MSY1_SCHPO
ID MSY1_SCHPO Reviewed; 1011 AA.
AC O74839;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 135.
DE RecName: Full=Mechanosensitive ion channel protein Msy1 {ECO:0000303|PubMed:22910366};
GN Name=msy1 {ECO:0000303|PubMed:22910366};
GN ORFNames=SPCC1183.11 {ECO:0000312|PomBase:SPCC1183.11},
GN SPCC31H12.01 {ECO:0000312|PomBase:SPCC1183.11};
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 INDUCTION.
RX PubMed=12529438; DOI=10.1091/mbc.e02-08-0499;
RA Chen D., Toone W.M., Mata J., Lyne R., Burns G., Kivinen K., Brazma A.,
RA Jones N., Baehler J.;
RT "Global transcriptional responses of fission yeast to environmental
RT stress.";
RL Mol. Biol. Cell 14:214-229(2003).
RN [3]
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98, 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).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION, DOMAIN, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF ASP-544; GLU-549; ASP-556; ASP-558; ASP-562; GLU-566;
RP GLU-567; GLU-569; GLU-574 AND GLU-578.
RX PubMed=22910366; DOI=10.1038/ncomms2014;
RA Nakayama Y., Yoshimura K., Iida H.;
RT "Organellar mechanosensitive channels in fission yeast regulate the hypo-
RT osmotic shock response.";
RL Nat. Commun. 3:1020-1020(2012).
RN [6]
RP FUNCTION.
RX PubMed=25041276; DOI=10.1111/1567-1364.12181;
RA Nakayama Y., Hirata A., Iida H.;
RT "Mechanosensitive channels Msy1 and Msy2 are required for maintaining
RT organelle integrity upon hypoosmotic shock in Schizosaccharomyces pombe.";
RL FEMS Yeast Res. 14:992-994(2014).
CC -!- FUNCTION: Regulates intracellular calcium levels and cell volume for
CC survival in response to hypo-osmotic shock. Acts as a mechanosensitive
CC calcium channel in response to membrane stretch. The conductance is
CC about 0.25 nanosiemens (PubMed:22910366). Involved in maintaining
CC vacuole integrity and protecting the nuclear envelope upon hypo-osmotic
CC shock (PubMed:25041276). {ECO:0000269|PubMed:22910366,
CC ECO:0000269|PubMed:25041276}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:22910366}; Multi-pass membrane protein
CC {ECO:0000305}. Note=Perinuclear endoplasmic reticulum.
CC {ECO:0000269|PubMed:22910366}.
CC -!- INDUCTION: By stress (PubMed:12529438). Up-regulated by both hyper- and
CC hypo-osmotic shocks (PubMed:22910366). {ECO:0000269|PubMed:12529438,
CC ECO:0000269|PubMed:22910366}.
CC -!- DOMAIN: EF-hand domain is involved in the detection of calcium
CC concentration. {ECO:0000305|PubMed:22910366}.
CC -!- DISRUPTION PHENOTYPE: Upon hypo-osmotic shock, the viability of the
CC cells is not significantly different from that of wild-type, but an
CC increase in cell volume is accompanied by an abnormally high increase
CC in intracellular calcium concentration compared to wild-type.
CC {ECO:0000269|PubMed:22910366}.
CC -!- SIMILARITY: Belongs to the MscS (TC 1.A.23) family. {ECO:0000305}.
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DR EMBL; CU329672; CAA21091.1; -; Genomic_DNA.
DR PIR; T40851; T40851.
DR PIR; T41289; T41289.
DR RefSeq; NP_587894.1; NM_001022886.2.
DR AlphaFoldDB; O74839; -.
DR BioGRID; 275624; 52.
DR STRING; 4896.SPCC1183.11.1; -.
DR iPTMnet; O74839; -.
DR MaxQB; O74839; -.
DR PaxDb; O74839; -.
DR PRIDE; O74839; -.
DR EnsemblFungi; SPCC1183.11.1; SPCC1183.11.1:pep; SPCC1183.11.
DR GeneID; 2539051; -.
DR KEGG; spo:SPCC1183.11; -.
DR PomBase; SPCC1183.11; msy1.
DR VEuPathDB; FungiDB:SPCC1183.11; -.
DR eggNOG; KOG4629; Eukaryota.
DR HOGENOM; CLU_010480_1_0_1; -.
DR InParanoid; O74839; -.
DR OMA; FMCALMT; -.
DR PhylomeDB; O74839; -.
DR PRO; PR:O74839; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; ISM:PomBase.
DR GO; GO:0097038; C:perinuclear endoplasmic reticulum; IDA:PomBase.
DR GO; GO:0005262; F:calcium channel activity; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; NAS:PomBase.
DR GO; GO:0015275; F:stretch-activated, cation-selective, calcium channel activity; IDA:PomBase.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IDA:PomBase.
DR GO; GO:0006884; P:cell volume homeostasis; IMP:PomBase.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IMP:PomBase.
DR Gene3D; 2.30.30.60; -; 1.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR010920; LSM_dom_sf.
DR InterPro; IPR016688; MscS-like_plants/fungi.
DR InterPro; IPR006685; MscS_channel.
DR InterPro; IPR023408; MscS_dom_sf.
DR Pfam; PF00924; MS_channel; 1.
DR PIRSF; PIRSF017209; Memb_At2g17000_prd; 1.
DR SUPFAM; SSF50182; SSF50182; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
PE 1: Evidence at protein level;
KW Calcium; Calcium channel; Calcium transport; Endoplasmic reticulum;
KW Ion channel; Ion transport; Membrane; Phosphoprotein; Reference proteome;
KW Stress response; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1011
FT /note="Mechanosensitive ion channel protein Msy1"
FT /id="PRO_0000372692"
FT TOPO_DOM 1..223
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 224..244
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 245..287
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 288..308
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 309..319
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 320..340
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 341..366
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 367..387
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 388..595
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 596..616
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 617..633
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 634..654
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 655..1011
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 543..578
FT /note="EF-hand"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 1..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 124..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 834..882
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 917..1011
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..96
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..177
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 925..952
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 953..979
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 996..1011
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 98
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MUTAGEN 544
FT /note="D->A: Viability decreases in a calcium-dependent
FT manner; when associated with A-549; A-556; A-558; A-562; A-
FT 566; A-567; A-569; A-574 and A-578."
FT /evidence="ECO:0000269|PubMed:22910366"
FT MUTAGEN 549
FT /note="E->A: Viability decreases in a calcium-dependent
FT manner; when associated with A-544; A-556; A-558; A-562; A-
FT 566; A-567; A-569; A-574 and A-578."
FT /evidence="ECO:0000269|PubMed:22910366"
FT MUTAGEN 556
FT /note="D->A: Viability decreases in a calcium-dependent
FT manner; when associated with A-544; A-549; A-558; A-562; A-
FT 566; A-567; A-569; A-574 and A-578."
FT /evidence="ECO:0000269|PubMed:22910366"
FT MUTAGEN 558
FT /note="D->A: Viability decreases in a calcium-dependent
FT manner; when associated with A-544; A-549; A-556; A-562; A-
FT 566; A-567; A-569; A-574 and A-578."
FT /evidence="ECO:0000269|PubMed:22910366"
FT MUTAGEN 562
FT /note="D->A: Viability decreases in a calcium-dependent
FT manner; when associated with A-544; A-549; A-556; A-558; A-
FT 566; A-567; A-569; A-574 and A-578."
FT /evidence="ECO:0000269|PubMed:22910366"
FT MUTAGEN 566
FT /note="E->A: Viability decreases in a calcium-dependent
FT manner; when associated with A-544; A-549; A-556; A-558; A-
FT 562; A-567; A-569; A-574 and A-578."
FT /evidence="ECO:0000269|PubMed:22910366"
FT MUTAGEN 567
FT /note="E->A: Viability decreases in a calcium-dependent
FT manner; when associated with A-544; A-549; A-556; A-558; A-
FT 562; A-566; A-569; A-574 and A-578."
FT /evidence="ECO:0000269|PubMed:22910366"
FT MUTAGEN 569
FT /note="E->A: Viability decreases in a calcium-dependent
FT manner; when associated with A-544; A-549; A-556; A-558; A-
FT 562; A-566; A-567; A-574 and A-578."
FT /evidence="ECO:0000269|PubMed:22910366"
FT MUTAGEN 574
FT /note="E->A: Viability decreases in a calcium-dependent
FT manner; when associated with A-544; A-549; A-556; A-558; A-
FT 562; A-566; A-567; A-569 and A-578."
FT /evidence="ECO:0000269|PubMed:22910366"
FT MUTAGEN 578
FT /note="E->A: Viability decreases in a calcium-dependent
FT manner; when associated with A-544; A-549; A-556; A-558; A-
FT 562; A-566; A-567; A-569 and A-574."
FT /evidence="ECO:0000269|PubMed:22910366"
SQ SEQUENCE 1011 AA; 114270 MW; 130268383BAC54F3 CRC64;
MSSPTSPTSS PGRHHWSNSK DGMPPEYTNQ DPNSDQADNE NSDAKAHQPQ HSPQHSTENQ
GHTGTSDTSS LEMELSKLHP ESKQRQLPHS PEHERSRSPI ASVVSYRSHM TLEDENQIFN
AEMAVRGSQS LQRRPTGRSV RGSMRRLSSH RSKSMRTSKS KKSGDYERTA ENEEAAQEAE
NHLDNFGVVT FGTEAPIKAP DHPVTIFGRI FKFIQQRSFY LRSLIYIIPL GVLLLIPVFI
GRFYHPQPPY RDELGHEYER HLHVGGVDLM WMAIWWEIIW LSIWAARYAA KVIPYFFAFF
VSFISNNVTK WRCMAVALEF PITLFLWMLA VYVSFLPIMT RRHIGDYGVP DHVRVKLPWQ
QSANNVLITL FITSIMNLVE KVLMQLIAMS LHRREYESRI LYNKFAINEL ARLYGYARQR
SFDFKDAIHR AQADVFKFAD HQHGKKRAAA ARVAQNALNK TTYKAISAFN FATDMVNKVA
GEITNREVEK SSSPKSVVLH LLKTTRGCQS LARCLFEALV NPENPDLVLD DFIPVYTDET
GEVDNATLEA CYSIFDRDLN GDITCEEIEL ACVEIGKERK SISASLRDLN DSISKLDGIC
MFIVAVITLF IFLYLIARNF SGVLTSAGTT LLGLSWLFSG SAQELLSSII FVFVKHPYDV
GDRVDVMING TVTSAMVKEI SIMSTEFRLL TGKVIQAPNS LLNTLWILNM RRSDGIADPV
TVNLKFGTTL QQIEQLRIKI IDFLKEEKRD YKPDLLTEVT DLPDLYSMSL CVVFFHKYNF
QDEVLRMRRR NMFMCALMTY MQELDIVSPI FNSPGKSKDS PMYVNFNNGS MEGVKLSGGN
DGGGTENHRD STVGGGILKN PKAYPYREPT PPGSSDSDTA SVSKKRVDFS LGTRHLMPAF
DDVADIGSKR LGRDSLPDAV IENAGTEAMR REAEERRRAE EEEYERSQQE SSSNEENENA
SRTSGARFSF SSKASRLSAR PSARTVPPLQ HISIQDLREP NENNTSKSAR L
