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MLCD_DICDI
ID   MLCD_DICDI              Reviewed;         147 AA.
AC   Q7Z2B8; Q54YE4;
DT   02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Myosin-ID light chain;
DE   AltName: Full=Calmodulin-like protein mlcD;
DE   AltName: Full=Myosin light chain mlcD;
DE            Short=MlcD;
GN   Name=mlcD; ORFNames=DDB_G0277917;
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], PROTEIN SEQUENCE OF 40-54 AND 126-140,
RP   FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=12826013; DOI=10.1042/bj20030656;
RA   De La Roche M.A., Lee S.F., Cote G.P.;
RT   "The Dictyostelium class I myosin, MyoD, contains a novel light chain that
RT   lacks high-affinity calcium-binding sites.";
RL   Biochem. J. 374:697-705(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBUNIT.
RX   PubMed=16415352; DOI=10.1074/jbc.m508670200;
RA   Crawley S.W., de la Roche M.A., Lee S.F., Li Z., Chitayat S., Smith S.P.,
RA   Cote G.P.;
RT   "Identification and characterization of an 8-kDa light chain associated
RT   with Dictyostelium discoideum MyoB, a class I myosin.";
RL   J. Biol. Chem. 281:6307-6315(2006).
RN   [3]
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).
CC   -!- FUNCTION: Functions as the light chain for myosin-D. Has low affinity
CC       for calcium. {ECO:0000269|PubMed:12826013,
CC       ECO:0000269|PubMed:16415352}.
CC   -!- SUBUNIT: Myosin I is a dimer of a heavy and a light chain. Inability to
CC       self-assemble into filaments (By similarity). Interacts with myoD. Does
CC       not interact with myoB or myoC. {ECO:0000250,
CC       ECO:0000269|PubMed:12826013, ECO:0000269|PubMed:16415352}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12826013}.
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DR   EMBL; AY280458; AAP34384.1; -; Genomic_DNA.
DR   EMBL; AAFI02000023; EAL68131.1; -; Genomic_DNA.
DR   RefSeq; XP_642258.1; XM_637166.1.
DR   AlphaFoldDB; Q7Z2B8; -.
DR   SMR; Q7Z2B8; -.
DR   STRING; 44689.DDB0214812; -.
DR   PaxDb; Q7Z2B8; -.
DR   PRIDE; Q7Z2B8; -.
DR   EnsemblProtists; EAL68131; EAL68131; DDB_G0277917.
DR   GeneID; 8621467; -.
DR   KEGG; ddi:DDB_G0277917; -.
DR   dictyBase; DDB_G0277917; mlcD.
DR   eggNOG; KOG0027; Eukaryota.
DR   HOGENOM; CLU_061288_2_0_1; -.
DR   InParanoid; Q7Z2B8; -.
DR   OMA; KDGKGMI; -.
DR   PhylomeDB; Q7Z2B8; -.
DR   Reactome; R-DDI-111932; CaMK IV-mediated phosphorylation of CREB.
DR   Reactome; R-DDI-111957; Cam-PDE 1 activation.
DR   Reactome; R-DDI-114608; Platelet degranulation.
DR   Reactome; R-DDI-1474151; Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
DR   Reactome; R-DDI-163615; PKA activation.
DR   Reactome; R-DDI-1855204; Synthesis of IP3 and IP4 in the cytosol.
DR   Reactome; R-DDI-203615; eNOS activation.
DR   Reactome; R-DDI-2871809; FCERI mediated Ca+2 mobilization.
DR   Reactome; R-DDI-4086398; Ca2+ pathway.
DR   Reactome; R-DDI-442729; CREB1 phosphorylation through the activation of CaMKII/CaMKK/CaMKIV cascasde.
DR   Reactome; R-DDI-5218920; VEGFR2 mediated vascular permeability.
DR   Reactome; R-DDI-5607763; CLEC7A (Dectin-1) induces NFAT activation.
DR   Reactome; R-DDI-5626467; RHO GTPases activate IQGAPs.
DR   Reactome; R-DDI-6798695; Neutrophil degranulation.
DR   Reactome; R-DDI-9009391; Extra-nuclear estrogen signaling.
DR   Reactome; R-DDI-9619229; Activation of RAC1 downstream of NMDARs.
DR   Reactome; R-DDI-9648002; RAS processing.
DR   PRO; PR:Q7Z2B8; -.
DR   Proteomes; UP000002195; Chromosome 3.
DR   GO; GO:0062201; C:actin wave; IDA:dictyBase.
DR   GO; GO:0070687; C:macropinocytic cup cytoskeleton; IDA:dictyBase.
DR   GO; GO:0016459; C:myosin complex; IDA:dictyBase.
DR   GO; GO:0005509; F:calcium ion binding; IDA:dictyBase.
DR   GO; GO:0030234; F:enzyme regulator activity; IBA:GO_Central.
DR   GO; GO:0032036; F:myosin heavy chain binding; IPI:dictyBase.
DR   CDD; cd00051; EFh; 1.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   Pfam; PF13202; EF-hand_5; 1.
DR   Pfam; PF13405; EF-hand_6; 1.
DR   SMART; SM00054; EFh; 2.
DR   SUPFAM; SSF47473; SSF47473; 1.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 3.
PE   1: Evidence at protein level;
KW   Calcium; Cytoplasm; Direct protein sequencing; Metal-binding;
KW   Motor protein; Myosin; Reference proteome; Repeat.
FT   CHAIN           1..147
FT                   /note="Myosin-ID light chain"
FT                   /id="PRO_0000391642"
FT   DOMAIN          8..43
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          79..114
FT                   /note="EF-hand 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          115..147
FT                   /note="EF-hand 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         21
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         23
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         25
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         27
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         32
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
SQ   SEQUENCE   147 AA;  16519 MW;  82F86317710FC854 CRC64;
     MASKLNEEAQ SEFKEGFALY DGNKDGKLEA AELANTLRWL GQNPSQSEIN EILREFGSNN
     QMGVDGLFNY LGRKVVDDFD EKEIIEAFQV FDKDGKGMIG ASDLRHILTN LGERLPEEQV
     EEMLRQAVGS GDGAINYEPF VRNMLKK
 
 
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