O60755 (GALR3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Galanin receptor type 3
Short name=GAL3-R
Short name=GALR-3

Gene names

Name:	GALR3
Synonyms:	GALNR3

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	368 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Receptor for the hormone galanin.
Subcellular location	Cell membrane; Multi-pass membrane protein.
Sequence similarities	Belongs to the G-protein coupled receptor 1 family.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Coding sequence diversity	Polymorphism
Domain	Transmembrane Transmembrane helix
Molecular function	G-protein coupled receptor Receptor Transducer
PTM	Disulfide bond Glycoprotein Lipoprotein Palmitate
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	feeding behavior Traceable author statement Ref.1. Source: ProtInc learning or memory Traceable author statement Ref.1. Source: ProtInc negative regulation of adenylate cyclase activity Traceable author statement Ref.3. Source: ProtInc
Cellular_component	integral to membrane Traceable author statement Ref.1. Source: ProtInc plasma membrane Traceable author statement. Source: Reactome
Molecular_function	galanin receptor activity Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 368	368	Galanin receptor type 3		PRO_0000069469
Regions
	Topological domain	1 – 20	20	Extracellular Potential
	Transmembrane	21 – 41	21	Helical; Name=1; Potential
	Topological domain	42 – 57	16	Cytoplasmic Potential
	Transmembrane	58 – 78	21	Helical; Name=2; Potential
	Topological domain	79 – 96	18	Extracellular Potential
	Transmembrane	97 – 118	22	Helical; Name=3; Potential
	Topological domain	119 – 138	20	Cytoplasmic Potential
	Transmembrane	139 – 159	21	Helical; Name=4; Potential
	Topological domain	160 – 184	25	Extracellular Potential
	Transmembrane	185 – 205	21	Helical; Name=5; Potential
	Topological domain	206 – 236	31	Cytoplasmic Potential
	Transmembrane	237 – 257	21	Helical; Name=6; Potential
	Topological domain	258 – 259	2	Extracellular Potential
	Transmembrane	260 – 280	21	Helical; Name=7; Potential
	Topological domain	281 – 368	88	Cytoplasmic Potential
	Compositional bias	218 – 225	8	Poly-Ala
	Compositional bias	310 – 318	9	Poly-Arg
Amino acid modifications
	Lipidation	308	1	S-palmitoyl cysteine By similarity
	Glycosylation	6	1	N-linked (GlcNAc...) Potential
	Disulfide bond	95 ↔ 172		By similarity
Natural variations
	Natural variant	342	1	R → G. Corresponds to variant rs8137541 [ dbSNP | Ensembl ].		VAR_049387
	Natural variant	349	1	Q → R. Corresponds to variant rs8137553 [ dbSNP | Ensembl ].		VAR_059322

Sequences

	Sequence		Length	Mass (Da)
	O60755 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: E8F46B66422C3150	FASTA	368	39,573
	10 20 30 40 50 60 MADAQNISLD SPGSVGAVAV PVVFALIFLL GTVGNGLVLA VLLQPGPSAW QEPGSTTDLF 70 80 90 100 110 120 ILNLAVADLC FILCCVPFQA TIYTLDAWLF GALVCKAVHL LIYLTMYASS FTLAAVSVDR 130 140 150 160 170 180 YLAVRHPLRS RALRTPRNAR AAVGLVWLLA ALFSAPYLSY YGTVRYGALE LCVPAWEDAR 190 200 210 220 230 240 RRALDVATFA AGYLLPVAVV SLAYGRTLRF LWAAVGPAGA AAAEARRRAT GRAGRAMLAV 250 260 270 280 290 300 AALYALCWGP HHALILCFWY GRFAFSPATY ACRLASHCLA YANSCLNPLV YALASRHFRA 310 320 330 340 350 360 RFRRLWPCGR RRRHRARRAL RRVRPASSGP PGCPGDARPS GRLLAGGGQG PEPREGPVHG GEAARGPE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloned human and rat galanin GALR3 receptors: pharmacology and activation of G-protein inwardly rectifying K+ channels." Smith K.E., Walker M.W., Artymyshyn R., Bard J., Borowsky B., Tamm J.A., Yao W.-J., Vaysse P.J.-J., Branchek T.A., Gerald C., Jones K.A. J. Biol. Chem. 273:23321-23326(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Homologue of the human galanin 2 receptor gene isolated from a human uterus cDNA library." Bennett M.M., Lescoe M.K., Gallipoli P.Z., Ramabhadran T.V. Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Uterus.
[3]	"Molecular characterization and expression of cloned human galanin receptors GALR2 and GALR3." Kolakowski L.F. Jr., O'Neill G.P., Howard A.D., Broussard S.R., Sullivan K.A., Feighner S.D., Sawzdargo M., Nguyen T., Kargman S., Shiao L.-L., Hreniuk D.L., Tan C.P., Evans J., Abramovitz M., Chateauneuf A., Coulombe N., Ng G., Johnson M.P. , Tharian A., Khoshbouei H., George S.R., Smith R.G., O'Dowd B.F. J. Neurochem. 71:2239-2251(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"Structural organization and chromosomal localization of three human galanin receptor genes." Iismaa T.P., Fathi Z., Hort Y.J., Iben L.G., Dutton J.L., Baker E., Sutherland G.R., Shine J. Ann. N. Y. Acad. Sci. 863:56-63(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"Isolation of cDNA coding for galanin receptor 3 (GALR3)." Eutsler E.P., Kopatz S.A., Sharma S.V. Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Retina.
[6]	"Genome-wide discovery and analysis of human seven transmembrane helix receptor genes." Suwa M., Sato T., Okouchi I., Arita M., Futami K., Matsumoto S., Tsutsumi S., Aburatani H., Asai K., Akiyama Y. Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[7]	"The DNA sequence of human chromosome 22." Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H. Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF073799 mRNA. Translation: AAC35944.1. AF067733 mRNA. Translation: AAC18860.1. AF129514, AF129513 Genomic DNA. Translation: AAD47348.2. AY587582 mRNA. Translation: AAS98215.1. AB065934 Genomic DNA. Translation: BAC06149.1. Z97630 Genomic DNA. Translation: CAB42831.1. CH471095 Genomic DNA. Translation: EAW60191.1.
IPI	IPI00031548.
RefSeq	NP_003605.1. NM_003614.1.
UniGene	Hs.158353.
3D structure databases
ProteinModelPortal	O60755.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000249041.
Protein family/group databases
GPCRDB	Search...
PTM databases
PhosphoSite	O60755.
Proteomic databases
PaxDb	O60755.
PRIDE	O60755.
Protocols and materials databases
DNASU	8484.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000249041; ENSP00000249041; ENSG00000128310.
GeneID	8484.
KEGG	hsa:8484.
UCSC	uc003aub.1. human.
Organism-specific databases
CTD	8484.
GeneCards	GC22P038219.
HGNC	HGNC:4134. GALR3.
MIM	603692. gene.
neXtProt	NX_O60755.
PharmGKB	PA28547.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG320953.
HOGENOM	HOG000230487.
HOVERGEN	HBG101447.
InParanoid	O60755.
KO	K04232.
OMA	HFLWAAV.
OrthoDB	EOG4K9BCJ.
PhylomeDB	O60755.
Enzyme and pathway databases
Reactome	REACT_111102. Signal Transduction.
Gene expression databases
Bgee	O60755.
CleanEx	HS_GALR3.
Genevestigator	O60755.
GermOnline	ENSG00000128310. Homo sapiens.
Family and domain databases
InterPro	IPR000405. Galanin_rcpt. IPR003908. Galnin_3_rcpt. IPR000276. GPCR_Rhodpsn. IPR017452. GPCR_Rhodpsn_7TM. [Graphical view]
Pfam	PF00001. 7tm_1. 1 hit. [Graphical view]
PRINTS	PR01420. GALANIN3R. PR00663. GALANINR. PR00237. GPCRRHODOPSN.
PROSITE	PS00237. G_PROTEIN_RECEP_F1_1. 1 hit. PS50262. G_PROTEIN_RECEP_F1_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	O60755.
ChEMBL	CHEMBL2731.
GenomeRNAi	8484.
NextBio	31747.
SOURCE	Search...

Entry information

Entry name

GALR3_HUMAN

Accession

Primary (citable) accession number: O60755
Secondary accession number(s): Q53YJ4

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	August 1, 1998
Last modified:	May 1, 2013
This is version 108 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.