985.XP_453301.1; -.
DR EnsemblFungi; CAH00397; CAH00397; KLLA0_D05401g.
DR GeneID; 2892699; -.
DR KEGG; kla:KLLA0_D05401g; -.
DR eggNOG; KOG3372; Eukaryota.
DR HOGENOM; CLU_068714_2_1_1; -.
DR InParanoid; Q6CRY8; -.
DR OMA; LHWNIQP; -.
DR Proteomes; UP000000598; Chromosome D.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005787; C:signal peptidase complex; IEA:EnsemblFungi.
DR GO; GO:0045047; P:protein targeting to ER; IEA:EnsemblFungi.
DR GO; GO:0006465; P:signal peptide processing; IEA:EnsemblFungi.
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..189
FT /note="Signal peptidase complex subunit 3"
FT /id="PRO_0000218948"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 13..35
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 36..189
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 189 AA; 21845 MW; 4B15FB4CB896DCBF CRC64;
MFSLNQRFQH VSSLALSCSF LVIALIAATS WLQLVKDNVF ELESQLSHIR SATRFAKQKR
YGGSAVNPTE VSKIRFNADF DFSRLFNWNT KQVFAYVTAE YEGDENPHTM NEITIWDKII
PSRDNATFTL SDIDAKYQLW DLESKITERP LTFKLHWNIQ PWFGFLINGE TTGSKTIELK
KPVDKQKGK