CLCN6_RABIT
ID CLCN6_RABIT Reviewed; 869 AA.
AC Q9TT16;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=H(+)/Cl(-) exchange transporter 6;
DE AltName: Full=Chloride channel protein 6;
DE Short=ClC-6;
DE AltName: Full=Chloride transport protein 6;
GN Name=CLCN6;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=New Zealand white; TISSUE=Corneal epithelium;
RA Rae J.L.;
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Voltage-gated channel mediating the exchange of chloride ions
CC against protons. Functions as antiporter and contributes to the
CC acidification of the late endosome lumen. The CLC channel family
CC contains both chloride channels and proton-coupled anion transporters
CC that exchange chloride or another anion for protons. The presence of
CC conserved gating glutamate residues is typical for family members that
CC function as antiporters. {ECO:0000250|UniProtKB:P51797}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 chloride(in) + H(+)(out) = 2 chloride(out) + H(+)(in);
CC Xref=Rhea:RHEA:29567, ChEBI:CHEBI:15378, ChEBI:CHEBI:17996;
CC Evidence={ECO:0000250|UniProtKB:P51797};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29568;
CC Evidence={ECO:0000250|UniProtKB:P51797};
CC -!- SUBCELLULAR LOCATION: Late endosome membrane
CC {ECO:0000250|UniProtKB:P51797}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P51797}.
CC -!- PTM: N-glycosylated on several asparagine residues.
CC {ECO:0000250|UniProtKB:P51797}.
CC -!- SIMILARITY: Belongs to the chloride channel (TC 2.A.49) family. ClC-
CC 6/CLCN6 subfamily. {ECO:0000305}.
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DR EMBL; AF209724; AAF22834.1; -; mRNA.
DR RefSeq; NP_001075543.1; NM_001082074.1.
DR AlphaFoldDB; Q9TT16; -.
DR SMR; Q9TT16; -.
DR STRING; 9986.ENSOCUP00000006313; -.
DR GeneID; 100008750; -.
DR KEGG; ocu:100008750; -.
DR CTD; 1185; -.
DR eggNOG; KOG0474; Eukaryota.
DR InParanoid; Q9TT16; -.
DR OrthoDB; 410280at2759; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015297; F:antiporter activity; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005247; F:voltage-gated chloride channel activity; ISS:UniProtKB.
DR GO; GO:0006821; P:chloride transport; ISS:UniProtKB.
DR Gene3D; 3.10.580.10; -; 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 InterPro; IPR002248; Cl_channel-6.
DR Pfam; PF00571; CBS; 2.
DR Pfam; PF00654; Voltage_CLC; 1.
DR PRINTS; PR00762; CLCHANNEL.
DR PRINTS; PR01117; CLCHANNEL6.
DR SMART; SM00116; CBS; 2.
DR SUPFAM; SSF54631; SSF54631; 1.
DR SUPFAM; SSF81340; SSF81340; 1.
DR PROSITE; PS51371; CBS; 2.
PE 2: Evidence at transcript level;
KW Antiport; ATP-binding; CBS domain; Chloride; Endosome; Glycoprotein;
KW Ion transport; Membrane; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..869
FT /note="H(+)/Cl(-) exchange transporter 6"
FT /id="PRO_0000094451"
FT TOPO_DOM 1..80
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 81..113
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 128..150
FT /note="Helical"
FT /evidence="ECO:0000250"
FT INTRAMEM 159..166
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 176..194
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 200..217
FT /note="Helical"
FT /evidence="ECO:0000250"
FT INTRAMEM 241..253
FT /note="Helical"
FT /evidence="ECO:0000250"
FT INTRAMEM 257..265
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 277..294
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 335..364
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 371..392
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 462..481
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 487..511
FT /note="Helical"
FT /evidence="ECO:0000250"
FT INTRAMEM 519..533
FT /note="Helical"
FT /evidence="ECO:0000250"
FT INTRAMEM 534..536
FT /note="Note=Loop between two helices"
FT /evidence="ECO:0000250"
FT INTRAMEM 537..548
FT /note="Helical"
FT /evidence="ECO:0000250"
FT INTRAMEM 549..552
FT /note="Note=Loop between two helices"
FT /evidence="ECO:0000250"
FT TRANSMEM 553..571
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 572..869
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT DOMAIN 605..662
FT /note="CBS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 807..868
FT /note="CBS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT REGION 668..687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 156..160
FT /note="Selectivity filter part_1"
FT /evidence="ECO:0000250"
FT MOTIF 198..202
FT /note="Selectivity filter part_2"
FT /evidence="ECO:0000250"
FT MOTIF 487..491
FT /note="Selectivity filter part_3"
FT /evidence="ECO:0000250"
FT BINDING 157
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250"
FT BINDING 489
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250"
FT BINDING 576
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250"
FT BINDING 630..632
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 849..852
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT SITE 200
FT /note="Mediates proton transfer from the outer aqueous
FT phase to the interior of the protein; involved in linking
FT H(+) and Cl(-) transport"
FT /evidence="ECO:0000250"
FT SITE 267
FT /note="Mediates proton transfer from the protein to the
FT inner aqueous phase"
FT /evidence="ECO:0000250"
FT MOD_RES 773
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35454"
FT CARBOHYD 410
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 422
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 432
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 869 AA; 97161 MW; 275248145AD21736 CRC64;
MAGCRGSLCC CCRWCCCCGE RETRTPEELT ILGETQEEED EILPRKDYES LDYDRCINDP
YLEVLETMDH KKGRWYEVVK WTVVFAIGVC TGLVGLFVDF FVQLFTQLKF GVVEASVEEC
SQKGCLALSL LELLGFNLTF VFLASLLVLI EPVAAGSGIP EIKCYLNGVK VPGIVRLRTL
LCKVFGVLFS VAGGLFVGKE GPMIHSGAVV GAGLPQFQSI SLRKIQFNFP YFRSDRDKRD
FVSAGAAAGI AAAFGAPIGA TLFSLEEGSS FWNQGLTWKV LFCSMSATFT LNFFRSGIQF
GSWGSFQLPG LLNFGEFKCS DSDKKCHLWT AMDMGFFVVM GVIGGLLGAT FNCLNKRLAK
YRMRNVHPKP KLVRVLESLL VSLVTTLVVF VASMVLGECR QMSSSSQISN GSLKLQVTSD
VNSSIKAFFC PNDTYNDMAT LFFNPQESAI LQLFHQDGTF SPITLALFFV LYFLLACWTY
GISVPSGLFV PSLLCGAAFG RLVANVLKSY IGLSHIYSGT FSLIGAAALL GGVVRMTISL
TVILIESTNE ITYGLPIMIT LMVAKWTGDF FNKGIYDIHV GLRGVPLLEW ETEVEMDKLR
ASDIMEPNLT YVYPHTRIQS LVSILRTTVH HAFPVVTENR GNEKEFMKGN QLISNNIKFK
KSSILTRAGE QRRRSQSMKS YPSSELRNVC DEHVASEEPA EKEDLLQQML ERRYTPYPNL
YPDQSPSEDW TMEERFRPLT FHGLILRSQL VTLLVRGVCY SESQSSASQP RLSYAEMAED
YPRFPDIHDL DLTLLNPRMI VDVTPYMNPS PFTVSPNTHV SQVFNLFRTM GLRHLPVVNA
VGEIVGIVTR HNLTYEFLQA RLRQHYQTI
