ID   SPCS2_XENTR             Reviewed;         201 AA.
AC   Q5M8Y1;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 78.
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;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (DEC-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). 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:0000250|UniProtKB:Q15005}.
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. 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:Q15005}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q28250}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:Q28250}.
CC   -!- SIMILARITY: Belongs to the SPCS2 family. {ECO:0000305}.
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DR   EMBL; BC087786; AAH87786.1; -; mRNA.
DR   RefSeq; NP_001011222.1; NM_001011222.1.
DR   AlphaFoldDB; Q5M8Y1; -.
DR   SMR; Q5M8Y1; -.
DR   STRING; 8364.ENSXETP00000054148; -.
DR   PaxDb; Q5M8Y1; -.
DR   PRIDE; Q5M8Y1; -.
DR   GeneID; 496658; -.
DR   KEGG; xtr:496658; -.
DR   CTD; 9789; -.
DR   Xenbase; XB-GENE-5826459; spcs2.
DR   eggNOG; KOG4072; Eukaryota.
DR   InParanoid; Q5M8Y1; -.
DR   Proteomes; UP000008143; Chromosome 2.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000040068; Expressed in neurula embryo and 12 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   InterPro; IPR009582; Spc2/SPCS2.
DR   PANTHER; PTHR13085; PTHR13085; 1.
DR   Pfam; PF06703; SPC25; 1.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..201
FT                   /note="Signal peptidase complex subunit 2"
FT                   /id="PRO_0000221163"
FT   TOPO_DOM        1..59
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q28250"
FT   TRANSMEM        60..80
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        81..86
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:Q28250"
FT   TRANSMEM        87..107
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        108..201
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q28250"
SQ   SEQUENCE   201 AA;  22958 MW;  1F6CD4AE6E70D7AE CRC64;
     MAARGGKNGL LEKWKIDDKP VKIDKWDGSA VKNSLDDAAK KVLLEKYRYV ENFCLIDGRL
     IICTISCVFA IVALVWDYLH PFPESKPVLA ICVISYFLMM GILTIYTSYK EKSIFLVAHR
     KDPAGMDPDD IWHLSSSLKR FDDKYTLKVT YISGKTKAQR DAEFTKSIAR FFDDNGTLVM
     DLFEPEVSKL HDSLAMEKKT K