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Protein

Myosin-IB

Gene

Myo61F

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in directing the movement of organelles along actin filaments.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi114 – 1218ATPBy similarity

GO - Molecular functioni

  • actin binding Source: FlyBase
  • ATPase activity, coupled Source: FlyBase
  • ATP binding Source: UniProtKB-KW
  • motor activity Source: FlyBase

GO - Biological processi

  • defense response to bacterium Source: FlyBase
  • determination of left/right symmetry Source: FlyBase
  • imaginal disc-derived male genitalia morphogenesis Source: FlyBase
  • mesoderm development Source: FlyBase
  • microvillus organization Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Motor protein, Myosin

Keywords - Ligandi

Actin-binding, ATP-binding, Calmodulin-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Myosin-IB
Short name:
MIB
Alternative name(s):
Brush border myosin IB
Short name:
BBMIB
Gene namesi
Name:Myo61F
ORF Names:CG9155
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0010246. Myo61F.

Subcellular locationi

  • Cytoplasm 1 Publication

  • Note: Protein shifts from the basolateral to apical domain in enterocytes and follicle cells.

GO - Cellular componenti

  • brush border Source: FlyBase
  • cell cortex Source: FlyBase
  • cytoplasm Source: FlyBase
  • myosin complex Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10351035Myosin-IBPRO_0000123455Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei304 – 3041Phosphoserine1 Publication
Modified residuei310 – 3101Phosphothreonine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ23979.
PRIDEiQ23979.

PTM databases

iPTMnetiQ23979.

Expressioni

Tissue specificityi

In the embryo, expressed in gastric caeca, midgut cells of the proventriculus, and in the mid and hindgut. In the larval and adult gut brush border, expressed in the microvilli. Also expressed at high levels in follicle cells during oogenesis.1 Publication

Developmental stagei

Expression starts at 8-12 hours embryonic development, continues to increase until third larval instar, disappears in pupae and is present at a low level in adults. Expression in embryogenesis is correlated with the formation of a brush border within the alimentary canal.2 Publications

Gene expression databases

BgeeiQ23979.
ExpressionAtlasiQ23979. differential.
GenevisibleiQ23979. DM.

Interactioni

GO - Molecular functioni

Protein-protein interaction databases

BioGridi63696. 2 interactions.
IntActiQ23979. 9 interactions.
STRINGi7227.FBpp0072567.

Structurei

3D structure databases

ProteinModelPortaliQ23979.
SMRiQ23979. Positions 18-1033.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini21 – 703683Myosin motorAdd
BLAST
Domaini696 – 71823IQ 1PROSITE-ProRule annotationAdd
BLAST
Domaini719 – 74123IQ 2PROSITE-ProRule annotationAdd
BLAST
Domaini742 – 76423IQ 3PROSITE-ProRule annotationAdd
BLAST
Domaini857 – 1035179TH1PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni592 – 5998Actin-bindingBy similarity

Sequence similaritiesi

Contains 3 IQ domains.PROSITE-ProRule annotation
Contains 1 myosin motor domain.Curated
Contains 1 TH1 (class I myosin tail homology) domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0164. Eukaryota.
COG5022. LUCA.
GeneTreeiENSGT00840000129697.
InParanoidiQ23979.
KOiK10356.
OMAiELCIKNM.
OrthoDBiEOG7V49XQ.
PhylomeDBiQ23979.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR000048. IQ_motif_EF-hand-BS.
IPR001609. Myosin_head_motor_dom.
IPR010926. Myosin_TH1.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00612. IQ. 1 hit.
PF00063. Myosin_head. 1 hit.
PF06017. Myosin_TH1. 1 hit.
[Graphical view]
PRINTSiPR00193. MYOSINHEAVY.
SMARTiSM00015. IQ. 3 hits.
SM00242. MYSc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS50096. IQ. 1 hit.
PS51456. MYOSIN_MOTOR. 1 hit.
PS51757. TH1. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform A (identifier: Q23979-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MASFNSQLKM ETGLHERDRA GVQDFVLLEN YQSEEAFIGN LKKRFQEDLI
60 70 80 90 100
YTYIGQVLIS VNPYKQLPIY TDDHVKAYRN KHFYEMPPHI FAVTDNAFRS
110 120 130 140 150
LIEENRGQCV LISGESGSGK TEASKKVLQF IAACSGNQTT VEGVKDKLLK
160 170 180 190 200
SNPVLEAFGN AKTNRNDNSS RFGKYMDIQF DFKGAPIGGN ILNYLLEKSR
210 220 230 240 250
VVAQMGGERN FHIFYQLLAG ADEALLQELR LERALDTYSY LTDGLNGTVT
260 270 280 290 300
RINDADSFKQ VQQALTVIDF TKEEQREIFG IVASILHLGN VGFTEVEGNA
310 320 330 340 350
KVNSRDLVVT AARLLGVNAS ELEAALTHRT IDARGDVVTS PLNQELAIYA
360 370 380 390 400
RDALAKAVYD RLFSWLVQRL NISLQAKETR ASRNNVMGIL DIYGFEIFQK
410 420 430 440 450
NSFEQFCINF CNEKLQQLFI ELTLKSEQDE YRREGIEWIP VEYFDNKVIC
460 470 480 490 500
NLIEEKHKGI ISILDEECLR PGEPTDKTFL EKLTQKLAQH HHYVCHEKAP
510 520 530 540 550
AHIKKIMLRD EFRLVHYAGE VTYSVNGFLD KNNDLLFRDL KETLSKAGNG
560 570 580 590 600
IVRNCFPEKE LRSLKRPETA ITQFRASLNN LMDILMCKEP SYIRCIKPND
610 620 630 640 650
LQTANVFNDE LVLHQVKYLG LMENLRVRRA GFAYRRTYEL FLERYKSLSK
660 670 680 690 700
STWPNYKGPG GPKAGVQQLV KDLGWDEEKY RVGETKLFIR WPRTLFDTED
710 720 730 740 750
AYQEKKHEIA AIIQAHWKGL MQRRKYLKLR AQVIIMQSYC RRKLAQQAAK
760 770 780 790 800
KRREAADKIR AFIKGFITRN DAPNGFNEEF IANAKRMWLL RLAKELPTKV
810 820 830 840 850
LDKSWPHAPG HCEEASGILH RLHRLHLARI YRLKLTPQQK RQFELKVLAE
860 870 880 890 900
KVFKGKKNNY ASSVSTWFQE DRIPKEHIQR VNDFVASTFG SEQLKYQSFC
910 920 930 940 950
TKFDRHGYKS RDRFILLSNK AIYVLDGKTY KQKHRLPLDK IDFTLTNHND
960 970 980 990 1000
DLMVIRIPLD LKKDKGDLIL IIPRIIEFST YIIDTVGTAS IVSIVDRNSL
1010 1020 1030
EHNVVKGKGG VIDIQTGAEP GVVRDKGHLV IIGTQ
Note: No experimental confirmation available.
Length:1,035
Mass (Da):118,990
Last modified:January 16, 2004 - v3
Checksum:iE7B153700A31D818
GO
Isoform B (identifier: Q23979-2) [UniParc]FASTAAdd to basket

Also known as: C

The sequence of this isoform differs from the canonical sequence as follows:
     1-9: Missing.

Show »
Length:1,026
Mass (Da):117,982
Checksum:i77E0C20A16F0EE3E
GO
Isoform D (identifier: Q23979-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     2-3: AS → YIEIKSLIFAIMDTKDYID

Note: No experimental confirmation available.
Show »
Length:1,052
Mass (Da):121,105
Checksum:i70BCF1A49E1F2E80
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti73 – 731D → N in AAA19591 (PubMed:8201616).Curated
Sequence conflicti230 – 2301R → G in AAA19591 (PubMed:8201616).Curated
Sequence conflicti251 – 2511R → S in AAA19591 (PubMed:8201616).Curated
Sequence conflicti271 – 2711T → G in AAA19591 (PubMed:8201616).Curated
Sequence conflicti554 – 5541N → S in AAA19591 (PubMed:8201616).Curated
Sequence conflicti554 – 5541N → S in L13070 (PubMed:8216259).Curated
Sequence conflicti560 – 5612EL → DV in L13070 (PubMed:8216259).Curated
Sequence conflicti610 – 6101E → Y in AAL39189 (PubMed:12537569).Curated
Sequence conflicti697 – 6971D → AI in L13070 (PubMed:8216259).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 99Missing in isoform B. 1 PublicationVSP_009274
Alternative sequencei2 – 32AS → YIEIKSLIFAIMDTKDYID in isoform D. CuratedVSP_035432

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U07596 mRNA. Translation: AAA19591.1.
AE014296 Genomic DNA. Translation: AAF47477.3.
AE014296 Genomic DNA. Translation: AAF47478.3.
AE014296 Genomic DNA. Translation: AAN11472.1.
AE014296 Genomic DNA. Translation: AAN11473.1.
AY069044 mRNA. Translation: AAL39189.1.
L13070 mRNA. No translation available.
AJ000879 Genomic DNA. Translation: CAA04367.1.
PIRiS45574.
RefSeqiNP_476934.2. NM_057586.4. [Q23979-3]
NP_728594.2. NM_167870.2. [Q23979-1]
NP_728595.1. NM_167871.2. [Q23979-2]
NP_728596.1. NM_167872.2. [Q23979-2]
UniGeneiDm.6432.

Genome annotation databases

EnsemblMetazoaiFBtr0072675; FBpp0072568; FBgn0010246. [Q23979-1]
GeneIDi38153.
KEGGidme:Dmel_CG9155.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U07596 mRNA. Translation: AAA19591.1.
AE014296 Genomic DNA. Translation: AAF47477.3.
AE014296 Genomic DNA. Translation: AAF47478.3.
AE014296 Genomic DNA. Translation: AAN11472.1.
AE014296 Genomic DNA. Translation: AAN11473.1.
AY069044 mRNA. Translation: AAL39189.1.
L13070 mRNA. No translation available.
AJ000879 Genomic DNA. Translation: CAA04367.1.
PIRiS45574.
RefSeqiNP_476934.2. NM_057586.4. [Q23979-3]
NP_728594.2. NM_167870.2. [Q23979-1]
NP_728595.1. NM_167871.2. [Q23979-2]
NP_728596.1. NM_167872.2. [Q23979-2]
UniGeneiDm.6432.

3D structure databases

ProteinModelPortaliQ23979.
SMRiQ23979. Positions 18-1033.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi63696. 2 interactions.
IntActiQ23979. 9 interactions.
STRINGi7227.FBpp0072567.

PTM databases

iPTMnetiQ23979.

Proteomic databases

PaxDbiQ23979.
PRIDEiQ23979.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0072675; FBpp0072568; FBgn0010246. [Q23979-1]
GeneIDi38153.
KEGGidme:Dmel_CG9155.

Organism-specific databases

CTDi38153.
FlyBaseiFBgn0010246. Myo61F.

Phylogenomic databases

eggNOGiKOG0164. Eukaryota.
COG5022. LUCA.
GeneTreeiENSGT00840000129697.
InParanoidiQ23979.
KOiK10356.
OMAiELCIKNM.
OrthoDBiEOG7V49XQ.
PhylomeDBiQ23979.

Miscellaneous databases

ChiTaRSiMyo61F. fly.
GenomeRNAii38153.
PROiQ23979.

Gene expression databases

BgeeiQ23979.
ExpressionAtlasiQ23979. differential.
GenevisibleiQ23979. DM.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR000048. IQ_motif_EF-hand-BS.
IPR001609. Myosin_head_motor_dom.
IPR010926. Myosin_TH1.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00612. IQ. 1 hit.
PF00063. Myosin_head. 1 hit.
PF06017. Myosin_TH1. 1 hit.
[Graphical view]
PRINTSiPR00193. MYOSINHEAVY.
SMARTiSM00015. IQ. 3 hits.
SM00242. MYSc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS50096. IQ. 1 hit.
PS51456. MYOSIN_MOTOR. 1 hit.
PS51757. TH1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The molecular cloning and characterization of Drosophila melanogaster myosin-IA and myosin-IB."
    Morgan N.S., Skovronsky D.M., Artavanis-Tsakonas S., Mooseker M.S.
    J. Mol. Biol. 239:347-356(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), DEVELOPMENTAL STAGE.
    Tissue: Head.
  2. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  3. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
    Strain: Berkeley.
  4. "A Drosophila full-length cDNA resource."
    Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
    Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
    Strain: Berkeley.
    Tissue: Head.
  5. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 347-706.
  6. Caggese C.
    Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 639-1035.
  7. "Characterization of myosin-IA and myosin-IB, two unconventional myosins associated with the Drosophila brush border cytoskeleton."
    Morgan N.S., Heintzelman M.B., Mooseker M.S.
    Dev. Biol. 172:51-71(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  8. "An integrated chemical, mass spectrometric and computational strategy for (quantitative) phosphoproteomics: application to Drosophila melanogaster Kc167 cells."
    Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A., Eng J.K., Aebersold R., Tao W.A.
    Mol. Biosyst. 3:275-286(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304 AND THR-310, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiMY61F_DROME
AccessioniPrimary (citable) accession number: Q23979
Secondary accession number(s): A4V191
, Q7KVC1, Q8T0U8, Q9W0H0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: January 16, 2004
Last modified: June 8, 2016
This is version 148 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.