ID A0A2H3J0T5_9EURO Unreviewed; 892 AA.
AC A0A2H3J0T5;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:PCH08679.1};
GN ORFNames=PENO1_005490 {ECO:0000313|EMBL:PCH08679.1};
OS Penicillium occitanis (nom. inval.).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=290292 {ECO:0000313|EMBL:PCH08679.1, ECO:0000313|Proteomes:UP000218381};
RN [1] {ECO:0000313|EMBL:PCH08679.1, ECO:0000313|Proteomes:UP000218381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL100 {ECO:0000313|EMBL:PCH08679.1,
RC ECO:0000313|Proteomes:UP000218381};
RX PubMed=28951729; DOI=10.3389/fmicb.2017.01627;
RA Bravo-Ruiz G., Sassi A.H., Marcet-Houben M., Di Pietro A., Gargouri A.,
RA Gabaldon T., Roncero M.I.G.;
RT "Regulatory Mechanisms of a Highly Pectinolytic Mutant of Penicillium
RT occitanis and Functional Analysis of a Candidate Gene in the Plant Pathogen
RT Fusarium oxysporum.";
RL Front. Microbiol. 8:1627-1627(2017).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PCH08679.1}.
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DR EMBL; NPFK01000007; PCH08679.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3J0T5; -.
DR OrthoDB; 54187at2759; -.
DR Proteomes; UP000218381; 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:SF26; DOMAIN PROTEIN, PUTATIVE (AFU_ORTHOLOGUE AFUA_5G10920)-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 Reference proteome {ECO:0000313|Proteomes:UP000218381};
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 31..52
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 114..133
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 158..177
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 408..432
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 452..474
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 506..527
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 547..573
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 594..616
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 622..643
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 664..684
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 690..714
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 31..179
FT /note="CSC1/OSCA1-like N-terminal transmembrane"
FT /evidence="ECO:0000259|Pfam:PF13967"
FT DOMAIN 202..395
FT /note="CSC1/OSCA1-like cytosolic"
FT /evidence="ECO:0000259|Pfam:PF14703"
FT DOMAIN 406..679
FT /note="CSC1/OSCA1-like 7TM region"
FT /evidence="ECO:0000259|Pfam:PF02714"
FT DOMAIN 793..884
FT /note="10TM putative phosphate transporter extracellular
FT tail"
FT /evidence="ECO:0000259|Pfam:PF12621"
FT REGION 742..787
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 751..770
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 892 AA; 99483 MW; E7C587379AEC7C99 CRC64;
MAWLKDGLSG LRSLAKRADD TSAAPTSLSG FISTLVPALL IAGAMVLAFI ILRRKYRRDY
MPRTFLPTLR DYERTPGSPT GLWNWIIAMY KLPDTYVLQH HSLDAYLLLR YMKLLVVISF
VGCCITWPIL FPINATGGAG NSQFDILSMS NVKNKARYFA HAFVGWIFFG FVFFLVTRES
IFYINLRQAY AFSPAYANRL SSRTVMFSSV PQDYLDEKKL RRMFGGERVK NVWIATDTSK
LEEKVKDRDD AAMKLEGAET ALIKQANVNR IKALKKNPAG DEQLEATADH TESGSVAARW
VKPKDRPTHR LKFLIGKKVD TIDWARAEIE RLNPEIEEEQ AKHRAADAKK VSAVFVEFYN
QNDAQDAYQS VAHNQPLHMA PRYIGVDPTQ VIWSNLRIMW WERVVRNFAT IAFICALIIF
WAIPVAFVGS ISNIDSLIAK LPWLGFINDV PTFIRGVITG LLPSVLLSVL MALLPPIIRL
CAKLGGAPTA AAVELWTQNA YFGFQVVQVF LVTTLSSAAS AVVEEIIQKP TDAASLLAAH
LPQAANFYVS YIVLQGLTFT SGALLGIVGL ILGKVLGKIL DKTPRKMYKR WMSLAGLSWG
TVLPPMSLLG VIAITYSIIA PLVMGFATVG LYLFYFAFRY QLLYVTNAQI DTQGRIYARA
LQHLLVGVYI AVVCLIGLFA IAAADQPIGA GPLVLMVIFL IFAILYHVSL NAALSPLLNY
LPKNLEAEEE ALLAESRNKI SPTASDGIDD PAEGASKEHN GYHDGIDTAE KGTAPHPSEL
PAPHKKPNLF TKFLRPDIYA DYATMRRLVP AHIEVPEYSP EVERDAYFHP SITSTVPLLW
VPRDELGVSK QEVEHTSRVI PISDEDAFVD EKGNVQWNNE TRPPIYEEKI YY
//
