ID V9DB10_9EURO Unreviewed; 972 AA.
AC V9DB10;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=CSC1/OSCA1-like 7TM region domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=G647_05285 {ECO:0000313|EMBL:ETI23483.1};
OS Cladophialophora carrionii CBS 160.54.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=1279043 {ECO:0000313|EMBL:ETI23483.1, ECO:0000313|Proteomes:UP000030678};
RN [1] {ECO:0000313|EMBL:ETI23483.1, ECO:0000313|Proteomes:UP000030678}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 160.54 {ECO:0000313|EMBL:ETI23483.1,
RC ECO:0000313|Proteomes:UP000030678};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Cladophialophora carrionii CBS 160.54.";
RL Submitted (MAR-2013) 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; KB822705; ETI23483.1; -; Genomic_DNA.
DR RefSeq; XP_008727838.1; XM_008729616.1.
DR AlphaFoldDB; V9DB10; -.
DR GeneID; 19983778; -.
DR VEuPathDB; FungiDB:G647_05285; -.
DR HOGENOM; CLU_002458_2_1_1; -.
DR OrthoDB; 54187at2759; -.
DR Proteomes; UP000030678; 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:SF53; DOMAIN PROTEIN, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR13018; PROBABLE MEMBRANE PROTEIN DUF221-RELATED; 1.
DR Pfam; PF14703; PHM7_cyt; 1.
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 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 35..55
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 115..134
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 162..181
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 455..479
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 499..525
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 546..575
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 595..622
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 643..662
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 668..686
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 731..760
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 35..183
FT /note="CSC1/OSCA1-like N-terminal transmembrane"
FT /evidence="ECO:0000259|Pfam:PF13967"
FT DOMAIN 206..441
FT /note="CSC1/OSCA1-like cytosolic"
FT /evidence="ECO:0000259|Pfam:PF14703"
FT DOMAIN 453..725
FT /note="CSC1/OSCA1-like 7TM region"
FT /evidence="ECO:0000259|Pfam:PF02714"
FT DOMAIN 872..957
FT /note="10TM putative phosphate transporter extracellular
FT tail"
FT /evidence="ECO:0000259|Pfam:PF12621"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 276..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..306
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..325
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 972 AA; 109738 MW; 5811B829DDEEEB37 CRC64;
MDATDPRVGS ARDNSTSPGL SRMVAGSNSS SGRNLLATLV PVLIWAAICI IIFIISRRKC
PRVYAPRTLL RSLEPHERSP PLPNGWFNWF RDFYKIPPAF VLNHSSLDGY LFLRFLRVLG
VICLVGIALL WPILLPLHAT GGAGNRELDA LTLGNVVSSN RFYAHAILAW VYFIFVLYMV
SRECIYYINL RQAYLLSPFY ANRLSSRTVL YVNVPRQYLD EDRLRWMLGD SVKRIWIPQT
TDELERMVKE REQTAMRLEK AEFALIRMAN AARTKALKKA QRESSKQHSS ASVSHHDVKD
ERTSSASKST AGEAVQASDS SDTTSRPAED GQERPLPDVN GSVASQWISH SSRPHHRPIA
NYGRRVDTIK WTRNQIKKLN SQIARVRRDL LFKTDGMLPS VFVEFETHTD AQNAYQTLTH
HRPLHMAQRY LGVRPFEILW HSLSMSWWET IARRFLIKAL ITALIIFWAI PSAAVGTISN
IEYLSEKVPF LGWIADLPGA VTSIISGVLP ALALSLLMSI VPGILRYCAR IGGVPTLTGI
ELYTQHAYFA FQVVQVFLIT TLTSAASAAV TKLLADPTTA KDLLSQNLPK ASNFYLSYFL
LQSLALGAGA LVQFGNLFHF HVFEKFSNNP RKTYLRWHRL QRIHWGGIFP VYTNLGVITL
TYALIAPIIL GFAIVGVGFL HIVFRYNLIY VYDSEIDTRG LVYPRALMQL LLGLYFSEIC
MIGLFSLRGA YVPVVLTAIL LALTGLVHTS LIDALGPLLW SLPKSLTKEE DQHLLGSRAT
NGRSRHLEDA EQYQQPHDFL NDEDGHVHGE NRTLEGADGA FSALGGGVKT MLTKKFKREL
PEVDLGMAAV GGFWMRWISP DPSQESNFLL RWLHPEVYSD YTILRQMVPQ DLPDPVYPEE
IERDIYYPPS MMMKPPTLWI PRDPGGVSRQ EVQHSEKALP TTDEHVTIDE KGQLTIDLDE
PRLVFDIGRL RY
//
