ID A0A317VZU6_ASPEC Unreviewed; 934 AA.
AC A0A317VZU6;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Mechanosensitive ion channel protein {ECO:0000256|PIRNR:PIRNR017209};
GN ORFNames=BO83DRAFT_215682 {ECO:0000313|EMBL:PWY78851.1};
OS Aspergillus eucalypticola (strain CBS 122712 / IBT 29274).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448314 {ECO:0000313|EMBL:PWY78851.1, ECO:0000313|Proteomes:UP000246171};
RN [1] {ECO:0000313|EMBL:PWY78851.1, ECO:0000313|Proteomes:UP000246171}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 122712 {ECO:0000313|EMBL:PWY78851.1,
RC ECO:0000313|Proteomes:UP000246171};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
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:PWY78851.1}.
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DR EMBL; MSFU01000006; PWY78851.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A317VZU6; -.
DR VEuPathDB; FungiDB:BO83DRAFT_215682; -.
DR OrthoDB; 1362946at2759; -.
DR Proteomes; UP000246171; 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:0055085; P:transmembrane transport; IEA:InterPro.
DR Gene3D; 2.30.30.60; -; 1.
DR Gene3D; 1.10.238.10; EF-hand; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
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:SF15; MECHANOSENSITIVE ION CHANNEL PROTEIN MSY1; 1.
DR PANTHER; PTHR31323; MECHANOSENSITIVE ION CHANNEL PROTEIN MSY2; 1.
DR Pfam; PF00924; MS_channel_2nd; 1.
DR PIRSF; PIRSF017209; Memb_At2g17000_prd; 1.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF50182; Sm-like ribonucleoproteins; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Endoplasmic reticulum {ECO:0000256|PIRNR:PIRNR017209};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR017209};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 163..185
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 191..211
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 282..299
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 505..528
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 446..481
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REGION 1..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 736..789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 836..934
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..125
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 758..775
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 836..857
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 859..898
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 906..926
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 934 AA; 104358 MW; 38D57E626D755608 CRC64;
MSTSMGDHLA PDHLEEKSKH RSEDGTPDSD EGTYVYDSAS NGNHLRVDTS YNDLDRTALA
SPVTAREEST RLEDDLAVME AERMVSRSTQ EAESKKSVHD GRPSTSRSRS RSRSRPNEHV
DEFDEATNPL HEKAAVYNPP ENPNTNIARF VKKLHESSFI IRYLTYILPL VIILLIPLLV
GALAYPNASV GGVRLLWFSV WLEIVWLTLW AGRIVSKLIP IPVNALASIF TNNAKKWRDL
AKQLELHATL FFWWLGVEIS FLPTMKNHHV DGNHATRSWE NTLNKIIISV FVWTILNLVE
KFIIQLIAIS FHTRTYADRI EINKFQIGSL TKLYDFSRRK ITAKDKEFEE QKQPSSNNGL
KIPFHYAGKA GRLAKGAFTK VGDVAGAVAA DFTGRTATNS NHPYQVVLAL LRTTSGCQVL
ARRLYRTLVR DGFETVFSGD LKEAFDNNDE AEAAFTMFDK DMNGDISMEE LESVCVEIGR
ERKAITASLK DLDSVVGRLD NILEFFVVII TLIVFLTLIS TSAAGVLTSA GSSILALSWL
FSATAQEFLQ SVIFVFIKHP FDVGDRVTVY GNSGDAGLGD DYFVKQISLL YTEFKKMQGH
VVQAPNSYLN GLFILNQRRS GALAEAVPIV IKYGTTLEQI DGLRQRLLEF VRSERREFQT
NILTEMREVT ENFSVTLNVV FFYKSNWQNE GLRLQRRNKF ICMLMLALQE IGIEGPRMNL
QGARVDIPFH VAGFPSHNMG APPGSSDGRP PPTPVYQQDS IPENTGSSSS VRQHSILRRG
ADAAAARARG DSMLTRKHVD FSLGMRDVSS GDVMGDVFED RGTRVDDVVR MANRETAERR
IQEEEEEQAE RQSRASGSHR RSHSNTSAAP SAARSGRQSM ESHGGHSLSS VSRGRFFRHR
NSISSRGPAD LEQGPTHGQQ SPQIRAVSPA MDEK
//
