ID   SPCS3_DICDI             Reviewed;         170 AA.
AC   B0G180;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Signal peptidase complex subunit 3;
GN   Name=spcs3; Synonyms=spc3; ORFNames=DDB_G0290851;
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: 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 (By similarity). Essential for the SPC catalytic
CC       activity, possibly by stabilizing and positioning the active center of
CC       the complex close to the lumenal surface (By similarity).
CC       {ECO:0000250|UniProtKB:P61009, ECO:0000250|UniProtKB:Q12133}.
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:P61008}; Single-pass type II membrane protein
CC       {ECO:0000250|UniProtKB:P61008}.
CC   -!- SIMILARITY: Belongs to the SPCS3 family. {ECO:0000305}.
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DR   EMBL; AAFI02000171; EDR41028.1; -; Genomic_DNA.
DR   RefSeq; XP_001733043.1; XM_001732991.1.
DR   AlphaFoldDB; B0G180; -.
DR   SMR; B0G180; -.
DR   STRING; 44689.DDB0237789; -.
DR   PaxDb; B0G180; -.
DR   EnsemblProtists; EDR41028; EDR41028; DDB_G0290851.
DR   GeneID; 8627862; -.
DR   KEGG; ddi:DDB_G0290851; -.
DR   dictyBase; DDB_G0290851; spc3.
DR   eggNOG; KOG3372; Eukaryota.
DR   HOGENOM; CLU_068714_1_0_1; -.
DR   InParanoid; B0G180; -.
DR   OMA; FGCFVTT; -.
DR   PhylomeDB; B0G180; -.
DR   PRO; PR:B0G180; -.
DR   Proteomes; UP000002195; Chromosome 5.
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..170
FT                   /note="Signal peptidase complex subunit 3"
FT                   /id="PRO_0000329961"
FT   TOPO_DOM        1..7
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P61008"
FT   TRANSMEM        8..28
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        29..170
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:P61008"
FT   CARBOHYD        131
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   170 AA;  19672 MW;  47625878DBC87F19 CRC64;
     MHSLSQRANT IVCFGGIVLV GVLLLNVLSR AFFSDHVDVD IKLNEIHRFN TQRNFEYSFI
     SIDLDANLEP LFNWNTKMLF LYVTAEYRTK QNVLSQVVVW DHILTEKSKA NIHEKRLSKY
     PIINQGLGLK NNTIKLTFNY NVVPISGILT RHQVGTSEFK FPTTYMKEAY