ID A0A3B3CGM5_ORYME Unreviewed; 218 AA.
AC A0A3B3CGM5;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Signal peptidase complex subunit 2 {ECO:0000256|ARBA:ARBA00017057, ECO:0000256|RuleBase:RU368033};
OS Oryzias melastigma (Marine medaka).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=30732 {ECO:0000313|Ensembl:ENSOMEP00000017048.1, ECO:0000313|Proteomes:UP000261560};
RN [1] {ECO:0000313|Ensembl:ENSOMEP00000017048.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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. Enhances the enzymatic activity of SPC and facilitates the
CC interactions between different components of the translocation site.
CC {ECO:0000256|RuleBase:RU368033}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU368033}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004477,
CC ECO:0000256|RuleBase:RU368033}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the SPCS2 family.
CC {ECO:0000256|ARBA:ARBA00007324, ECO:0000256|RuleBase:RU368033}.
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DR AlphaFoldDB; A0A3B3CGM5; -.
DR STRING; 30732.ENSOMEP00000017048; -.
DR PaxDb; 30732-ENSOMEP00000017048; -.
DR Ensembl; ENSOMET00000025694.1; ENSOMEP00000017048.1; ENSOMEG00000018731.1.
DR GeneTree; ENSGT00440000038181; -.
DR OMA; INKWDGT; -.
DR OrthoDB; 2903540at2759; -.
DR Proteomes; UP000261560; Unplaced.
DR GO; GO:0005787; C:signal peptidase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006465; P:signal peptide processing; IEA:UniProtKB-UniRule.
DR InterPro; IPR009582; Spc2/SPCS2.
DR PANTHER; PTHR13085; MICROSOMAL SIGNAL PEPTIDASE 25 KDA SUBUNIT; 1.
DR PANTHER; PTHR13085:SF0; SIGNAL PEPTIDASE COMPLEX SUBUNIT 2; 1.
DR Pfam; PF06703; SPC25; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW ECO:0000256|RuleBase:RU368033};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU368033};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU368033};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU368033}.
FT TRANSMEM 77..96
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368033"
FT TRANSMEM 102..123
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368033"
SQ SEQUENCE 218 AA; 24883 MW; 337F4347AF27F83D CRC64;
MFVQITTSGW ELLKLKMAAA RNGKSGLLEK WRIDEKPVKI DKWDGAAVKN SLDDAAKKVL
LEKYGYVENF QLVDGRLLIC TVSCLFAMLA LVWDYLHPFP ESRPVLACCV VSYFIMMGVL
TLYTSYKEKN IFLVALQRDP AGMDPDHVWQ LASSLKRFDD QYTLRVSFTD GKTRRSREAD
FTKSVSAFFD QNGTLVMDQF ERSVSRLHDA LASDKKTK
//
