ID A0A165EDN4_9BASI Unreviewed; 955 AA.
AC A0A165EDN4;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Chloride channel protein {ECO:0000256|RuleBase:RU361221};
GN ORFNames=CALCODRAFT_438348 {ECO:0000313|EMBL:KZT54631.1};
OS Calocera cornea HHB12733.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC Dacrymycetales; Dacrymycetaceae; Calocera.
OX NCBI_TaxID=1353952 {ECO:0000313|EMBL:KZT54631.1, ECO:0000313|Proteomes:UP000076842};
RN [1] {ECO:0000313|EMBL:KZT54631.1, ECO:0000313|Proteomes:UP000076842}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12733 {ECO:0000313|EMBL:KZT54631.1,
RC ECO:0000313|Proteomes:UP000076842};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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}.
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DR EMBL; KV424010; KZT54631.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165EDN4; -.
DR InParanoid; A0A165EDN4; -.
DR OrthoDB; 150430at2759; -.
DR Proteomes; UP000076842; 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:SF6; CHLORIDE CHANNEL PROTEIN; 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:UP000076842};
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 212..233
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 308..329
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 463..486
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 498..516
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 537..556
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 576..595
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 633..655
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 661..680
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT DOMAIN 898..955
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT REGION 1..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 955 AA; 105210 MW; 0DA9B5921C6B6BAC CRC64;
MADTRVPPPP IVTDPVSPPR SDDGTQPHAG PLSAPSSPLW RRRRLEHLGH VRTGSLGGDS
APNSATFAPG HRPATSYGSF PSPISKRTTR SRKRVFTLPQ LSTFGISSSH RSPSRETLTS
PREEEPLLRG RQSNFFESIR RPPSAYDADW AAAQHSSSAT EDGARANGIR VWYSSFSSVD
WLHDAIKDSI RLLRLRRRRS IRGKMLNNLD RFIGWLVVTL VGFITACIAW LIVRSEGWLF
DLKEGYCSDG WWKAKRFCCP MLNDDELSFS TLAEDEVCPA WTPWMEALGP AWQIGNKWIG
LERWTIEYIA FTVVACLLSF ISCMLTIHLT KSTTFVTRKD SGLYSATFDK TISTPELEGL
PSKHASTSTP DEGQLDVTPR KLMYFASGSG IPEIKTILSG FVIHGYLGGR VLFTKAVGLA
LSVASGLSLG KEGPFVHIAC CVGNIVSRFF PKYESNEGKR REILSAASAA GVAVAFGAPI
GGVLFSLEEV SYYFPPKVMW RSFFCALIAA VTLKFLDPFG TGKIVLFKVT YDKDWHFLEL
FVFVFLGIFG GVYGAYFSRL NYLWSKHVRG KTWLKTHPAA EVFLVTLLTT GLCFLNRYTR
MGGPELVYNL FAECSSTKGH EGLCVREREE VHAVLGAIAV TLLVKGALTI ITFGIKVPAG
IFIPTLGVGA CFGRIVGLAL QTLQTQRPDL AIFSFCKPGE DCIIPGVYAM VGAAATLSGV
TRTTVSLAVI MFELTDSLTY ALPVSLAVLV AKTIADRIEP KGIYDLVIEL NQLPYLDSKH
QYVWGALMVA DVTDRKVDII RVEQENTVQS LRDKLINAVN EGAGDSGFPI LAPGEDGDKL
IGYIGANELE HALSIVAERP DAPCHFHHAT AHDLMNSTIS SLYNTPVPQD LYDFSIYMDQ
APLTVAAHAP LELVQQLFVK LGARYVIVLN DDCSYHGVID RKAWLRFLHG LEEKE
//
