位置:首页 > 蛋白库 > MLR1_SCHPO
MLR1_SCHPO
ID   MLR1_SCHPO              Reviewed;         184 AA.
AC   Q9UUG5;
DT   14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 143.
DE   RecName: Full=Myosin regulatory light chain 1;
GN   Name=rlc1; ORFNames=SPAC926.03;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   IDENTIFICATION, AND CHARACTERIZATION.
RX   PubMed=11069761; DOI=10.1242/jcs.113.23.4157;
RA   Le Goff X., Motegi F., Salimova E., Mabuchi I., Simanis V.;
RT   "The S. pombe rlc1 gene encodes a putative myosin regulatory light chain
RT   that binds the type II myosins myo3p and myo2p.";
RL   J. Cell Sci. 113:4157-4163(2000).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RX   PubMed=18257517; DOI=10.1021/pr7006335;
RA   Wilson-Grady J.T., Villen J., Gygi S.P.;
RT   "Phosphoproteome analysis of fission yeast.";
RL   J. Proteome Res. 7:1088-1097(2008).
CC   -!- SUBUNIT: Binds to myosin II chains myo2 and myo3.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- MISCELLANEOUS: This chain binds calcium. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CU329670; CAB54151.1; -; Genomic_DNA.
DR   PIR; T39201; T39201.
DR   RefSeq; NP_594364.1; NM_001019785.2.
DR   AlphaFoldDB; Q9UUG5; -.
DR   SMR; Q9UUG5; -.
DR   BioGRID; 279962; 20.
DR   STRING; 4896.SPAC926.03.1; -.
DR   iPTMnet; Q9UUG5; -.
DR   MaxQB; Q9UUG5; -.
DR   PaxDb; Q9UUG5; -.
DR   PRIDE; Q9UUG5; -.
DR   EnsemblFungi; SPAC926.03.1; SPAC926.03.1:pep; SPAC926.03.
DR   GeneID; 2543545; -.
DR   KEGG; spo:SPAC926.03; -.
DR   PomBase; SPAC926.03; rlc1.
DR   VEuPathDB; FungiDB:SPAC926.03; -.
DR   eggNOG; KOG0031; Eukaryota.
DR   HOGENOM; CLU_061288_9_2_1; -.
DR   InParanoid; Q9UUG5; -.
DR   OMA; FECFDEN; -.
DR   PhylomeDB; Q9UUG5; -.
DR   Reactome; R-SPO-5627123; RHO GTPases activate PAKs.
DR   PRO; PR:Q9UUG5; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0071341; C:medial cortical node; IDA:PomBase.
DR   GO; GO:0110085; C:mitotic actomyosin contractile ring; IDA:PomBase.
DR   GO; GO:0120106; C:mitotic actomyosin contractile ring, distal actin filament layer; IDA:PomBase.
DR   GO; GO:0016460; C:myosin II complex; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0005509; F:calcium ion binding; ISM:PomBase.
DR   GO; GO:0140659; F:cytoskeletal motor regulator activity; EXP:PomBase.
DR   GO; GO:0017022; F:myosin binding; IPI:PomBase.
DR   GO; GO:0032036; F:myosin heavy chain binding; IBA:GO_Central.
DR   GO; GO:0031032; P:actomyosin structure organization; IBA:GO_Central.
DR   GO; GO:1902404; P:mitotic actomyosin contractile ring contraction; IMP:PomBase.
DR   GO; GO:0000281; P:mitotic cytokinesis; IBA:GO_Central.
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; PF00036; EF-hand_1; 1.
DR   SMART; SM00054; EFh; 2.
DR   SUPFAM; SSF47473; SSF47473; 1.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 2.
PE   1: Evidence at protein level;
KW   Calcium; Cytoplasm; Metal-binding; Motor protein; Myosin; Phosphoprotein;
KW   Reference proteome; Repeat.
FT   CHAIN           1..184
FT                   /note="Myosin regulatory light chain 1"
FT                   /id="PRO_0000198764"
FT   DOMAIN          45..80
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          114..149
FT                   /note="EF-hand 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         58
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         60
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         62
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         64
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         69
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   MOD_RES         36
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
SQ   SEQUENCE   184 AA;  19997 MW;  0E7CD52BF74ADD1E CRC64;
     MFSSKENSLG AKRAPFSSNT TSSQRVAAQA AKRASSGAFA QLTSSQIQEL KEAFALLDKD
     GDGNIGREDV KTMLTSLNQD ASEDSINHMF ESINPPINLA AFLTAMGSML CRISPRNDLL
     EAFSTFDDTQ SGKIPISTMR DALSSMGDRM DPQEVESILR SYTSHGVFYY EKFVDAIAGS
     KDSN
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024