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Protein

H(+)/Cl(-) exchange transporter 3

Gene

CLCN3

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Mediates the exchange of chloride ions against protons. Functions as antiporter and contributes to the acidification of the endosome and synaptic vesicle lumen, and may thereby affect vesicle trafficking and exocytosis. May play an important role in neuronal cell function through regulation of membrane excitability by protein kinase C. It could help neuronal cells to establish short-term memory (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei239 – 2391ChlorideBy similarity
Sitei282 – 2821Mediates proton transfer from the outer aqueous phase to the interior of the protein; involved in linking H(+) and Cl(-) transportBy similarity
Sitei339 – 3391Mediates proton transfer from the protein to the inner aqueous phaseBy similarity
Binding sitei527 – 5271Chloride; via amide nitrogenBy similarity
Binding sitei630 – 6301ChlorideBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi689 – 6913ATPBy similarity
Nucleotide bindingi796 – 7994ATPBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Antiport, Ion transport, Transport

Keywords - Ligandi

ATP-binding, Chloride, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
H(+)/Cl(-) exchange transporter 3
Alternative name(s):
Chloride channel protein 3
Short name:
ClC-3
Chloride transporter ClC-3
Gene namesi
Name:CLCN3
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
Proteomesi
  • UP000001811 Componenti: Unplaced

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 125125CytoplasmicBy similarityAdd
BLAST
Transmembranei126 – 16338HelicalBy similarityAdd
BLAST
Transmembranei209 – 23224HelicalBy similarityAdd
BLAST
Intramembranei241 – 2488HelicalBy similarity
Transmembranei258 – 27619HelicalBy similarityAdd
BLAST
Transmembranei282 – 30120HelicalBy similarityAdd
BLAST
Intramembranei313 – 32513HelicalBy similarityAdd
BLAST
Intramembranei329 – 3379HelicalBy similarity
Transmembranei349 – 36719HelicalBy similarityAdd
BLAST
Transmembranei391 – 41626HelicalBy similarityAdd
BLAST
Transmembranei423 – 44321HelicalBy similarityAdd
BLAST
Transmembranei500 – 52021HelicalBy similarityAdd
BLAST
Transmembranei525 – 54420HelicalBy similarityAdd
BLAST
Intramembranei572 – 58615HelicalBy similarityAdd
BLAST
Intramembranei590 – 60112HelicalBy similarityAdd
BLAST
Intramembranei602 – 6054Note=Loop between two helicesBy similarity
Transmembranei606 – 62419HelicalBy similarityAdd
BLAST
Topological domaini625 – 818194CytoplasmicBy similarityAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle, Endosome, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 818818H(+)/Cl(-) exchange transporter 3PRO_0000094441Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi177 – 1771N-linked (GlcNAc...)Sequence analysis
Glycosylationi451 – 4511N-linked (GlcNAc...)Sequence analysis
Glycosylationi479 – 4791N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

N-glycosylated.By similarity

Keywords - PTMi

Glycoprotein

Proteomic databases

PRIDEiO18894.

Interactioni

GO - Molecular functioni

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000005386.

Structurei

3D structure databases

ProteinModelPortaliO18894.
SMRiO18894. Positions 211-811.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini658 – 72265CBS 1PROSITE-ProRule annotationAdd
BLAST
Domaini755 – 81258CBS 2PROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi238 – 2425Selectivity filter part_1By similarity
Motifi280 – 2845Selectivity filter part_2By similarity
Motifi525 – 5295Selectivity filter part_3By similarity

Sequence similaritiesi

Contains 2 CBS domains.PROSITE-ProRule annotation

Keywords - Domaini

CBS domain, Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0475. Eukaryota.
COG0038. LUCA.
HOGENOMiHOG000164493.
InParanoidiO18894.
KOiK05012.

Family and domain databases

Gene3Di1.10.3080.10. 3 hits.
InterProiIPR000644. CBS_dom.
IPR014743. Cl-channel_core.
IPR001807. Cl-channel_volt-gated.
IPR002245. Cl_channel-3.
[Graphical view]
PfamiPF00571. CBS. 2 hits.
PF00654. Voltage_CLC. 1 hit.
[Graphical view]
PRINTSiPR00762. CLCHANNEL.
PR01114. CLCHANNEL3.
SMARTiSM00116. CBS. 2 hits.
[Graphical view]
SUPFAMiSSF81340. SSF81340. 3 hits.
PROSITEiPS51371. CBS. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O18894-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MESEQLFHRG YYRNSYNSIT SASSDEELLD GAGVIMDFQT SEDDNLLDGD
60 70 80 90 100
TAVGTHYTMT NGGSINSSTH LLDLLDEPIP GVGTYDDFHT IDWVREKCKD
110 120 130 140 150
RERHRRINSK KKESAWEMTK SLYDAWSGWL VVTLTGLASG ALAGLIDIAA
160 170 180 190 200
DWMTDLKEGI CLSALWYNHE QCCWGSNETT FEERDKCPQW KTWAELIIGQ
210 220 230 240 250
AEGPGSYIMN YIMYIFWALS FAFLAVSLVK VFAPYACGSG IPEIKTILSG
260 270 280 290 300
FIIRGYLGKW TLMIKTITLV LAVASGLSLG KEGPLVHVAC CCGNIFSYLF
310 320 330 340 350
PKYSTNEAKK REVLSAASAA GVSVAFGAPI GGVLFSLEEV SYYFPLKTLW
360 370 380 390 400
RSFFAALVAA FVLRSINPFG NSRLVLFYVE YHTPWYLFEL FPFILLGVFG
410 420 430 440 450
GLWGAFFIRA NIAWCRRRKS TKFGKYPVLE VIIVAAITAV IAFPNPYTRL
460 470 480 490 500
NTSELIKELF TDCGPLESSS LCDYRNDMNA SKIVDDIPDR PAGIGVYSAI
510 520 530 540 550
WQLCLALIFK IIMTVFTFGI KVPSGLFIPS MAIGAIAGRI VGIAVEQLAY
560 570 580 590 600
YHHDWFIFKE WCEVGADCIT PGLYAMVGAA ACLGGVTRMT VSLVVIVFEL
610 620 630 640 650
TGGLEYIVPL MAAVMTSKWV GDAFGREGIY EAHIRLNGYP FLDAKEEFTH
660 670 680 690 700
TTLAADVMRP RRNDPPLAVL TQDNMTVDDI ENMINETSYN GFPVIMSKES
710 720 730 740 750
QRLVGFALRR DLTIAIESAR KKQEGIVGSS RVCFAQHTPS LPAESPRPLK
760 770 780 790 800
LRSILDMSPF TVTDHTPMEI VVDIFRKLGL RQCLVTHNGR LLGIITKKDI
810
LRHMAQTANQ DPASIMFN
Length:818
Mass (Da):90,966
Last modified:April 14, 2009 - v3
Checksum:i30FF0A6A2D6EF3B8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF029348 mRNA. Translation: AAB95163.1.
RefSeqiNP_001075498.1. NM_001082029.1.
XP_008272119.1. XM_008273897.1.
UniGeneiOcu.2190.

Genome annotation databases

GeneIDi100008673.
KEGGiocu:100008673.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF029348 mRNA. Translation: AAB95163.1.
RefSeqiNP_001075498.1. NM_001082029.1.
XP_008272119.1. XM_008273897.1.
UniGeneiOcu.2190.

3D structure databases

ProteinModelPortaliO18894.
SMRiO18894. Positions 211-811.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000005386.

Proteomic databases

PRIDEiO18894.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100008673.
KEGGiocu:100008673.

Organism-specific databases

CTDi1182.

Phylogenomic databases

eggNOGiKOG0475. Eukaryota.
COG0038. LUCA.
HOGENOMiHOG000164493.
InParanoidiO18894.
KOiK05012.

Family and domain databases

Gene3Di1.10.3080.10. 3 hits.
InterProiIPR000644. CBS_dom.
IPR014743. Cl-channel_core.
IPR001807. Cl-channel_volt-gated.
IPR002245. Cl_channel-3.
[Graphical view]
PfamiPF00571. CBS. 2 hits.
PF00654. Voltage_CLC. 1 hit.
[Graphical view]
PRINTSiPR00762. CLCHANNEL.
PR01114. CLCHANNEL3.
SMARTiSM00116. CBS. 2 hits.
[Graphical view]
SUPFAMiSSF81340. SSF81340. 3 hits.
PROSITEiPS51371. CBS. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Rae J.L., Shepard A.R.
    Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: New Zealand white.
    Tissue: Corneal endothelium.

Entry informationi

Entry nameiCLCN3_RABIT
AccessioniPrimary (citable) accession number: O18894
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 21, 2003
Last sequence update: April 14, 2009
Last modified: May 11, 2016
This is version 94 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

The CLC channel family contains both chloride channels and proton-coupled anion transporters that exchange chloride or another anion for protons. The presence of conserved gating glutamate residues is typical for family members that function as antiporters (By similarity).By similarity

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.