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MLR_DICDI
ID   MLR_DICDI               Reviewed;         161 AA.
AC   P13833; Q552B5; Q75JL0;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   25-MAY-2022, entry version 123.
DE   RecName: Full=Myosin regulatory light chain;
DE   AltName: Full=RMLC;
GN   Name=mlcR; Synonyms=mlcA; ORFNames=DDB_G0276077;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2550795; DOI=10.1128/mcb.9.7.3073-3080.1989;
RA   Tafuri S.R., Rushforth A.M., Kuczmarski E.R., Chisholm R.L.;
RT   "Dictyostelium discoideum myosin: isolation and characterization of cDNAs
RT   encoding the regulatory light chain.";
RL   Mol. Cell. Biol. 9:3073-3080(1989).
RN   [2]
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   [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   -!- SUBUNIT: Myosin is a hexamer of 2 heavy chains and 4 light chains (two
CC       regulatory light chains and two essential light chains).
CC   -!- MISCELLANEOUS: The sequences of all three RMLC calcium-binding domains
CC       have diverged significantly from that of calmodulin. Therefore, it
CC       seems unlikely that these light chains bind calcium. It is potential
CC       that phosphorylation has taken over the role of calcium-binding in the
CC       regulation of Dictyostelium myosin.
CC   -!- MISCELLANEOUS: In D.discoideum, cAMP stimulation induces RMLC
CC       phosphorylation; this chain is phosphorylated on a serine residue.
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DR   EMBL; M25251; AAA33226.1; -; mRNA.
DR   EMBL; AAFI02000014; EAL69338.1; -; Genomic_DNA.
DR   PIR; A32496; A30938.
DR   RefSeq; XP_643313.1; XM_638221.1.
DR   AlphaFoldDB; P13833; -.
DR   SMR; P13833; -.
DR   STRING; 44689.DDB0185146; -.
DR   PaxDb; P13833; -.
DR   EnsemblProtists; EAL69338; EAL69338; DDB_G0276077.
DR   GeneID; 8620359; -.
DR   KEGG; ddi:DDB_G0276077; -.
DR   dictyBase; DDB_G0276077; mlcR.
DR   eggNOG; KOG0027; Eukaryota.
DR   HOGENOM; CLU_061288_2_1_1; -.
DR   InParanoid; P13833; -.
DR   OMA; FPPDMCG; -.
DR   PhylomeDB; P13833; -.
DR   Reactome; R-DDI-5627123; RHO GTPases activate PAKs.
DR   PRO; PR:P13833; -.
DR   Proteomes; UP000002195; Chromosome 2.
DR   GO; GO:0042641; C:actomyosin; IDA:dictyBase.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0016460; C:myosin II complex; IDA:dictyBase.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0140660; F:cytoskeletal motor activator activity; IDA:dictyBase.
DR   GO; GO:0032036; F:myosin heavy chain binding; IDA:dictyBase.
DR   GO; GO:0000281; P:mitotic cytokinesis; IMP:dictyBase.
DR   GO; GO:0031034; P:myosin filament assembly; IDA:dictyBase.
DR   GO; GO:0031038; P:myosin II filament organization; IDA:dictyBase.
DR   GO; GO:1903610; P:regulation of calcium-dependent ATPase activity; IDA:dictyBase.
DR   GO; GO:1903013; P:response to differentiation-inducing factor 1; HDA:dictyBase.
DR   GO; GO:0030587; P:sorocarp development; IMP:dictyBase.
DR   CDD; cd00051; EFh; 1.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR002048; EF_hand_dom.
DR   Pfam; PF13499; EF-hand_7; 1.
DR   SMART; SM00054; EFh; 3.
DR   SUPFAM; SSF47473; SSF47473; 1.
DR   PROSITE; PS50222; EF_HAND_2; 3.
PE   2: Evidence at transcript level;
KW   Motor protein; Myosin; Phosphoprotein; Reference proteome; Repeat.
FT   CHAIN           1..161
FT                   /note="Myosin regulatory light chain"
FT                   /id="PRO_0000198759"
FT   DOMAIN          20..55
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          56..91
FT                   /note="EF-hand 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          93..128
FT                   /note="EF-hand 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   MOD_RES         13
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         14
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   161 AA;  18323 MW;  354B704B20F4E2C3 CRC64;
     MASTKRRLNR EESSVVLGEE QVAELKEAFE LFDKDRTGFI KKDALKTTCK QFGVFVMEDQ
     LDAMFAEADT TKSGAIGFPE FMSMMSRRMK QTSNEQILMN AFKTFDPEGN GYILTKDLSK
     ALTTLGDKLT EAELQELLSI SENEQKQVKY DLFVNTLFSK K
 
 
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