ID   SPCS3_BOVIN             Reviewed;         180 AA.
AC   Q3SZU5;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 80.
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;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). Essential for the SPC catalytic
CC       activity, possibly by stabilizing and positioning the active center of
CC       the complex close to the lumenal surface (By similarity).
CC       {ECO:0000250|UniProtKB:P61009, ECO:0000250|UniProtKB:Q12133}.
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:P61009}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:P61008}; Single-pass type II membrane protein
CC       {ECO:0000250|UniProtKB:P61008}.
CC   -!- SIMILARITY: Belongs to the SPCS3 family. {ECO:0000305}.
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DR   EMBL; BC102708; AAI02709.1; -; mRNA.
DR   RefSeq; NP_001070461.1; NM_001076993.1.
DR   AlphaFoldDB; Q3SZU5; -.
DR   SMR; Q3SZU5; -.
DR   STRING; 9913.ENSBTAP00000018803; -.
DR   PeptideAtlas; Q3SZU5; -.
DR   Ensembl; ENSBTAT00000018803; ENSBTAP00000018803; ENSBTAG00000014146.
DR   GeneID; 767917; -.
DR   KEGG; bta:767917; -.
DR   CTD; 60559; -.
DR   VEuPathDB; HostDB:ENSBTAG00000014146; -.
DR   VGNC; VGNC:58352; SPCS3.
DR   GeneTree; ENSGT00390000009223; -.
DR   InParanoid; Q3SZU5; -.
DR   OMA; FGCFVTT; -.
DR   OrthoDB; 1514162at2759; -.
DR   Proteomes; UP000009136; Chromosome 27.
DR   Bgee; ENSBTAG00000014146; Expressed in spermatocyte and 106 other tissues.
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   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   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Glycoprotein; Membrane; Reference proteome;
KW   Signal-anchor; Transmembrane; Transmembrane helix.
FT   CHAIN           1..180
FT                   /note="Signal peptidase complex subunit 3"
FT                   /id="PRO_0000244604"
FT   TOPO_DOM        1..11
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P61008"
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:0000250|UniProtKB:P61008"
FT   CARBOHYD        141
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
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