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CLCN3_RABIT
ID   CLCN3_RABIT             Reviewed;         818 AA.
AC   O18894;
DT   21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   14-APR-2009, sequence version 3.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=H(+)/Cl(-) exchange transporter 3;
DE   AltName: Full=Chloride channel protein 3;
DE            Short=ClC-3;
DE   AltName: Full=Chloride transporter ClC-3;
GN   Name=CLCN3;
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 endothelium;
RA   Rae J.L., Shepard A.R.;
RL   Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Strongly outwardly rectifying, electrogenic
CC       H(+)/Cl(-)exchanger which mediates the exchange of chloride ions
CC       against protons (By similarity). The CLC channel family contains both
CC       chloride channels and proton-coupled anion transporters that exchange
CC       chloride or another anion for protons (By similarity). The presence of
CC       conserved gating glutamate residues is typical for family members that
CC       function as antiporters (By similarity). {ECO:0000250|UniProtKB:P51790,
CC       ECO:0000250|UniProtKB:P51791}.
CC   -!- SUBCELLULAR LOCATION: Early endosome membrane
CC       {ECO:0000250|UniProtKB:P51790}; Multi-pass membrane protein
CC       {ECO:0000255}. Late endosome membrane {ECO:0000250|UniProtKB:P51790};
CC       Multi-pass membrane protein {ECO:0000255}. Lysosome membrane
CC       {ECO:0000250|UniProtKB:P51791}; Multi-pass membrane protein
CC       {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:P51792}; Multi-pass
CC       membrane protein {ECO:0000255}.
CC   -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:P51790}.
CC   -!- SIMILARITY: Belongs to the chloride channel (TC 2.A.49) family. ClC-
CC       3/CLCN3 subfamily. {ECO:0000305}.
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DR   EMBL; AF029348; AAB95163.1; -; mRNA.
DR   RefSeq; NP_001075498.1; NM_001082029.1.
DR   RefSeq; XP_008272119.1; XM_008273897.2.
DR   AlphaFoldDB; O18894; -.
DR   SMR; O18894; -.
DR   STRING; 9986.ENSOCUP00000005386; -.
DR   Ensembl; ENSOCUT00000044580; ENSOCUP00000036091; ENSOCUG00000006220.
DR   GeneID; 100008673; -.
DR   KEGG; ocu:100008673; -.
DR   CTD; 1182; -.
DR   eggNOG; KOG0475; Eukaryota.
DR   GeneTree; ENSGT00940000153763; -.
DR   InParanoid; O18894; -.
DR   Proteomes; UP000001811; Chromosome 2.
DR   Bgee; ENSOCUG00000006220; Expressed in blood and 16 other tissues.
DR   ExpressionAtlas; O18894; baseline.
DR   GO; GO:0005769; C:early endosome; ISS:UniProtKB.
DR   GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0010008; C:endosome membrane; ISS:UniProtKB.
DR   GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005770; C:late endosome; ISS:UniProtKB.
DR   GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005765; C:lysosomal membrane; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0055037; C:recycling endosome; ISS:UniProtKB.
DR   GO; GO:0012506; C:vesicle membrane; ISS:UniProtKB.
DR   GO; GO:0015297; F:antiporter activity; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0030165; F:PDZ domain binding; ISS:UniProtKB.
DR   GO; GO:0005247; F:voltage-gated chloride channel activity; ISS:UniProtKB.
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; IPR002245; Cl_channel-3.
DR   Pfam; PF00571; CBS; 2.
DR   Pfam; PF00654; Voltage_CLC; 1.
DR   PRINTS; PR00762; CLCHANNEL.
DR   PRINTS; PR01114; CLCHANNEL3.
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; Cell membrane; Chloride; Endosome;
KW   Glycoprotein; Ion transport; Lysosome; Membrane; Nucleotide-binding;
KW   Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..818
FT                   /note="H(+)/Cl(-) exchange transporter 3"
FT                   /id="PRO_0000094441"
FT   TOPO_DOM        1..125
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P35523"
FT   TRANSMEM        126..163
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P35523"
FT   TRANSMEM        209..232
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P35523"
FT   INTRAMEM        241..248
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P35523"
FT   TRANSMEM        258..276
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P35523"
FT   TRANSMEM        282..301
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P35523"
FT   INTRAMEM        313..325
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P35523"
FT   INTRAMEM        329..337
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P35523"
FT   TRANSMEM        349..367
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P35523"
FT   TRANSMEM        391..416
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P35523"
FT   TRANSMEM        423..443
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P35523"
FT   TRANSMEM        500..520
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P35523"
FT   TRANSMEM        525..544
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P35523"
FT   INTRAMEM        572..586
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P35523"
FT   INTRAMEM        590..601
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P35523"
FT   INTRAMEM        602..605
FT                   /note="Note=Loop between two helices"
FT                   /evidence="ECO:0000250|UniProtKB:P35523"
FT   TRANSMEM        606..624
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P35523"
FT   TOPO_DOM        625..818
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P35523"
FT   DOMAIN          658..722
FT                   /note="CBS 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT   DOMAIN          755..812
FT                   /note="CBS 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT   MOTIF           28..29
FT                   /note="Di-leucine internalization motif; mediates targeting
FT                   to late endosome and lysosome membranes"
FT                   /evidence="ECO:0000250|UniProtKB:P51791"
FT   MOTIF           46..47
FT                   /note="Di-leucine internalization motif; mediates targeting
FT                   to late endosome and lysosome membranes"
FT                   /evidence="ECO:0000250|UniProtKB:P51791"
FT   MOTIF           71..75
FT                   /note="Di-leucine internalization motif; mediates targeting
FT                   to late endosome and lysosome membranes"
FT                   /evidence="ECO:0000250|UniProtKB:P51791"
FT   MOTIF           238..242
FT                   /note="Selectivity filter part_1"
FT                   /evidence="ECO:0000250"
FT   MOTIF           280..284
FT                   /note="Selectivity filter part_2"
FT                   /evidence="ECO:0000250"
FT   MOTIF           525..529
FT                   /note="Selectivity filter part_3"
FT                   /evidence="ECO:0000250"
FT   BINDING         239
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /evidence="ECO:0000250"
FT   BINDING         527
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /evidence="ECO:0000250"
FT   BINDING         630
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /evidence="ECO:0000250"
FT   BINDING         689..691
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         796..799
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   SITE            282
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            339
FT                   /note="Mediates proton transfer from the protein to the
FT                   inner aqueous phase"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        177
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        451
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        479
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   818 AA;  90966 MW;  30FF0A6A2D6EF3B8 CRC64;
     MESEQLFHRG YYRNSYNSIT SASSDEELLD GAGVIMDFQT SEDDNLLDGD TAVGTHYTMT
     NGGSINSSTH LLDLLDEPIP GVGTYDDFHT IDWVREKCKD RERHRRINSK KKESAWEMTK
     SLYDAWSGWL VVTLTGLASG ALAGLIDIAA DWMTDLKEGI CLSALWYNHE QCCWGSNETT
     FEERDKCPQW KTWAELIIGQ AEGPGSYIMN YIMYIFWALS FAFLAVSLVK VFAPYACGSG
     IPEIKTILSG FIIRGYLGKW TLMIKTITLV LAVASGLSLG KEGPLVHVAC CCGNIFSYLF
     PKYSTNEAKK REVLSAASAA GVSVAFGAPI GGVLFSLEEV SYYFPLKTLW RSFFAALVAA
     FVLRSINPFG NSRLVLFYVE YHTPWYLFEL FPFILLGVFG GLWGAFFIRA NIAWCRRRKS
     TKFGKYPVLE VIIVAAITAV IAFPNPYTRL NTSELIKELF TDCGPLESSS LCDYRNDMNA
     SKIVDDIPDR PAGIGVYSAI WQLCLALIFK IIMTVFTFGI KVPSGLFIPS MAIGAIAGRI
     VGIAVEQLAY YHHDWFIFKE WCEVGADCIT PGLYAMVGAA ACLGGVTRMT VSLVVIVFEL
     TGGLEYIVPL MAAVMTSKWV GDAFGREGIY EAHIRLNGYP FLDAKEEFTH TTLAADVMRP
     RRNDPPLAVL TQDNMTVDDI ENMINETSYN GFPVIMSKES QRLVGFALRR DLTIAIESAR
     KKQEGIVGSS RVCFAQHTPS LPAESPRPLK LRSILDMSPF TVTDHTPMEI VVDIFRKLGL
     RQCLVTHNGR LLGIITKKDI LRHMAQTANQ DPASIMFN
 
 
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