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P34092

- MYOB_DICDI

UniProt

P34092 - MYOB_DICDI

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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

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

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
Complete GO annotation...

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 leading edge Source: dictyBase
  3. cell projection Source: UniProtKB-KW
  4. phagocytic cup lip Source: dictyBase
  5. phagocytic vesicle Source: dictyBase
  6. phagocytic vesicle membrane Source: dictyBase
  7. unconventional myosin complex Source: dictyBase
Complete GO annotation...

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
Domaini717 – 912196Myosin tailSequence AnalysisAdd
BLAST
Domaini1053 – 111159SH3PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni547 – 62781Actin-bindingAdd
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

Myosin tail domain 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 myosin tail domain.Curated
Contains 1 SH3 domain.PROSITE-ProRule annotation

Keywords - Domaini

SH3 domain

Phylogenomic databases

eggNOGiCOG5022.
InParanoidiP34092.
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 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSKKVQAKQG TDDLVMLPKV SEDEICENLK KRYMNDFIYT NIGPVLISVN
60 70 80 90 100
PFRNLNNSGP DFIEAYRGKH AQEVPPHVYQ LAESAYRAMK NDQENQCVII
110 120 130 140 150
SGESGAGKTE AAKLIMGYVS AISGSTEKVE YVKHVILESN PLLEAFGNAK
160 170 180 190 200
TLRNNNSSRF GKYFEIQFDK AGDPVGGKIY NYLLEKSRVV YQNPGERNFH
210 220 230 240 250
IFYQLLAGAS AQEKRDYVLS SPESYYYLNQ SQCYTVDGIN DVSDYAEVRQ
260 270 280 290 300
AMDTIGLTAQ EQSDIIRIVA CVLHIGNIYF IEDDKGNAAI YDPNALELAA
310 320 330 340 350
SMLCIDSATL QNAILFRVIN TGGAGGAGNR RSTYNVPQNV EQANGTRDAL
360 370 380 390 400
ARTIYDRMFS WLVERVNQSL SYYKSPYQNV IGILDIFGFE IFEKNGFEQF
410 420 430 440 450
CINFVNEKLQ QFFIELTLKA EQEEYVREGI KWEPIKYFNN QIVCDLIEGK
460 470 480 490 500
SPPGIFSLLD DICSTLHAQS TGTDQKFLEK MAGIYDGHLH WRGMTGAFAI
510 520 530 540 550
KHYAGEVTYE AEGFSDKNKD TLFFDLIEAI QCSKMPFLAS LFNEDTGSLQ
560 570 580 590 600
KKRPTTAGFK IKTSAGELMK ALSQCTPHYI RCIKPNETKK AKDWENSRVK
610 620 630 640 650
HQVQYLGLLE NVRVRRAGFA YRNTFDKVLK RYKKLSSKTW GIWGEWKGDA
660 670 680 690 700
IEGCKTIFQD MNLEAGQWQL GKTKVFIRHP ETVFLLEEAL DKKDFDCTAK
710 720 730 740 750
IQKAFRNWKA KKHSLEQRAQ IAHMFKDKKE RQRNSIDRKF TSDYIDFENQ
760 770 780 790 800
FGLQEAMQNA HKKERVVFAD TVIKIDRRAK QKNYEMVLTD QALYFVEKSI
810 820 830 840 850
KKKVLVHTLI RRVGLREIKG VSISTLSDNV IVFHLPEHDQ VIENDKKTEI
860 870 880 890 900
IIVLVEYFKA IGGGSLNVQF SDRINYTLKK GEQKEISFQK SEQCPTLVVK
910 920 930 940 950
KGGKGLIGTI ASGLPSSTDS TPKNYNPNSM SQASSRPAPQ QSAGRGRGMP
960 970 980 990 1000
QGAGQPQPQQ PQQQQRPMPQ PQQGGGARPM PQPQQGGGAR PMGAPQQGGA
1010 1020 1030 1040 1050
PQQGAGRQLP QPTQQGGAPG GRGAPMGRGA PGGGPAGAGG RPLPTVAKPA
1060 1070 1080 1090 1100
PQPSRPTAKA LYDYDASSTD ELSFKEGDII FIVQKDNGGW TQGELKSGQK
1110
GWAPTNYLQY N
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.
InParanoidi P34092.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 106 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