SPCS3_DROME
ID SPCS3_DROME Reviewed; 179 AA.
AC Q9VCA9;
DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Signal peptidase complex subunit 3;
DE AltName: Full=Microsomal signal peptidase 22 kDa subunit;
DE Short=SPC22;
DE Short=SPase 22 kDa subunit;
GN Name=Spase22-23; ORFNames=CG5677;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4]
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 [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: Essential component of the signal peptidase complex (SPC)
CC which catalyzes the cleavage of N-terminal signal sequences from
CC nascent proteins as they are translocated into the lumen of the
CC endoplasmic reticulum (By similarity). Essential for the SPC catalytic
CC activity, possibly by stabilizing and positioning the active center of
CC the complex close to the lumenal surface (By similarity).
CC {ECO:0000250|UniProtKB:P61009, ECO:0000250|UniProtKB:Q12133}.
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:P61009}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P61008}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:P61008}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown reduces infection by West
CC Nile virus (WNV) and Dengue virus type 2 (DENV-2).
CC {ECO:0000269|PubMed:27383988}.
CC -!- SIMILARITY: Belongs to the SPCS3 family. {ECO:0000305}.
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DR EMBL; AE014297; AAF56264.1; -; Genomic_DNA.
DR EMBL; AY070615; AAL48086.1; -; mRNA.
DR RefSeq; NP_001247279.1; NM_001260350.2.
DR RefSeq; NP_651234.1; NM_142977.5.
DR AlphaFoldDB; Q9VCA9; -.
DR SMR; Q9VCA9; -.
DR BioGRID; 67815; 2.
DR DIP; DIP-22148N; -.
DR STRING; 7227.FBpp0293581; -.
DR GlyGen; Q9VCA9; 2 sites.
DR PaxDb; Q9VCA9; -.
DR PRIDE; Q9VCA9; -.
DR DNASU; 42885; -.
DR EnsemblMetazoa; FBtr0084564; FBpp0083949; FBgn0039172.
DR EnsemblMetazoa; FBtr0305044; FBpp0293581; FBgn0039172.
DR GeneID; 42885; -.
DR KEGG; dme:Dmel_CG5677; -.
DR CTD; 42885; -.
DR FlyBase; FBgn0039172; Spase22-23.
DR VEuPathDB; VectorBase:FBgn0039172; -.
DR eggNOG; KOG3372; Eukaryota.
DR GeneTree; ENSGT00940000169388; -.
DR HOGENOM; CLU_068714_1_0_1; -.
DR InParanoid; Q9VCA9; -.
DR OMA; FGCFVTT; -.
DR OrthoDB; 1514162at2759; -.
DR PhylomeDB; Q9VCA9; -.
DR BioGRID-ORCS; 42885; 1 hit in 1 CRISPR screen.
DR ChiTaRS; Spase22-23; fly.
DR GenomeRNAi; 42885; -.
DR PRO; PR:Q9VCA9; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0039172; Expressed in male reproductive gland and 25 other tissues.
DR ExpressionAtlas; Q9VCA9; baseline and differential.
DR Genevisible; Q9VCA9; DM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; IPR007653; SPC3.
DR PANTHER; PTHR12804; PTHR12804; 1.
DR Pfam; PF04573; SPC22; 1.
DR PIRSF; PIRSF016089; SPC22; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Glycoprotein; Membrane; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..179
FT /note="Signal peptidase complex subunit 3"
FT /id="PRO_0000218944"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P61008"
FT TRANSMEM 13..33
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 34..179
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P61008"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 141
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 179 AA; 20304 MW; 0B8440032A2B2DB5 CRC64;
MHTVLTRGNA TVAYTLSVLA CLTFSCFLST VFLDYRTDAN INTVRVLVKN VPDYGASREK
HDLGFVTFDL QTNLTGIFNW NVKQLFLYLT AEYQTPANQL NQVVLWDKII LRGDNAVLDF
KNMNTKYYFW DDGNGLKDNR NVSLYLSWNI IPNAGLLPSV QATGKHLFKF PADYATSSI
