ID   SPCS1_DICDI             Reviewed;          80 AA.
AC   Q54Y83;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Signal peptidase complex subunit 1;
GN   Name=spcs1; Synonyms=spc1; ORFNames=DDB_G0278371;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
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 (By similarity). Dispensable for SPC enzymatic activity (By
CC       similarity). {ECO:0000250|UniProtKB:P46965,
CC       ECO:0000250|UniProtKB:Q9Y6A9}.
CC   -!- SUBUNIT: Component of the signal peptidase complex (SPC) composed of a
CC       catalytic subunit sec11 and three accessory subunits spcs1, spcs2 and
CC       spcs3. The complex induces a local thinning of the ER membrane which is
CC       used to measure the length of the signal peptide (SP) h-region of
CC       protein substrates. This ensures the selectivity of the complex towards
CC       h-regions shorter than 18-20 amino acids.
CC       {ECO:0000250|UniProtKB:Q9Y6A9}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:P83362}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P83362}.
CC   -!- SIMILARITY: Belongs to the SPCS1 family. {ECO:0000305}.
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DR   EMBL; AAFI02000023; EAL68358.1; -; Genomic_DNA.
DR   RefSeq; XP_642319.1; XM_637227.1.
DR   AlphaFoldDB; Q54Y83; -.
DR   SMR; Q54Y83; -.
DR   STRING; 44689.DDB0237784; -.
DR   PaxDb; Q54Y83; -.
DR   EnsemblProtists; EAL68358; EAL68358; DDB_G0278371.
DR   GeneID; 8621525; -.
DR   KEGG; ddi:DDB_G0278371; -.
DR   dictyBase; DDB_G0278371; spc1.
DR   eggNOG; KOG4112; Eukaryota.
DR   HOGENOM; CLU_134505_3_1_1; -.
DR   InParanoid; Q54Y83; -.
DR   OMA; IHLTLWT; -.
DR   PhylomeDB; Q54Y83; -.
DR   PRO; PR:Q54Y83; -.
DR   Proteomes; UP000002195; Chromosome 3.
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; IPR037713; Spc1.
DR   InterPro; IPR009542; Spc1/SPCS1.
DR   PANTHER; PTHR13202; PTHR13202; 1.
DR   PANTHER; PTHR13202:SF0; PTHR13202:SF0; 1.
DR   Pfam; PF06645; SPC12; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..80
FT                   /note="Signal peptidase complex subunit 1"
FT                   /id="PRO_0000329963"
FT   TOPO_DOM        1..9
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P83362"
FT   TRANSMEM        10..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        31..33
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:P83362"
FT   TRANSMEM        34..54
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        55..80
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P83362"
SQ   SEQUENCE   80 AA;  9297 MW;  5D202A20E9DF20B9 CRC64;
     MDFEGQKLAE YIYQYTIIIF GVIGWIIGFI KQDFSITFYS VALGTFLSLI LCLPNWKIYC
     QHPLSWQKPI VQSTPTDKSK