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MYOK_DICDI
ID   MYOK_DICDI              Reviewed;         858 AA.
AC   Q9XXV8; Q555W0; Q86J00; Q9UA70;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Myosin-K heavy chain;
GN   Name=myoK; Synonyms=myoIG; ORFNames=DDB_G0274575;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RC   STRAIN=AX2;
RX   PubMed=10049776; DOI=10.1006/bbrc.1999.0264;
RA   Yazu M., Adachi H., Sutoh K.;
RT   "Novel Dictyostelium unconventional myosin MyoK is a class I myosin with
RT   the longest loop-1 insert and the shortest tail.";
RL   Biochem. Biophys. Res. Commun. 255:711-716(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RC   STRAIN=AX2;
RX   PubMed=10403059; DOI=10.1007/bf02738122;
RA   Schwarz E.C., Geissler H., Soldati T.;
RT   "A potentially exhaustive screening strategy reveals two novel divergent
RT   myosins in Dictyostelium.";
RL   Cell Biochem. Biophys. 30:413-435(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=12097910; DOI=10.1038/nature00847;
RA   Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA   Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA   Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA   Noegel A.A.;
RT   "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL   Nature 418:79-85(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
RN   [5]
RP   FUNCTION.
RX   PubMed=10652255; DOI=10.1242/jcs.113.4.621;
RA   Schwarz E.C., Neuhaus E.M., Kistler C., Henkel A.W., Soldati T.;
RT   "Dictyostelium myosin IK is involved in the maintenance of cortical tension
RT   and affects motility and phagocytosis.";
RL   J. Cell Sci. 113:621-633(2000).
RN   [6]
RP   NOMENCLATURE.
RX   PubMed=16857047; DOI=10.1186/1471-2164-7-183;
RA   Kollmar M.;
RT   "Thirteen is enough: the myosins of Dictyostelium discoideum and their
RT   light chains.";
RL   BMC Genomics 7:183-183(2006).
CC   -!- FUNCTION: Myosins are actin-based motor molecules with ATPase activity.
CC       Involved in phagocytosis and motility, and in the maintenance and
CC       dynamics of cell cortex. {ECO:0000269|PubMed:10049776,
CC       ECO:0000269|PubMed:10652255}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10403059}.
CC       Note=Enriched in actin cortex regions.
CC   -!- DEVELOPMENTAL STAGE: Expression stimulated at early developmental
CC       stages, before aggregation. {ECO:0000269|PubMed:10049776}.
CC   -!- DOMAIN: The head domain possess two actin-binding sites, a classic ATP-
CC       dependent one and a secondary salt-dependent one (located inside the
CC       GPR domain).
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Myosin family. {ECO:0000305}.
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DR   EMBL; AB017909; BAA76319.1; -; Genomic_DNA.
DR   EMBL; AF090534; AAD47904.1; -; mRNA.
DR   EMBL; AAFI02000012; EAL70180.1; -; Genomic_DNA.
DR   PIR; JG0183; JG0183.
DR   RefSeq; XP_643950.1; XM_638858.1.
DR   AlphaFoldDB; Q9XXV8; -.
DR   SMR; Q9XXV8; -.
DR   BioGRID; 1244381; 1.
DR   STRING; 44689.DDB0185086; -.
DR   PaxDb; Q9XXV8; -.
DR   EnsemblProtists; EAL70180; EAL70180; DDB_G0274575.
DR   GeneID; 8619378; -.
DR   KEGG; ddi:DDB_G0274575; -.
DR   dictyBase; DDB_G0274575; myoK.
DR   eggNOG; KOG0162; Eukaryota.
DR   HOGENOM; CLU_000192_7_5_1; -.
DR   InParanoid; Q9XXV8; -.
DR   OMA; HEEGMKW; -.
DR   PhylomeDB; Q9XXV8; -.
DR   PRO; PR:Q9XXV8; -.
DR   Proteomes; UP000002195; Chromosome 2.
DR   GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR   GO; GO:0031252; C:cell leading edge; IDA:dictyBase.
DR   GO; GO:0005737; C:cytoplasm; IDA:dictyBase.
DR   GO; GO:0032009; C:early phagosome; IDA:dictyBase.
DR   GO; GO:0070685; C:macropinocytic cup; IDA:dictyBase.
DR   GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR   GO; GO:0001891; C:phagocytic cup; IDA:dictyBase.
DR   GO; GO:0097203; C:phagocytic cup lip; IDA:dictyBase.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0001726; C:ruffle; IDA:dictyBase.
DR   GO; GO:0051015; F:actin filament binding; IDA:dictyBase.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000146; F:microfilament motor activity; IBA:GO_Central.
DR   GO; GO:0005522; F:profilin binding; IPI:dictyBase.
DR   GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR   GO; GO:0043327; P:chemotaxis to cAMP; IBA:GO_Central.
DR   GO; GO:0030866; P:cortical actin cytoskeleton organization; IMP:dictyBase.
DR   GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR   GO; GO:0006911; P:phagocytosis, engulfment; IMP:dictyBase.
DR   GO; GO:2000147; P:positive regulation of cell motility; IMP:dictyBase.
DR   GO; GO:0050766; P:positive regulation of phagocytosis; IMP:dictyBase.
DR   GO; GO:0030050; P:vesicle transport along actin filament; IBA:GO_Central.
DR   Gene3D; 3.40.850.10; -; 2.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR001609; Myosin_head_motor_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00063; Myosin_head; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM00242; MYSc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS51456; MYOSIN_MOTOR; 1.
PE   2: Evidence at transcript level;
KW   Actin-binding; ATP-binding; Cytoplasm; Motor protein; Myosin;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..858
FT                   /note="Myosin-K heavy chain"
FT                   /id="PRO_0000328607"
FT   DOMAIN          7..820
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT   REGION          121..265
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          712..722
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000250"
FT   REGION          821..858
FT                   /note="Tail"
FT   COMPBIAS        178..231
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         100..107
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        659
FT                   /note="Y -> C (in Ref. 2; AAD47904)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   858 AA;  94364 MW;  E459F2AFDC9C2C1E CRC64;
     MFRLFSSGVD DLVLVSNPSN GEVTSQIGAR FDRELIYTNI GEVLIAVNPY KALPITGPEF
     IKLYQNASGS DASPHIYALA ERAYRRMVDE NESQCVIISG ESGAGKTVSA KLILQYVTSV
     SPNNSSGGGI GGSGGGNGGI PQYDGGSDDR PSPPMGRGMG MPGMVGRGGL PTRGGGPPSR
     GGGPPPTRGR GGPPPPIPQN RGAPPPVSNG GAPPPVARGP VAPPPTRGAP PTRGGGPANR
     GGRGGGPPPV STSRGGGGYG GSSKTVDVEH IKKVILDSNP LMEAIGNAKT VRNDNSSRFG
     KYLEIQFDDN NAPVGGLIST FLLEKTRVTF QQKNERNFHI FYQMLGGLDQ TTKSEWGLTQ
     ATDFYYLAQS KCTTVEDVDD GKDFHEVKAA METVGISRDE QTEIFRILAA ILHVGNIRFQ
     GEAPASVIDE TPLQWAASLL GCDPTFLCQS LNHRQIQSGS ARHTQYQVPQ NPDQSAGLRD
     ALAKTLYERI FDFIVARVNK AMSFSGNCKV IGVLDIYGFE VFERNSFEQF CINYVNERLQ
     QIFIDLTVRG EQREYHEEGM KWKDISFFDN KIVVDLIDGN KPPGIMRVLD DVCKTVHAVD
     SAAADIKFME KLIHSIQSHP HLVISNTGSS ADEFTIKHYA GEVSYSIEEF CFKNNDNLYA
     SIVGCLQNST YQFIVSLFPE NIQDNKQAPT TSSFKIRQSS SYLVTRLSAC TPHYIRCIKP
     NDKKQPMNFV SSRVEHQVKY LGILENIKVK RSGYAYRQLK DIFLNRFGKI MDVQPRNVQE
     FVEYITRTHK DINADEFEEG KTKIFVKNPE TIFVMEDLLM QKIDPIGYKN RVQAYKENEK
     LAQMKQGKHS MKQKCLIQ
 
 
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