Reviewed, UniProtKB/Swiss-Prot P27619 (DYN_DROME)

Names and origin

Protein names

Recommended name:
    Dynamin
    EC=3.6.5.5
Alternative name(s):
    dDyn
    Protein shibire

Gene names

Name:	shi
ORF Names:	CG18102

Organism

Drosophila melanogaster (Fruit fly) [Complete proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	877 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Microtubule-associated force-producing protein which is involved in the production of microtubule bundles and which is able to bind and hydrolyze GTP. Implicated in endocytic protein sorting.
Catalytic activity	GTP + H2O = GDP + phosphate.
Subcellular location	Cytoplasm. Cytoplasm › cytoskeleton. Note: Microtubule-associated.
Miscellaneous	Shibire mutation is the cause of temperature-sensitive paralysis. This is believed to be due to a reversible block of endocytosis, which prevents membrane cycling and thus depletes synaptic vesicles. 'Shibire' means 'paralyzed' in Japanese.
Sequence similarities	Belongs to the dynamin family. Contains 1 GED domain. Contains 1 PH domain.
Sequence caution	The sequence CAA42061.1 differs from that shown. Reason: Miscellaneous discrepancy. Chimeric cDNA. There is a 6 amino acid insertion at position 634 due to a chimera of DNA from chromosome arms X and 3L. The sequence CAA42067.1 differs from that shown. Reason: Miscellaneous discrepancy. Chimeric cDNA. There is a 6 amino acid insertion at position 634 due to a chimera of DNA from chromosome arms X and 3L. The sequence CAA42068.1 differs from that shown. Reason: Miscellaneous discrepancy. Chimeric cDNA. There is a 6 amino acid insertion at position 634 due to a chimera of DNA from chromosome arms X and 3L.

Ontologies

Keywords
Biological process	Endocytosis
Cellular component	Cytoplasm Cytoskeleton Microtubule
Coding sequence diversity	Alternative splicing
Ligand	GTP-binding Nucleotide-binding
Molecular function	Hydrolase Motor protein
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	adherens junction maintenance Inferred from mutant phenotype. Source: FlyBase border follicle cell migration Inferred from mutant phenotype. Source: FlyBase conditioned taste aversion Inferred from mutant phenotype. Source: FlyBase cytokinesis Inferred from mutant phenotype. Source: FlyBase epithelial cell migration, open tracheal system Inferred from mutant phenotype. Source: FlyBase larval feeding behavior Inferred from mutant phenotype. Source: FlyBase male courtship behavior, veined wing generated song production Inferred from mutant phenotype. Source: FlyBase morphogenesis of a polarized epithelium Inferred from mutant phenotype. Source: FlyBase olfactory learning Inferred from direct assay. Source: FlyBase pole cell formation Traceable author statement. Source: FlyBase proboscis extension reflex Inferred from mutant phenotype. Source: FlyBase receptor-mediated endocytosis Non-traceable author statement. Source: FlyBase regulation of actin cytoskeleton organization Inferred from genetic interaction. Source: FlyBase regulation of short-term neuronal synaptic plasticity Inferred from mutant phenotype. Source: FlyBase regulation of synapse structure and activity Inferred from mutant phenotype. Source: FlyBase response to heat Inferred from mutant phenotype. Source: FlyBase salivary gland morphogenesis Inferred from mutant phenotype. Source: FlyBase short-term memory Inferred from mutant phenotype. Source: FlyBase sperm individualization Inferred from mutant phenotype. Source: FlyBase synaptic vesicle budding from presynaptic membrane Inferred from mutant phenotype. Source: FlyBase synaptic vesicle membrane organization Inferred from mutant phenotype. Source: FlyBase
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell microtubule Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from direct assay. Source: FlyBase synapse Inferred from mutant phenotype. Source: FlyBase
Molecular function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activity Non-traceable author statement. Source: FlyBase actin binding Inferred from direct assay. Source: FlyBase microtubule binding Inferred from direct assay. Source: FlyBase motor activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P27619-1)

Also known as: 4; D; F;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P27619-2)

Also known as: 3; A; B;

The sequence of this isoform differs from the canonical sequence as follows:
     830-830: V → R
     831-877: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 877	877	Dynamin		PRO_0000206576
Regions
	Domain	513 – 621	109	PH
	Domain	650 – 741	92	GED
	Nucleotide binding	33 – 40	8	GTP Potential
	Nucleotide binding	131 – 135	5	GTP Potential
	Nucleotide binding	200 – 203	4	GTP Potential
	Compositional bias	744 – 827	84	Pro-rich
Amino acid modifications
	Modified residue	756	1	Phosphoserine Ref.6
	Modified residue	764	1	Phosphoserine Ref.6
	Modified residue	767	1	Phosphoserine Ref.6
Natural variations
	Alternative sequence	830	1	V → R in isoform 2.		VSP_001330
	Alternative sequence	831 – 877	47	Missing in isoform 2.		VSP_001331
Experimental info
	Mutagenesis	141	1	G → S in allele shi-TS2; temperature sensitive larval and adult paralysis. Ref.2
	Mutagenesis	268	1	G → D in allele shi-TS1; temperature sensitive larval and adult paralysis. Ref.2
	Sequence conflict	594	1	K → R in CAA42067. Ref.1
	Sequence conflict	594	1	K → R in CAA42068. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (4) (D) (F) [UniParc]. Last modified February 28, 2003. Version 2. Checksum: 5B85F96491490B14	FASTA	877	97,809
	10 20 30 40 50 60 MDSLITIVNK LQDAFTSLGV HMQLDLPQIA VVGGQSAGKS SVLENFVGKD FLPRGSGIVT 70 80 90 100 110 120 RRPLILQLIN GVTEYGEFLH IKGKKFSSFD EIRKEIEDET DRVTGSNKGI SNIPINLRVY 130 140 150 160 170 180 SPHVLNLTLI DLPGLTKVAI GDQPVDIEQQ IKQMIFQFIR KETCLILAVT PANTDLANSD 190 200 210 220 230 240 ALKLAKEVDP QGVRTIGVIT KLDLMDEGTD ARDILENKLL PLRRGYIGVV NRSQKDIEGR 250 260 270 280 290 300 KDIHQALAAE RKFFLSHPSY RHMADRLGTP YLQRVLNQQL TNHIRDTLPG LRDKLQKQML 310 320 330 340 350 360 TLEKEVEEFK HFQPGDASIK TKAMLQMIQQ LQSDFERTIE GSGSALVNTN ELSGGAKINR 370 380 390 400 410 420 IFHERLRFEI VKMACDEKEL RREISFAIRN IHGIRVGLFT PDMAFEAIVK RQIALLKEPV 430 440 450 460 470 480 IKCVDLVVQE LSVVVRMCTA KMSRYPRLRE ETERIITTHV RQREHSCKEQ ILLLIDFELA 490 500 510 520 530 540 YMNTNHEDFI GFANAQNKSE NANKTGTRQL GNQVIRKGHM VIQNLGIMKG GSRPYWFVLT 550 560 570 580 590 600 SESISWYKDE DEKEKKFMLP LDGLKLRDIE QGFMSMSRRV TFALFSPDGR NVYKDYKQLE 610 620 630 640 650 660 LSCETVEDVE SWKASFLRAG VYPEKQETQE NGDESASEES SSDPQLERQV ETIRNLVDSY 670 680 690 700 710 720 MKIVTKTTRD MVPKAIMMLI INNAKDFING ELLAHLYASG DQAQMMEESA ESATRREEML 730 740 750 760 770 780 RMYRACKDAL QIIGDVSMAT VSSPLPPPVK NDWLPSGLDN PRLSPPSPGG VRGKPGPPAQ 790 800 810 820 830 840 SSLGGRNPPL PPSTGRPAPA IPNRPGGGAP PLPGGRPGGS LPPPMLPSRV SGAVGGAIVQ 850 860 870 QSGANRYVPE SMRGQVNQAV GQAAINELSN AFSSRFK
	Isoform 2 (3) (A) (B). Checksum: E7F891A4A849B29D	FASTA	830	93,031
	10 20 30 40 50 60 MDSLITIVNK LQDAFTSLGV HMQLDLPQIA VVGGQSAGKS SVLENFVGKD FLPRGSGIVT 70 80 90 100 110 120 RRPLILQLIN GVTEYGEFLH IKGKKFSSFD EIRKEIEDET DRVTGSNKGI SNIPINLRVY 130 140 150 160 170 180 SPHVLNLTLI DLPGLTKVAI GDQPVDIEQQ IKQMIFQFIR KETCLILAVT PANTDLANSD 190 200 210 220 230 240 ALKLAKEVDP QGVRTIGVIT KLDLMDEGTD ARDILENKLL PLRRGYIGVV NRSQKDIEGR 250 260 270 280 290 300 KDIHQALAAE RKFFLSHPSY RHMADRLGTP YLQRVLNQQL TNHIRDTLPG LRDKLQKQML 310 320 330 340 350 360 TLEKEVEEFK HFQPGDASIK TKAMLQMIQQ LQSDFERTIE GSGSALVNTN ELSGGAKINR 370 380 390 400 410 420 IFHERLRFEI VKMACDEKEL RREISFAIRN IHGIRVGLFT PDMAFEAIVK RQIALLKEPV 430 440 450 460 470 480 IKCVDLVVQE LSVVVRMCTA KMSRYPRLRE ETERIITTHV RQREHSCKEQ ILLLIDFELA 490 500 510 520 530 540 YMNTNHEDFI GFANAQNKSE NANKTGTRQL GNQVIRKGHM VIQNLGIMKG GSRPYWFVLT 550 560 570 580 590 600 SESISWYKDE DEKEKKFMLP LDGLKLRDIE QGFMSMSRRV TFALFSPDGR NVYKDYKQLE 610 620 630 640 650 660 LSCETVEDVE SWKASFLRAG VYPEKQETQE NGDESASEES SSDPQLERQV ETIRNLVDSY 670 680 690 700 710 720 MKIVTKTTRD MVPKAIMMLI INNAKDFING ELLAHLYASG DQAQMMEESA ESATRREEML 730 740 750 760 770 780 RMYRACKDAL QIIGDVSMAT VSSPLPPPVK NDWLPSGLDN PRLSPPSPGG VRGKPGPPAQ 790 800 810 820 830 SSLGGRNPPL PPSTGRPAPA IPNRPGGGAP PLPGGRPGGS LPPPMLPSRR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Multiple forms of dynamin are encoded by shibire, a Drosophila gene involved in endocytosis." Chen M.S., Obar R.A., Schroeder C.C., Austin T.W., Poodry C.A., Wadsworth S.C., Vallee R.B. Nature 351:583-586(1991) [PubMed: 1828536] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2). Strain: Canton-S. Tissue: Head.
[2]	"Dynamin-like protein encoded by the Drosophila shibire gene associated with vesicular traffic." van der Bliek A.M., Meyerowitz E.M. Nature 351:411-414(1991) [PubMed: 1674590] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), MUTAGENESIS OF GLY-141 AND GLY-268. Strain: Oregon-R.
[3]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[4]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract] Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
[5]	Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A. , Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E. Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Strain: Berkeley. Tissue: Embryo.
[6]	"Phosphoproteome analysis of Drosophila melanogaster embryos." Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P. J. Proteome Res. 7:1675-1682(2008) [PubMed: 18327897] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-756; SER-764 AND SER-767, MASS SPECTROMETRY. Tissue: Embryo.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X59448 mRNA. Translation: CAA42067.1. Sequence problems. X59449 mRNA. Translation: CAA42068.1. Sequence problems. X59435 mRNA. Translation: CAA42061.1. Sequence problems. X59436 mRNA. Translation: CAA42062.1. AE014298 Genomic DNA. Translation: AAF48536.2. AE014298 Genomic DNA. Translation: AAS65368.1. BT010049 mRNA. Translation: AAQ22518.1.
PIR	S15413. S16130. S17974. S17975. S34399.
RefSeq	NP_001036278.1. NP_001036279.1. NP_001162766.1. NP_001162768.1. NP_524853.2. NP_727910.1. NP_727911.1. NP_996465.1. NP_996466.1. NP_996467.1. NP_996468.1.
UniGene	Dm.3444
3D structure databases
SMR	P27619. Positions 1-299, 514-625.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-17621N.
IntAct	P27619. 6 interactions.
STRING	P27619.
Genome annotation databases
Ensembl	FBtr0074118; FBpp0073928; FBgn0003392; Drosophila melanogaster. [Genome view] FBtr0074119; FBpp0073929; FBgn0003392; Drosophila melanogaster. [Genome view] FBtr0074120; FBpp0073930; FBgn0003392; Drosophila melanogaster. [Genome view] FBtr0074121; FBpp0089278; FBgn0003392; Drosophila melanogaster. [Genome view] FBtr0074122; FBpp0089279; FBgn0003392; Drosophila melanogaster. [Genome view] FBtr0074123; FBpp0089280; FBgn0003392; Drosophila melanogaster. [Genome view] FBtr0074124; FBpp0089277; FBgn0003392; Drosophila melanogaster. [Genome view] FBtr0111036; FBpp0110335; FBgn0003392; Drosophila melanogaster. [Genome view] FBtr0111037; FBpp0110336; FBgn0003392; Drosophila melanogaster. [Genome view]
GeneID	45928.
KEGG	dme:Dmel_CG18102.
UCSC	CG18102-RA. d. melanogaster.
Organism-specific databases
CTD	45928.
FlyBase	FBgn0003392. shi.
Phylogenomic databases
eggNOG	inNOG08398.
InParanoid	P27619.
OMA	FANAQNK.
PhylomeDB	P27619.
Enzyme and pathway databases
BioCyc	DMEL-XXX-02:DMEL-XXX-02-002077-MONOMER.
BRENDA	3.6.5.5. 48.
Gene expression databases
Bgee	P27619.
GermOnline	CG18102. Drosophila melanogaster.
Family and domain databases
InterPro	IPR000375. Dynamin_central. IPR001401. Dynamin_GTPase. IPR019762. Dynamin_GTPase_CS. IPR003130. GED. IPR020850. GTPase_effector_domain_GED. IPR011993. PH_type. IPR001849. Pleckstrin_homology. [Graphical view]
Gene3D	G3DSA:2.30.29.30. PH_type. 1 hit.
Pfam	PF01031. Dynamin_M. 1 hit. PF00350. Dynamin_N. 1 hit. PF02212. GED. 1 hit. PF00169. PH. 1 hit. [Graphical view]
PRINTS	PR00195. DYNAMIN.
SMART	SM00053. DYNc. 1 hit. SM00302. GED. 1 hit. SM00233. PH. 1 hit. [Graphical view]
PROSITE	PS00410. DYNAMIN. 1 hit. PS51388. GED. 1 hit. PS50003. PH_DOMAIN. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	838489.

Entry information

Entry name

DYN_DROME

Accession

Primary (citable) accession number: P27619
Secondary accession number(s): Q0KHS4, Q9VXM2

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	February 28, 2003
Last modified:	February 9, 2010
This is version 110 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project