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Entry version 88 (16 Oct 2019)
Sequence version 3 (10 May 2017)
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Protein

Extracellular calcium-sensing receptor

Gene

CASR

Organism
Sus scrofa (Pig)
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 transcript 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 that senses changes in the extracellular concentration of calcium ions and plays a key role in maintaining calcium homeostasis. Senses fluctuations in the circulating calcium concentration and modulates the production of parathyroid hormone (PTH) in parathyroid glands (By similarity). The activity of this receptor is mediated by a G-protein that activates a phosphatidylinositol-calcium second messenger system. The G-protein-coupled receptor activity is activated by a co-agonist mechanism: aromatic amino acids, such as Trp or Phe, act concertedly with divalent cations, such as calcium or magnesium, to achieve full receptor activation (By similarity).By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

In resting state, adopts an open conformation, anion-binding promoting the inactive configuration (By similarity). Upon aromatic amino acid-binding, the groove in the extracellular venus flytrap module is closed, thereby inducing the formation of a novel homodimer interface between subunits (By similarity). Calcium ions stabilize the active state by enhancing homodimer interactions between membrane-proximal domains to fully activate the receptor (By similarity). In contrast to human protein, not activated by AMG 416, a D-amino acid-containing peptide agonist: this is probably due to the absence of a Cys residue at position 482, which forms a disulfide bond with the AMG 416 peptide agonist in human and that is replaced by a Tyr residue in pig (PubMed:26290606).By similarity1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi81Calcium; via carbonyl oxygenBy similarity1
Metal bindingi84CalciumBy similarity1
Metal bindingi87Calcium; via carbonyl oxygenBy similarity1
Metal bindingi88Calcium; via carbonyl oxygenBy similarity1
Metal bindingi100CalciumBy similarity1
Metal bindingi145CalciumBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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 sitei147Aromatic amino acidBy similarity1
Binding sitei168Aromatic amino acid; via carbonyl oxygenBy similarity1
Binding sitei170Aromatic amino acidBy similarity1
Metal bindingi231CalciumBy similarity1
Metal bindingi234CalciumBy similarity1
Binding sitei297Aromatic amino acidBy similarity1
Metal bindingi557Calcium; via carbonyl oxygenBy similarity1

<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

GO - Biological processi

<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
LigandCalcium, Metal-binding

<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:
Extracellular calcium-sensing receptor
Short name:
CaSR
Alternative name(s):
Parathyroid cell calcium-sensing receptor
Short name:
PCaR1
<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:CASR
Synonyms:PCAR1
<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>OrganismiSus scrofa (Pig)
<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 identifieri9823 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
<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
  • UP000008227 <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

<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 domaini20 – 612ExtracellularCuratedAdd BLAST593
<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>Transmembranei613 – 635Helical; Name=1Sequence analysisAdd BLAST23
Topological domaini636 – 649CytoplasmicCuratedAdd BLAST14
Transmembranei650 – 670Helical; Name=2Sequence analysisAdd BLAST21
Topological domaini671 – 681ExtracellularCuratedAdd BLAST11
Transmembranei682 – 700Helical; Name=3Sequence analysisAdd BLAST19
Topological domaini701 – 724CytoplasmicCuratedAdd BLAST24
Transmembranei725 – 745Helical; Name=4Sequence analysisAdd BLAST21
Topological domaini746 – 769ExtracellularCuratedAdd BLAST24
Transmembranei770 – 792Helical; Name=5Sequence analysisAdd BLAST23
Topological domaini793 – 805CytoplasmicCuratedAdd BLAST13
Transmembranei806 – 828Helical; Name=6Sequence analysisAdd BLAST23
Topological domaini829 – 836ExtracellularCurated8
Transmembranei837 – 862Helical; Name=7Sequence analysisAdd BLAST26
Topological domaini863 – 1079CytoplasmicCuratedAdd BLAST217

Keywords - Cellular componenti

Cell membrane, Membrane

<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 denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 19Sequence analysisAdd BLAST19
<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_000020689420 – 1079Extracellular calcium-sensing receptorAdd BLAST1060

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 bondi60 ↔ 101By similarity
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi90N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Disulfide bondi129InterchainBy similarity
Glycosylationi130N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Disulfide bondi131InterchainBy similarity
Disulfide bondi236 ↔ 561By similarity
Glycosylationi261N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi287N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi358 ↔ 395By similarity
Glycosylationi386N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi400N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi437 ↔ 449By similarity
Glycosylationi446N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi468N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi488N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi541N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Disulfide bondi542 ↔ 562By similarity
Disulfide bondi546 ↔ 565By similarity
Disulfide bondi568 ↔ 582By similarity
Disulfide bondi585 ↔ 598By similarity
Glycosylationi594N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
<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 residuei920PhosphoserineBy similarity1
Modified residuei1062PhosphoserineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

N-glycosylated.By similarity
Ubiquitinated by RNF19A; which induces proteasomal degradation.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
O62714

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSSSCG00000011878 Expressed in 1 organ(s), highest expression level in adult mammalian kidney

<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; disulfide-linked.

Interacts with VCP and RNF19A (By similarity).

Interacts with ARRB1 (By similarity).

By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
9823.ENSSSCP00000012651

<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

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
O62714

Database of comparative protein structure models

More...
ModBasei
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>Regioni22 – 188Ligand-binding 1 (LB1)By similarityAdd BLAST167
Regioni66 – 70Anion bindingBy similarity5
Regioni189 – 324Ligand-binding 2 (LB2)By similarityAdd BLAST136
Regioni415 – 417Anion bindingBy similarity3
Regioni542 – 612Cysteine-rich (CR)By similarityAdd BLAST71
Regioni880 – 900Interaction with RNF19ABy similarityAdd BLAST21

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The extracellular regions of the homodimer interact in a side-by-side fashion while facing opposite directions. Each extracellular region consists of three domains, LB1 (ligand-binding 1), LB2 and CR (cysteine-rich). The two lobe-shaped domains LB1 and LB2 form a venus flytrap module. In the inactive configuration, the venus flytrap modules of both protomers are in the open conformation associated with the resting state (open-open) and the interdomain cleft is empty. In addition, each protomer contains three anions, which reinforce the inactive conformation, and one calcium ion. In the active configuration, both protomers of extracellular regions have the closed conformation associated with agonist-binding (closed-closed). The ligand-binding cleft of each protomer is solely occupied by an aromatic amino-acid. Calcium is bound at four novel sites, including one at the homodimer interface. Agonist-binding induces large conformational changes within the extracellular region homodimer: first, the venus flytrap module of each protomer undergoes domain closure. Second, the LB2 regions of the two protomers approach each other, resulting in an expansion of the homodimer interactions involving LB2 domains. Third, the CR regions of the two subunits interact to form a large homodimer interface that is unique to the active state. The CR regions are brought into close contact by the motion involving LB2 since the two domains are rigidly associated within each subunit.By similarity

<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

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1056 Eukaryota
ENOG410XR6W LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000157596

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
O62714

Identification of Orthologs from Complete Genome Data

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OMAi
PLPMDTF

Database of Orthologous Groups

More...
OrthoDBi
327938at2759

TreeFam database of animal gene trees

More...
TreeFami
TF331269

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.10.50.30, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001828 ANF_lig-bd_rcpt
IPR000337 GPCR_3
IPR011500 GPCR_3_9-Cys_dom
IPR038550 GPCR_3_9-Cys_sf
IPR017978 GPCR_3_C
IPR000068 GPCR_3_Ca_sens_rcpt-rel
IPR017979 GPCR_3_CS
IPR028082 Peripla_BP_I

The PANTHER Classification System

More...
PANTHERi
PTHR24061 PTHR24061, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00003 7tm_3, 1 hit
PF01094 ANF_receptor, 1 hit
PF07562 NCD3G, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00592 CASENSINGR
PR00248 GPCRMGR

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF53822 SSF53822, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00979 G_PROTEIN_RECEP_F3_1, 1 hit
PS00980 G_PROTEIN_RECEP_F3_2, 1 hit
PS00981 G_PROTEIN_RECEP_F3_3, 1 hit
PS50259 G_PROTEIN_RECEP_F3_4, 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>. The information is filed in different subsections. The current subsections and their content are listed below:<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.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

O62714-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAFSSCCWIL LALTWCTSAY GPDQRAQKKG DIILGGLFPI HFGVAAKDQN
60 70 80 90 100
LESRPESVEC IRYNFRGFRW LQAMIFAIEE INSSPALLPN MTLGYRIFDT
110 120 130 140 150
CNTVSKALEA TLSFVAQNKI DSLNLDEFCN CSEHIPSTIA VVGATGSGIS
160 170 180 190 200
TAVANLLGLF YIPQVSYASS SRLLSNKNQF KSFLRTIPND EHQATAMADI
210 220 230 240 250
IEYFRWNWVG TIAADDDYGR PGIEKFREEA EERDICIDFS ELISQYSDEE
260 270 280 290 300
EIQQVVEVIQ NSTAKVIVVF SSGPDLEPLI KEIVRRNITG KIWLASEAWA
310 320 330 340 350
SSSLIAMPEY FHVVGGTIGF ALKAGQIPGF REFLQKVHPS KSVHNGFAKE
360 370 380 390 400
FWEETFNCHL QEGAKGPLTT DTFLRGHEEG GGRISNSSTA FRPLCTGDEN
410 420 430 440 450
ISSVETPYMD YTHLRISYNV YLAVYSIAHA LQDIYTCIPG RGLFTNGSCA
460 470 480 490 500
DIKKVEAWQV LKHLRHLNFT SNMGEQVTFD EYGDLAGNYS IINWHLSPED
510 520 530 540 550
GSIVFKEVGY YNVYAKKGER LFINEEKILW SGFSREVPFS NCSRDCLAGT
560 570 580 590 600
RKGIIEGEPT CCFECVECPD GEYSDETDAS ACDKCPDDFW SNENHTSCIA
610 620 630 640 650
KEIEFLSWTE PFGIALTLFA VLGIFLTAFV LGVFIKFRNT PIVKATNREL
660 670 680 690 700
SYLLLFSLLC CFSSSLFFIG EPQDWTCRLR QPAFGISFVL CISCILVKTN
710 720 730 740 750
RVLLVFEAKI PTSFHRKWWG LNLQFLLVFL CTFMQIVICA IWLYTAPPSS
760 770 780 790 800
YRNHELEDEI IFITCHEGSL MALGFLIGYT CLLAAICFFF AFKSRKLPEN
810 820 830 840 850
FNEAKFITFS MLIFFIVWIS FIPAYASTYG KFVSAVEVIA ILAASFGLLA
860 870 880 890 900
CIFFNKVYII LFKPSRNTIE EVRCSTAAHA FKVAARATLR RSNVSRQRSS
910 920 930 940 950
SLGGSTGSTP SSSISSKSNS EDPFPQPERQ KKQQPLALTQ HVPQPQAPST
960 970 980 990 1000
PQPQPQLQQQ PRCKQKVIFG SGTVTFSLSF DEPQKSATAH RNSTHQNSLE
1010 1020 1030 1040 1050
AQKNNDALTR HQALLPLQCG EADAELTAQE TGLQGSVGGD HHPEMEDPEE
1060 1070
MSPALVMSNS RSFVISGGGS TVTENMLHS
Length:1,079
Mass (Da):120,361
Last modified:May 10, 2017 - 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:iD018DB2983E0FCCA
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 conflicti633V → A in AAC15660 (PubMed:10449918).Curated1
Sequence conflicti633V → A in AAC15661 (PubMed:10449918).Curated1
Sequence conflicti633V → A in AAC15662 (PubMed:10449918).Curated1
Sequence conflicti981D → H in AAC15660 (PubMed:10449918).Curated1
Sequence conflicti981D → H in AAC15661 (PubMed:10449918).Curated1
Sequence conflicti981D → H in AAC15662 (PubMed:10449918).Curated1
Sequence conflicti986 – 988SAT → NAM in AAC15660 (PubMed:10449918).Curated3
Sequence conflicti986 – 988SAT → NAM in AAC15661 (PubMed:10449918).Curated3
Sequence conflicti986 – 988SAT → NAM in AAC15662 (PubMed:10449918).Curated3

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
KT309043 mRNA Translation: ALB08481.1
CU694886 Genomic DNA No translation available.
AF041025 Genomic DNA Translation: AAC15660.1
AF041026 Genomic DNA Translation: AAC15661.1
AF041027 Genomic DNA Translation: AAC15662.1

NCBI Reference Sequences

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RefSeqi
XP_005654095.1, XM_005654038.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSSSCT00000012993; ENSSSCP00000012651; ENSSSCG00000011878
ENSSSCT00000064997; ENSSSCP00000041077; ENSSSCG00000011878

Database of genes from NCBI RefSeq genomes

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GeneIDi
100520980

<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
KT309043 mRNA Translation: ALB08481.1
CU694886 Genomic DNA No translation available.
AF041025 Genomic DNA Translation: AAC15660.1
AF041026 Genomic DNA Translation: AAC15661.1
AF041027 Genomic DNA Translation: AAC15662.1
RefSeqiXP_005654095.1, XM_005654038.2

3D structure databases

SMRiO62714
ModBaseiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000012651

Protein family/group databases

Information system for G protein-coupled receptors (GPCRs)

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GPCRDBi
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Proteomic databases

PRIDEiO62714

Genome annotation databases

EnsembliENSSSCT00000012993; ENSSSCP00000012651; ENSSSCG00000011878
ENSSSCT00000064997; ENSSSCP00000041077; ENSSSCG00000011878
GeneIDi100520980

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
846

Phylogenomic databases

eggNOGiKOG1056 Eukaryota
ENOG410XR6W LUCA
GeneTreeiENSGT00940000157596
InParanoidiO62714
OMAiPLPMDTF
OrthoDBi327938at2759
TreeFamiTF331269

Gene expression databases

BgeeiENSSSCG00000011878 Expressed in 1 organ(s), highest expression level in adult mammalian kidney

Family and domain databases

Gene3Di2.10.50.30, 1 hit
InterProiView protein in InterPro
IPR001828 ANF_lig-bd_rcpt
IPR000337 GPCR_3
IPR011500 GPCR_3_9-Cys_dom
IPR038550 GPCR_3_9-Cys_sf
IPR017978 GPCR_3_C
IPR000068 GPCR_3_Ca_sens_rcpt-rel
IPR017979 GPCR_3_CS
IPR028082 Peripla_BP_I
PANTHERiPTHR24061 PTHR24061, 1 hit
PfamiView protein in Pfam
PF00003 7tm_3, 1 hit
PF01094 ANF_receptor, 1 hit
PF07562 NCD3G, 1 hit
PRINTSiPR00592 CASENSINGR
PR00248 GPCRMGR
SUPFAMiSSF53822 SSF53822, 1 hit
PROSITEiView protein in PROSITE
PS00979 G_PROTEIN_RECEP_F3_1, 1 hit
PS00980 G_PROTEIN_RECEP_F3_2, 1 hit
PS00981 G_PROTEIN_RECEP_F3_3, 1 hit
PS50259 G_PROTEIN_RECEP_F3_4, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<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 nameiCASR_PIG
<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: O62714
Secondary accession number(s): F1SQ21, O62715, O62716
<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 11, 2004
Last sequence update: May 10, 2017
Last modified: October 16, 2019
This is version 88 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

<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
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