ID A0A3N7EWE1_POPTR Unreviewed; 430 AA.
AC A0A3N7EWE1;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Chloride channel protein {ECO:0000256|RuleBase:RU361221};
GN ORFNames=POPTR_004G209901 {ECO:0000313|EMBL:RQO89629.1};
OS Populus trichocarpa (Western balsam poplar) (Populus balsamifera subsp.
OS trichocarpa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Salicaceae; Saliceae; Populus.
OX NCBI_TaxID=3694 {ECO:0000313|EMBL:RQO89629.1, ECO:0000313|Proteomes:UP000006729};
RN [1] {ECO:0000313|EMBL:RQO89629.1, ECO:0000313|Proteomes:UP000006729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nisqually {ECO:0000313|Proteomes:UP000006729};
RX PubMed=16973872; DOI=10.1126/science.1128691;
RA Tuskan G.A., Difazio S., Jansson S., Bohlmann J., Grigoriev I.,
RA Hellsten U., Putnam N., Ralph S., Rombauts S., Salamov A., Schein J.,
RA Sterck L., Aerts A., Bhalerao R.R., Bhalerao R.P., Blaudez D., Boerjan W.,
RA Brun A., Brunner A., Busov V., Campbell M., Carlson J., Chalot M.,
RA Chapman J., Chen G.L., Cooper D., Coutinho P.M., Couturier J., Covert S.,
RA Cronk Q., Cunningham R., Davis J., Degroeve S., Dejardin A.,
RA Depamphilis C., Detter J., Dirks B., Dubchak I., Duplessis S., Ehlting J.,
RA Ellis B., Gendler K., Goodstein D., Gribskov M., Grimwood J., Groover A.,
RA Gunter L., Hamberger B., Heinze B., Helariutta Y., Henrissat B.,
RA Holligan D., Holt R., Huang W., Islam-Faridi N., Jones S.,
RA Jones-Rhoades M., Jorgensen R., Joshi C., Kangasjarvi J., Karlsson J.,
RA Kelleher C., Kirkpatrick R., Kirst M., Kohler A., Kalluri U., Larimer F.,
RA Leebens-Mack J., Leple J.C., Locascio P., Lou Y., Lucas S., Martin F.,
RA Montanini B., Napoli C., Nelson D.R., Nelson C., Nieminen K., Nilsson O.,
RA Pereda V., Peter G., Philippe R., Pilate G., Poliakov A., Razumovskaya J.,
RA Richardson P., Rinaldi C., Ritland K., Rouze P., Ryaboy D., Schmutz J.,
RA Schrader J., Segerman B., Shin H., Siddiqui A., Sterky F., Terry A.,
RA Tsai C.J., Uberbacher E., Unneberg P., Vahala J., Wall K., Wessler S.,
RA Yang G., Yin T., Douglas C., Marra M., Sandberg G., Van de Peer Y.,
RA Rokhsar D.;
RT "The genome of black cottonwood, Populus trichocarpa (Torr. & Gray).";
RL Science 313:1596-1604(2006).
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|ARBA:ARBA00009476, 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; CM009293; RQO89629.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N7EWE1; -.
DR Proteomes; UP000006729; Chromosome 4.
DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR GO; GO:0005247; F:voltage-gated chloride channel activity; IEA:UniProtKB-UniRule.
DR CDD; cd04592; CBS_pair_voltage-gated_CLC_euk_bac; 1.
DR CDD; cd00400; Voltage_gated_ClC; 1.
DR Gene3D; 3.10.580.10; CBS-domain; 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; PTHR43427; CHLORIDE CHANNEL PROTEIN CLC-E; 1.
DR PANTHER; PTHR43427:SF6; CHLORIDE CHANNEL PROTEIN CLC-E; 1.
DR Pfam; PF00571; CBS; 1.
DR Pfam; PF00654; Voltage_CLC; 1.
DR PRINTS; PR00762; CLCHANNEL.
DR SMART; SM00116; CBS; 2.
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|RuleBase:RU361221};
KW Ion channel {ECO:0000256|ARBA:ARBA00023303};
KW Ion transport {ECO:0000256|RuleBase:RU361221};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361221};
KW Reference proteome {ECO:0000313|Proteomes:UP000006729};
KW Signal {ECO:0000256|SAM:SignalP};
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 SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..430
FT /note="Chloride channel protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018004390"
FT TRANSMEM 59..76
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 165..190
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 196..213
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT DOMAIN 294..353
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT REGION 216..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..250
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 430 AA; 47214 MW; 857796E15155F5BE CRC64;
MRLLLVVFLL WSRCCGHLQV IQKHHSQTPL LWLYLALSYL GSEPAFKVPD YDFRSPSELP
LYLLLGILCG LVSLTLSRCT SFMLSTVNHL HRTVGIPSAA FPVLGVKIVA TSLCRASGLV
GGYYAPSLFI GAATGMAYGK FINIAVAQSS PTLQLSFLEV ASPQAYGLVG MAATLAGVCQ
VPLTAVLLLF ELTQDYRIVL PLLGAVGLSS WVTSGQKRRR DGKGTTKLNE GNRRPTQEPE
MSSSETSGLS SDYALTEKAP YENNPCEIES SLCIDDSSIE TEVFEKNVLV SEAMRTRYVT
VLMSTLLTEA VSLMLAEKQS CAMVVDDNNI LIGLLTLADI DDFSKIIKSE NRITKELLVT
ELCSLDGKRC QVPWIAKPSM DLLSVQIIMD RHGVNQVPVV SEHIEDHKRQ PVGLLDRECI
SVTFRFLHNI
//
