ID W1PPK1_AMBTC Unreviewed; 84 AA.
AC W1PPK1;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Signal peptidase complex subunit 2 {ECO:0000256|ARBA:ARBA00017057, ECO:0000256|RuleBase:RU368033};
GN ORFNames=AMTR_s00029p00219780 {ECO:0000313|EMBL:ERN09704.1};
OS Amborella trichopoda.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Amborellales; Amborellaceae; Amborella.
OX NCBI_TaxID=13333 {ECO:0000313|EMBL:ERN09704.1, ECO:0000313|Proteomes:UP000017836};
RN [1] {ECO:0000313|Proteomes:UP000017836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24357323;
RG Amborella Genome Project;
RT "The Amborella genome and the evolution of flowering plants.";
RL Science 342:1241089-1241089(2013).
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 EMBL; KI392980; ERN09704.1; -; Genomic_DNA.
DR AlphaFoldDB; W1PPK1; -.
DR STRING; 13333.W1PPK1; -.
DR EnsemblPlants; ERN09704; ERN09704; AMTR_s00029p00219780.
DR Gramene; ERN09704; ERN09704; AMTR_s00029p00219780.
DR eggNOG; ENOG502QVCN; Eukaryota.
DR HOGENOM; CLU_2530481_0_0_1; -.
DR OMA; LLWIRLM; -.
DR Proteomes; UP000017836; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000017836};
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 53..70
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368033"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 84 AA; 9279 MW; C909D3F878A26196 CRC64;
MASSSSKGSS DKNPKKANLN DQNSMKHLLD ETVTEVVTSK GYAEDFTLSN TRLFIGVIII
AIALAAQFYP KKFPENRDFL IACH
//
