ID   SPCS2_DANRE             Reviewed;         201 AA.
AC   Q5BJI9;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   12-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 82.
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; ORFNames=zgc:110364;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Olfactory epithelium;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (MAR-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). 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 (SPC) composed of a
CC       catalytic subunit sec11a and three accessory subunits spcs1, spcs2 and
CC       spcs3. The complex induces a local thinning of the ER membrane which is
CC       used to measure the length of the signal peptide (SP) h-region of
CC       protein substrates. This ensures the selectivity of the complex towards
CC       h-regions shorter than 18-20 amino acids.
CC       {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; BC091463; AAH91463.1; -; mRNA.
DR   RefSeq; NP_001013487.1; NM_001013469.1.
DR   AlphaFoldDB; Q5BJI9; -.
DR   SMR; Q5BJI9; -.
DR   STRING; 7955.ENSDARP00000062851; -.
DR   PaxDb; Q5BJI9; -.
DR   PeptideAtlas; Q5BJI9; -.
DR   GeneID; 541342; -.
DR   KEGG; dre:541342; -.
DR   CTD; 9789; -.
DR   ZFIN; ZDB-GENE-050320-32; spcs2.
DR   eggNOG; KOG4072; Eukaryota.
DR   InParanoid; Q5BJI9; -.
DR   OrthoDB; 1395649at2759; -.
DR   PhylomeDB; Q5BJI9; -.
DR   Reactome; R-DRE-422085; Synthesis, secretion, and deacylation of Ghrelin.
DR   PRO; PR:Q5BJI9; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
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_0000221162"
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;  23110 MW;  4E1D994B0FBF9395 CRC64;
     MAARNGKNSI LEKWRIDEKP VKIDKWDGAA VKNSLDDAAK KVLIEKYGYL ESFNLVDGRL
     FICTVSCLFT IVALIWDYLH PFPESKPVLA CCVVSYFIMM GILTLYTSYK EKNIFLVAMQ
     KDPAGMDPDH SWCLSSSLKR FDDQYTLRMS FTDGKTKQSR ETEFTKSVSV FFDENGTLVM
     DQYEKYVSKL HDTLATEKKT K