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SYB_DROME
ID   SYB_DROME               Reviewed;         152 AA.
AC   P18489; B7YZD5; B7YZD6; Q3HKB4; Q8MKX1; Q9V5I6;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 3.
DT   03-AUG-2022, entry version 174.
DE   RecName: Full=Synaptobrevin {ECO:0000303|PubMed:8229205};
GN   Name=Syb {ECO:0000303|PubMed:8229205, ECO:0000312|FlyBase:FBgn0003660};
GN   ORFNames=CG12210 {ECO:0000312|FlyBase:FBgn0003660};
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 [MRNA] (ISOFORM SYB-A).
RX   PubMed=2560644; DOI=10.1016/0896-6273(89)90193-1;
RA   Suedhof T.C., Baumert M., Perin M.S., Jahn R.;
RT   "A synaptic vesicle membrane protein is conserved from mammals to
RT   Drosophila.";
RL   Neuron 2:1475-1481(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORMS SYB-A AND
RP   SYB-B), AND TISSUE SPECIFICITY.
RX   PubMed=8406010; DOI=10.1016/0378-1119(93)90291-a;
RA   Chin A.C., Burgess R.W., Wong B.R., Schwarz T.L., Scheller R.H.;
RT   "Differential expression of transcripts from syb, a Drosophila melanogaster
RT   gene encoding VAMP (synaptobrevin) that is abundant in non-neuronal
RT   cells.";
RL   Gene 131:175-181(1993).
RN   [3]
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   [4]
RP   GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND SYB-B).
RC   STRAIN=Berkeley; TISSUE=Embryo;
RA   Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA   Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA   Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA   Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA   Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL   Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=8229205; DOI=10.1523/jneurosci.13-11-04924.1993;
RA   DiAntonio A., Burgess R.W., Chin A.C., Deitcher D.L., Scheller R.H.,
RA   Schwarz T.L.;
RT   "Identification and characterization of Drosophila genes for synaptic
RT   vesicle proteins.";
RL   J. Neurosci. 13:4924-4935(1993).
RN   [7]
RP   FUNCTION, SUBUNIT, AND DISRUPTION PHENOTYPE.
RX   PubMed=12364587; DOI=10.1073/pnas.202335999;
RA   Bhattacharya S., Stewart B.A., Niemeyer B.A., Burgess R.W., McCabe B.D.,
RA   Lin P., Boulianne G., O'Kane C.J., Schwarz T.L.;
RT   "Members of the synaptobrevin/vesicle-associated membrane protein (VAMP)
RT   family in Drosophila are functionally interchangeable in vivo for
RT   neurotransmitter release and cell viability.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:13867-13872(2002).
RN   [8]
RP   UBIQUITINATION.
RX   PubMed=23353890; DOI=10.1038/emboj.2013.1;
RA   Yamazaki Y., Schoenherr C., Varshney G.K., Dogru M., Hallberg B.,
RA   Palmer R.H.;
RT   "Goliath family E3 ligases regulate the recycling endosome pathway via
RT   VAMP3 ubiquitylation.";
RL   EMBO J. 32:524-537(2013).
RN   [9]
RP   UBIQUITINATION.
RX   PubMed=26974662; DOI=10.1038/ncb3325;
RA   Yamazaki Y., Palmer L., Alexandre C., Kakugawa S., Beckett K., Gaugue I.,
RA   Palmer R.H., Vincent J.P.;
RT   "Godzilla-dependent transcytosis promotes Wingless signalling in Drosophila
RT   wing imaginal discs.";
RL   Nat. Cell Biol. 18:451-457(2016).
RN   [10]
RP   SUBCELLULAR LOCATION.
RX   PubMed=27323327; DOI=10.1038/ncb3374;
RA   Caviglia S., Brankatschk M., Fischer E.J., Eaton S., Luschnig S.;
RT   "Staccato/Unc-13-4 controls secretory lysosome-mediated lumen fusion during
RT   epithelial tube anastomosis.";
RL   Nat. Cell Biol. 18:727-739(2016).
CC   -!- FUNCTION: Involved in the targeting and/or fusion of transport vesicles
CC       to their target membrane. {ECO:0000269|PubMed:12364587}.
CC   -!- SUBUNIT: Part of the SNARE core complex containing Snap25 and syntaxin.
CC       {ECO:0000269|PubMed:12364587}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic
CC       vesicle membrane {ECO:0000250|UniProtKB:Q9W0C1}; Single-pass type IV
CC       membrane protein {ECO:0000255}. Cell membrane
CC       {ECO:0000269|PubMed:27323327}; Single-pass type IV membrane protein
CC       {ECO:0000255}. Note=Neuronal synaptic vesicles (By similarity). In
CC       embryos, expressed in the plasma membrane of tracheal cells
CC       (PubMed:27323327). {ECO:0000250|UniProtKB:P63027,
CC       ECO:0000269|PubMed:27323327}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC         Comment=The ratio of isoform Syb-A to isoform Syb-B is highly
CC         regulated during development.;
CC       Name=Syb-A; Synonyms=C;
CC         IsoId=P18489-1; Sequence=Displayed;
CC       Name=Syb-B; Synonyms=B;
CC         IsoId=P18489-2; Sequence=VSP_006327, VSP_006328;
CC       Name=A;
CC         IsoId=P18489-3; Sequence=VSP_016074;
CC       Name=D;
CC         IsoId=P18489-4; Sequence=VSP_016074, VSP_006327, VSP_006328;
CC   -!- TISSUE SPECIFICITY: Not nervous system-specific; abundant in cells of
CC       the gut and Malpighian tubules. {ECO:0000269|PubMed:8229205,
CC       ECO:0000269|PubMed:8406010}.
CC   -!- PTM: Ubiquitinated by gzl, regulating endocytic trafficking
CC       (PubMed:23353890). In wing imaginal disks, ubiquitination by gzl
CC       promotes transcytosis of wingless (wg) to the basolateral surface
CC       (PubMed:26974662). {ECO:0000269|PubMed:23353890,
CC       ECO:0000269|PubMed:26974662}.
CC   -!- DISRUPTION PHENOTYPE: Cell lethality. {ECO:0000269|PubMed:12364587}.
CC   -!- SIMILARITY: Belongs to the synaptobrevin family. {ECO:0000305}.
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DR   EMBL; X76200; CAA53793.1; -; mRNA.
DR   EMBL; L14270; AAA28923.1; -; Genomic_DNA.
DR   EMBL; L14270; AAA28924.1; -; Genomic_DNA.
DR   EMBL; AE013599; AAF58820.1; -; Genomic_DNA.
DR   EMBL; AE013599; AAM68777.1; -; Genomic_DNA.
DR   EMBL; AE013599; ACL83087.1; -; Genomic_DNA.
DR   EMBL; AE013599; ACL83088.1; -; Genomic_DNA.
DR   EMBL; BT003769; AAO41448.1; -; mRNA.
DR   EMBL; BT009942; AAQ22411.1; -; mRNA.
DR   PIR; JC1521; JC1521.
DR   PIR; JC1522; JC1522.
DR   RefSeq; NP_001137633.1; NM_001144161.2. [P18489-1]
DR   RefSeq; NP_001137634.1; NM_001144162.2. [P18489-4]
DR   RefSeq; NP_001286278.1; NM_001299349.1. [P18489-3]
DR   RefSeq; NP_523680.1; NM_078956.4. [P18489-3]
DR   RefSeq; NP_724906.1; NM_165756.3. [P18489-2]
DR   AlphaFoldDB; P18489; -.
DR   SMR; P18489; -.
DR   BioGRID; 61901; 62.
DR   IntAct; P18489; 3.
DR   STRING; 7227.FBpp0271782; -.
DR   PaxDb; P18489; -.
DR   PRIDE; P18489; -.
DR   DNASU; 36080; -.
DR   EnsemblMetazoa; FBtr0088362; FBpp0087450; FBgn0003660. [P18489-3]
DR   EnsemblMetazoa; FBtr0088363; FBpp0087451; FBgn0003660. [P18489-2]
DR   EnsemblMetazoa; FBtr0273274; FBpp0271782; FBgn0003660. [P18489-1]
DR   EnsemblMetazoa; FBtr0273275; FBpp0271783; FBgn0003660. [P18489-4]
DR   EnsemblMetazoa; FBtr0339455; FBpp0308541; FBgn0003660. [P18489-3]
DR   GeneID; 36080; -.
DR   KEGG; dme:Dmel_CG12210; -.
DR   CTD; 36080; -.
DR   FlyBase; FBgn0003660; Syb.
DR   VEuPathDB; VectorBase:FBgn0003660; -.
DR   eggNOG; KOG0860; Eukaryota.
DR   GeneTree; ENSGT00940000170580; -.
DR   InParanoid; P18489; -.
DR   OMA; CQDTFAT; -.
DR   PhylomeDB; P18489; -.
DR   Reactome; R-DME-181429; Serotonin Neurotransmitter Release Cycle.
DR   Reactome; R-DME-181430; Norepinephrine Neurotransmitter Release Cycle.
DR   Reactome; R-DME-199992; trans-Golgi Network Vesicle Budding.
DR   Reactome; R-DME-210500; Glutamate Neurotransmitter Release Cycle.
DR   Reactome; R-DME-212676; Dopamine Neurotransmitter Release Cycle.
DR   Reactome; R-DME-264642; Acetylcholine Neurotransmitter Release Cycle.
DR   Reactome; R-DME-432720; Lysosome Vesicle Biogenesis.
DR   Reactome; R-DME-432722; Golgi Associated Vesicle Biogenesis.
DR   Reactome; R-DME-449836; Other interleukin signaling.
DR   Reactome; R-DME-6798695; Neutrophil degranulation.
DR   Reactome; R-DME-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR   Reactome; R-DME-8856828; Clathrin-mediated endocytosis.
DR   Reactome; R-DME-888590; GABA synthesis, release, reuptake and degradation.
DR   Reactome; R-DME-9609523; Insertion of tail-anchored proteins into the endoplasmic reticulum membrane.
DR   SignaLink; P18489; -.
DR   BioGRID-ORCS; 36080; 0 hits in 3 CRISPR screens.
DR   GenomeRNAi; 36080; -.
DR   PRO; PR:P18489; -.
DR   Proteomes; UP000000803; Chromosome 2R.
DR   Bgee; FBgn0003660; Expressed in saliva-secreting gland and 31 other tissues.
DR   ExpressionAtlas; P18489; baseline and differential.
DR   Genevisible; P18489; DM.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043005; C:neuron projection; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0031201; C:SNARE complex; IBA:GO_Central.
DR   GO; GO:0008021; C:synaptic vesicle; ISS:FlyBase.
DR   GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005484; F:SNAP receptor activity; ISS:FlyBase.
DR   GO; GO:0000149; F:SNARE binding; IDA:UniProtKB.
DR   GO; GO:0019905; F:syntaxin binding; IBA:GO_Central.
DR   GO; GO:0007269; P:neurotransmitter secretion; NAS:FlyBase.
DR   GO; GO:0031340; P:positive regulation of vesicle fusion; IDA:UniProtKB.
DR   GO; GO:0016081; P:synaptic vesicle docking; ISS:FlyBase.
DR   GO; GO:0006906; P:vesicle fusion; IDA:UniProtKB.
DR   GO; GO:0016192; P:vesicle-mediated transport; ISS:FlyBase.
DR   InterPro; IPR001388; Synaptobrevin.
DR   InterPro; IPR016444; Synaptobrevin/VAMP.
DR   InterPro; IPR042855; V_SNARE_CC.
DR   PANTHER; PTHR45701; PTHR45701; 1.
DR   Pfam; PF00957; Synaptobrevin; 1.
DR   PRINTS; PR00219; SYNAPTOBREVN.
DR   PROSITE; PS00417; SYNAPTOBREVIN; 1.
DR   PROSITE; PS50892; V_SNARE; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Coiled coil; Cytoplasmic vesicle;
KW   Membrane; Reference proteome; Synapse; Transmembrane; Transmembrane helix;
KW   Ubl conjugation.
FT   CHAIN           1..152
FT                   /note="Synaptobrevin"
FT                   /id="PRO_0000206741"
FT   TOPO_DOM        1..110
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        111..130
FT                   /note="Helical; Anchor for type IV membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        131..152
FT                   /note="Vesicular"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          47..107
FT                   /note="v-SNARE coiled-coil homology"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00290"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          133..152
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         16..39
FT                   /note="DFPILPPPPNANDNYNQFGDHQIR -> E (in isoform A and
FT                   isoform D)"
FT                   /evidence="ECO:0000303|Ref.5"
FT                   /id="VSP_016074"
FT   VAR_SEQ         130..132
FT                   /note="VWP -> LFN (in isoform D and isoform Syb-B)"
FT                   /evidence="ECO:0000303|Ref.5"
FT                   /id="VSP_006327"
FT   VAR_SEQ         133..152
FT                   /note="Missing (in isoform D and isoform Syb-B)"
FT                   /evidence="ECO:0000303|Ref.5"
FT                   /id="VSP_006328"
FT   CONFLICT        93
FT                   /note="F -> S (in Ref. 2; AAA28924/AAA28923)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   152 AA;  16712 MW;  FB5E7DE5789DAA09 CRC64;
     MENNEAPSPS GSNNNDFPIL PPPPNANDNY NQFGDHQIRN NNAAQKKLQQ TQAKVDEVVG
     IMRVNVEKVL ERDQKLSELG ERADQLEQGA SQFEQQAGKL KRKQWWANMK MMIILGVIAV
     VLLIIVLVSV WPSSSDSGSG GGNKAITQAP PH
 
 
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