Glutamate-gated chloride channel subunit beta precursor

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Q17328 (GLUCB_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 89. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Glutamate-gated chloride channel subunit beta
Short name=Glu-Cl subunit beta

Alternative name(s):
Avermectin-sensitive glutamate-gated chloride channel subunit

Gene names

Name:	glc-2
ORF Names:	F25F8.2

Organism

Caenorhabditis elegans

Taxonomic identifier

6239 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis

Protein attributes

Sequence length	434 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Glutamate gated chloride channel that is dual gated by glutamate and avermectin.
Subunit structure	Homomultimer By similarity.
Subcellular location	Cell junction › synapse › postsynaptic cell membrane; Multi-pass membrane protein By similarity. Cell membrane; Multi-pass membrane protein By similarity.
Sequence similarities	Belongs to the ligand-gated ion channel (TC 1.A.9) family. Glutamate-gated chloride channel (TC 1.A.9.4) subfamily. [View classification]

Ontologies

Keywords
Biological process	Ion transport Transport
Cellular component	Cell junction Cell membrane Membrane Postsynaptic cell membrane Synapse
Domain	Signal Transmembrane Transmembrane helix
Ligand	Chloride
Molecular function	Chloride channel Ionic channel Ligand-gated ion channel Receptor
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	embryo development ending in birth or egg hatching Inferred from mutant phenotype. Source: WormBase
Cellular component	cell junction Inferred from electronic annotation. Source: UniProtKB-KW chloride channel complex Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell postsynaptic membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	chloride channel activity Inferred from electronic annotation. Source: UniProtKB-KW extracellular ligand-gated ion channel activity Inferred from electronic annotation. Source: InterPro receptor activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 22

Potential

Chain

23 – 434

412

Glutamate-gated chloride channel subunit beta

PRO_0000255716

Regions

Topological domain

23 – 248

226

Extracellular Potential

Transmembrane

249 – 269

Helical; Potential

Transmembrane

276 – 295

Helical; Potential

Transmembrane

310 – 330

Helical; Potential

Topological domain

331 – 402

Cytoplasmic Potential

Transmembrane

403 – 423

Helical; Potential

Amino acid modifications

Glycosylation

N-linked (GlcNAc...) Ref.3

Glycosylation

216

N-linked (GlcNAc...) Potential

Glycosylation

426

N-linked (GlcNAc...) Potential

Sequences

Sequence

Length

Mass (Da)

Tools

Q17328 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 754B973359834F75
Show »

FASTA

434

49,893

        10         20         30         40         50         60 
MTTPSSFSIL LLLLLMPVVT NGEYSMQSEQ EILNALLKNY DMRVRPPPAN SSTEGAVNVR 

        70         80         90        100        110        120 
VNIMIRMLSK IDVVNMEYSI QLTFREQWID PRLAYENLGF YNPPAFLTVP HVKKSLWIPD 

       130        140        150        160        170        180 
TFFPTEKAAH RHLIDMENMF LRIYPDGKIL YSSRISLTSS CPMRLQLYPL DYQSCNFDLV 

       190        200        210        220        230        240 
SYAHTMNDIM YEWDPSTPVQ LKPGVGSDLP NFILKNYTTN ADCTSHTNTG SYGCLRMQLL 

       250        260        270        280        290        300 
FKRQFSYYLV QLYAPTTMIV IVSWVSFWID LHSTAGRVAL GVTTLLTMTT MQSAINAKLP 

       310        320        330        340        350        360 
PVSYVKVVDV WLGACQTFVF GALLEYAFVS YQDSVRQNDR SREKAARKAQ RRREKLEMVD 

       370        380        390        400        410        420 
AEVYQPPCTC HTFEARETFR DKVRRYFTKP DYLPAKIDFY ARFVVPLAFL AFNVIYWVSC 

       430 
LIMSANASTP ESLV

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of an avermectin-sensitive glutamate-gated chloride channel from Caenorhabditis elegans." Cully D.F., Vassilatis D.K., Liu K.K., Paress P.S., Van der Ploeg L.H.T., Schaeffer J.M., Arena J.P. Nature 371:707-711(1994) [PubMed: 7935817] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Bristol N2.
[2]	"Genome sequence of the nematode C. elegans: a platform for investigating biology." The C. elegans sequencing consortium Science 282:2012-2018(1998) [PubMed: 9851916] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Bristol N2.
[3]	"Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis elegans and suggests an atypical translocation mechanism for integral membrane proteins." Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T., Taoka M., Takahashi N., Isobe T. Mol. Cell. Proteomics 6:2100-2109(2007) [PubMed: 17761667] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-50, MASS SPECTROMETRY. Strain: Bristol N2.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U14525 mRNA. Translation: AAA50786.1. FO080262 Genomic DNA. Translation: CCD62432.1.
PIR	S50865.
RefSeq	NP_491470.1. NM_059069.3.
UniGene	Cel.19753.
3D structure databases
HSSP	HSSP built from PDB template 1VRY based on UniProtKB P23415.
ProteinModelPortal	Q17328.
SMR	Q17328. Positions 28-420.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-27494N.
MINT	MINT-1047253.
Proteomic databases
PRIDE	Q17328.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	F25F8.2; F25F8.2; F25F8.2.
GeneID	172103.
KEGG	cel:F25F8.2.
NMPDR	fig\|6239.3.peg.1029.
UCSC	F25F8.2. c. elegans.
Organism-specific databases
CTD	172103.
WormBase	F25F8.2; CE09636; WBGene00001592; glc-2.
Phylogenomic databases
eggNOG	meNOG04494.
GeneTree	EMGT00050000005201.
HOGENOM	HBG506497.
InParanoid	Q17328.
OMA	NIMIRML.
PhylomeDB	Q17328.
Gene expression databases
ArrayExpress	Q17328.
Family and domain databases
InterPro	IPR006028. GABAA_rcpt. IPR015680. Glu_Cl_Channel. IPR006202. Neur_chan_lig-bd. IPR006201. Neur_channel. IPR006029. Neurotrans-gated_channel_TM. IPR018000. Neurotransmitter_ion_chnl_CS. [Graphical view]
Gene3D	G3DSA:2.70.170.10. Neur_chan_lig_bd. 1 hit.
KO	K05273.
PANTHER	PTHR18945:SF26. Glu_Cl_Channel. 1 hit. PTHR18945. Neur_channel. 1 hit.
Pfam	PF02931. Neur_chan_LBD. 1 hit. PF02932. Neur_chan_memb. 1 hit. [Graphical view]
PRINTS	PR00253. GABAARECEPTR. PR00252. NRIONCHANNEL.
SUPFAM	SSF90112. Neu_channel_TM. 1 hit. SSF63712. Neur_chan_LBD. 1 hit.
TIGRFAMs	TIGR00860. LIC. 1 hit.
PROSITE	PS00236. NEUROTR_ION_CHANNEL. 1 hit. [Graphical view]
ProtoNet	Search...
Other
DrugBank	DB00602. Ivermectin.
NextBio	874023.

Entry information

Entry name

GLUCB_CAEEL

Accession

Primary (citable) accession number: Q17328
Secondary accession number(s): O02524

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2006
Last sequence update:	November 1, 1996
Last modified:	December 14, 2011
This is version 89 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Caenorhabditis annotation project

Relevant documents

Caenorhabditis elegans

Caenorhabditis elegans: entries, gene names and cross-references to WormPep

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents