MLR4_SCHPO
ID MLR4_SCHPO Reviewed; 141 AA.
AC Q09196;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Myosin regulatory light chain cdc4;
GN Name=cdc4; ORFNames=SPAP8A3.08;
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 [GENOMIC DNA].
RX PubMed=7622565; DOI=10.1083/jcb.130.3.651;
RA McCollum D., Balasubramanian M.K., Pelcher L.E., Hemmingsen S.M.,
RA Gould K.L.;
RT "Schizosaccharomyces pombe cdc4+ gene encodes a novel EF-hand protein
RT essential for cytokinesis.";
RL J. Cell Biol. 130:651-660(1995).
RN [2]
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 [3]
RP PHOSPHORYLATION AT SER-2 AND SER-6.
RX PubMed=10364209; DOI=10.1074/jbc.274.25.17691;
RA McCollum D., Feoktistova A., Gould K.L.;
RT "Phosphorylation of the myosin-II light chain does not regulate the timing
RT of cytokinesis in fission yeast.";
RL J. Biol. Chem. 274:17691-17695(1999).
RN [4]
RP INTERACTION.
RX PubMed=11087749; DOI=10.1074/jbc.m008715200;
RA Desautels M., Den Haese J.P., Slupsky C.M., McIntosh L.P., Hemmingsen S.M.;
RT "Cdc4p, a contractile ring protein essential for cytokinesis in
RT Schizosaccharomyces pombe, interacts with a phosphatidylinositol 4-
RT kinase.";
RL J. Biol. Chem. 276:5932-5942(2001).
RN [5]
RP STRUCTURE BY NMR.
RX PubMed=11087750; DOI=10.1074/jbc.m008716200;
RA Slupsky C.M., Desautels M., Huebert T., Zhao R., Hemmingsen S.M.,
RA McIntosh L.P.;
RT "Structure of Cdc4p, a contractile ring protein essential for cytokinesis
RT in Schizosaccharomyces pombe.";
RL J. Biol. Chem. 276:5943-5951(2001).
CC -!- FUNCTION: Involved in cytokinesis. Required for the formation and
CC function of the contractile ring.
CC -!- SUBUNIT: Binds to myosin II chains myo2 and myo3. Interacts with vps27
CC and a PI 4-kinase pik1. {ECO:0000269|PubMed:11087749}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- PTM: Phosphorylated on either Ser-2 or Ser-6 but not both.
CC Phosphorylation is not essential for the function of the protein.
CC {ECO:0000269|PubMed:10364209}.
CC -!- MISCELLANEOUS: In vitro, this chain does not seem to bind calcium.
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DR EMBL; L42454; AAA67467.1; -; Genomic_DNA.
DR EMBL; CU329670; CAB55175.1; -; Genomic_DNA.
DR PIR; T39245; T39245.
DR RefSeq; NP_594947.1; NM_001020378.2.
DR PDB; 1GGW; NMR; -; A=2-141.
DR PDBsum; 1GGW; -.
DR AlphaFoldDB; Q09196; -.
DR BMRB; Q09196; -.
DR SMR; Q09196; -.
DR BioGRID; 278195; 38.
DR STRING; 4896.SPAP8A3.08.1; -.
DR iPTMnet; Q09196; -.
DR MaxQB; Q09196; -.
DR PaxDb; Q09196; -.
DR EnsemblFungi; SPAP8A3.08.1; SPAP8A3.08.1:pep; SPAP8A3.08.
DR GeneID; 2541699; -.
DR KEGG; spo:SPAP8A3.08; -.
DR PomBase; SPAP8A3.08; cdc4.
DR VEuPathDB; FungiDB:SPAP8A3.08; -.
DR eggNOG; KOG0027; Eukaryota.
DR HOGENOM; CLU_061288_13_1_1; -.
DR InParanoid; Q09196; -.
DR OMA; DIRYMLT; -.
DR PhylomeDB; Q09196; -.
DR Reactome; R-SPO-5627123; RHO GTPases activate PAKs.
DR EvolutionaryTrace; Q09196; -.
DR PRO; PR:Q09196; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0032153; C:cell division site; HDA:PomBase.
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:0016460; C:myosin II complex; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000917; P:division septum assembly; IEA:UniProtKB-KW.
DR GO; GO:1903475; P:mitotic actomyosin contractile ring assembly; IMP:PomBase.
DR GO; GO:1902404; P:mitotic actomyosin contractile ring contraction; EXP:PomBase.
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 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 3D-structure; Calcium; Cell cycle; Cell division; Cytoplasm; Metal-binding;
KW Motor protein; Myosin; Phosphoprotein; Reference proteome; Repeat;
KW Septation.
FT CHAIN 1..141
FT /note="Myosin regulatory light chain cdc4"
FT /id="PRO_0000198763"
FT DOMAIN 3..38
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 74..109
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 109..141
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 87
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 89
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 91
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 93
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 98
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:10364209"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:10364209"
FT TURN 6..8
FT /evidence="ECO:0007829|PDB:1GGW"
FT HELIX 9..14
FT /evidence="ECO:0007829|PDB:1GGW"
FT STRAND 17..23
FT /evidence="ECO:0007829|PDB:1GGW"
FT HELIX 25..34
FT /evidence="ECO:0007829|PDB:1GGW"
FT HELIX 41..48
FT /evidence="ECO:0007829|PDB:1GGW"
FT STRAND 53..56
FT /evidence="ECO:0007829|PDB:1GGW"
FT HELIX 57..64
FT /evidence="ECO:0007829|PDB:1GGW"
FT STRAND 68..73
FT /evidence="ECO:0007829|PDB:1GGW"
FT HELIX 76..84
FT /evidence="ECO:0007829|PDB:1GGW"
FT HELIX 96..107
FT /evidence="ECO:0007829|PDB:1GGW"
FT HELIX 112..121
FT /evidence="ECO:0007829|PDB:1GGW"
FT TURN 130..132
FT /evidence="ECO:0007829|PDB:1GGW"
FT HELIX 133..139
FT /evidence="ECO:0007829|PDB:1GGW"
SQ SEQUENCE 141 AA; 15661 MW; 691731DD7C6A68A9 CRC64;
MSTDDSPYKQ AFSLFDRHGT GRIPKTSIGD LLRACGQNPT LAEITEIEST LPAEVDMEQF
LQVLNRPNGF DMPGDPEEFV KGFQVFDKDA TGMIGVGELR YVLTSLGEKL SNEEMDELLK
GVPVKDGMVN YHDFVQMILA N
