ID A0A0D1ZC12_9EURO Unreviewed; 974 AA.
AC A0A0D1ZC12;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=CSC1/OSCA1-like 7TM region domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=PV08_11471 {ECO:0000313|EMBL:KIW10507.1};
OS Exophiala spinifera.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=91928 {ECO:0000313|EMBL:KIW10507.1, ECO:0000313|Proteomes:UP000053328};
RN [1] {ECO:0000313|EMBL:KIW10507.1, ECO:0000313|Proteomes:UP000053328}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 89968 {ECO:0000313|EMBL:KIW10507.1,
RC ECO:0000313|Proteomes:UP000053328};
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 spinifera CBS89968.";
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; KN847500; KIW10507.1; -; Genomic_DNA.
DR RefSeq; XP_016230723.1; XM_016385779.1.
DR AlphaFoldDB; A0A0D1ZC12; -.
DR GeneID; 27338554; -.
DR VEuPathDB; FungiDB:PV08_11471; -.
DR HOGENOM; CLU_009187_1_0_1; -.
DR OrthoDB; 1330110at2759; -.
DR Proteomes; UP000053328; 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:SF154; DOMAIN PROTEIN, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G11660)-RELATED; 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:UP000053328};
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 42..64
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 128..145
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 165..192
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 399..422
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 442..462
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 489..511
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 531..553
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 600..631
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 652..677
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 683..703
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 42..192
FT /note="CSC1/OSCA1-like N-terminal transmembrane"
FT /evidence="ECO:0000259|Pfam:PF13967"
FT DOMAIN 216..382
FT /note="CSC1/OSCA1-like cytosolic"
FT /evidence="ECO:0000259|Pfam:PF14703"
FT DOMAIN 393..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 776..795
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 819..853
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 867..915
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 939..974
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 827..852
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 882..896
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 946..962
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 974 AA; 110204 MW; E9A84AB52FE97D2F CRC64;
MSAIKALSPR QTSSPVDPNL SPGEQVLKLI SNPFQASIQI NAFWASLATS LGFSAALALL
FCFVRPRNTI IYAPRLKNAD KDHAPPPLGR GLLGWVEPVN KASEPFLVDR IGMDAVIFLR
FTRMLRNMFL ILAFVGIAIM IPVNVTLGSK GASNGSSAFT IMTPLFIFGS GLWAQVVLAW
FIDIVVIYFL WYNYRRVHQL RRAYLSSPEY QHSLHSRTLL VRDIPPKMRS NEGIARIVEE
VNPAGAAPRA RIGRNVTVLP ELIEEYEETV KELESVLAKY MKNPDRLPAH RPTMKAPRKY
KGTTANGKVD AIEYLTDRIR TLEMEISDIR ERVDSRDAMP YGFATYDQIS QAHIAAFKTR
GKRPQGTKIR LAPRPNDIIW SNLKLSRSTR RSKRIMNGIW IVVLTVIWTP INAGIAVFLS
NLSNLALVWP AFKTSLNAHK SWWAIVQGIA SPAITSLVYL VLPSIFRRLQ VRAGDVTKTE
RERHVLRNLY GFFTFNNLII FSIFSAVWQY VTIVIEYDRQ GNDTWTSLRK GNLFLSITTS
LCQISPFWVT WLLQRNMGAA IDLAQLWHLT YVWFARTFMA PTPRQNIEWT APPVFDYASY
YNYFLFYTTV ALCYSTLQPI VLVVTALYFS IDCFLKKYLL MYVFVTKTES GGQFWVTMFN
RIVFAVMLSN VIIAVVVKAR GTWALVAAIA PLLFIMVAFK WYCMKTFDLD LKYYSRGGMQ
DPEELAAKHH AHEKISSKFG HPALYKPLMT PMVHAKAKHL LGEIYRGRLD SDGGQAATLP
GIAMQPLSPS KQPPSDVPFE IVPEAQQDFH FYRNRPEFRD NAGDTLSERS HTPISMSGYG
KESYNSPPSS RAMSPVVAAG AGVHTYSPPQ EYRGVPHRKQ VDQSHVPSQF KTNKNRRSVG
GGDLGLRPQG PYTDPYDDRT TLLHGVGDVR APTGEFMSMD RWRSSSQGRD GPRTRDHTPV
EEMNSGYDYF RGRQ
//
