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Database: UniProt
Entry: A0A0E0P9R4_ORYRU
LinkDB: A0A0E0P9R4_ORYRU
Original site: A0A0E0P9R4_ORYRU 
ID   A0A0E0P9R4_ORYRU        Unreviewed;       172 AA.
AC   A0A0E0P9R4;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=Signal peptidase complex subunit 2 {ECO:0000256|ARBA:ARBA00017057, ECO:0000256|RuleBase:RU368033};
OS   Oryza rufipogon (Brownbeard rice) (Asian wild rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=4529 {ECO:0000313|EnsemblPlants:ORUFI04G15340.1, ECO:0000313|Proteomes:UP000008022};
RN   [1] {ECO:0000313|Proteomes:UP000008022}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. W1943 {ECO:0000313|Proteomes:UP000008022};
RA   Zhao Q.;
RL   Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:ORUFI04G15340.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (JUN-2015) 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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|RuleBase:RU368033}.
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DR   AlphaFoldDB; A0A0E0P9R4; -.
DR   STRING; 4529.A0A0E0P9R4; -.
DR   EnsemblPlants; ORUFI04G15340.1; ORUFI04G15340.1; ORUFI04G15340.
DR   Gramene; ORUFI04G15340.1; ORUFI04G15340.1; ORUFI04G15340.
DR   eggNOG; ENOG502QVCN; Eukaryota.
DR   HOGENOM; CLU_100048_0_0_1; -.
DR   OMA; INKWDGT; -.
DR   Proteomes; UP000008022; Unassembled WGS sequence.
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; 2.
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   Reference proteome {ECO:0000313|Proteomes:UP000008022};
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        52..70
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU368033"
SQ   SEQUENCE   172 AA;  18958 MW;  BC7BF9CD506F3DDB CRC64;
     MASDGAAATP AKASPKKANL LDPHSIKHLL DETISDVVKS KGYAEDTRLG NWKLAIGAAV
     IAIALLAQFY PKKFPQNRDY TKEKDAIMFT HPPAGSFNST GLVISSKLPR FSDMYTITIA
     SADPQSISAN KPVHFTKSVT KWFTKEGVLV EGLFWKDVER LIDDYNTERK GK
//
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