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Q5JXX5 (GLRA4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glycine receptor subunit alpha-4
Gene names
Name:GLRA4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length417 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

The glycine receptor is a neurotransmitter-gated ion channel. Binding of glycine to its receptor increases the chloride conductance and thus produces hyperpolarization (inhibition of neuronal firing).

Subunit structure

Pentamer composed of alpha and beta subunits By similarity.

Subcellular location

Cell junctionsynapsepostsynaptic cell membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein By similarity.

Miscellaneous

The alpha subunit binds strychnine By similarity.

Sequence similarities

Belongs to the ligand-gated ion channel (TC 1.A.9) family. Glycine receptor (TC 1.A.9.3) subfamily. GLRA4 sub-subfamily. [View classification]

Caution

Is shorter at the N-terminus compared to its mouse ortholog due to the presence of a premature stop codon.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2828 Potential
Chain29 – 417389Glycine receptor subunit alpha-4
PRO_0000338609

Regions

Topological domain29 – 258230Extracellular Potential
Transmembrane259 – 27921Helical; Potential
Topological domain280 – 32142Cytoplasmic Potential
Transmembrane322 – 34221Helical; Potential
Topological domain343 – 41775Extracellular Potential

Amino acid modifications

Glycosylation721N-linked (GlcNAc...) Potential
Disulfide bond172 ↔ 186 By similarity
Disulfide bond233 ↔ 244 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5JXX5 [UniParc].

Last modified November 3, 2009. Version 3.
Checksum: 7F3B1A5B26B7F0E6

FASTA41747,728
        10         20         30         40         50         60 
MTTLVPATLS FLLLWTLPGQ VLLRVALAKE EVKSGTKGSQ PMSPSDFLDK LMGRTSGYDA 

        70         80         90        100        110        120 
RIRPNFKGPP VNVTCNIFIN SFSSITKTTM DYRVNVFLRQ QWNDPRLSYR EYPDDSLDLD 

       130        140        150        160        170        180 
PSMLDSIWKP DLFFANEKGA NFHEVTTDNK LLRIFKNGNV LYSIRLTLIL SCLMDLKNFP 

       190        200        210        220        230        240 
MDIQTCTMQL ESFGYTMKDL VFEWLEDAPA VQVAEGLTLP QFILRDEKDL GCCTKHYNTG 

       250        260        270        280        290        300 
KFTCIEVKFH LERQMGYYLI QMYIPSLLIV ILSWVSFWIN MDAAPARVGL GITTVLTMTT 

       310        320        330        340        350        360 
QSSGSRASLP KVSYVKAIDI WMAVCLLFVF AALLEYAAIN FVSRQHKEFI RLRRRQRRQR 

       370        380        390        400        410 
LEEDIIQESR FYFRGYGLGH CLQARDGGPM EGSGIYSPQP PAPLLREGET TRKLYVD 

« Hide

References

[1]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z93848, AL049610 Genomic DNA. Translation: CAI41994.2.
AL049610, Z93848 Genomic DNA. Translation: CAI42158.2.
CCDSCCDS43980.2.
RefSeqNP_001019623.2. NM_001024452.2.
UniGeneHs.533289.

3D structure databases

ProteinModelPortalQ5JXX5.
SMRQ5JXX5. Positions 55-349.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000361700.

Chemistry

GuidetoPHARMACOLOGY426.

PTM databases

PhosphoSiteQ5JXX5.

Polymorphism databases

DMDM262527577.

Proteomic databases

PaxDbQ5JXX5.
PRIDEQ5JXX5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000372617; ENSP00000361700; ENSG00000188828.
GeneID441509.
KEGGhsa:441509.
UCSCuc010nou.2. human.

Organism-specific databases

CTD441509.
GeneCardsGC0XM102962.
HGNCHGNC:31715. GLRA4.
HPAHPA044759.
neXtProtNX_Q5JXX5.
PharmGKBPA142671731.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG265706.
HOGENOMHOG000231336.
HOVERGENHBG051707.
InParanoidQ5JXX5.
KOK05271.
OMASYREYPD.
OrthoDBEOG712TVZ.
PhylomeDBQ5JXX5.
TreeFamTF315453.

Enzyme and pathway databases

ReactomeREACT_15518. Transmembrane transport of small molecules.

Gene expression databases

BgeeQ5JXX5.
CleanExHS_GLRA4.
GenevestigatorQ5JXX5.

Family and domain databases

Gene3D2.70.170.10. 1 hit.
InterProIPR006028. GABAA/Glycine_rcpt.
IPR008127. Glycine_rcpt_A.
IPR006202. Neur_chan_lig-bd.
IPR006201. Neur_channel.
IPR006029. Neurotrans-gated_channel_TM.
IPR018000. Neurotransmitter_ion_chnl_CS.
[Graphical view]
PANTHERPTHR18945. PTHR18945. 1 hit.
PfamPF02931. Neur_chan_LBD. 1 hit.
PF02932. Neur_chan_memb. 1 hit.
[Graphical view]
PRINTSPR00253. GABAARECEPTR.
PR01673. GLYRALPHA.
PR00252. NRIONCHANNEL.
SUPFAMSSF63712. SSF63712. 1 hit.
SSF90112. SSF90112. 1 hit.
TIGRFAMsTIGR00860. LIC. 1 hit.
PROSITEPS00236. NEUROTR_ION_CHANNEL. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiGLRA4.
GenomeRNAi441509.
NextBio110250.
PROQ5JXX5.

Entry information

Entry nameGLRA4_HUMAN
AccessionPrimary (citable) accession number: Q5JXX5
Entry history
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: November 3, 2009
Last modified: July 9, 2014
This is version 65 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM