(data stored in ACNUC10083 zone)

SWISSPROT: CLCN7_BOVIN

ID   CLCN7_BOVIN             Reviewed;         809 AA.
AC   Q4PKH3;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   11-DEC-2019, entry version 96.
DE   RecName: Full=H(+)/Cl(-) exchange transporter 7;
DE   AltName: Full=Chloride channel 7 alpha subunit;
DE   AltName: Full=Chloride channel protein 7;
DE            Short=ClC-7;
GN   Name=CLCN7;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Lens epithelium;
RA   Rae J.L.;
RT   "Ion channels in ocular epithelia.";
RL   Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Slowly voltage-gated channel mediating the exchange of
CC       chloride ions against protons. Functions as antiporter and contributes
CC       to the acidification of the lysosome lumen (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Chloride channel 7 are heteromers of alpha (CLCN7) and beta
CC       (OSTM1) subunits. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}.
CC   -!- MISCELLANEOUS: The CLC channel family contains both chloride channels
CC       and proton-coupled anion transporters that exchange chloride or another
CC       anion for protons. The presence of conserved gating glutamate residues
CC       is typical for family members that function as antiporters (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the chloride channel (TC 2.A.49) family. ClC-
CC       7/CLCN7 subfamily. {ECO:0000305}.
DR   EMBL; DQ073465; AAY82470.1; -; mRNA.
DR   RefSeq; NP_001020502.1; NM_001025331.1.
DR   STRING; 9913.ENSBTAP00000021122; -.
DR   PaxDb; Q4PKH3; -.
DR   PRIDE; Q4PKH3; -.
DR   Ensembl; ENSBTAT00000021122; ENSBTAP00000021122; ENSBTAG00000015889.
DR   GeneID; 513545; -.
DR   KEGG; bta:513545; -.
DR   CTD; 1186; -.
DR   VGNC; VGNC:27401; CLCN7.
DR   eggNOG; KOG0474; Eukaryota.
DR   eggNOG; COG0038; LUCA.
DR   GeneTree; ENSGT00940000158458; -.
DR   HOGENOM; HOG000231081; -.
DR   InParanoid; Q4PKH3; -.
DR   KO; K05016; -.
DR   OMA; DYDVCEN; -.
DR   OrthoDB; 410280at2759; -.
DR   TreeFam; TF313867; -.
DR   Reactome; R-BTA-2672351; Stimuli-sensing channels.
DR   Proteomes; UP000009136; Chromosome 25.
DR   Bgee; ENSBTAG00000015889; Expressed in 9 organ(s), highest expression level in adult mammalian kidney.
DR   ExpressionAtlas; Q4PKH3; baseline and differential.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR   GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0015297; F:antiporter activity; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0015108; F:chloride transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0005247; F:voltage-gated chloride channel activity; IEA:InterPro.
DR   Gene3D; 1.10.3080.10; -; 1.
DR   InterPro; IPR000644; CBS_dom.
DR   InterPro; IPR014743; Cl-channel_core.
DR   InterPro; IPR001807; Cl-channel_volt-gated.
DR   InterPro; IPR002249; Cl_channel-7.
DR   Pfam; PF00571; CBS; 2.
DR   Pfam; PF00654; Voltage_CLC; 1.
DR   PRINTS; PR00762; CLCHANNEL.
DR   PRINTS; PR01118; CLCHANNEL7.
DR   SMART; SM00116; CBS; 2.
DR   SUPFAM; SSF81340; SSF81340; 1.
DR   PROSITE; PS51371; CBS; 2.
PE   2: Evidence at transcript level;
DR   PRODOM; Q4PKH3.
DR   SWISS-2DPAGE; Q4PKH3.
KW   Antiport; ATP-binding; CBS domain; Chloride; Ion transport; Lysosome;
KW   Membrane; Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..809
FT                   /note="H(+)/Cl(-) exchange transporter 7"
FT                   /id="PRO_0000244028"
FT   TOPO_DOM        1..130
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        131..163
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        178..201
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   INTRAMEM        210..217
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        227..245
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        251..268
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   INTRAMEM        292..304
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   INTRAMEM        308..316
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        326..345
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        379..409
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        414..436
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        491..511
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        516..539
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   INTRAMEM        549..563
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   INTRAMEM        564..566
FT                   /note="Note=Loop between two helices"
FT                   /evidence="ECO:0000250"
FT   INTRAMEM        567..578
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   INTRAMEM        579..582
FT                   /note="Note=Loop between two helices"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        583..601
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        602..809
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   DOMAIN          635..699
FT                   /note="CBS 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT   DOMAIN          745..803
FT                   /note="CBS 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT   NP_BIND         662..664
FT                   /note="ATP"
FT                   /evidence="ECO:0000250"
FT   NP_BIND         787..790
FT                   /note="ATP"
FT                   /evidence="ECO:0000250"
FT   MOTIF           207..211
FT                   /note="Selectivity filter part_1"
FT                   /evidence="ECO:0000250"
FT   MOTIF           249..253
FT                   /note="Selectivity filter part_2"
FT                   /evidence="ECO:0000250"
FT   MOTIF           516..520
FT                   /note="Selectivity filter part_3"
FT                   /evidence="ECO:0000250"
FT   BINDING         208
FT                   /note="Chloride"
FT                   /evidence="ECO:0000250"
FT   BINDING         518
FT                   /note="Chloride; via amide nitrogen"
FT                   /evidence="ECO:0000250"
FT   BINDING         606
FT                   /note="Chloride"
FT                   /evidence="ECO:0000250"
FT   SITE            251
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            318
FT                   /note="Mediates proton transfer from the protein to the
FT                   inner aqueous phase"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         9
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O70496"
FT   MOD_RES         64
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P51798"
FT   MOD_RES         805
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P51798"
SQ   SEQUENCE   809 AA;  88831 MW;  B8A07A7B840FD7F3 CRC64;
     MANVSKKVSW SGRDLDDDEA APLLRRAPRL GVPAGEAAPL LNGAGPAAAR ASPHSAFFRI
     GQLSSVELDD ELLDPDMDPP HPFPREIPHN EKLLSLKYES LDYDNSENQL FLEEERRINH
     TAFRTVEIKR WVICAMVGIL TGLVACFIDI VVEKLAGLKY RLVKDNIDRF TEHGGLSFSL
     LLWAALNAAF VLLGSTIVAF IEPVAAGSGI PQIKCFLNGV KIPHVVRLKT LVIKVSGVIL
     SVVGGLAVGK EGPMIHSGSV IAAGISQGRS TSLKRDFKIF EYFRRDTEKR DFVSAGAAAG
     VSAAFGAPVG GVLFSLEEGA SFWNQFLTWR IFFASMISTF TLNFVLSIYH GNAWDLSSPG
     LINFGRFDTE TMVYVIHEIP IFIAMGVVGG ILGAVFNALN YWLTMFRIRY VHRPCLQVVE
     ATLVAAVTAT AAFVLIYSSR DCQPLRGSSV SYPLQLFCAD GEYNSMAVAF FNTPEKSVVS
     LFHDPPGSYN PMTLGLFTLV YFFLACWTYG LTVSAGVFIP SLLIGAAWGR LFGISLSYIT
     GAAVWADPGK YALMGAAAQL GGIVRMTLSL TVIMMEATSS VTYGFPIMLV LMTAKIVGDV
     FIEGLYDMHI QLQSVPFLHW EAPVTSHSLT AREVMSTPVT CLRRREKVGV IVDVLSSTAS
     NHNGFPVVED ADGTQPARLQ GLILRSQLIV LLKHKVFVER SSMGLLRRRL RLKDFRDAYP
     RFPPIQSIHV SQDERECTMD LSEFMNPSPY TVPQEASLPR VFKLFRALGL RHLVVVDNCN
     QVVGLVTRKD LARYRLGKGG LEELSLAQT
//

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