ID   SPCS1_PONAB             Reviewed;         169 AA.
AC   Q5RF96; A0A0A0MXR3; A0A2J8THX8;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-OCT-2019, sequence version 2.
DT   03-AUG-2022, entry version 71.
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   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Wilson R.K., Mardis E.;
RT   "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Pollen A., Hastie A., Hormozdiari F., Dougherty M., Liu R., Chaisson M.,
RA   Hoppe E., Hill C., Pang A., Hillier L., Baker C., Armstrong J.,
RA   Shendure J., Paten B., Wilson R., Chao H., Schneider V., Ventura M.,
RA   Kronenberg Z., Murali S., Gordon D., Cantsilieris S., Munson K., Nelson B.,
RA   Raja A., Underwood J., Diekhans M., Fiddes I., Haussler D., Eichler E.;
RT   "High-resolution comparative analysis of great ape genomes.";
RL   Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 33-169.
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAH89561.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; ABGA01132836; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; NDHI03003498; PNJ32564.1; -; Genomic_DNA.
DR   EMBL; NDHI03003498; PNJ32565.1; -; Genomic_DNA.
DR   EMBL; CR857265; CAH89561.1; ALT_INIT; mRNA.
DR   RefSeq; NP_001127168.1; NM_001133696.2.
DR   AlphaFoldDB; Q5RF96; -.
DR   SMR; Q5RF96; -.
DR   STRING; 9601.ENSPPYP00000015441; -.
DR   Ensembl; ENSPPYT00000016054; ENSPPYP00000015441; ENSPPYG00000013798.
DR   GeneID; 100174219; -.
DR   KEGG; pon:100174219; -.
DR   CTD; 28972; -.
DR   eggNOG; KOG4112; Eukaryota.
DR   GeneTree; ENSGT00390000018321; -.
DR   HOGENOM; CLU_134505_1_0_1; -.
DR   InParanoid; Q5RF96; -.
DR   OMA; PGPWETS; -.
DR   OrthoDB; 1589808at2759; -.
DR   Proteomes; UP000001595; Chromosome 3.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005787; C:signal peptidase complex; IEA:InterPro.
DR   GO; GO:0043022; F:ribosome binding; IEA:Ensembl.
DR   GO; GO:0006465; P:signal peptide processing; IEA:InterPro.
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   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..169
FT                   /note="Signal peptidase complex subunit 1"
FT                   /id="PRO_0000215156"
FT   TOPO_DOM        1..93
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P83362"
FT   TRANSMEM        94..114
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        115
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:P83362"
FT   TRANSMEM        116..136
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        137..169
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P83362"
FT   REGION          148..169
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   169 AA;  18404 MW;  57E2EEEC930FCE85 CRC64;
     MARGGDTGCT GPSETSASGA VAIAFPGLEG PPADAQYQTL ALTVPKSWSP SPRSLPPALS
     CPPPQPAMLE HLSSLPTQMD YKGQKLAEQM FQGIILFSAI VGFIYGYVAE QFGWTVYIVM
     AGFAFSCLLT LPPWPIYRRH PLKWLPVQES STDDKKPGER KIKRHAKNN