SPCS3_CANLF
ID SPCS3_CANLF Reviewed; 180 AA.
AC P61008; P12280; Q9H0S7;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2004, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Signal peptidase complex subunit 3;
DE AltName: Full=Microsomal signal peptidase 22/23 kDa subunit;
DE Short=SPC22/23;
DE Short=SPase 22/23 kDa subunit;
GN Name=SPCS3; Synonyms=SPC22;
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.
RX PubMed=3053702; DOI=10.1016/s0021-9258(18)37498-2;
RA Shelness G.S., Kanwar Y.S., Blobel G.;
RT "cDNA-derived primary structure of the glycoprotein component of canine
RT microsomal signal peptidase complex.";
RL J. Biol. Chem. 263:17063-17070(1988).
RN [2]
RP FUNCTION, IDENTIFICATION IN THE SIGNAL PEPTIDASE COMPLEX, SUBCELLULAR
RP LOCATION, AND GLYCOSYLATION AT ASN-141.
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 FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, AND GLYCOSYLATION AT ASN-141.
RX PubMed=8444896; DOI=10.1016/s0021-9258(18)53520-1;
RA Shelness G.S., Lin L., Nicchitta C.V.;
RT "Membrane topology and biogenesis of eukaryotic signal peptidase.";
RL J. Biol. Chem. 268:5201-5208(1993).
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 (PubMed:3511473, PubMed:8444896). Essential for
CC the SPC catalytic activity, possibly by stabilizing and positioning the
CC active center of the complex close to the lumenal surface (By
CC similarity). {ECO:0000250|UniProtKB:Q12133, ECO:0000269|PubMed:3511473,
CC ECO:0000269|PubMed:8444896}.
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:P61009,
CC ECO:0000269|PubMed:3511473}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:3511473, ECO:0000269|PubMed:8444896}; Single-pass
CC type II membrane protein {ECO:0000269|PubMed:8444896}.
CC -!- PTM: Occurs in 2 differentially glycosylated forms (22 kDa and 23 kDa).
CC {ECO:0000269|PubMed:3511473, ECO:0000269|PubMed:8444896}.
CC -!- SIMILARITY: Belongs to the SPCS3 family. {ECO:0000305}.
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DR EMBL; J04067; AAA30894.1; -; mRNA.
DR PIR; A31788; A31788.
DR RefSeq; NP_001003314.1; NM_001003314.1.
DR AlphaFoldDB; P61008; -.
DR SMR; P61008; -.
DR CORUM; P61008; -.
DR STRING; 9612.ENSCAFP00000035192; -.
DR MEROPS; X45.001; -.
DR iPTMnet; P61008; -.
DR Ensembl; ENSCAFT00000039350; ENSCAFP00000035192; ENSCAFG00000025347.
DR Ensembl; ENSCAFT00030018803; ENSCAFP00030016411; ENSCAFG00030010127.
DR Ensembl; ENSCAFT00040011067; ENSCAFP00040009582; ENSCAFG00040005914.
DR Ensembl; ENSCAFT00845033569; ENSCAFP00845026279; ENSCAFG00845018970.
DR GeneID; 404005; -.
DR CTD; 60559; -.
DR VEuPathDB; HostDB:ENSCAFG00845018970; -.
DR VGNC; VGNC:82299; SPCS3.
DR eggNOG; KOG3372; Eukaryota.
DR GeneTree; ENSGT00390000009223; -.
DR InParanoid; P61008; -.
DR OrthoDB; 1514162at2759; -.
DR Proteomes; UP000002254; Chromosome 16.
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 GO; GO:0019082; P:viral protein processing; IEA:Ensembl.
DR InterPro; IPR007653; SPC3.
DR PANTHER; PTHR12804; PTHR12804; 1.
DR Pfam; PF04573; SPC22; 1.
DR PIRSF; PIRSF016089; SPC22; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Endoplasmic reticulum; Glycoprotein; Membrane;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..180
FT /note="Signal peptidase complex subunit 3"
FT /id="PRO_0000218937"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:8444896"
FT TRANSMEM 12..32
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..180
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:8444896"
FT CARBOHYD 141
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:8444896,
FT ECO:0000305|PubMed:3511473"
FT CONFLICT 141
FT /note="N -> E (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 180 AA; 20313 MW; 342AB8E0F3F6D71A CRC64;
MNTVLSRANS LFAFSLSVMA ALTFGCFITT AFKDRSVPVR LHVSRIMLKN VEDFTGPRER
SDLGFITFDI TADLENIFDW NVKQLFLYLS AEYSTKNNAL NQVVLWDKIV LRGDNPKLLL
KDMKTKYFFF DDGNGLKGNR NVTLTLSWNV VPNAGILPLV TGSGHVSVPF PDTYEITKSY
