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UniProtKB - P32249 (GP183_HUMAN)

Entry version 167 (10 Apr 2019)
Sequence version 3 (02 Sep 2008)
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Protein

G-protein coupled receptor 183

Gene

GPR183

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

G-protein coupled receptor expressed in lymphocytes that acts as a chemotactic receptor for B-cells, T-cells, splenic dendritic cells, monocytes/macrophages and astrocytes (By similarity). Receptor for oxysterol 7-alpha,25-dihydroxycholesterol (7-alpha,25-OHC) and other related oxysterols (PubMed:21796212, PubMed:22875855, PubMed:22930711). Mediates cell positioning and movement of a number of cells by binding the 7-alpha,25-OHC ligand that forms a chemotactic gradient (By similarity). Binding of 7-alpha,25-OHC mediates the correct localization of B-cells during humoral immune responses (By similarity). Guides B-cell movement along the B-cell zone-T-cell zone boundary and later to interfollicular and outer follicular regions (By similarity). Its specific expression during B-cell maturation helps position B-cells appropriately for mounting T-dependent antibody responses (By similarity). Collaborates with CXCR5 to mediate B-cell migration; probably by forming a heterodimer with CXCR5 that affects the interaction between of CXCL13 and CXCR5 (PubMed:22913878). Also acts as a chemotactic receptor for some T-cells upon binding to 7-alpha,25-OHC ligand (By similarity). Promotes follicular helper T (Tfh) cells differentiation by positioning activated T-cells at the follicle-T-zone interface, promoting contact of newly activated CD4 T-cells with activated dendritic cells and exposing them to Tfh-cell-promoting inducible costimulator (ICOS) ligand (By similarity). Expression in splenic dendritic cells is required for their homeostasis, localization and ability to induce B- and T-cell responses: GPR183 acts as a chemotactic receptor in dendritic cells that mediates the accumulation of CD4+ dendritic cells in bridging channels (By similarity). Regulates migration of astrocytes and is involved in communication between astrocytes and macrophages (PubMed:25297897). Promotes osteoclast precursor migration to bone surfaces (By similarity). Signals constitutively through G(i)-alpha, but not G(s)-alpha or G(q)-alpha (PubMed:21673108, PubMed:25297897). Signals constitutively also via MAPK1/3 (ERK1/2) (By similarity).By similarity7 Publications

Miscellaneous

GSK682753A (8-[(2E)-3-(4-chlorophenyl)prop-2-enoyl]-3-[(3,4-dichlorophenyl)methyl]-1-oxa-3,8-diazaspiro[4.5]decan-2-one), an inverse agonist, selectively inhibits the constitutive activity of GPR183 with high potency and efficacy (PubMed:21673108, PubMed:23772388). Specifically inhibited by NIBR189 ((2E)-3-(4-Bromophenyl)-1-[4-(4-methoxybenzoyl)-1-piperazinyl]-2-propene-1-one).2 Publications

Caution

It is uncertain whether Met-1 or Met-5 is the initiator.Curated

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei87Oxysterol agonist1 Publication1
Binding sitei112Oxysterol agonist1 Publication1
Binding sitei116Oxysterol agonist1 Publication1
Binding sitei260Oxysterol agonist1 Publication1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionG-protein coupled receptor, Receptor, Transducer
Biological processAdaptive immunity, Immunity

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-373076 Class A/1 (Rhodopsin-like receptors)
R-HSA-418594 G alpha (i) signalling events

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
G-protein coupled receptor 183Curated
Alternative name(s):
Epstein-Barr virus-induced G-protein coupled receptor 21 Publication
Short name:
EBI21 Publication
Short name:
EBV-induced G-protein coupled receptor 21 Publication
Short name:
hEBI21 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:GPR183Imported
Synonyms:EBI21 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 13

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		HostDB:ENSG00000169508.6

Human Gene Nomenclature Database

More...HGNCi		HGNC:3128 GPR183

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		605741 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P32249

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 31ExtracellularSequence analysisAdd BLAST31
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei32 – 57Helical; Name=1Sequence analysisAdd BLAST26
Topological domaini58 – 77CytoplasmicSequence analysisAdd BLAST20
Transmembranei78 – 95Helical; Name=2Sequence analysisAdd BLAST18
Topological domaini96 – 105ExtracellularSequence analysis10
Transmembranei106 – 127Helical; Name=3Sequence analysisAdd BLAST22
Topological domaini128 – 149CytoplasmicSequence analysisAdd BLAST22
Transmembranei150 – 168Helical; Name=4Sequence analysisAdd BLAST19
Topological domaini169 – 192ExtracellularSequence analysisAdd BLAST24
Transmembranei193 – 215Helical; Name=5Sequence analysisAdd BLAST23
Topological domaini216 – 241CytoplasmicSequence analysisAdd BLAST26
Transmembranei242 – 265Helical; Name=6Sequence analysisAdd BLAST24
Topological domaini266 – 287ExtracellularSequence analysisAdd BLAST22
Transmembranei288 – 312Helical; Name=7Sequence analysisAdd BLAST25
Topological domaini313 – 361CytoplasmicSequence analysisAdd BLAST49

Keywords - Cellular componenti

Cell membrane, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi21C → A: Strongly reduced localization to the cell membrane and reduced protein expression levels. 1 Publication1
Mutagenesisi77D → A: Loss of receptor activation without affecting oxysterol agonist-binding. 2 Publications1
Mutagenesisi77D → R: Strong decrease in oxysterol agonist-binding and receptor activation. 1 Publication1
Mutagenesisi85P → A: Strongly reduced localization to the cell membrane. 1 Publication1
Mutagenesisi87R → A: Strong decrease in oxysterol agonist-binding and receptor activation. 3 Publications1
Mutagenesisi87R → K: Slight decrease in oxysterol agonist-binding and receptor activation. 2 Publications1
Mutagenesisi87R → W: Slight decrease in oxysterol agonist-binding and receptor activation. 1 Publication1
Mutagenesisi90Y → A: 10-fold reduction in receptor activation. Strongly reduced localization to the cell membrane. 2 Publications1
Mutagenesisi104C → A: Abolishes localization to the cell membrane without affecting protein expression levels. 1 Publication1
Mutagenesisi111F → A or Y: 500-fold decrease of IC(50) for GSK682753A. No effect on oxysterol agonist-binding and receptor activation. 2 Publications1
Mutagenesisi112Y → A or F: Strong decrease in oxysterol agonist-binding and receptor activation. 2 Publications1
Mutagenesisi114N → A: Strongly reduced localization to the cell membrane. 1 Publication1
Mutagenesisi115T → A or F: No effect. 1 Publication1
Mutagenesisi116Y → A or F: Strong decrease in oxysterol agonist-binding and receptor activation. 2 Publications1
Mutagenesisi181C → A: Abolishes localization to the cell membrane without affecting protein expression levels. 1 Publication1
Mutagenesisi183E → A: Strong reduction in ligand potency. 1 Publication1
Mutagenesisi197L → A: Reduced localization to the cell membrane and reduced receptor function. 1 Publication1
Mutagenesisi205Y → A or F: No effect. 1 Publication1
Mutagenesisi256C → A: Increased receptor activation. 1 Publication1
Mutagenesisi257F → A: Increased receptor activation. Strongly reduced localization to the cell membrane. 2 Publications1
Mutagenesisi260Y → A or F: Strong decrease in oxysterol agonist-binding and receptor activation. 2 Publications1
Mutagenesisi261H → A: Reduced localization to the cell membrane and reduced receptor function. 1 Publication1
Mutagenesisi264I → A: Reduced localization to the cell membrane and reduced receptor function. 1 Publication1
Mutagenesisi280C → A: Strongly reduced localization to the cell membrane and reduced protein expression levels. 1 Publication1
Mutagenesisi287Q → A: 10-fold reduction in receptor activation. 1 Publication1
Mutagenesisi291H → A: 10-fold reduction in receptor activation. 1 Publication1
Mutagenesisi291H → A: Reduced localization to the cell membrane and reduced receptor function. 1 Publication1
Mutagenesisi294V → A: Reduced localization to the cell membrane and reduced receptor function. 1 Publication1
Mutagenesisi297M → A: Reduced localization to the cell membrane and reduced receptor function, without affecting oxysterol agonist-binding. 1 Publication1
Mutagenesisi297M → I: Reduced localization to the cell membrane and reduced receptor function. Reduced oxysterol agonist-binding. 1 Publication1

Organism-specific databases

DisGeNET

More...DisGeNETi		1880

Open Targets

More...OpenTargetsi		ENSG00000169508

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA162390174

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL3259470

IUPHAR/BPS Guide to PHARMACOLOGY

More...GuidetoPHARMACOLOGYi		81

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		GPR183

Domain mapping of disease mutations (DMDM)

More...DMDMi		205371788

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000694111 – 361G-protein coupled receptor 183Add BLAST361

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi104 ↔ 181PROSITE-ProRule annotation
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei328PhosphoserineBy similarity1

Keywords - PTMi

Disulfide bond, Phosphoprotein

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P32249

MaxQB - The MaxQuant DataBase

More...MaxQBi		P32249

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P32249

PeptideAtlas

More...PeptideAtlasi		P32249

PRoteomics IDEntifications database

More...PRIDEi		P32249

ProteomicsDB human proteome resource

More...ProteomicsDBi		54857

PTM databases

CarbonylDB database of protein carbonylation sites

More...CarbonylDBi		P32249

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P32249

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		P32249

SwissPalm database of S-palmitoylation events

More...SwissPalmi		P32249

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed abundantly in lymphoid tissues such as spleen and lymph node, and in B- and T-lymphocytes (PubMed:16540462, PubMed:8383238). Also highly expressed in lung, heart and gastrointestinal tract, and weakly expressed in the urogenital system and brain (PubMed:16540462, PubMed:8383238). Expressed in astrocytes (PubMed:25297897).3 Publications

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Induced following Epstein-Barr virus (EBV) infection (PubMed:8383238).1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000169508 Expressed in 190 organ(s), highest expression level in vermiform appendix

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P32249 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P32249 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		CAB033690
HPA028847

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer and heterodimer (PubMed:22913878). Heterodimerizes with CXCR5; leading to modulate the interaction between of CXCL13 and CXCR5 (PubMed:22913878).1 Publication

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		108212, 36 interactors

Protein interaction database and analysis system

More...IntActi		P32249, 2 interactors

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000365596

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P32249

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		P32249

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni126 – 134Interaction with G proteins9

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the G-protein coupled receptor 1 family.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		ENOG410IEQQ Eukaryota
ENOG4110QC8 LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00950000182719

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000043070

The HOVERGEN Database of Homologous Vertebrate Genes

More...HOVERGENi		HBG101355

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P32249

KEGG Orthology (KO)

More...KOi		K04305

Identification of Orthologs from Complete Genome Data

More...OMAi		TTCMEYP

Database of Orthologous Groups

More...OrthoDBi		760173at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P32249

TreeFam database of animal gene trees

More...TreeFami		TF350009

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR000276 GPCR_Rhodpsn
IPR017452 GPCR_Rhodpsn_7TM

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00001 7tm_1, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00237 GPCRRHODOPSN

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM01381 7TM_GPCR_Srsx, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00237 G_PROTEIN_RECEP_F1_1, 1 hit
PS50262 G_PROTEIN_RECEP_F1_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

P32249-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MDIQMANNFT PPSATPQGND CDLYAHHSTA RIVMPLHYSL VFIIGLVGNL 
        60         70         80         90        100
LALVVIVQNR KKINSTTLYS TNLVISDILF TTALPTRIAY YAMGFDWRIG 
       110        120        130        140        150
DALCRITALV FYINTYAGVN FMTCLSIDRF IAVVHPLRYN KIKRIEHAKG 
       160        170        180        190        200
VCIFVWILVF AQTLPLLINP MSKQEAERIT CMEYPNFEET KSLPWILLGA 
       210        220        230        240        250
CFIGYVLPLI IILICYSQIC CKLFRTAKQN PLTEKSGVNK KALNTIILII 
       260        270        280        290        300
VVFVLCFTPY HVAIIQHMIK KLRFSNFLEC SQRHSFQISL HFTVCLMNFN 
       310        320        330        340        350
CCMDPFIYFF ACKGYKRKVM RMLKRQVSVS ISSAVKSAPE ENSREMTETQ 
       360 
MMIHSKSSNG K
Length:361
Mass (Da):41,224
Last modified:September 2, 2008 - v3
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iB5A2171F34C9C67B
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti6A → V in BAD97110 (Ref. 3) Curated1
Sequence conflicti179I → N in BAG36232 (PubMed:14702039).Curated1
Sequence conflicti325R → Q in BAG36232 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_054147338A → V in an acute myeloid leukemia sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs1466524306Ensembl.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
L08177 mRNA Translation: AAA35924.1
AK292091 mRNA Translation: BAF84780.1
AK313443 mRNA Translation: BAG36232.1
AK223390 mRNA Translation: BAD97110.1
AL160155 Genomic DNA No translation available.
CH471085 Genomic DNA Translation: EAX09018.1
BC020752 mRNA Translation: AAH20752.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS9492.1

Protein sequence database of the Protein Information Resource

More...PIRi		B45680

NCBI Reference Sequences

More...RefSeqi		NP_004942.1, NM_004951.4
XP_016875894.1, XM_017020405.1

UniGene gene-oriented nucleotide sequence clusters

More...UniGenei		Hs.784

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000376414; ENSP00000365596; ENSG00000169508

Database of genes from NCBI RefSeq genomes

More...GeneIDi		1880

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:1880

UCSC genome browser

More...UCSCi		uc001vog.4 human

Keywords - Coding sequence diversityi

Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L08177 mRNA Translation: AAA35924.1
AK292091 mRNA Translation: BAF84780.1
AK313443 mRNA Translation: BAG36232.1
AK223390 mRNA Translation: BAD97110.1
AL160155 Genomic DNA No translation available.
CH471085 Genomic DNA Translation: EAX09018.1
BC020752 mRNA Translation: AAH20752.1
CCDSiCCDS9492.1
PIRiB45680
RefSeqiNP_004942.1, NM_004951.4
XP_016875894.1, XM_017020405.1
UniGeneiHs.784

3D structure databases

ProteinModelPortaliP32249
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108212, 36 interactors
IntActiP32249, 2 interactors
STRINGi9606.ENSP00000365596

Chemistry databases

BindingDBiP32249
ChEMBLiCHEMBL3259470
GuidetoPHARMACOLOGYi81

Protein family/group databases

Information system for G protein-coupled receptors (GPCRs)

More...GPCRDBi		Search...

PTM databases

CarbonylDBiP32249
iPTMnetiP32249
PhosphoSitePlusiP32249
SwissPalmiP32249

Polymorphism and mutation databases

BioMutaiGPR183
DMDMi205371788

Proteomic databases

jPOSTiP32249
MaxQBiP32249
PaxDbiP32249
PeptideAtlasiP32249
PRIDEiP32249
ProteomicsDBi54857

Protocols and materials databases

The DNASU plasmid repository

More...DNASUi		1880
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000376414; ENSP00000365596; ENSG00000169508
GeneIDi1880
KEGGihsa:1880
UCSCiuc001vog.4 human

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		1880
DisGeNETi1880
EuPathDBiHostDB:ENSG00000169508.6

GeneCards: human genes, protein and diseases

More...GeneCardsi		GPR183
HGNCiHGNC:3128 GPR183
HPAiCAB033690
HPA028847
MIMi605741 gene
neXtProtiNX_P32249
OpenTargetsiENSG00000169508
PharmGKBiPA162390174

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiENOG410IEQQ Eukaryota
ENOG4110QC8 LUCA
GeneTreeiENSGT00950000182719
HOGENOMiHOG000043070
HOVERGENiHBG101355
InParanoidiP32249
KOiK04305
OMAiTTCMEYP
OrthoDBi760173at2759
PhylomeDBiP32249
TreeFamiTF350009

Enzyme and pathway databases

ReactomeiR-HSA-373076 Class A/1 (Rhodopsin-like receptors)
R-HSA-418594 G alpha (i) signalling events

Miscellaneous databases

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		GPR183

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		1880

Protein Ontology

More...PROi		PR:P32249

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000169508 Expressed in 190 organ(s), highest expression level in vermiform appendix
ExpressionAtlasiP32249 baseline and differential
GenevisibleiP32249 HS

Family and domain databases

InterProiView protein in InterPro
IPR000276 GPCR_Rhodpsn
IPR017452 GPCR_Rhodpsn_7TM
PfamiView protein in Pfam
PF00001 7tm_1, 1 hit
PRINTSiPR00237 GPCRRHODOPSN
SMARTiView protein in SMART
SM01381 7TM_GPCR_Srsx, 1 hit
PROSITEiView protein in PROSITE
PS00237 G_PROTEIN_RECEP_F1_1, 1 hit
PS50262 G_PROTEIN_RECEP_F1_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiGP183_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P32249
Secondary accession number(s): B2R8N5, Q53F99, Q5JUH7
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: September 2, 2008
Last modified: April 10, 2019
This is version 167 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Human chromosome 13
    Human chromosome 13: entries, gene names and cross-references to MIM
  6. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
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