SPCS2_CANLF
ID SPCS2_CANLF Reviewed; 226 AA.
AC Q28250;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 125.
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; Synonyms=SPC25;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Liver;
RX PubMed=7929230; DOI=10.1016/s0021-9258(18)47255-9;
RA Greenburg G., Blobel G.;
RT "cDNA-derived primary structure of the 25-kDa subunit of canine microsomal
RT signal peptidase complex.";
RL J. Biol. Chem. 269:25354-25358(1994).
RN [2]
RP FUNCTION, IDENTIFICATION IN THE SIGNAL PEPTIDASE COMPLEX, AND SUBCELLULAR
RP LOCATION.
RX PubMed=3511473; DOI=10.1073/pnas.83.3.581;
RA Evans E.A., Gilmore R., Blobel G.;
RT "Purification of microsomal signal peptidase as a complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:581-585(1986).
RN [3]
RP SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=8632014; DOI=10.1074/jbc.271.7.3925;
RA Kalies K.-U., Hartmann E.;
RT "Membrane topology of the 12- and the 25-kDa subunits of the mammalian
RT signal peptidase complex.";
RL J. Biol. Chem. 271:3925-3929(1996).
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 (PubMed:3511473). 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:0000269|PubMed:3511473}.
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 (PubMed:3511473). Component of the signal
CC peptidase complex paralog C (SPC-C) composed of a catalytic subunit
CC SEC11C and three accessory subunits SPCS1, SPCS2 and SPCS3
CC (PubMed:3511473). Within the complex, interacts with SEC11A or SEC11C
CC and SPCS1 (By similarity). The complex induces a local thinning of the
CC ER membrane which is used to measure the length of the signal peptide
CC (SP) h-region of protein substrates (By similarity). This ensures the
CC selectivity of the complex towards h-regions shorter than 18-20 amino
CC acids (By similarity). {ECO:0000250|UniProtKB:Q15005,
CC ECO:0000269|PubMed:3511473}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:3511473, ECO:0000269|PubMed:8632014}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:8632014}.
CC -!- SIMILARITY: Belongs to the SPCS2 family. {ECO:0000305}.
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DR EMBL; U12687; AAA21254.1; -; mRNA.
DR PIR; A55012; A55012.
DR RefSeq; NP_001003324.1; NM_001003324.2.
DR AlphaFoldDB; Q28250; -.
DR SMR; Q28250; -.
DR CORUM; Q28250; -.
DR STRING; 9612.ENSCAFP00000042144; -.
DR MEROPS; X44.001; -.
DR PaxDb; Q28250; -.
DR PRIDE; Q28250; -.
DR Ensembl; ENSCAFT00030031158; ENSCAFP00030027188; ENSCAFG00030016843.
DR Ensembl; ENSCAFT00040033516; ENSCAFP00040029164; ENSCAFG00040018129.
DR Ensembl; ENSCAFT00845010762; ENSCAFP00845008397; ENSCAFG00845006071.
DR GeneID; 404016; -.
DR KEGG; cfa:404016; -.
DR CTD; 9789; -.
DR VEuPathDB; HostDB:ENSCAFG00845006071; -.
DR eggNOG; KOG4072; Eukaryota.
DR GeneTree; ENSGT00440000038181; -.
DR HOGENOM; CLU_094622_0_0_1; -.
DR InParanoid; Q28250; -.
DR OMA; DMRKYDD; -.
DR OrthoDB; 1395649at2759; -.
DR TreeFam; TF314545; -.
DR Proteomes; UP000002254; Chromosome 21.
DR Bgee; ENSCAFG00000032663; Expressed in thyroid gland and 45 other tissues.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005787; C:signal peptidase complex; IDA:UniProtKB.
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 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; Endoplasmic reticulum; Membrane;
KW Reference proteome; 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_0000221157"
FT TOPO_DOM 2..86
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:8632014"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 108..111
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:8632014"
FT TRANSMEM 112..132
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 133..226
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:8632014"
FT REGION 1..37
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; 24942 MW; 85830E5484593176 CRC64;
MAAASAQGGR TGGGGGSSGP GGGPTCGSGS GRSGLLDKWK IDDKPVKIDK WDGSAVKNSL
DDSAKKVLLE KYKYVENFGL IDGRLTICTI SCFFAIVALI WDYMHPFPES KPVLALCVIS
YFVMMGILTI YTSYKEKSIF LVAHRKDPTG MDPDDIWQLS SSLKRFDDKY TLKLTFISGR
TKQQREAEFT KSIAKFFDHS GTLVMDAYEP EISRLHDSLA TERKIK
