STNB_DROME
ID STNB_DROME Reviewed; 1262 AA.
AC Q24212; A4V4V9; Q7PLF4; Q9W5J3;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 4.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Protein stoned-B;
DE Short=Stn-B;
DE Short=StonedB;
GN Name=stnB; ORFNames=CG12473;
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].
RC STRAIN=Oregon-R; TISSUE=CNS;
RX PubMed=8844157; DOI=10.1093/genetics/143.4.1699;
RA Andrews J., Smith M., Merakovsky J., Coulson M., Hannan F., Kelly L.E.;
RT "The stoned locus of Drosophila melanogaster produces a dicistronic
RT transcript and encodes two distinct polypeptides.";
RL Genetics 143:1699-1711(1996).
RN [2]
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]
RP FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=10407025; DOI=10.1523/jneurosci.19-14-05847.1999;
RA Fergestad T., Davis W.S., Broadie K.;
RT "The stoned proteins regulate synaptic vesicle recycling in the presynaptic
RT terminal.";
RL J. Neurosci. 19:5847-5860(1999).
RN [5]
RP INTERACTION WITH SYT.
RX PubMed=11069931; DOI=10.1523/jneurosci.20-22-08254.2000;
RA Phillips A.M., Smith M., Ramaswami M., Kelly L.E.;
RT "The products of the Drosophila stoned locus interact with synaptic
RT vesicles via synaptotagmin.";
RL J. Neurosci. 20:8254-8261(2000).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11160392; DOI=10.1523/jneurosci.21-04-01218.2001;
RA Fergestad T., Broadie K.;
RT "Interaction of stoned and synaptotagmin in synaptic vesicle endocytosis.";
RL J. Neurosci. 21:1218-1227(2001).
RN [7]
RP FUNCTION.
RX PubMed=11312288; DOI=10.1523/jneurosci.21-09-03034.2001;
RA Stimson D.T., Estes P.S., Rao S., Krishnan K.S., Kelly L.E., Ramaswami M.;
RT "Drosophila stoned proteins regulate the rate and fidelity of synaptic
RT vesicle internalization.";
RL J. Neurosci. 21:3034-3044(2001).
RN [8]
RP RNA EDITING OF POSITION 1186.
RX PubMed=12907802; DOI=10.1126/science.1086763;
RA Hoopengardner B., Bhalla T., Staber C., Reenan R.;
RT "Nervous system targets of RNA editing identified by comparative
RT genomics.";
RL Science 301:832-836(2003).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-623 AND SER-626, AND
RP 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).
CC -!- FUNCTION: Adapter protein involved in endocytic recycling of synaptic
CC vesicles membranes. May act by mediating the retrieval of synaptotagmin
CC protein Syt from the plasma membrane, thereby facilitating the
CC internalization of multiple synaptic vesicles from the plasma membrane.
CC {ECO:0000269|PubMed:10407025, ECO:0000269|PubMed:11160392,
CC ECO:0000269|PubMed:11312288}.
CC -!- SUBUNIT: Interacts with the second C2 domain of Syt.
CC {ECO:0000269|PubMed:11069931}.
CC -!- INTERACTION:
CC Q24212; P21521: Syt1; NbExp=5; IntAct=EBI-604879, EBI-484504;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10407025,
CC ECO:0000269|PubMed:11160392}. Synapse {ECO:0000269|PubMed:10407025,
CC ECO:0000269|PubMed:11160392}. Note=Colocalizes with synaptic vesicle
CC pools. Colocalizes with the endocytic network within synaptic boutons.
CC {ECO:0000269|PubMed:10407025, ECO:0000269|PubMed:11160392}.
CC -!- DEVELOPMENTAL STAGE: Present at synaptic connections both in the CNS
CC and in neuromuscular junctions in the mature embryo (20-22h) and
CC throughout larval development. In the third instar larva, it is
CC expressed in all synaptic bouton types, including I, II and III
CC boutons. {ECO:0000269|PubMed:10407025}.
CC -!- DOMAIN: The Asn-Pro-Phe (NPF) motifs, which are found in proteins
CC involved in the endocytic pathway, are known to interact with the EH
CC domain. {ECO:0000250}.
CC -!- RNA EDITING: Modified_positions=1186 {ECO:0000269|PubMed:12907802};
CC Note=Partially edited.;
CC -!- MISCELLANEOUS: StnA, which is involved in the same pathway, is derived
CC from the same bicistronic transcript that encodes these two different
CC proteins.
CC -!- SIMILARITY: Belongs to the Stoned B family. {ECO:0000305}.
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DR EMBL; U54982; AAC16666.1; -; mRNA.
DR EMBL; AE014298; ABI31012.2; -; Genomic_DNA.
DR EMBL; AE014298; EAA46059.3; -; Genomic_DNA.
DR PIR; T13353; T13353.
DR RefSeq; NP_001036318.2; NM_001042853.3.
DR RefSeq; NP_001036319.2; NM_001042854.3.
DR RefSeq; NP_001285539.1; NM_001298610.1.
DR AlphaFoldDB; Q24212; -.
DR BioGRID; 607063; 3.
DR ELM; Q24212; -.
DR IntAct; Q24212; 4.
DR STRING; 7227.FBpp0291230; -.
DR iPTMnet; Q24212; -.
DR PaxDb; Q24212; -.
DR EnsemblMetazoa; FBtr0302020; FBpp0291230; FBgn0016975.
DR EnsemblMetazoa; FBtr0302021; FBpp0291231; FBgn0016975.
DR EnsemblMetazoa; FBtr0344111; FBpp0310530; FBgn0016975.
DR GeneID; 4379834; -.
DR KEGG; dme:Dmel_CG12473; -.
DR UCSC; CG12473-RB; d. melanogaster.
DR CTD; 4379834; -.
DR FlyBase; FBgn0016975; stnB.
DR VEuPathDB; VectorBase:FBgn0016975; -.
DR eggNOG; KOG2677; Eukaryota.
DR InParanoid; Q24212; -.
DR PhylomeDB; Q24212; -.
DR Reactome; R-DME-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-DME-8856828; Clathrin-mediated endocytosis.
DR BioGRID-ORCS; 4379834; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 4379834; -.
DR PRO; PR:Q24212; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0016975; Expressed in brain and 4 other tissues.
DR Genevisible; Q24212; DM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030136; C:clathrin-coated vesicle; IBA:GO_Central.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0030139; C:endocytic vesicle; IDA:UniProtKB.
DR GO; GO:0048786; C:presynaptic active zone; IDA:FlyBase.
DR GO; GO:0008021; C:synaptic vesicle; IGI:FlyBase.
DR GO; GO:0035615; F:clathrin adaptor activity; IBA:GO_Central.
DR GO; GO:0097110; F:scaffold protein binding; IPI:FlyBase.
DR GO; GO:0007268; P:chemical synaptic transmission; IMP:FlyBase.
DR GO; GO:0030100; P:regulation of endocytosis; IBA:GO_Central.
DR GO; GO:1900242; P:regulation of synaptic vesicle endocytosis; IMP:FlyBase.
DR GO; GO:0099504; P:synaptic vesicle cycle; IEP:FlyBase.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; IMP:UniProtKB.
DR GO; GO:0048489; P:synaptic vesicle transport; IMP:UniProtKB.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR InterPro; IPR036168; AP2_Mu_C_sf.
DR InterPro; IPR028565; MHD.
DR InterPro; IPR012320; SHD_dom.
DR InterPro; IPR017110; Stonin.
DR Pfam; PF00928; Adap_comp_sub; 1.
DR PIRSF; PIRSF037099; Stonin; 1.
DR SUPFAM; SSF49447; SSF49447; 1.
DR PROSITE; PS51072; MHD; 1.
DR PROSITE; PS51070; SHD; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Endocytosis; Phosphoprotein; Reference proteome; Repeat;
KW RNA editing; Synapse.
FT CHAIN 1..1262
FT /note="Protein stoned-B"
FT /id="PRO_0000185735"
FT DOMAIN 728..902
FT /note="SHD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00403"
FT DOMAIN 906..1219
FT /note="MHD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00404"
FT REGION 17..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 49..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 225..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 474..507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 643..709
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 847..1108
FT /note="Interaction with Syt"
FT REGION 1226..1262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 3..5
FT /note="NPF 1"
FT MOTIF 19..21
FT /note="NPF 2"
FT MOTIF 33..35
FT /note="NPF 3"
FT MOTIF 43..45
FT /note="NPF 4"
FT MOTIF 210..212
FT /note="NPF 5"
FT MOTIF 493..495
FT /note="NPF 6"
FT MOTIF 673..675
FT /note="NPF 7"
FT COMPBIAS 86..101
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..125
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..269
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..344
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..405
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..448
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 693..709
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1243..1262
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 623
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 626
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VARIANT 1186
FT /note="T -> A (in RNA edited version)"
FT CONFLICT 657..658
FT /note="RG -> VE (in Ref. 1; AAC16666)"
FT /evidence="ECO:0000305"
FT CONFLICT 1012
FT /note="L -> V (in Ref. 1; AAC16666)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1262 AA; 137781 MW; 877E3EE6B964C23A CRC64;
MANPFLMDED LDGCDAAANP FLMQSEPEPS SDNPFMAATV ASNPFAFGAD DLELGAEPEA
EATHDNDLDP AMSFFGTTIE AEDDTLSLKS GAEEEDEGKK PPQSQPQLQS HAHPHPPPPR
PLVPPQSTQD LISTVSSQLD ETSSELLGRI PATRSPSPVS MRDLHSPSPT PDSGLADLLD
VSVDSGSSAH TQGIEADLIS GVAGGVRLDN PFAVPTAVPN IQAAVPLPAT PIKQPPRPPP
PRPAPPRPAP PGQAAPQRPP PPLAAVNPPP AAPEADDLLD MFGTTACKPA KPPPPKSKED
ILSLFEQPHV PLSQPASKPD LLHDDLDETI GEGEPPEQEE PDTEQSNEIS SRDEPVFTSL
LIRPDESTHD ITSQPQAATG LERQVNNMAA PSGTASTQRA TTPDIEITTV EDLPRSDDED
EPEAMQEPET ETKPQIEPDT EPEIVSEHSP PTERLVTQAA LVDGELIAAE PEPEEMDTGL
DFPLASSGQL SANPFASPDE EEPNFAPMPA AVANIFAVND PDSQMETPKA PSHTANIFAS
DPDEFDAFSA KFDSVKKDNI SIMDGFGGSG AITPTGGDAW GGSAFGSTTI SANACGDTNS
ADDGFGNDDD DFYAMQAPAR ADSVESVDKD FSVVIRPMAE ETSGVAPQLA PPPPPARGVN
QAQTTSLPGL TVNPFEDVSG FPAPGLPPTD GTAIKRTDSQ DTPQTPLYDE DVSQPLEEFP
RLHYIGPGWE MQLRQPNKKK ITGQRFWKKI VVRLVVQNDV PVVQLLNQAG DKQPFQELPL
QPSYSVSEIG AQQYDQFGKI FTMKLQYIFY KERPGVRPGQ VTKAERITNK LTKFAQYAIA
GDYEGVKEFG SDLKKLGLPV EHAPQSSQLF KIGSMNYEDM KQFSVCIEEA LFKIPALRER
ALTYKMEEVQ VTAVDEITVE QDFEGKILKQ IARVRLFFLA FLTGMPTIEL GVNDMWRQGK
EVVGRHDIIP VATEEWIRLE AVEFHSVVNQ KEYERTRTIK FQPPDANYIE LLRFRVRPPK
NRELPLQLKA TWCVSGNKVE LRADILVPGF TSRKLGQIPC EDVSVRFPIP ECWIYLFRVE
KHFRYGSVKS AHRRTGKIKG IERILGAVDT LQESLIEVTS GQAKYEHHHR AIVWRCPRLP
KEGQGAYTTH QLVCRMALTS YDQIPSELAP YAFVEFTMPA TQVSHTTVRS VSVQDSDGDE
PPEKYVRYLA RHEYKVGIET THGESTNAYL AATRPIREEP PTTATKPTAS PVAPSDSDTD
SN
