ID R4XB06_TAPDE Unreviewed; 827 AA.
AC R4XB06;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Mechanosensitive ion channel protein {ECO:0000256|PIRNR:PIRNR017209};
GN ORFNames=TAPDE_003147 {ECO:0000313|EMBL:CCG83008.1};
OS Taphrina deformans (strain PYCC 5710 / ATCC 11124 / CBS 356.35 / IMI 108563
OS / JCM 9778 / NBRC 8474) (Peach leaf curl fungus) (Lalaria deformans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; Taphrinomycetes;
OC Taphrinales; Taphrinaceae; Taphrina.
OX NCBI_TaxID=1097556 {ECO:0000313|EMBL:CCG83008.1, ECO:0000313|Proteomes:UP000013776};
RN [1] {ECO:0000313|EMBL:CCG83008.1, ECO:0000313|Proteomes:UP000013776}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PYCC 5710 / ATCC 11124 / CBS 356.35 / IMI 108563 / JCM 9778 /
RC NBRC 8474 {ECO:0000313|Proteomes:UP000013776};
RX PubMed=23631913; DOI=10.1128/mBio.00055-13;
RA Cisse O.H., Almeida J.M.G.C.F., Fonseca A., Kumar A.A., Salojaervi J.,
RA Overmyer K., Hauser P.M., Pagni M.;
RT "Genome sequencing of the plant pathogen Taphrina deformans, the causal
RT agent of peach leaf curl.";
RL MBio 4:e00055-e00013(2013).
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|PIRNR:PIRNR017209}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the MscS (TC 1.A.23) family.
CC {ECO:0000256|PIRNR:PIRNR017209}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CCG83008.1}.
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DR EMBL; CAHR02000117; CCG83008.1; -; Genomic_DNA.
DR AlphaFoldDB; R4XB06; -.
DR STRING; 1097556.R4XB06; -.
DR VEuPathDB; FungiDB:TAPDE_003147; -.
DR eggNOG; KOG4629; Eukaryota.
DR Proteomes; UP000013776; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
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; IPR023408; MscS_beta-dom_sf.
DR InterPro; IPR006685; MscS_channel_2nd.
DR PANTHER; PTHR31323; MECHANOSENSITIVE ION CHANNEL PROTEIN MSY2; 1.
DR PANTHER; PTHR31323:SF1; MECHANOSENSITIVE ION CHANNEL PROTEIN MSY2; 1.
DR Pfam; PF00924; MS_channel_2nd; 1.
DR PIRSF; PIRSF017209; Memb_At2g17000_prd; 1.
DR SUPFAM; SSF50182; Sm-like ribonucleoproteins; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|PIRNR:PIRNR017209};
KW Kinase {ECO:0000313|EMBL:CCG83008.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR017209};
KW Reference proteome {ECO:0000313|Proteomes:UP000013776};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:CCG83008.1};
KW Transferase {ECO:0000313|EMBL:CCG83008.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 108..128
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 140..159
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 193..212
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 232..259
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 464..484
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 496..522
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 411..446
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REGION 1..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 696..729
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 776..827
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..56
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 703..729
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 780..814
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 827 AA; 93186 MW; 922900A429F7D308 CRC64;
MAGTPQRQFV ELRDLSPPLR GDHSYVRSTS FEENERRKEE YDNQYGNHDQ LDSEQTYHEN
DTSSQSPIVE NEKQPKIRRR KAWKEANQRT RVTKAGLFYR KVMDFSFITR WLLFILPLAI
LLAVPIVVGS FETHAQIGGV RIVWLFLWIE IVWVGLWGAK LVARLLPYVF RFVVSVVSIS
TTKYAGMLKA LEVPISLFFW SLICLSTFSP IMTRNPTQRA ENDTGLKSWE SIMAKILTAA
FFSSAFFLGE KILIQLIALN FHKVQYEMRI TENKWAVQML AKLLSHSRTM FPRFGGDFME
EDHLLEPAAF TGLHQRGRES RMGSTGAVTP MQFVNGARRV FQVGAGIVGA VGSEVSGKKL
DINQSTYSIV VEALLNQTRT DALARRIWLS FVQEGNEALL PEDILEVFGQ DEQENAEAAF
TFFDEDLNGD VSLDEMLMKC TEVAKERRAI SASLKDTDSA IGKLDAVLVV IVGIIAVFIF
IALLDTSFKT LLATSATGLL SLSFVFATTC QEIMGSLIFL FVKHPFDVSD RIIIADKQYI
VQEMSLMFTI LKRTDGTQVQ APNSLLNTLF IDNVRRSAAM SETLNLDIDF DTTFEQIEAL
RTEMFDFIQR ESRDFQQVFD ITINDISSLS KMKISMSIKH KANWQNDALR AQRRNKWMCA
LTMAVRKLGI VASGPGSGDP KNPFIVSQVS FDSKKAGDPF STPAGATSIS SSGQRMDSHS
QLPEFDTTLG TRDLNTRAFD VDLRREGESE RIDARLPFTI AEENDFLIDD EDEKQGLIGN
GKANQASRSD GLARQSTHAS RLSESISRTM TGRRQSRRSS NRDDDRV
//
