CAM2_SCHPO
ID CAM2_SCHPO Reviewed; 143 AA.
AC O14008;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Myosin 1 light chain cam2;
DE AltName: Full=Calmodulin-2;
GN Name=cam2 {ECO:0000312|EMBL:CAB10132.1}; ORFNames=SPAC29A4.05;
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] {ECO:0000312|EMBL:CAB10132.1}
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] {ECO:0000305}
RP FUNCTION.
RX PubMed=12161753; DOI=10.1038/ng951;
RA Mata J., Lyne R., Burns G., Baehler J.;
RT "The transcriptional program of meiosis and sporulation in fission yeast.";
RL Nat. Genet. 32:143-147(2002).
RN [3] {ECO:0000305}
RP GENE NAME, AND INTERACTION WITH MYO1.
RX PubMed=15504913; DOI=10.1083/jcb.200404045;
RA Lord M., Pollard T.D.;
RT "UCS protein Rng3p activates actin filament gliding by fission yeast
RT myosin-II.";
RL J. Cell Biol. 167:315-325(2004).
RN [4] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17202724; DOI=10.1247/csf.06027;
RA Itadani A., Nakamura T., Shimoda C.;
RT "Localization of type I myosin and F-actin to the leading edge region of
RT the forespore membrane in Schizosaccharomyces pombe.";
RL Cell Struct. Funct. 31:181-195(2006).
RN [5] {ECO:0000305}
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [6]
RP FUNCTION, AND INTERACTION WITH PIK1.
RX PubMed=21693583; DOI=10.1242/jcs.067850;
RA Sammons M.R., James M.L., Clayton J.E., Sladewski T.E., Sirotkin V.,
RA Lord M.;
RT "A calmodulin-related light chain from fission yeast that functions with
RT myosin-I and PI 4-kinase.";
RL J. Cell Sci. 124:2466-2477(2011).
CC -!- FUNCTION: Plays a role in meiosis and sporulation.
CC {ECO:0000269|PubMed:12161753, ECO:0000269|PubMed:17202724,
CC ECO:0000269|PubMed:21693583}.
CC -!- SUBUNIT: Interacts with myo1 and pik1. {ECO:0000269|PubMed:15504913,
CC ECO:0000269|PubMed:21693583}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372,
CC ECO:0000269|PubMed:17202724}. Prospore membrane. Note=Accumulates at
CC the cell poles in interphase cells and at the medial septation site in
CC post-mitotic cells, colocalizing with myo1 and F-actin patches. During
CC the mating process, a single dot is detected a the tip of the mating
CC projection. During meiosis I, dots disperse into the cell periphery and
CC the cytoplasm. At metaphase II, intense signals appear near meu14 rings
CC which are formed at the leading edge of expanding forespore membranes.
CC Localization is dependent upon myo1 with the exception of the
CC localization to mating projections. {ECO:0000269|PubMed:16823372,
CC ECO:0000269|PubMed:17202724}.
CC -!- INDUCTION: Five-fold increase in meiosis in mei4-dependent manner.
CC {ECO:0000269|PubMed:17202724}.
CC -!- DISRUPTION PHENOTYPE: Cells are viable and complete sporulation
CC normally at 28 degrees Celsius, but form four-spored asci poorly at 34
CC degrees Celsius. In sporulation-defective cells, the forespore membrane
CC (FSM) is formed abnormally and F-actin localization is aberrant. Only
CC fragmented or anucleated FSMs are formed and F-actin dots remain at
CC peripheral regions of mother cells even during meiosis II. Sporulation
CC defect is alleviated by overexpressing myo1 from which IQ domain is
CC deleted. {ECO:0000269|PubMed:17202724}.
CC -!- SIMILARITY: Belongs to the calmodulin family. {ECO:0000255}.
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DR EMBL; CU329670; CAB10132.1; -; Genomic_DNA.
DR PIR; T38484; T38484.
DR RefSeq; NP_594877.1; NM_001020306.2.
DR AlphaFoldDB; O14008; -.
DR SMR; O14008; -.
DR BioGRID; 279065; 11.
DR STRING; 4896.SPAC29A4.05.1; -.
DR iPTMnet; O14008; -.
DR MaxQB; O14008; -.
DR PaxDb; O14008; -.
DR PRIDE; O14008; -.
DR EnsemblFungi; SPAC29A4.05.1; SPAC29A4.05.1:pep; SPAC29A4.05.
DR GeneID; 2542611; -.
DR KEGG; spo:SPAC29A4.05; -.
DR PomBase; SPAC29A4.05; cam2.
DR VEuPathDB; FungiDB:SPAC29A4.05; -.
DR eggNOG; KOG0027; Eukaryota.
DR HOGENOM; CLU_061288_2_0_1; -.
DR InParanoid; O14008; -.
DR OMA; MVQEADP; -.
DR PhylomeDB; O14008; -.
DR Reactome; R-SPO-111932; CaMK IV-mediated phosphorylation of CREB.
DR Reactome; R-SPO-114608; Platelet degranulation.
DR Reactome; R-SPO-1474151; Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
DR Reactome; R-SPO-203615; eNOS activation.
DR Reactome; R-SPO-2871809; FCERI mediated Ca+2 mobilization.
DR Reactome; R-SPO-4086398; Ca2+ pathway.
DR Reactome; R-SPO-442729; CREB1 phosphorylation through the activation of CaMKII/CaMKK/CaMKIV cascasde.
DR Reactome; R-SPO-5218920; VEGFR2 mediated vascular permeability.
DR Reactome; R-SPO-5607763; CLEC7A (Dectin-1) induces NFAT activation.
DR Reactome; R-SPO-5626467; RHO GTPases activate IQGAPs.
DR Reactome; R-SPO-6798695; Neutrophil degranulation.
DR Reactome; R-SPO-9009391; Extra-nuclear estrogen signaling.
DR Reactome; R-SPO-9619229; Activation of RAC1 downstream of NMDARs.
DR PRO; PR:O14008; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:1990819; C:actin fusion focus; IDA:PomBase.
DR GO; GO:0005938; C:cell cortex; IDA:PomBase.
DR GO; GO:0051286; C:cell tip; IDA:PomBase.
DR GO; GO:0030863; C:cortical cytoskeleton; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0043332; C:mating projection tip; IDA:PomBase.
DR GO; GO:0031097; C:medial cortex; IDA:PomBase.
DR GO; GO:0045160; C:myosin I complex; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005628; C:prospore membrane; IDA:PomBase.
DR GO; GO:0005509; F:calcium ion binding; ISM:PomBase.
DR GO; GO:0030234; F:enzyme regulator activity; IPI:PomBase.
DR GO; GO:0030036; P:actin cytoskeleton organization; IMP:PomBase.
DR GO; GO:0030048; P:actin filament-based movement; IC:PomBase.
DR GO; GO:0030437; P:ascospore formation; IMP:PomBase.
DR GO; GO:0032120; P:ascospore-type prospore membrane formation; IMP:PomBase.
DR GO; GO:0000917; P:division septum assembly; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW Cell cycle; Cell division; Cytoplasm; Meiosis; Membrane;
KW Reference proteome; Repeat; Septation; Sporulation.
FT CHAIN 1..143
FT /note="Myosin 1 light chain cam2"
FT /id="PRO_0000334492"
FT DOMAIN 6..41
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 75..110
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 111..143
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
SQ SEQUENCE 143 AA; 16218 MW; 320B01DE79909468 CRC64;
MPASKEQTDE MKEAFVLYDI DKDGLIPTSH VGSVLRSLGI NVTDAELAKL SNELGDAIDE
KKFMSFVSNK LRETESEEEY IKAFRVFDKD NSGYIETAKF ADYMKTLGEK LSDNEVQLMV
QEADPTNSGS FDYYDFVQRI MAK
