ID A0A0D1ZLC0_9EURO Unreviewed; 1279 AA.
AC A0A0D1ZLC0;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=DUF221-domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=PV11_03112 {ECO:0000313|EMBL:KIV87578.1};
OS Exophiala sideris.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=1016849 {ECO:0000313|EMBL:KIV87578.1, ECO:0000313|Proteomes:UP000053599};
RN [1] {ECO:0000313|EMBL:KIV87578.1, ECO:0000313|Proteomes:UP000053599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121828 {ECO:0000313|EMBL:KIV87578.1,
RC ECO:0000313|Proteomes:UP000053599};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala sideris CBS121828.";
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; KN846951; KIV87578.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D1ZLC0; -.
DR HOGENOM; CLU_002458_2_0_1; -.
DR OrthoDB; 54187at2759; -.
DR Proteomes; UP000053599; 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 InterPro; IPR022257; PHM7_ext.
DR PANTHER; PTHR13018; PROBABLE MEMBRANE PROTEIN DUF221-RELATED; 1.
DR PANTHER; PTHR13018:SF20; SPORULATION-SPECIFIC PROTEIN 75; 1.
DR Pfam; PF14703; PHM7_cyt; 2.
DR Pfam; PF12621; PHM7_ext; 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:UP000053599};
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..48
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 109..127
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 168..186
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 653..672
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 710..730
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 751..775
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 803..827
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 873..891
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 911..933
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 945..963
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 27..188
FT /note="CSC1/OSCA1-like N-terminal transmembrane"
FT /evidence="ECO:0000259|Pfam:PF13967"
FT DOMAIN 212..289
FT /note="CSC1/OSCA1-like cytosolic"
FT /evidence="ECO:0000259|Pfam:PF14703"
FT DOMAIN 561..644
FT /note="CSC1/OSCA1-like cytosolic"
FT /evidence="ECO:0000259|Pfam:PF14703"
FT DOMAIN 658..930
FT /note="CSC1/OSCA1-like 7TM region"
FT /evidence="ECO:0000259|Pfam:PF02714"
FT DOMAIN 1200..1270
FT /note="10TM putative phosphate transporter extracellular
FT tail"
FT /evidence="ECO:0000259|Pfam:PF12621"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 338..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 405..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1006..1031
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1093..1156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..362
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 405..419
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..450
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1012..1031
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1098..1112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1113..1135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1136..1154
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1279 AA; 143811 MW; 66005A05F6098642 CRC64;
MSLNETLTLG GNSTAGSSKS GQTASQFAAS LITSLAIFGI EVALFLLIKD RFARIYQPRT
YLVPERERTK ASPPGWWKWI KPVFTTSNSE FVQKCGLDAY FFLRYLRTLL KIFVPAALII
LPILIPLNAV HGRGGDYAVG ANANASNVTG LDTLAWGNVA PDHTGRYWAH WLLALSLIIW
VCYVAFDELR NYIRMRQAYL TSPQHRLRAS ATTVLVSSIP QKWCSVEALD GLYDVFPGGL
RNIWINRNFD ELNDKIKRRD KLAATLEAAE TDLIKKCFKK NEENIAKADK EAGKKVSKEE
KKLRATVKNE AGDHAAHGHG LTTGNPHQVE HHLRDVLDGP DARHSSASSS DDDEEVDEPQ
RNKRTIPIPI LGEGISAVTQ GLDNIGNRLL GGIRGVNKGV NNTIDRSNGF VAPDVDQEQS
ASTSDEKSKP ESEDTGAKSE QRKTFGQKKT VHAKDASATA LSNNRGRSAE KSGRDLAPSS
PLSRSSTKRD DQGRPENSLS TFQKVKKAIG LGSEEKEPVD YPQAFEWGFE HDPDDALWRH
YLAEKDRDTT RLPIFGWSWM PSLPLIGEKV DTIRYCRKEV ARLNVEIEED QAHPERFPLM
NSAFIQFNHQ VAAHMACQTL SHHLPKQMAP RIVEIDPNDV IWDNMSIPWW QRYVRTGAVV
AIVTGMIILW AFPVAFTSAL SQLDTAAETF TWLHWVLSIP SWFRSVLQGV LPAALLGLLT
FLLPLILRYL AKVQGIQSGM LVELSVQQYY FAFLFVQLFL VVSIASALTQ FFALFESVDG
FTNIPALLGT NIPKASNYFF SYMLLQALSV SAGALVQVGS LISWFVLAPL FDSTARAKFQ
RQTQLSNVQW GTFFPVYTNL ACIGLIYSVI SPLILIFNII TFALFWFAYR YNTLYVTRFT
RDTGGLLYPN AINTTFVGLY VMEIALIGMF FLVRDTAGDV ACSGQAIGMI ILLILTAGYQ
ILLNEAFGPL FRYLPITLED DAVRRDEEFA RAMQAKHIGL IEEEDEAEDL EGQLERKERQ
ERDDDRQEHE YELERIKADK QARLEKVKSE ELPELEPYEF QNPEITMDLD QQSKGVRIAK
NLAQKTTGTT MQLLGRAVSR KEQRKSWADR DNVHNQRSTS FGQWSASQSQ SHSRANSEAR
PRHGSNKRHI SPPREVFNKL NNFNPLLGNE KDVEAQRAAR NQLTDAIFSG VSDELEDLTP
DERDRLVQRA FQHSALRARR PVIWIPRDEL GVSDDEVHRM GKFSSHIWVS NVRQGLDSKG
RCVYSGAPPD FSEVDLIQL
//
