ID A0A1V6RT36_9EURO Unreviewed; 913 AA.
AC A0A1V6RT36;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Chloride channel protein {ECO:0000256|RuleBase:RU361221};
GN ORFNames=PENVUL_c031G10239 {ECO:0000313|EMBL:OQE04654.1};
OS Penicillium vulpinum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=29845 {ECO:0000313|EMBL:OQE04654.1, ECO:0000313|Proteomes:UP000191518};
RN [1] {ECO:0000313|Proteomes:UP000191518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 29486 {ECO:0000313|Proteomes:UP000191518};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU361221}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU361221}.
CC -!- SIMILARITY: Belongs to the chloride channel (TC 2.A.49) family.
CC {ECO:0000256|RuleBase:RU361221}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU361221}.
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:OQE04654.1}.
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DR EMBL; MDYP01000031; OQE04654.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6RT36; -.
DR OrthoDB; 150430at2759; -.
DR Proteomes; UP000191518; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043227; C:membrane-bounded organelle; IEA:UniProt.
DR GO; GO:0005247; F:voltage-gated chloride channel activity; IEA:UniProtKB-UniRule.
DR CDD; cd03684; ClC_3_like; 1.
DR Gene3D; 1.10.3080.10; Clc chloride channel; 1.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR014743; Cl-channel_core.
DR InterPro; IPR001807; Cl-channel_volt-gated.
DR PANTHER; PTHR45711; CHLORIDE CHANNEL PROTEIN; 1.
DR PANTHER; PTHR45711:SF3; CLC CHANNEL; 1.
DR Pfam; PF00654; Voltage_CLC; 1.
DR PRINTS; PR00762; CLCHANNEL.
DR SUPFAM; SSF54631; CBS-domain pair; 1.
DR SUPFAM; SSF81340; Clc chloride channel; 1.
DR PROSITE; PS51371; CBS; 1.
PE 3: Inferred from homology;
KW CBS domain {ECO:0000256|PROSITE-ProRule:PRU00703};
KW Chloride {ECO:0000256|ARBA:ARBA00023214, ECO:0000256|RuleBase:RU361221};
KW Ion transport {ECO:0000256|RuleBase:RU361221};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361221};
KW Reference proteome {ECO:0000313|Proteomes:UP000191518};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU361221};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU361221}; Transport {ECO:0000256|RuleBase:RU361221}.
FT TRANSMEM 185..212
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 267..287
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 378..395
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 401..417
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 429..453
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 503..523
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 543..561
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 599..620
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 626..650
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT DOMAIN 859..913
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT REGION 1..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 308..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..340
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 913 AA; 100141 MW; 87937F85F6ADAD75 CRC64;
MPRSLPKLSS ASREQEDIEN TRNAQTAPPS PNAYRRSQSY LSETHTEYQS LDAPLEITET
TSLLGPAQDF RRRAPRRSYT STSGLSGTGP DSFRRILAAG NLRRTRNHSR ANSTGKRFSR
RGSIDGDSRP ASLPPSTKDN LAASSFLDER TWYDQFTSTD WVHDSIADGA RLRLLRQRKD
VRGRLLAAFD GAQGWILVAL IGCITASIAY FVDVTEGSVF DLKEGFCTTR VFRNRRTCCE
GRASCEAWRP WSRIFSPSGT ENQWVDFVMF VFWVMTLALI SCALTLLTKT VVPSSISLAT
LDENLGAESR GTRSGNGVGA LGSPLSETDT SSSPHRNLPN NPSRPAMIYY SAAGSGVAEV
KVINSGFVLH GYMGLKTLVI KTIGLIFSVS SGLSLGKEGP YVHIATCIGN ICCRLFAKYN
QNDGKRREVL SASAASGVAV AFGAPIGGVL FSLEEVSYYF PPKTLFRTFF CCIAATLSLK
FLNPYGTGKI VLFEVRYLSD WQIFELFIFI LLGVMGGAAG ALFIKASSLW ARSFRRIPAI
KRWPMLEVFL VALVTGLLSF WNRYTKLPVT ELLFELASPC ESNVENTGLC PRTDGILEVV
HYLLVAFVIK SFLTIITFGI KVPAGIYVPS MVVGGLMGRI VGHLIQYWAL RHPTFFLFDS
CPAAAGIESC VTPGVYALIA AGATMCGVTR LSVTLAVILF ELTGSLNHVL PFSLSILCAK
WTADAIEPRS IYDLLTDMNS YPFLDNKLQP TTDAELGDIV RPVRKNRLID ISASPFVPAT
NLRSKLEHLL MAGELDSGLP ILRDGVLAGL IPAPDLEYAL DTLGDGEENT ICLMTMDAST
AVYDSDNEDM EQVDFSQYID PAPIALDVHS PIDLVYQCFA KLGLRYLCVT QDGKYVGLVH
KKSFVKFMKE NSD
//
