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 24-JAN-2024, entry version 148.
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}.
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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; 284812.Q9UUG5; -.
DR iPTMnet; Q9UUG5; -.
DR MaxQB; Q9UUG5; -.
DR PaxDb; 4896-SPAC926-03-1; -.
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 Gene3D; 1.10.238.10; EF-hand; 2.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR PANTHER; PTHR23049; MYOSIN REGULATORY LIGHT CHAIN 2; 1.
DR PANTHER; PTHR23049:SF34; MYOSIN REGULATORY LIGHT CHAIN SQH; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR SMART; SM00054; EFh; 2.
DR SUPFAM; SSF47473; EF-hand; 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
//
