ID A0A165BR49_EXIGL Unreviewed; 1022 AA.
AC A0A165BR49;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=DUF221-domain-containing protein {ECO:0000313|EMBL:KZV81098.1};
GN ORFNames=EXIGLDRAFT_629065 {ECO:0000313|EMBL:KZV81098.1};
OS Exidia glandulosa HHB12029.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Auriculariales; Exidiaceae; Exidia.
OX NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV81098.1, ECO:0000313|Proteomes:UP000077266};
RN [1] {ECO:0000313|EMBL:KZV81098.1, ECO:0000313|Proteomes:UP000077266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12029 {ECO:0000313|EMBL:KZV81098.1,
RC ECO:0000313|Proteomes:UP000077266};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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; KV426419; KZV81098.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165BR49; -.
DR InParanoid; A0A165BR49; -.
DR OrthoDB; 366603at2759; -.
DR Proteomes; UP000077266; 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:UP000077266};
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 27..49
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 110..131
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 186..207
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 434..460
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 488..507
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 527..546
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 576..603
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 649..667
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 688..706
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 712..730
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 28..208
FT /note="CSC1/OSCA1-like N-terminal transmembrane"
FT /evidence="ECO:0000259|Pfam:PF13967"
FT DOMAIN 230..421
FT /note="CSC1/OSCA1-like cytosolic"
FT /evidence="ECO:0000259|Pfam:PF14703"
FT DOMAIN 432..706
FT /note="CSC1/OSCA1-like 7TM region"
FT /evidence="ECO:0000259|Pfam:PF02714"
FT REGION 869..904
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 926..1022
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 880..903
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1022 AA; 113688 MW; E8BB0FEF8EE848E2 CRC64;
MAFNNDTDTG PDLPPGSPAL RQFEGPWFSM QLSLSLALGL FSFALFSFCR RRWPLLFSPR
TKLKGAAVVA HVGTSASGWI LPTIRVSELS VLQIVGLDAA VLLNFLKTSF YLFLACSGLA
MAILMPVNVY VGRSMGGDGD DDDDDPDTGG GWLRLLSFPE GGGNGGNKGG GTAPDDWLDL
ISEANAYLFV QFLFTYMFTF VAMRFLYSNY KRFVRARQLF SLELVHSIQA RTVMVSYLPP
HLRGERALAT YYENMGFAVE SVSVCREIGA LKPLLDKRTA ALLALESAWT SYVGNPCAVE
AYDPSQAGPL IDIDLPPGHD SSLNPPPRLV VPHRPRPTLR PKWYSLERVD AIEHLEAHFR
ALDEQVRKKR RSGKFRATHC AFVTFESMSS AQAVSQLVTA PVPSSTTACL SPEPRDIVWA
NMTLSPRGQR TRDLAVSAFI VLMFFFWALP VTALSSLLSY EEIQRVMPWL GRLIDSSDAV
RAFVQNSLPS IALITLNGLL PFLFEGLSYL QGFRARSWIE YSLLKKYFLF LLVNVVFEFL
LASTYWQLIR DLANSPAKVP EKLAMALQKG NARHFFLSYV ILQGFGIMPL QLLNLGVIIP
RFFYRAFITR TPRDFAELNA PPMVNYGAVY PQAILVFVIT MLYSVIQPLI LFFGAAYFGI
SYVVYKYKLL FVFYKPYESQ GQAWPITFVR MMWGVLIFQV FMAGIFLLKQ SFILASLMAP
LILFTTYWTW SMDALFGPLS NFVGLSSVCE VQRGEDSDEV ARLRSGHPVS WSQSNLNRRR
YAQNDETLYV APEDDRTDYS QPPMTNWYDG VLNTGKRRYG HPALTGILPS PWLPLKKGQT
LANYLDGRRR AKGGDGDGND AVVLTLRRRK SMARPDVRRQ SSIPLSQQQQ GASQDTLTHG
ANPWDSASVL AGRQVSHRLS FDHATGVINL PEEDDDDERE PERDLEAGAG GAVDESSSDS
EYGSASSMSG DGAHAALSDI AEHEHGRETS GEGTSGGASS AGGTRHRTYY HHPEKRKSMT
IS
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