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A76A_DROME
ID   A76A_DROME              Reviewed;         386 AA.
AC   Q9VVW1; O46224;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 2.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=Accessory gland protein Acp76A;
DE   Flags: Precursor;
GN   Name=Acp76A; ORFNames=CG3801;
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|EMBL:AAG38149.1};
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND TISSUE SPECIFICITY.
RC   STRAIN=Canton-S; TISSUE=Male accessory gland;
RX   PubMed=9474779; DOI=10.1016/s0965-1748(97)00056-8;
RA   Wolfner M.F., Harada H.A., Bertram M.J., Stelick T.J., Kraus K.W.,
RA   Kalb J.M., Lung Y.O., Neubaum D.M., Park M., Tram U.K.;
RT   "New genes for male accessory gland proteins in Drosophila melanogaster.";
RL   Insect Biochem. Mol. Biol. 27:825-834(1997).
RN   [2] {ECO:0000305}
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   [3]
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   [4] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 22-386.
RC   STRAIN=ZIM10C, ZIM12C, ZIM16C, ZIM18C, ZIM28C, ZIM30C, ZIM34C, ZIM53C,
RC   ZIM5C, and ZIM7C;
RX   PubMed=11102381; DOI=10.1093/genetics/156.4.1879;
RA   Begun D.J., Whitley P., Todd B.L., Waldrip-Dail H.M., Clark A.G.;
RT   "Molecular population genetics of male accessory gland proteins in
RT   Drosophila.";
RL   Genetics 156:1879-1888(2000).
CC   -!- FUNCTION: Responsible for physiological and behavioral changes in mated
CC       female flies. May play a role in accessory protein regulation and/or in
CC       the coagulation of seminal fluid to form a mating plug.
CC       {ECO:0000269|PubMed:9474779}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Main cells of accessory gland and seminal fluid.
CC       {ECO:0000269|PubMed:9474779}.
CC   -!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}.
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DR   EMBL; U90947; AAB96393.1; -; Genomic_DNA.
DR   EMBL; AE014296; AAF49196.1; -; Genomic_DNA.
DR   EMBL; AY010627; AAG38149.1; -; Genomic_DNA.
DR   EMBL; AY010628; AAG38150.1; -; Genomic_DNA.
DR   EMBL; AY010629; AAG38151.1; -; Genomic_DNA.
DR   EMBL; AY010630; AAG38152.1; -; Genomic_DNA.
DR   EMBL; AY010631; AAG38153.1; -; Genomic_DNA.
DR   EMBL; AY010632; AAG38154.1; -; Genomic_DNA.
DR   EMBL; AY010633; AAG38155.1; -; Genomic_DNA.
DR   EMBL; AY010634; AAG38156.1; -; Genomic_DNA.
DR   EMBL; AY010635; AAG38157.1; -; Genomic_DNA.
DR   EMBL; AY010636; AAG38158.1; -; Genomic_DNA.
DR   RefSeq; NP_524153.1; NM_079429.2.
DR   AlphaFoldDB; Q9VVW1; -.
DR   SMR; Q9VVW1; -.
DR   STRING; 7227.FBpp0074805; -.
DR   GlyGen; Q9VVW1; 2 sites.
DR   PaxDb; Q9VVW1; -.
DR   EnsemblMetazoa; FBtr0075038; FBpp0074805; FBgn0015586.
DR   GeneID; 40078; -.
DR   KEGG; dme:Dmel_CG3801; -.
DR   CTD; 40078; -.
DR   FlyBase; FBgn0015586; Acp76A.
DR   VEuPathDB; VectorBase:FBgn0015586; -.
DR   eggNOG; KOG2392; Eukaryota.
DR   OrthoDB; 1124079at2759; -.
DR   PhylomeDB; Q9VVW1; -.
DR   BioGRID-ORCS; 40078; 0 hits in 1 CRISPR screen.
DR   GenomeRNAi; 40078; -.
DR   PRO; PR:Q9VVW1; -.
DR   Proteomes; UP000000803; Chromosome 3L.
DR   Bgee; FBgn0015586; Expressed in male reproductive gland and 9 other tissues.
DR   ExpressionAtlas; Q9VVW1; differential.
DR   Genevisible; Q9VVW1; DM.
DR   GO; GO:0005615; C:extracellular space; IDA:FlyBase.
DR   GO; GO:0007610; P:behavior; IEA:UniProtKB-KW.
DR   GO; GO:0010466; P:negative regulation of peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0019953; P:sexual reproduction; HEP:FlyBase.
DR   Gene3D; 2.30.39.10; -; 1.
DR   Gene3D; 3.30.497.10; -; 1.
DR   InterPro; IPR023795; Serpin_CS.
DR   InterPro; IPR023796; Serpin_dom.
DR   InterPro; IPR000215; Serpin_fam.
DR   InterPro; IPR036186; Serpin_sf.
DR   InterPro; IPR042178; Serpin_sf_1.
DR   InterPro; IPR042185; Serpin_sf_2.
DR   PANTHER; PTHR11461; PTHR11461; 1.
DR   Pfam; PF00079; Serpin; 1.
DR   SMART; SM00093; SERPIN; 1.
DR   SUPFAM; SSF56574; SSF56574; 1.
DR   PROSITE; PS00284; SERPIN; 1.
PE   2: Evidence at transcript level;
KW   Behavior; Glycoprotein; Protease inhibitor; Reference proteome; Secreted;
KW   Serine protease inhibitor; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000305"
FT   CHAIN           23..386
FT                   /note="Accessory gland protein Acp76A"
FT                   /id="PRO_0000032528"
FT   SITE            339..340
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        24
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        378
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VARIANT         22
FT                   /note="Q -> H (in strain: ZIM5C, ZIM10C, ZIM16C, ZIM18C,
FT                   ZIM28C, ZIM30C, ZIM34C and ZIM53C)"
FT                   /evidence="ECO:0000305"
FT   VARIANT         22
FT                   /note="Q -> P (in strain: ZIM7C and ZIM12C)"
FT                   /evidence="ECO:0000305"
FT   VARIANT         332..337
FT                   /note="EVVDDI -> GKRNTR (in strain: ZIM28C)"
FT   VARIANT         338
FT                   /note="D -> N (in strain: Canton-S and ZIM34C)"
FT   VARIANT         359
FT                   /note="I -> V (in strain: Canton-S, ZIM12C and ZIM16C)"
FT   VARIANT         381
FT                   /note="K -> M (in strain: ZIM5C and ZIM16C)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        7
FT                   /note="I -> T (in Ref. 1; AAB96393)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        64..65
FT                   /note="NN -> TI (in Ref. 4; AAG38149/AAG38150)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        91
FT                   /note="Y -> S (in Ref. 4; AAG38149/AAG38150/AAG38151/
FT                   AAG38152/AAG38153/AAG38154/AAG38155/AAG38156/AAG38157/
FT                   AAG38158)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        141
FT                   /note="K -> T (in Ref. 4; AAG38149/AAG38150/AAG38151/
FT                   AAG38152/AAG38153/AAG38154/AAG38155/AAG38156/AAG38157/
FT                   AAG38158)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        145
FT                   /note="E -> A (in Ref. 4; AAG38149/AAG38150/AAG38151/
FT                   AAG38152/AAG38153/AAG38154/AAG38155/AAG38156/AAG38157/
FT                   AAG38158)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        165..167
FT                   /note="NAG -> YAA (in Ref. 4; AAG38149/AAG38150)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        172
FT                   /note="A -> S (in Ref. 4; AAG38149/AAG38150/AAG38151/
FT                   AAG38152/AAG38153/AAG38154/AAG38155/AAG38156/AAG38157/
FT                   AAG38158)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        182
FT                   /note="W -> C (in Ref. 4; AAG38149/AAG38150/AAG38151/
FT                   AAG38152/AAG38153/AAG38154/AAG38155/AAG38156/AAG38157/
FT                   AAG38158)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        191
FT                   /note="N -> I (in Ref. 4; AAG38149/AAG38150/AAG38151/
FT                   AAG38152/AAG38153/AAG38154/AAG38155/AAG38156/AAG38157/
FT                   AAG38158)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        202
FT                   /note="Y -> H (in Ref. 4; AAG38149/AAG38150/AAG38151/
FT                   AAG38152/AAG38153/AAG38154/AAG38155/AAG38156/AAG38157/
FT                   AAG38158)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        238
FT                   /note="N -> Y (in Ref. 4; AAG38149/AAG38150/AAG38151/
FT                   AAG38152/AAG38153/AAG38154/AAG38155/AAG38156/AAG38157/
FT                   AAG38158)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   386 AA;  43967 MW;  D2640A616B3F0FC8 CRC64;
     MGNHQVIFLV LCTSLLFQNT IQQNVSFQLI REIDRYTPEN FVLSVLNIEM ILFEIHAAKA
     VESNNDLERS LIINFGYSEA RQEVLDWGLR YKKASSAKFQ MANKVAVSQK LPLSQKLRLV
     NEVLMTSAKK YDVTKDVRPS KLMDEWLSSH LDGVLANFVQ EKKLNAGENI VAISGMTVTP
     LWASHFQSEI NRYFVNNPGT GYASKDPTCV PMMHSLSSFE TMSTDEAKGI YIPFSSANLG
     MLILLPRKGV TCKDILDNLN NQINVEYNDH KDVHLLLPIF KEKFDYNIAK FFNGINIEDT
     FKDSAFKSKA KIKINNFRVN HGIRFQPILR LEVVDDIDTG KTETFEVNRP FVFVIKDKIN
     VYAVGRIENL DGLTDKVNCS KKYADL
 
 
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