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SPART_DROME
ID   SPART_DROME             Reviewed;         553 AA.
AC   Q9VN45; Q86MQ7;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 130.
DE   RecName: Full=Protein spartin {ECO:0000303|PubMed:23439121};
GN   Name=spartin {ECO:0000312|FlyBase:FBgn0037265}; ORFNames=CG12001;
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] {ECO:0000312|EMBL:AAF52106.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
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:0000305, ECO:0000312|EMBL:AAF52106.1}
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] {ECO:0000305, ECO:0000312|EMBL:AAO74698.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND RNA EDITING OF POSITION 325.
RC   STRAIN=Berkeley {ECO:0000312|EMBL:AAO74698.1};
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 (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000305}
RP   RNA EDITING OF POSITION 325.
RX   PubMed=17018572; DOI=10.1261/rna.254306;
RA   Stapleton M., Carlson J.W., Celniker S.E.;
RT   "RNA editing in Drosophila melanogaster: new targets and functional
RT   consequences.";
RL   RNA 12:1922-1932(2006).
RN   [5] {ECO:0000305}
RP   FUNCTION, INTERACTION WITH EPS-15, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=23439121; DOI=10.1016/j.neuron.2012.12.015;
RA   Nahm M., Lee M.J., Parkinson W., Lee M., Kim H., Kim Y.J., Kim S.,
RA   Cho Y.S., Min B.M., Bae Y.C., Broadie K., Lee S.;
RT   "Spartin regulates synaptic growth and neuronal survival by inhibiting BMP-
RT   mediated microtubule stabilization.";
RL   Neuron 77:680-695(2013).
CC   -!- FUNCTION: During postembryonic development, functions with endocytic
CC       adapter Eps-15 in neurons to restrain synaptic growth, by inhibiting
CC       BMP signaling, and to control synaptic endocytosis. Required
CC       presynaptically for neuromuscular junction (NMJ) neurotransmission.
CC       Inhibits neuronal BMP signaling by promoting endocytic internalization
CC       and subsequent endosomal trafficking of the BMP receptor wit. In this
CC       way, regulates the Fmr1 translational regulator controlling Futsch
CC       expression to modulate neuronal microtubule stability, which controls
CC       both synaptogenesis and neuronal survival.
CC       {ECO:0000269|PubMed:23439121}.
CC   -!- SUBUNIT: Interacts with Eps-15 (via C-terminal region); the interaction
CC       is required for spartin localization to the NMJ presynaptic membrane.
CC       {ECO:0000269|PubMed:23439121}.
CC   -!- SUBCELLULAR LOCATION: Presynaptic cell membrane
CC       {ECO:0000269|PubMed:23439121}. Early endosome
CC       {ECO:0000269|PubMed:23439121}. Lipid droplet
CC       {ECO:0000269|PubMed:23439121}. Note=Colocalizes with Eps-15 at
CC       presynaptic cell membrane. {ECO:0000269|PubMed:23439121}.
CC   -!- TISSUE SPECIFICITY: Expressed in larval brain, ventral nerve cord and
CC       neuropil (at protein level). {ECO:0000269|PubMed:23439121}.
CC   -!- RNA EDITING: Modified_positions=325 {ECO:0000269|PubMed:17018572,
CC       ECO:0000269|Ref.3}; Note=Partially edited. Target of Adar.
CC       {ECO:0000269|PubMed:17018572};
CC   -!- DISRUPTION PHENOTYPE: Mutant larvae show an overgrowth of the third-
CC       instar NMJ, with an overall bouton number and satellite bouton number
CC       increase of 40% and 90%, respectively, compared with wild type. Mutant
CC       larvae also show a decrease in the amplitude of evoked excitatory
CC       junction currents (EJCs), but normal spontaneous miniature EJCs (mEJCs)
CC       and axonal transport. Adult mutants display reduced locomotor activity
CC       and progressive vacuolization in the brain, which is associated with
CC       neurodegeneration. {ECO:0000269|PubMed:23439121}.
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DR   EMBL; AE014297; AAF52106.1; -; Genomic_DNA.
DR   EMBL; BT006015; AAO74698.1; -; mRNA.
DR   RefSeq; NP_001246910.1; NM_001259981.1.
DR   RefSeq; NP_649485.1; NM_141228.2.
DR   AlphaFoldDB; Q9VN45; -.
DR   SMR; Q9VN45; -.
DR   BioGRID; 65801; 10.
DR   IntAct; Q9VN45; 3.
DR   STRING; 7227.FBpp0078501; -.
DR   PaxDb; Q9VN45; -.
DR   PRIDE; Q9VN45; -.
DR   EnsemblMetazoa; FBtr0078861; FBpp0078501; FBgn0037265.
DR   EnsemblMetazoa; FBtr0308820; FBpp0300977; FBgn0037265.
DR   GeneID; 40582; -.
DR   KEGG; dme:Dmel_CG12001; -.
DR   UCSC; CG12001-RA; d. melanogaster.
DR   CTD; 40582; -.
DR   FlyBase; FBgn0037265; spartin.
DR   VEuPathDB; VectorBase:FBgn0037265; -.
DR   eggNOG; KOG2709; Eukaryota.
DR   GeneTree; ENSGT00390000012235; -.
DR   HOGENOM; CLU_019310_1_0_1; -.
DR   InParanoid; Q9VN45; -.
DR   OMA; DACALIQ; -.
DR   OrthoDB; 650471at2759; -.
DR   PhylomeDB; Q9VN45; -.
DR   BioGRID-ORCS; 40582; 1 hit in 1 CRISPR screen.
DR   GenomeRNAi; 40582; -.
DR   PRO; PR:Q9VN45; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0037265; Expressed in seminal fluid secreting gland and 22 other tissues.
DR   ExpressionAtlas; Q9VN45; baseline and differential.
DR   Genevisible; Q9VN45; DM.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0005769; C:early endosome; IDA:FlyBase.
DR   GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
DR   GO; GO:0042734; C:presynaptic membrane; IDA:FlyBase.
DR   GO; GO:0043195; C:terminal bouton; IDA:FlyBase.
DR   GO; GO:0031267; F:small GTPase binding; IPI:FlyBase.
DR   GO; GO:0051301; P:cell division; IBA:GO_Central.
DR   GO; GO:0030514; P:negative regulation of BMP signaling pathway; IGI:FlyBase.
DR   GO; GO:0045886; P:negative regulation of synaptic assembly at neuromuscular junction; IMP:FlyBase.
DR   GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR   GO; GO:0002092; P:positive regulation of receptor internalization; IGI:FlyBase.
DR   InterPro; IPR007330; MIT_dom.
DR   InterPro; IPR009686; Senescence/spartin_C.
DR   InterPro; IPR045036; Spartin-like.
DR   PANTHER; PTHR21068; PTHR21068; 1.
DR   Pfam; PF06911; Senescence; 1.
DR   SMART; SM00745; MIT; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Cell projection; Developmental protein; Endosome;
KW   Lipid droplet; Membrane; Neurodegeneration; Neurogenesis;
KW   Reference proteome; RNA editing; Synapse.
FT   CHAIN           1..553
FT                   /note="Protein spartin"
FT                   /id="PRO_0000337156"
FT   DOMAIN          15..96
FT                   /note="MIT"
FT   DOMAIN          325..509
FT                   /note="Senescence"
FT                   /evidence="ECO:0000255"
FT   REGION          105..130
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        107..123
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VARIANT         325
FT                   /note="I -> V (in RNA edited version)"
FT                   /evidence="ECO:0000269|PubMed:17018572"
SQ   SEQUENCE   553 AA;  59784 MW;  31F3EFC7C5C6E357 CRC64;
     MAEEESEFLE AYAGIRTAYK AAMTQVDLAV SHEEQESPGQ AIVAYELALR MIEDTFGIPV
     GLPNKIDTVQ AEWNDACALI QKLKSAETEL RYRLKVLRSQ KQSIDDSAVE ATEESRAEMD
     TKRPPLLAEN PSTQYGIANA SGAPKTYREL AAGLRELLAV RDAKVLLDEL FRAQVKMYRI
     EASGSVTTIS GSSTMSLVMC TVGGKWKYLS GIYFIQCSMP NEGTAGIWLY PLVPSITNCY
     QTEYGAFIFP DMECQQPGNA FGLMLTKEGQ TSRTEDELED LQQFFLDLLE AVLAGTVVQL
     KSPTSQRAGL ASDTVSGSEQ VSRHIVSAAD FIASNLVRGA EKTGGFMLRS TPYIISKMTP
     ASMDAQVPSS VQTSVEVAQK VTHAAAGMTG WIAGKVGTAS MAVGRYLAPH IQEQGSKLLQ
     KGFGYDTSEA NSTMEGAMTI AAGAVEGVST VFDGLETSAK ILGSSLSENS VKIIEHKYGQ
     QTGNLASGTF DTVGNVFVVS QNVNYITPKG IAKKMVKRTG EAVVSDYKRD LRKSESHYIN
     AGSLYPDLRA LKE
 
 
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