ID   SPCS2_DICDI             Reviewed;         183 AA.
AC   Q55E35;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 2.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Signal peptidase complex subunit 2;
GN   Name=spcs2; Synonyms=spc2; ORFNames=DDB_G0270510;
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). Enhances the enzymatic activity of SPC and
CC       facilitates the interactions between different components of the
CC       translocation site (By similarity). {ECO:0000250|UniProtKB:Q04969,
CC       ECO:0000250|UniProtKB:Q15005}.
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:Q15005}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q28250}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:Q28250}.
CC   -!- SIMILARITY: Belongs to the SPCS2 family. {ECO:0000305}.
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DR   EMBL; AAFI02000005; EAL72605.2; -; Genomic_DNA.
DR   RefSeq; XP_645946.2; XM_640854.2.
DR   AlphaFoldDB; Q55E35; -.
DR   SMR; Q55E35; -.
DR   STRING; 44689.DDB0237785; -.
DR   PaxDb; Q55E35; -.
DR   EnsemblProtists; EAL72605; EAL72605; DDB_G0270510.
DR   GeneID; 8616890; -.
DR   KEGG; ddi:DDB_G0270510; -.
DR   dictyBase; DDB_G0270510; spc2.
DR   eggNOG; KOG4072; Eukaryota.
DR   HOGENOM; CLU_100048_0_0_1; -.
DR   InParanoid; Q55E35; -.
DR   OMA; DMRKYDD; -.
DR   PhylomeDB; Q55E35; -.
DR   PRO; PR:Q55E35; -.
DR   Proteomes; UP000002195; Chromosome 1.
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; IPR009582; Spc2/SPCS2.
DR   PANTHER; PTHR13085; PTHR13085; 1.
DR   Pfam; PF06703; SPC25; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..183
FT                   /note="Signal peptidase complex subunit 2"
FT                   /id="PRO_0000329962"
FT   TOPO_DOM        1..52
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q28250"
FT   TRANSMEM        53..73
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        74..80
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:Q28250"
FT   TRANSMEM        81..101
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        102..183
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q28250"
SQ   SEQUENCE   183 AA;  20796 MW;  8761F96D14EFAD39 CRC64;
     MSTTTTTTTT EKPIQVTLYD SNTIKQTLDD SIVKYVTSAL SYTQNQKLNY TKVLFGLIGC
     TLAAIAQFYP IPFPKNKPVL ILCVALYVVI SLILYYINIF IQKDYILQAS KSNDEIKVAT
     VLQKYDPNYQ VKIENAKNSS INVPFSKSID LYFDTKGTFL ESNFHNDLSV QFKKFAKLNV
     KDK