ID   SPCS1_BOVIN             Reviewed;         102 AA.
AC   Q3T134;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Signal peptidase complex subunit 1;
DE   AltName: Full=Microsomal signal peptidase 12 kDa subunit;
DE            Short=SPase 12 kDa subunit;
GN   Name=SPCS1;
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=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-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). Dispensable for SPC enzymatic activity (By
CC       similarity). {ECO:0000250|UniProtKB:P46965,
CC       ECO:0000250|UniProtKB:Q9Y6A9}.
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 SPCS2 and SPCS3. The complex induces a local thinning of
CC       the ER membrane which is used to measure the length of the signal
CC       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:Q9Y6A9}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:P83362}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P83362}.
CC   -!- PTM: May be phosphorylated. {ECO:0000250|UniProtKB:Q9Y6A9}.
CC   -!- SIMILARITY: Belongs to the SPCS1 family. {ECO:0000305}.
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DR   EMBL; BC102144; AAI02145.1; -; mRNA.
DR   RefSeq; NP_001029576.1; NM_001034404.2.
DR   AlphaFoldDB; Q3T134; -.
DR   SMR; Q3T134; -.
DR   STRING; 9913.ENSBTAP00000006231; -.
DR   PaxDb; Q3T134; -.
DR   GeneID; 511453; -.
DR   KEGG; bta:511453; -.
DR   CTD; 28972; -.
DR   eggNOG; KOG4112; Eukaryota.
DR   HOGENOM; CLU_134505_1_0_1; -.
DR   InParanoid; Q3T134; -.
DR   OrthoDB; 1589808at2759; -.
DR   TreeFam; TF106122; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
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   InterPro; IPR037713; Spc1.
DR   InterPro; IPR009542; Spc1/SPCS1.
DR   PANTHER; PTHR13202; PTHR13202; 1.
DR   PANTHER; PTHR13202:SF0; PTHR13202:SF0; 1.
DR   Pfam; PF06645; SPC12; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..102
FT                   /note="Signal peptidase complex subunit 1"
FT                   /id="PRO_0000244605"
FT   TOPO_DOM        1..19
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P83362"
FT   TRANSMEM        20..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        43..46
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:P83362"
FT   TRANSMEM        47..69
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        70..102
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P83362"
FT   REGION          81..102
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   102 AA;  11805 MW;  3DE2798887FF28B5 CRC64;
     MLEHLSSLPT QMDYKGQKLA EQMFQGIILF SAIVGFIYGY LAEQFGWTVY IVMAGFAFSC
     LLTLPPWPIY RRHPLKWLPV QDSSTEDKKP GERKVKRHAK NN