SPCS1_DROME
ID SPCS1_DROME Reviewed; 98 AA.
AC Q9VAL0;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 02-FEB-2004, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Signal peptidase complex subunit 1;
DE AltName: Full=Microsomal signal peptidase 12 kDa subunit;
DE Short=SPase 12 kDa subunit;
GN Name=Spase12; ORFNames=CG11500;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP IDENTIFICATION.
RX PubMed=15901661; DOI=10.1242/dev.01863;
RA Abrams E.W., Andrew D.J.;
RT "CrebA regulates secretory activity in the Drosophila salivary gland and
RT epidermis.";
RL Development 132:2743-2758(2005).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-84; SER-85; SER-86 AND
RP SER-88, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [5]
RP FUNCTION (MICROBIAL INFECTION), AND DISRUPTION PHENOTYPE (MICROBIAL
RP INFECTION).
RX PubMed=27383988; DOI=10.1038/nature18625;
RA Zhang R., Miner J.J., Gorman M.J., Rausch K., Ramage H., White J.P.,
RA Zuiani A., Zhang P., Fernandez E., Zhang Q., Dowd K.A., Pierson T.C.,
RA Cherry S., Diamond M.S.;
RT "A CRISPR screen defines a signal peptide processing pathway required by
RT flaviviruses.";
RL Nature 535:164-168(2016).
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). Dispensable for SPC enzymatic activity (By
CC similarity). {ECO:0000250|UniProtKB:P46965,
CC ECO:0000250|UniProtKB:Q9Y6A9}.
CC -!- FUNCTION: (Microbial infection) Plays an important role in infection by
CC flaviviruses such as West Nile virus and Dengue virus type 2.
CC {ECO:0000269|PubMed:27383988}.
CC -!- SUBUNIT: Component of the signal peptidase complex (SPC) composed of a
CC catalytic subunit twr/SEC11 and three accessory subunits Spase12/SPCS1,
CC Spase25/SPCS2 and Spase22-23/SPCS3. The complex induces a local
CC thinning of the ER membrane which is used to measure the length of the
CC signal peptide (SP) h-region of protein substrates. This ensures the
CC selectivity of the complex towards h-regions shorter than 18-20 amino
CC acids. {ECO:0000250|UniProtKB:Q9Y6A9}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P83362}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P83362}.
CC -!- DISRUPTION PHENOTYPE: (Microbial infection) RNAi-mediated knockdown
CC reduces infection by West Nile virus (WNV) and Dengue virus type 2
CC (DENV-2). {ECO:0000269|PubMed:27383988}.
CC -!- SIMILARITY: Belongs to the SPCS1 family. {ECO:0000305}.
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DR EMBL; AE014297; AAF56894.2; -; Genomic_DNA.
DR RefSeq; NP_788760.1; NM_176583.3.
DR AlphaFoldDB; Q9VAL0; -.
DR SMR; Q9VAL0; -.
DR IntAct; Q9VAL0; 4.
DR STRING; 7227.FBpp0084801; -.
DR iPTMnet; Q9VAL0; -.
DR PaxDb; Q9VAL0; -.
DR PRIDE; Q9VAL0; -.
DR DNASU; 50096; -.
DR EnsemblMetazoa; FBtr0085435; FBpp0084801; FBgn0040623.
DR GeneID; 50096; -.
DR KEGG; dme:Dmel_CG11500; -.
DR CTD; 50096; -.
DR FlyBase; FBgn0040623; Spase12.
DR VEuPathDB; VectorBase:FBgn0040623; -.
DR eggNOG; KOG4112; Eukaryota.
DR GeneTree; ENSGT00390000018321; -.
DR HOGENOM; CLU_134505_1_1_1; -.
DR InParanoid; Q9VAL0; -.
DR OMA; IHLTLWT; -.
DR OrthoDB; 1589808at2759; -.
DR PhylomeDB; Q9VAL0; -.
DR BioGRID-ORCS; 50096; 1 hit in 1 CRISPR screen.
DR GenomeRNAi; 50096; -.
DR PRO; PR:Q9VAL0; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0040623; Expressed in spermathecum and 29 other tissues.
DR ExpressionAtlas; Q9VAL0; differential.
DR Genevisible; Q9VAL0; DM.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
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; IPR037713; Spc1.
DR InterPro; IPR009542; Spc1/SPCS1.
DR PANTHER; PTHR13202; PTHR13202; 1.
DR PANTHER; PTHR13202:SF0; PTHR13202:SF0; 1.
DR Pfam; PF06645; SPC12; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Membrane; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..98
FT /note="Signal peptidase complex subunit 1"
FT /id="PRO_0000215159"
FT TOPO_DOM 1..18
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P83362"
FT TRANSMEM 19..38
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 39..42
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P83362"
FT TRANSMEM 43..65
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 66..98
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P83362"
FT REGION 78..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..98
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 84
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 88
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
SQ SEQUENCE 98 AA; 11059 MW; AFB19561B602B409 CRC64;
MLDIQTHMDF AGQGKAERWS RFIITFFGIV GLVYGAFVQQ FSQTVYILGA GFVLSSLITI
PPWPLYRRNA LKWQKPIDTD AKSSSSESGD EGKKKKKQ
