MSY2_SCHPO
ID MSY2_SCHPO Reviewed; 840 AA.
AC O14050;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 135.
DE RecName: Full=Mechanosensitive ion channel protein Msy2 {ECO:0000303|PubMed:22910366};
GN Name=msy2 {ECO:0000303|PubMed:22910366};
GN ORFNames=SPAC2C4.17c {ECO:0000312|PomBase:SPAC2C4.17c};
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 FUNCTION, SUBCELLULAR LOCATION, INDUCTION, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF ASP-394; ASP-395; GLU-396; ASP-399; ASP-405; ASP-407;
RP ASP-415; GLU-416; GLU-418; GLU-423 AND GLU-427.
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 [3]
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 (PubMed:22910366). Involved
CC in maintaining vacuole integrity and protecting the nuclear envelope
CC upon hypo-osmotic shock (PubMed:25041276).
CC {ECO:0000269|PubMed:22910366, ECO:0000269|PubMed:25041276}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:22910366}; Multi-pass membrane protein
CC {ECO:0000305}. Note=Cortical endoplasmic reticulum.
CC {ECO:0000269|PubMed:22910366}.
CC -!- INDUCTION: Up-regulated by both hyper- and hypo-osmotic shocks.
CC {ECO:0000269|PubMed:22910366}.
CC -!- DOMAIN: EF-hand domain is involved in the detection of calcium
CC concentration. {ECO:0000250|UniProtKB:O74839}.
CC -!- DISRUPTION PHENOTYPE: Upon hypo-osmotic shock, cells display excessive
CC increase in cell volume compared to wild-type and undergo cell death.
CC {ECO:0000269|PubMed:22910366}.
CC -!- SIMILARITY: Belongs to the MscS (TC 1.A.23) family. {ECO:0000305}.
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DR EMBL; CU329670; CAB16377.1; -; Genomic_DNA.
DR PIR; T38528; T38528.
DR RefSeq; NP_594520.1; NM_001019949.2.
DR AlphaFoldDB; O14050; -.
DR SMR; O14050; -.
DR BioGRID; 277930; 29.
DR STRING; 4896.SPAC2C4.17c.1; -.
DR iPTMnet; O14050; -.
DR MaxQB; O14050; -.
DR PaxDb; O14050; -.
DR PRIDE; O14050; -.
DR EnsemblFungi; SPAC2C4.17c.1; SPAC2C4.17c.1:pep; SPAC2C4.17c.
DR GeneID; 2541425; -.
DR KEGG; spo:SPAC2C4.17c; -.
DR PomBase; SPAC2C4.17c; msy2.
DR VEuPathDB; FungiDB:SPAC2C4.17c; -.
DR eggNOG; KOG4629; Eukaryota.
DR HOGENOM; CLU_018836_0_0_1; -.
DR InParanoid; O14050; -.
DR OMA; LAKRIWM; -.
DR PhylomeDB; O14050; -.
DR PRO; PR:O14050; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0032541; C:cortical endoplasmic reticulum; IDA: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:0005262; F:calcium channel activity; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0008381; F:mechanosensitive ion channel activity; ISM:PomBase.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IBA:GO_Central.
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 Endoplasmic reticulum; Membrane; Reference proteome; Stress response;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..840
FT /note="Mechanosensitive ion channel protein Msy2"
FT /id="PRO_0000316597"
FT TOPO_DOM 1..68
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 69..89
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 90..100
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 101..121
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 122..126
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 148..151
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 173..225
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 226..246
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 247..449
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 450..491
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 492..840
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 392..427
FT /note="EF-hand"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 677..730
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 775..819
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 677..708
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 709..730
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 394
FT /note="D->A: Viability does not decrease in a calcium-
FT dependent manner; when associated with A-395; A-396; A-399;
FT A-405; A-407; A-415; A-416; A-418; A-423 and A-427."
FT /evidence="ECO:0000269|PubMed:22910366"
FT MUTAGEN 395
FT /note="D->A: Viability does not decrease in a calcium-
FT dependent manner; when associated with A-394; A-396; A-399;
FT A-405; A-407; A-415; A-416; A-418; A-423 and A-427."
FT /evidence="ECO:0000269|PubMed:22910366"
FT MUTAGEN 396
FT /note="E->A: Viability does not decrease in a calcium-
FT dependent manner; when associated with A-394; A-395; A-399;
FT A-405; A-407; A-415; A-416; A-418; A-423 and A-427."
FT /evidence="ECO:0000269|PubMed:22910366"
FT MUTAGEN 399
FT /note="D->A: Viability does not decrease in a calcium-
FT dependent manner; when associated with A-394; A-395; A-396;
FT A-405; A-407; A-415; A-416; A-418; A-423 and A-427."
FT /evidence="ECO:0000269|PubMed:22910366"
FT MUTAGEN 405
FT /note="D->A: Viability does not decrease in a calcium-
FT dependent manner; when associated with A-394; A-395; A-396;
FT A-399; A-407; A-415; A-416; A-418; A-423 and A-427."
FT /evidence="ECO:0000269|PubMed:22910366"
FT MUTAGEN 407
FT /note="D->A: Viability does not decrease in a calcium-
FT dependent manner; when associated with A-394; A-395; A-396;
FT A-399; A-405; A-415; A-416; A-418; A-423 and A-427."
FT /evidence="ECO:0000269|PubMed:22910366"
FT MUTAGEN 415
FT /note="D->A: Viability does not decrease in a calcium-
FT dependent manner; when associated with A-394; A-395; A-396;
FT A-399; A-405; A-407; A-416; A-418; A-423 and A-427."
FT /evidence="ECO:0000269|PubMed:22910366"
FT MUTAGEN 416
FT /note="E->A: Viability does not decrease in a calcium-
FT dependent manner; when associated with A-394; A-395; A-396;
FT A-399; A-405; A-407; A-415; A-418; A-423 and A-427."
FT /evidence="ECO:0000269|PubMed:22910366"
FT MUTAGEN 418
FT /note="E->A: Viability does not decrease in a calcium-
FT dependent manner; when associated with A-394; A-395; A-396;
FT A-399; A-405; A-407; A-415; A-416; A-423 and A-427."
FT /evidence="ECO:0000269|PubMed:22910366"
FT MUTAGEN 423
FT /note="E->A: Viability does not decrease in a calcium-
FT dependent manner; when associated with A-394; A-395; A-396;
FT A-399; A-405; A-407; A-415; A-416; A-418 and A-427."
FT /evidence="ECO:0000269|PubMed:22910366"
FT MUTAGEN 427
FT /note="E->A: Viability does not decrease in a calcium-
FT dependent manner; when associated with A-394; A-395; A-396;
FT A-399; A-405; A-407; A-415; A-416; A-418 and A-423."
FT /evidence="ECO:0000269|PubMed:22910366"
SQ SEQUENCE 840 AA; 94644 MW; 777552F01B77BE10 CRC64;
MNEHRREPHR RSGYQDDSAF TNTEKLVDEL DHNVEPEQLL EKNRTDFKLM YVIVKFYRWF
NNLSFITRWI TIWFPLAGAL VIPLAVGVSP YPNAKLGGVR IFWIFVWLEV AWGGFWVSRV
IARLLPYILY PLMGILPFTM YKYTVILTAL EMPLAIFFCS IVCVCTFSPI MIGKGNFTST
TVTTTTSATA TPTASASSNA VESVFVTKTA ASVPSWIKVI TKILGAAVVT SIVLLLEKIF
LHFIGFHYHE VQYQYRITDN KRNTAVLAKL LTAALDAPYH DSPRVRRQDY LLGLIDTRSM
SESKGSGNGK LRKVKKISKN AKRIFSKTRN AISTAFTDML GKHAKDLTPE QEFILETIRS
KKKCLALARK IWYSLVPEGE DCFQKEDLIG LIPDDEINDI FHILDNDYSR TVTLDEMEQF
TREISIEFRS ISSSLRDVDL ALGKLDRVGL GVVGIIAVLT FISFLDTSFA TILAAFGTTL
LSLSFVFSTS AQELMSSIIF LFSKHPFDIS DVVIVNNIKY EVVSLSLLFT VFRTMGGSTV
QAPNSLLNTL FIENLRRSQP QSETITIVSP FATDFKQLER LRDLLLTFVK ENERDFRPII
DLNVSDFSTL DSLKFTVTYY YKSNWQNVSL QCVRRNKFMC ALKNAIATTN LPAVADPVRG
SPDYPFVIEQ YNLERPEYSK TASRPQFSDI SSTASSNSLS NKPGFAHSES RNYHTHDEDN
SSDDNHKRED RGHLPAQYLR QSVATWQIPN LISAIEAYDS QNESSQENAT YTVVESNGNA
NGDNTATNSQ GATDNGQTTT NTTQNNVDNT QATTDNTQAN TDNMQVAIDY SQNMDGQIQY
