ID A0A1S3D4N2_DIACI Unreviewed; 188 AA.
AC A0A1S3D4N2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Signal peptidase complex subunit 2 {ECO:0000256|ARBA:ARBA00017057, ECO:0000256|RuleBase:RU368033};
GN Name=LOC103511381 {ECO:0000313|RefSeq:XP_008474325.1};
OS Diaphorina citri (Asian citrus psyllid).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Paraneoptera; Hemiptera; Sternorrhyncha; Psylloidea; Psyllidae;
OC Diaphorininae; Diaphorina.
OX NCBI_TaxID=121845 {ECO:0000313|Proteomes:UP000079169, ECO:0000313|RefSeq:XP_008474325.1};
RN [1] {ECO:0000313|RefSeq:XP_008474325.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-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 RefSeq; XP_008474325.1; XM_008476103.3.
DR AlphaFoldDB; A0A1S3D4N2; -.
DR STRING; 121845.A0A1S3D4N2; -.
DR PaxDb; 121845-A0A1S3D4N2; -.
DR GeneID; 103511381; -.
DR KEGG; dci:103511381; -.
DR OMA; INKWDGT; -.
DR OrthoDB; 2903540at2759; -.
DR Proteomes; UP000079169; 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 Reference proteome {ECO:0000313|Proteomes:UP000079169};
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"
FT TRANSMEM 82..103
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368033"
SQ SEQUENCE 188 AA; 21603 MW; 96685DB6C69F0F4E CRC64;
MSNKSEKTSE EKPIIAVNKW DGSAVKNALD DAVKDVLIKK YNYTECFRLM DGRLLICGIA
VSVAMFALLW DHLYPFPQSR PVLIMCVTTY FLMMGILTLY TTYKEKGIFA VAKKDHIVWE
ASSYLKKYDD MYNLVLQYKD TKTGVTRSEQ FNKSVANYFD ETGLLLPDLV ENDVSRLHNS
ILAEKKKE
//
