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Database: UniProt
Entry: A0A0D2DDA3_9EURO
LinkDB: A0A0D2DDA3_9EURO
Original site: A0A0D2DDA3_9EURO 
ID   A0A0D2DDA3_9EURO        Unreviewed;      1276 AA.
AC   A0A0D2DDA3;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=CSC1/OSCA1-like 7TM region domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PV05_00522 {ECO:0000313|EMBL:KIW60292.1};
OS   Exophiala xenobiotica.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=348802 {ECO:0000313|EMBL:KIW60292.1, ECO:0000313|Proteomes:UP000054342};
RN   [1] {ECO:0000313|EMBL:KIW60292.1, ECO:0000313|Proteomes:UP000054342}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 118157 {ECO:0000313|EMBL:KIW60292.1,
RC   ECO:0000313|Proteomes:UP000054342};
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 xenobiotica CBS118157.";
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; KN847317; KIW60292.1; -; Genomic_DNA.
DR   RefSeq; XP_013320876.1; XM_013465422.1.
DR   AlphaFoldDB; A0A0D2DDA3; -.
DR   GeneID; 25322430; -.
DR   HOGENOM; CLU_002458_2_0_1; -.
DR   OrthoDB; 54187at2759; -.
DR   Proteomes; UP000054342; 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:UP000054342};
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        651..674
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        708..728
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        749..776
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        796..825
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        871..889
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        909..931
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        943..961
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..288
FT                   /note="CSC1/OSCA1-like cytosolic"
FT                   /evidence="ECO:0000259|Pfam:PF14703"
FT   DOMAIN          560..642
FT                   /note="CSC1/OSCA1-like cytosolic"
FT                   /evidence="ECO:0000259|Pfam:PF14703"
FT   DOMAIN          656..928
FT                   /note="CSC1/OSCA1-like 7TM region"
FT                   /evidence="ECO:0000259|Pfam:PF02714"
FT   DOMAIN          1196..1267
FT                   /note="10TM putative phosphate transporter extracellular
FT                   tail"
FT                   /evidence="ECO:0000259|Pfam:PF12621"
FT   REGION          310..360
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          405..497
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1033..1060
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1086..1160
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        331..360
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        417..431
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1033..1054
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1090..1117
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1118..1136
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1276 AA;  144530 MW;  F0DABFC85F6A4DFC CRC64;
     MSLNSTLDLG GSTTASESKS GQTASQFAAS LVTSIAIFGI QVALFLLIKD RFARIYQPRT
     YLVPERERTK PTDPGWWKWI KPVFVTSNSE FVQKCGLDAY FFLRYLRTLL KIFVPAAMVI
     LPILIPLNVV DGRGGRYATG RHENSTNVTG LDQLAWGNVA PDHTGRYWAH WLLALGLIVW
     VCYVAYDELR NYIRMRQAYL TSPQHRLRAS ATTVLVSAIP QKWCNVEALD GLYDVFPGGL
     RNIWINRNFD ELSEKIKRRD KLAATLEAAE TELIKKCFKK NEENIKKADK EAGKKLSKQE
     KELRATIRNE EGDQAAHGHG ITTGNPHQVN HRLRDVLDGP SDRSMSPSDG EEDVVEEPRH
     TRRAIPIPVI GEGISAVTHG LDTIGNRLLG GIRGVNKGVN DTIDTTNGFV ASEPKQASSS
     DDDEPSRQHD NSGSGTHRNA FHQEKKHRAH DATAGAQPAD GDRGRSKEKL GRYDRPSSPI
     SQSSTMRDEK TRPEKPLTKF EKFKKAIGLG SEEKDPVDYP PAFEWNFEQD PDDAVWRRYL
     TEKDRETMRL PIFGWQWMPS LPLMGEKVDT IRYCRKEVAR LNVEIEDDQA HPERFPLMNS
     AFIQFNHQVA AHMACQAVSH HVPKHMAPRM VEIDPNDVIW DNMSMPWWQR YVRTGGVVAI
     VTGMIILWAV PVAFTSALSQ LDTAAKTWTW LHWVLSIPAW FRSVIQGVLP PALLGLLTFL
     LPLILRFLCK VQGIQSGMLV EISVQRYYFA FLFVQLFLVV SIASALTQFF ALFTSVDGFT
     NIPALLGTNI PKASNYFFSY MLLQALSVSA GALVQVGSLI GWFILAPLFD STARAKFKRQ
     TELSNVRWGT FFPVYTNLAC IGLIYSVISP LILIFNVITF SLFWFVYRYN TLYVTRFTRD
     TGGLLYPNAI NTTFVGLYVM EIALIGMFFL VRDSAGSVAC SGQAIGMIII LILTAGYQLL
     LNEAFSPLFR YLPITLEDDA VRRDEEFARA MQNKQGLLEA DNQVEDLEDQ LERKERQSME
     EDRNEQEYEL QRIKADRDAR LEKQETHKPD LEPSEYQNPE IVMNLDQDSR GLRIAKSVTQ
     KATDTTKHLV VRNLGRKERP KSWADRDNER NRRASNFGEW EDTPSQGRSR APSEVPAQGH
     TTHKRRVSPP RDVFNKLNNF NPITGTEKDI EAQRAARNQL ADALFGGVSD ELEDLTPEER
     DRLVQRAFQH SALRARRPVI WIPRDELGVS DDEVHRMGRF SSHIWVSNVR QGLDSKGRCV
     YSGAPPDFSE VDLIQL
//
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