ID   SPCS2_MACFA             Reviewed;         226 AA.
AC   Q4R512;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=Signal peptidase complex subunit 2;
DE   AltName: Full=Microsomal signal peptidase 25 kDa subunit;
DE            Short=SPase 25 kDa subunit;
GN   Name=SPCS2; ORFNames=QflA-13117;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Frontal cortex;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
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 paralog A (SPC-A)
CC       composed of a catalytic subunit SEC11A and three accessory subunits
CC       SPCS1, SPCS2 and SPCS3. Component of the signal peptidase complex
CC       paralog C (SPC-C) composed of a catalytic subunit SEC11C and three
CC       accessory subunits SPCS1, SPCS2 and SPCS3. Within the complex,
CC       interacts with SEC11A or SEC11C and SPCS1. The complex induces a local
CC       thinning of the ER membrane which is used to measure the length of the
CC       signal peptide (SP) h-region of protein substrates. This ensures the
CC       selectivity of the complex towards h-regions shorter than 18-20 amino
CC       acids. {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; AB169732; BAE01813.1; -; mRNA.
DR   RefSeq; NP_001274217.1; NM_001287288.1.
DR   AlphaFoldDB; Q4R512; -.
DR   SMR; Q4R512; -.
DR   STRING; 9541.XP_005579146.1; -.
DR   GeneID; 102116673; -.
DR   CTD; 9789; -.
DR   VEuPathDB; HostDB:ENSMFAG00000040665; -.
DR   eggNOG; KOG4072; Eukaryota.
DR   OMA; DMRKYDD; -.
DR   OrthoDB; 1395649at2759; -.
DR   Proteomes; UP000233100; Chromosome 14.
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; IPR009582; Spc2/SPCS2.
DR   PANTHER; PTHR13085; PTHR13085; 1.
DR   Pfam; PF06703; SPC25; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Endoplasmic reticulum; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q15005"
FT   CHAIN           2..226
FT                   /note="Signal peptidase complex subunit 2"
FT                   /id="PRO_0000221159"
FT   TOPO_DOM        2..86
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q28250"
FT   TRANSMEM        87..107
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        108..111
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:Q28250"
FT   TRANSMEM        112..132
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        133..226
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q28250"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15005"
FT   MOD_RES         169
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15005"
FT   MOD_RES         191
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15005"
SQ   SEQUENCE   226 AA;  25014 MW;  656ECCC7C5451166 CRC64;
     MAAAATQGGR SGGLGGNSGA GGGSNCGTGS GRSGLLDKWK IDDKPVKIDK WDGSAVKNSL
     DDSAKKVLLE KYKYVENFGL IDGRLTICTI SCFFAIVALI WDYMHPFPES KPVLALCVIS
     YFVMMGILTI YTSYKEKSIF LVAHRKDPTG MDPDDIWQLS SSLKRFDDKY TLKLTFISGR
     TKQQREAEFT KSIAKFFDHS GTLVMDAYEP EISRLHDSLA VERKIK