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P34092

- MYOB_DICDI

UniProt

P34092 - MYOB_DICDI

Protein

Myosin IB heavy chain

Gene

myoB

Organism
Dictyostelium discoideum (Slime mold)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 105 (01 Oct 2014)
      Sequence version 2 (04 Dec 2007)
      Previous versions | rss
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    Functioni

    Myosin is a protein that binds to actin and has ATPase activity that is activated by actin. Myosin IB may have a role in chemotaxis and aggregation; it could serve to stabilize and even retract cortical structures, such as pseudopods and lamellopods. Involved in the whole cell motility of aggregation-stages cells. Overexpression results in significant decrease in the rate of cellular translocation and fluid-phase pinocytosis and abnormalities in the normal rearrangement of the actin cytoskeleton.3 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi102 – 1098ATPSequence Analysis

    GO - Molecular functioni

    1. actin-dependent ATPase activity Source: dictyBase
    2. actin filament binding Source: dictyBase
    3. ATP binding Source: dictyBase
    4. microfilament motor activity Source: dictyBase
    5. myosin I head/neck binding Source: dictyBase
    6. protein binding Source: dictyBase

    GO - Biological processi

    1. actin-myosin filament sliding Source: dictyBase
    2. ATP catabolic process Source: GOC
    3. cellular component movement Source: dictyBase
    4. chemotaxis Source: UniProtKB-KW
    5. exocytosis Source: dictyBase
    6. metabolic process Source: GOC
    7. phagocytosis Source: dictyBase
    8. phagosome reneutralization Source: dictyBase
    9. regulation of post-lysosomal vacuole size Source: dictyBase
    10. response to other organism Source: dictyBase

    Keywords - Molecular functioni

    Motor protein, Myosin

    Keywords - Biological processi

    Chemotaxis

    Keywords - Ligandi

    Actin-binding, ATP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Myosin IB heavy chain
    Gene namesi
    Name:myoB
    Synonyms:dmiB, myoA
    ORF Names:DDB_G0289117
    OrganismiDictyostelium discoideum (Slime mold)
    Taxonomic identifieri44689 [NCBI]
    Taxonomic lineageiEukaryotaAmoebozoaMycetozoaDictyosteliidaDictyostelium
    ProteomesiUP000002195: Chromosome 5, UP000002195: Unassembled WGS sequence

    Organism-specific databases

    dictyBaseiDDB_G0289117. myoB.

    Subcellular locationi

    Cell projectionpseudopodium. Cytoplasmcell cortex
    Note: Highest concentration just beneath the plasma membrane in the anterior pseudopod at the leading edge of the cell and at sites of cell-cell contact in both stationary and aggregation stage cells. Also found in macropinocytic structures.

    GO - Cellular componenti

    1. actomyosin Source: dictyBase
    2. cell cortex Source: UniProtKB-SubCell
    3. cell leading edge Source: dictyBase
    4. phagocytic cup lip Source: dictyBase
    5. phagocytic vesicle Source: dictyBase
    6. phagocytic vesicle membrane Source: dictyBase
    7. pseudopodium Source: UniProtKB-SubCell
    8. unconventional myosin complex Source: dictyBase

    Keywords - Cellular componenti

    Cell projection, Cytoplasm

    Pathology & Biotechi

    Disruption phenotypei

    Shows defects in pseudopod formation and translocation. Also shows slower speed of locomoting, aggregation-stage cells and significant reduction in initial rate of phagocytosis. MyoB and myoC double mutant exhibits profound defects in growth, endocytosis and rearrangment of F-actin. Expression of the full-length myoB heavy chain in these cells fully rescues the double mutant defects. myoB and myoD double mutant exhibits reduction in the speed of whole cell translocation. myoB, myoC and myoD triple mutant exhibits reduction in the speed of whole cell translocation.5 Publications

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi332 – 3321S → A: Fail to complement the null phenotype. 2 Publications
    Mutagenesisi332 – 3321S → E: Forms a complex in the presence and absence of Ca(2+). 2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11111111Myosin IB heavy chainPRO_0000123366Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei332 – 3321PhosphoserineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Expressioni

    Developmental stagei

    Rises dramatically during early development.1 Publication

    Interactioni

    Subunit structurei

    Myosin I heavy chain is single-headed. Dimer of a heavy and a light chain. Inability to self-assemble into filaments.

    Protein-protein interaction databases

    STRINGi44689.DDB_0191351.

    Structurei

    3D structure databases

    ProteinModelPortaliP34092.
    SMRiP34092. Positions 1059-1109.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini9 – 691683Myosin motorAdd
    BLAST
    Domaini1053 – 111159SH3PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni547 – 62781Actin-bindingAdd
    BLAST
    Regioni695 – 921227Tail homology region 1 (TH.1)Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi922 – 1052131Ala/Gly/Pro-rich (TH.2)Add
    BLAST
    Compositional biasi951 – 101565Asn-richAdd
    BLAST
    Compositional biasi955 – 96511Poly-GlnAdd
    BLAST

    Domaini

    TH.1 binds directly to anionic phospholipid membranes; myosins I could therefore move actin relative to membranes and vice versa. TH.2 and SH3 bind tightly to F-actin; this together with the nucleotide-sensitive site in the head, allows single molecules of myosin I to cross-link actin filaments.

    Sequence similaritiesi

    Contains 1 myosin motor domain.Curated
    Contains 1 SH3 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    SH3 domain

    Phylogenomic databases

    eggNOGiCOG5022.
    KOiK10356.
    OMAiLFRVINT.
    PhylomeDBiP34092.

    Family and domain databases

    Gene3Di3.40.50.300. 2 hits.
    InterProiIPR001609. Myosin_head_motor_dom.
    IPR010926. Myosin_tail_2.
    IPR027417. P-loop_NTPase.
    IPR001452. SH3_domain.
    [Graphical view]
    PfamiPF00063. Myosin_head. 1 hit.
    PF06017. Myosin_TH1. 1 hit.
    PF00018. SH3_1. 1 hit.
    [Graphical view]
    PRINTSiPR00193. MYOSINHEAVY.
    PR00452. SH3DOMAIN.
    SMARTiSM00242. MYSc. 1 hit.
    SM00326. SH3. 1 hit.
    [Graphical view]
    SUPFAMiSSF50044. SSF50044. 1 hit.
    SSF52540. SSF52540. 1 hit.
    PROSITEiPS51456. MYOSIN_MOTOR. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P34092-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSKKVQAKQG TDDLVMLPKV SEDEICENLK KRYMNDFIYT NIGPVLISVN     50
    PFRNLNNSGP DFIEAYRGKH AQEVPPHVYQ LAESAYRAMK NDQENQCVII 100
    SGESGAGKTE AAKLIMGYVS AISGSTEKVE YVKHVILESN PLLEAFGNAK 150
    TLRNNNSSRF GKYFEIQFDK AGDPVGGKIY NYLLEKSRVV YQNPGERNFH 200
    IFYQLLAGAS AQEKRDYVLS SPESYYYLNQ SQCYTVDGIN DVSDYAEVRQ 250
    AMDTIGLTAQ EQSDIIRIVA CVLHIGNIYF IEDDKGNAAI YDPNALELAA 300
    SMLCIDSATL QNAILFRVIN TGGAGGAGNR RSTYNVPQNV EQANGTRDAL 350
    ARTIYDRMFS WLVERVNQSL SYYKSPYQNV IGILDIFGFE IFEKNGFEQF 400
    CINFVNEKLQ QFFIELTLKA EQEEYVREGI KWEPIKYFNN QIVCDLIEGK 450
    SPPGIFSLLD DICSTLHAQS TGTDQKFLEK MAGIYDGHLH WRGMTGAFAI 500
    KHYAGEVTYE AEGFSDKNKD TLFFDLIEAI QCSKMPFLAS LFNEDTGSLQ 550
    KKRPTTAGFK IKTSAGELMK ALSQCTPHYI RCIKPNETKK AKDWENSRVK 600
    HQVQYLGLLE NVRVRRAGFA YRNTFDKVLK RYKKLSSKTW GIWGEWKGDA 650
    IEGCKTIFQD MNLEAGQWQL GKTKVFIRHP ETVFLLEEAL DKKDFDCTAK 700
    IQKAFRNWKA KKHSLEQRAQ IAHMFKDKKE RQRNSIDRKF TSDYIDFENQ 750
    FGLQEAMQNA HKKERVVFAD TVIKIDRRAK QKNYEMVLTD QALYFVEKSI 800
    KKKVLVHTLI RRVGLREIKG VSISTLSDNV IVFHLPEHDQ VIENDKKTEI 850
    IIVLVEYFKA IGGGSLNVQF SDRINYTLKK GEQKEISFQK SEQCPTLVVK 900
    KGGKGLIGTI ASGLPSSTDS TPKNYNPNSM SQASSRPAPQ QSAGRGRGMP 950
    QGAGQPQPQQ PQQQQRPMPQ PQQGGGARPM PQPQQGGGAR PMGAPQQGGA 1000
    PQQGAGRQLP QPTQQGGAPG GRGAPMGRGA PGGGPAGAGG RPLPTVAKPA 1050
    PQPSRPTAKA LYDYDASSTD ELSFKEGDII FIVQKDNGGW TQGELKSGQK 1100
    GWAPTNYLQY N 1111
    Length:1,111
    Mass (Da):124,257
    Last modified:December 4, 2007 - v2
    Checksum:iB326A1DDF85B86AC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti207 – 2071A → R in AAA33229. (PubMed:2762320)Curated
    Sequence conflicti365 – 3651R → K in AAA33229. (PubMed:2762320)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M26037 Genomic DNA. Translation: AAA33229.1.
    AAFI02000130 Genomic DNA. Translation: EAL62866.1.
    PIRiA33284.
    RefSeqiXP_636382.1. XM_631290.1.

    Genome annotation databases

    EnsemblProtistsiDDB0191351; DDB0191351; DDB_G0289117.
    GeneIDi8626983.
    KEGGiddi:DDB_G0289117.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M26037 Genomic DNA. Translation: AAA33229.1 .
    AAFI02000130 Genomic DNA. Translation: EAL62866.1 .
    PIRi A33284.
    RefSeqi XP_636382.1. XM_631290.1.

    3D structure databases

    ProteinModelPortali P34092.
    SMRi P34092. Positions 1059-1109.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 44689.DDB_0191351.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblProtistsi DDB0191351 ; DDB0191351 ; DDB_G0289117 .
    GeneIDi 8626983.
    KEGGi ddi:DDB_G0289117.

    Organism-specific databases

    dictyBasei DDB_G0289117. myoB.

    Phylogenomic databases

    eggNOGi COG5022.
    KOi K10356.
    OMAi LFRVINT.
    PhylomeDBi P34092.

    Family and domain databases

    Gene3Di 3.40.50.300. 2 hits.
    InterProi IPR001609. Myosin_head_motor_dom.
    IPR010926. Myosin_tail_2.
    IPR027417. P-loop_NTPase.
    IPR001452. SH3_domain.
    [Graphical view ]
    Pfami PF00063. Myosin_head. 1 hit.
    PF06017. Myosin_TH1. 1 hit.
    PF00018. SH3_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00193. MYOSINHEAVY.
    PR00452. SH3DOMAIN.
    SMARTi SM00242. MYSc. 1 hit.
    SM00326. SH3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50044. SSF50044. 1 hit.
    SSF52540. SSF52540. 1 hit.
    PROSITEi PS51456. MYOSIN_MOTOR. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Dictyostelium discoideum contains a gene encoding a myosin I heavy chain."
      Jung G., Saxe C.L. III, Kimmel A.R., Hammer J.A. III
      Proc. Natl. Acad. Sci. U.S.A. 86:6186-6190(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: AX3.
    2. "The genome of the social amoeba Dictyostelium discoideum."
      Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N.
      , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.
      Nature 435:43-57(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: AX4.
    3. "Sequence, expression pattern, intracellular localization, and targeted disruption of the Dictyostelium myosin ID heavy chain isoform."
      Jung G., Fukui Y., Martin B., Hammer J.A. III
      J. Biol. Chem. 268:14981-14990(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 481-490; 656-666 AND 783-798, SUBCELLULAR LOCATION.
      Strain: AX3.
    4. "Myosin I is located at the leading edges of locomoting Dictyostelium amoebae."
      Fukui Y., Lynch T.J., Brzeska H., Korn E.D.
      Nature 341:328-331(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    5. "Generation and characterization of Dictyostelium cells deficient in a myosin I heavy chain isoform."
      Jung G., Hammer J.A. III
      J. Cell Biol. 110:1955-1964(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE.
    6. "Myosin IB null mutants of Dictyostelium exhibit abnormalities in motility."
      Wessels D., Murray J., Jung G., Hammer J.A. III, Soll D.R.
      Cell Motil. Cytoskeleton 20:301-315(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE.
    7. "Dictyostelium myosin I double mutants exhibit conditional defects in pinocytosis."
      Novak K.D., Peterson M.D., Reedy M.C., Titus M.A.
      J. Cell Biol. 131:1205-1221(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE.
    8. "Localization of Dictyostelium myoB and myoD to filopodia and cell-cell contact sites using isoform-specific antibodies."
      Morita Y.S., Jung G., Hammer J.A. III, Fukui Y.
      Eur. J. Cell Biol. 71:371-379(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    9. "Dictyostelium mutants lacking multiple classic myosin I isoforms reveal combinations of shared and distinct functions."
      Jung G., Wu X., Hammer J.A. III
      J. Cell Biol. 133:305-323(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, FUNCTION.
    10. "Myosin I overexpression impairs cell migration."
      Novak K.D., Titus M.A.
      J. Cell Biol. 136:633-647(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. "The myosin I SH3 domain and TEDS rule phosphorylation site are required for in vivo function."
      Novak K.D., Titus M.A.
      Mol. Biol. Cell 9:75-88(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE, MUTAGENESIS OF SER-332.
    12. "Thirteen is enough: the myosins of Dictyostelium discoideum and their light chains."
      Kollmar M.
      BMC Genomics 7:183-183(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NOMENCLATURE.
    13. "Identification and characterization of an 8-kDa light chain associated with Dictyostelium discoideum MyoB, a class I myosin."
      Crawley S.W., de la Roche M.A., Lee S.F., Li Z., Chitayat S., Smith S.P., Cote G.P.
      J. Biol. Chem. 281:6307-6315(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF SER-332.

    Entry informationi

    Entry nameiMYOB_DICDI
    AccessioniPrimary (citable) accession number: P34092
    Secondary accession number(s): Q54HY1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1994
    Last sequence update: December 4, 2007
    Last modified: October 1, 2014
    This is version 105 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

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

    External Data

    Dasty 3