SEMS_DROME
ID SEMS_DROME Reviewed; 275 AA.
AC Q9VP95; C1C3F2; Q4QQ23; Q4QQ30;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Seminase {ECO:0000303|PubMed:22253601};
DE EC=3.4.21.- {ECO:0000305};
DE Flags: Precursor;
GN Name=Sems {ECO:0000312|FlyBase:FBgn0037036};
GN ORFNames=CG10586 {ECO:0000312|FlyBase:FBgn0037036};
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 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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] {ECO:0000312|EMBL:ACO34939.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:ACO34939.1};
RA Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, CLEAVAGE, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=22253601; DOI=10.1371/journal.pgen.1002435;
RA LaFlamme B.A., Ram K.R., Wolfner M.F.;
RT "The Drosophila melanogaster seminal fluid protease 'seminase' regulates
RT proteolytic and post-mating reproductive processes.";
RL PLoS Genet. 8:E1002435-E1002435(2012).
RN [5] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24514904; DOI=10.1534/genetics.113.160101;
RA Laflamme B.A., Avila F.W., Michalski K., Wolfner M.F.;
RT "A Drosophila protease cascade member, seminal metalloprotease-1, is
RT activated stepwise by male factors and requires female factors for full
RT activity.";
RL Genetics 196:1117-1129(2014).
CC -!- FUNCTION: Seminal fluid protease which is required for cleavage and
CC probably also activation of the metalloprotease Semp1 (PubMed:22253601,
CC PubMed:24514904). Also required for a number of female post-mating
CC responses independent of Semp1 including egg laying and sperm usage
CC (PubMed:22253601). {ECO:0000269|PubMed:22253601,
CC ECO:0000269|PubMed:24514904}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22253601}.
CC Note=Secreted into seminal fluid. {ECO:0000269|PubMed:22253601}.
CC -!- TISSUE SPECIFICITY: Produced in the male accessory glands and secreted
CC into seminal fluid. {ECO:0000269|PubMed:22253601}.
CC -!- PTM: Undergoes cleavage in the male during mating with a cleaved
CC product detected in the ejaculatory duct and/or bulb of males by 8-10
CC minutes after the start of mating. Further cleavage occurs in the mated
CC female. {ECO:0000269|PubMed:22253601}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in males results in a
CC number of effects in females mated with these males including impaired
CC processing of the metalloprotease Semp1 and the accessory gland
CC proteins Acp26Aa and Acp36DE, lower levels of egg laying after the
CC first day post-mating, higher rates of sexual receptivity to subsequent
CC males and failure to release stored sperm from the female seminal
CC receptacle. {ECO:0000269|PubMed:22253601, ECO:0000269|PubMed:24514904}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255,
CC ECO:0000255|PROSITE-ProRule:PRU00274}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ACO34939.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE014296; AAF51660.1; -; Genomic_DNA.
DR EMBL; BT023574; AAY84974.1; -; mRNA.
DR EMBL; BT023586; AAY84986.1; -; mRNA.
DR EMBL; BT023593; AAY84993.1; -; mRNA.
DR EMBL; BT081381; ACO34939.1; ALT_INIT; mRNA.
DR RefSeq; NP_649270.1; NM_141013.2.
DR AlphaFoldDB; Q9VP95; -.
DR SMR; Q9VP95; -.
DR STRING; 7227.FBpp0077991; -.
DR MEROPS; S01.A29; -.
DR GlyGen; Q9VP95; 1 site.
DR PaxDb; Q9VP95; -.
DR PRIDE; Q9VP95; -.
DR DNASU; 40315; -.
DR EnsemblMetazoa; FBtr0078335; FBpp0077991; FBgn0037036.
DR GeneID; 40315; -.
DR KEGG; dme:Dmel_CG10586; -.
DR UCSC; CG10586-RA; d. melanogaster.
DR CTD; 40315; -.
DR FlyBase; FBgn0037036; Sems.
DR VEuPathDB; VectorBase:FBgn0037036; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000162823; -.
DR HOGENOM; CLU_006842_7_1_1; -.
DR InParanoid; Q9VP95; -.
DR OMA; MRYYNNF; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; Q9VP95; -.
DR BioGRID-ORCS; 40315; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 40315; -.
DR PRO; PR:Q9VP95; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0037036; Expressed in male reproductive gland and 5 other tissues.
DR Genevisible; Q9VP95; DM.
DR GO; GO:0005615; C:extracellular space; HDA:FlyBase.
DR GO; GO:0017171; F:serine hydrolase activity; HDA:FlyBase.
DR GO; GO:0004252; F:serine-type endopeptidase activity; ISM:FlyBase.
DR GO; GO:0045434; P:negative regulation of female receptivity, post-mating; IMP:FlyBase.
DR GO; GO:0006508; P:proteolysis; ISM:FlyBase.
DR GO; GO:0019953; P:sexual reproduction; HEP:FlyBase.
DR GO; GO:0046693; P:sperm storage; IMP:FlyBase.
DR GO; GO:0031638; P:zymogen activation; IMP:FlyBase.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 1.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Hydrolase; Protease; Reference proteome;
KW Secreted; Serine protease; Signal; Zymogen.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..?
FT /note="Activation peptide"
FT /evidence="ECO:0000305"
FT /id="PRO_0000436916"
FT CHAIN ?..275
FT /note="Seminase"
FT /evidence="ECO:0000305"
FT /id="PRO_5004338390"
FT DOMAIN 44..268
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 85
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 131
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 224
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT CARBOHYD 23
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 70..86
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 194..210
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 220..244
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ SEQUENCE 275 AA; 30337 MW; 44A51A2CB717A74D CRC64;
MKRLLFLFLL AGILINNHAL QHNETIDLKK LAKIVLPPAY QTRVIGGRVT TNAKLGGYLV
AMRYFNNFIC GGTLIHELIV LTAAHCFEDR AEKEAWSVDG GISRLSEKGI RRQVKRFIKS
AQFKMVTMNM DVAVVLLNRP MVGKNIGTLS LCSTALTPGQ TMDVSGWGMT NPDDEGPGHM
LRTVSVPVIE KRICREAYRE SVSISDSMFC ASVLGKKDAC TYDSGGPLVY EKQVCGIVSF
GIGCASRRYP GVYTDVHYVK PFIVKGIKAL LSRSR
