ID A0A0C3PRC6_PISTI Unreviewed; 984 AA.
AC A0A0C3PRC6;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=CSC1/OSCA1-like 7TM region domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=M404DRAFT_964822 {ECO:0000313|EMBL:KIO11616.1};
OS Pisolithus tinctorius Marx 270.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Sclerodermatineae; Pisolithaceae; Pisolithus.
OX NCBI_TaxID=870435 {ECO:0000313|EMBL:KIO11616.1, ECO:0000313|Proteomes:UP000054217};
RN [1] {ECO:0000313|EMBL:KIO11616.1, ECO:0000313|Proteomes:UP000054217}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Marx 270 {ECO:0000313|EMBL:KIO11616.1,
RC ECO:0000313|Proteomes:UP000054217};
RG DOE Joint Genome Institute;
RA Kuo A., Kohler A., Costa M.D., Nagy L.G., Floudas D., Copeland A.,
RA Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A.,
RA Lipzen A., Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA Hua S.X.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000054217}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Marx 270 {ECO:0000313|Proteomes:UP000054217};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the CSC1 (TC 1.A.17) family.
CC {ECO:0000256|ARBA:ARBA00007779}.
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DR EMBL; KN831949; KIO11616.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C3PRC6; -.
DR STRING; 870435.A0A0C3PRC6; -.
DR HOGENOM; CLU_002458_3_0_1; -.
DR InParanoid; A0A0C3PRC6; -.
DR OrthoDB; 366603at2759; -.
DR Proteomes; UP000054217; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005227; F:calcium-activated cation channel activity; IEA:InterPro.
DR InterPro; IPR045122; Csc1-like.
DR InterPro; IPR003864; CSC1/OSCA1-like_7TM.
DR InterPro; IPR027815; CSC1/OSCA1-like_cyt.
DR InterPro; IPR032880; Csc1/OSCA1-like_N.
DR PANTHER; PTHR13018:SF83; CALCIUM PERMEABLE STRESS-GATED CATION CHANNEL 1; 1.
DR PANTHER; PTHR13018; PROBABLE MEMBRANE PROTEIN DUF221-RELATED; 1.
DR Pfam; PF14703; PHM7_cyt; 1.
DR Pfam; PF02714; RSN1_7TM; 1.
DR Pfam; PF13967; RSN1_TM; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000054217};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 32..54
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 116..135
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 162..182
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 403..429
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 457..476
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 496..515
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 545..572
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 618..636
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 657..675
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 681..700
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 33..183
FT /note="CSC1/OSCA1-like N-terminal transmembrane"
FT /evidence="ECO:0000259|Pfam:PF13967"
FT DOMAIN 206..390
FT /note="CSC1/OSCA1-like cytosolic"
FT /evidence="ECO:0000259|Pfam:PF14703"
FT DOMAIN 401..674
FT /note="CSC1/OSCA1-like 7TM region"
FT /evidence="ECO:0000259|Pfam:PF02714"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 841..984
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 844..871
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 872..896
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 923..942
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 984 AA; 111140 MW; 9491A5D6B1ABB87D CRC64;
MSSLASLLSD TDSGDPDLPP GSPPTYKFEG PWFATQLLLA SSIGLVSFLV FSYFRSRWPL
VFASRTKLKG FSPHEAHAHS AFFGWILPTI RTSEFTILQI VGLDAAVLLS FYKTSFYLFS
VCSIFATVIL MPINWKWTTA TYDDPSSPNR DWLDLISDAN SYLTVHFLFT YLFTILALYF
LYKNYRRYIR ARQLFSLELV HSMPGRTVMV TSLPLHLRSE RALAEYFENM GLSVESVSVC
REVTTLKALL DERTKALLEL ESGWTNYVGN PSAVESYDPS ENVISQVDPS ILEGQPARLV
VPHRKRPTVR PGWFSAKVDA LEYLEAKFKE ADEKVRKWRR VGKFKATHVA FVTFEKMSSA
QIAAQTAHSS DPWQIKTRQA PEPRDIVWDN IGTTPGSLFA RELLVLGAVG LLLFFWVLPI
TALASLLSYK EIKKVMPWLG QLIDTNDKIR AIVQNSLPSV AIITLNALLP FILEGLTYFQ
GYKARSMIEY SLLRKYFLFL LVNVVFIFLL ASTYWQLVRD LANSPAKIPE KLAEALQKGR
AKHFFLSYVI LQGFGIIPLQ LLNLGVIIPR IILRIFVTRT PRDFAELNAP PMINYGVVYP
QAILIFVITI LYSVVQPLIV VFGAIYFGVG YLVYKYKLLF VFFKPYESQG QAWPITFVRL
IWGIVIFQVF MIGILTLRQC YIMSSLLVPL LVGTVAWSWY IHSAMRPLSH AVSLNSVCEV
ERGEETVVTR LREEHPVSRS QSNLSRRRYA QNDDTLYVAP EDERTDYSQP PMANWYYGVL
NTGKRRYGHP ALTGVLPEPW LPLKKGQMLV NGLRNGGSRA AADSTQGIVL SLRNRYSMLR
NKIRSSRRSR DAPDGENAEM ASPDEERGHA SDNSTTNPWA GARGSRTQST LSHRLSFDPG
SGVIMLPEDD GWLEEEDDSS GEDYSNTSPP SGDGQGNVSQ EDLGMSDDHP PSTPMTPSPR
RRHATYYHHP DRRRATLPGA FPQS
//
