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Database: UniProt
Entry: A0A2K5N9V5_CERAT
LinkDB: A0A2K5N9V5_CERAT
Original site: A0A2K5N9V5_CERAT 
ID   A0A2K5N9V5_CERAT        Unreviewed;       157 AA.
AC   A0A2K5N9V5;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Signal peptidase complex subunit 2 {ECO:0000256|ARBA:ARBA00017057, ECO:0000256|RuleBase:RU368033};
OS   Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Cercocebus.
OX   NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000034125.1, ECO:0000313|Proteomes:UP000233060};
RN   [1] {ECO:0000313|Ensembl:ENSCATP00000034125.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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. Enhances the enzymatic activity of SPC and facilitates the
CC       interactions between different components of the translocation site.
CC       {ECO:0000256|RuleBase:RU368033}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU368033}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004477,
CC       ECO:0000256|RuleBase:RU368033}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the SPCS2 family.
CC       {ECO:0000256|ARBA:ARBA00007324, ECO:0000256|RuleBase:RU368033}.
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DR   AlphaFoldDB; A0A2K5N9V5; -.
DR   Ensembl; ENSCATT00000058401.1; ENSCATP00000034125.1; ENSCATG00000039999.1.
DR   GeneTree; ENSGT00440000038181; -.
DR   Proteomes; UP000233060; Unplaced.
DR   Bgee; ENSCATG00000039999; Expressed in pituitary gland and 12 other cell types or tissues.
DR   GO; GO:0005787; C:signal peptidase complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006465; P:signal peptide processing; IEA:UniProtKB-UniRule.
DR   InterPro; IPR009582; Spc2/SPCS2.
DR   PANTHER; PTHR13085; MICROSOMAL SIGNAL PEPTIDASE 25 KDA SUBUNIT; 1.
DR   PANTHER; PTHR13085:SF0; SIGNAL PEPTIDASE COMPLEX SUBUNIT 2; 1.
DR   Pfam; PF06703; SPC25; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW   ECO:0000256|RuleBase:RU368033}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233060};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   157 AA;  17066 MW;  D2EEC8BDA34A41D9 CRC64;
     MAAAATQGGR SGGLGGNSGA GGGSNCGTGS GRSGLLEKWK IDDKPVKIDK WDGSAVKNSL
     DDSAKKEKSI FLVAHRKDPT GMDPDDIWQL SSSLKRFDDK YTLKLTFISG RTKQQREAEF
     TKSIAKFFDH SGTLVMDAYE PEISRLHDSL AIERKIK
//
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