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Entry version 124 (05 Jun 2019)
Sequence version 1 (01 Jun 1994)
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Protein

Extracellular calcium-sensing receptor

Gene

CASR

Organism
Bos taurus (Bovine)
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 (PubMed:8255296). 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 (PubMed:8255296). 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 similarity1 Publication

<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. 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. Calcium ions stabilize the active state by enhancing homodimer interactions between membrane-proximal domains to fully activate the receptor.By similarity

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 bindingi82Calcium; via carbonyl oxygenBy similarity1
Metal bindingi85CalciumBy similarity1
Metal bindingi88Calcium; via carbonyl oxygenBy similarity1
Metal bindingi89Calcium; via carbonyl oxygenBy similarity1
Metal bindingi101CalciumBy similarity1
Metal bindingi146CalciumBy 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 sitei148Aromatic amino acidBy similarity1
Binding sitei169Aromatic amino acid; via carbonyl oxygenBy similarity1
Binding sitei171Aromatic amino acidBy similarity1
Metal bindingi232CalciumBy similarity1
Metal bindingi235CalciumBy similarity1
Binding sitei298Aromatic amino acidBy similarity1
Metal bindingi558Calcium; 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 receptor1 Publication
Short name:
BoPCaR11 Publication
Short name:
PCaR11 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:CASR
Synonyms:GPRC2A, PCAR11 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>OrganismiBos taurus (Bovine)
<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 identifieri9913 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
<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
  • UP000009136 <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 1

Organism-specific databases

Vertebrate Gene Nomenclature Database

More...
VGNCi
VGNC:26788 CASR

<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 – 613ExtracellularSequence analysisAdd BLAST594
<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>Transmembranei614 – 636Helical; Name=1Sequence analysisAdd BLAST23
Topological domaini637 – 650CytoplasmicSequence analysisAdd BLAST14
Transmembranei651 – 671Helical; Name=2Sequence analysisAdd BLAST21
Topological domaini672 – 682ExtracellularSequence analysisAdd BLAST11
Transmembranei683 – 701Helical; Name=3Sequence analysisAdd BLAST19
Topological domaini702 – 725CytoplasmicSequence analysisAdd BLAST24
Transmembranei726 – 746Helical; Name=4Sequence analysisAdd BLAST21
Topological domaini747 – 770ExtracellularSequence analysisAdd BLAST24
Transmembranei771 – 793Helical; Name=5Sequence analysisAdd BLAST23
Topological domaini794 – 806CytoplasmicSequence analysisAdd BLAST13
Transmembranei807 – 829Helical; Name=6Sequence analysisAdd BLAST23
Topological domaini830 – 837ExtracellularSequence analysis8
Transmembranei838 – 863Helical; Name=7Sequence analysisAdd BLAST26
Topological domaini864 – 1085CytoplasmicSequence analysisAdd BLAST222

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

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL1075316

<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_000001294520 – 1085Extracellular calcium-sensing receptorAdd BLAST1066

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 bondi61 ↔ 102By 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>Glycosylationi91N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi130InterchainBy similarity
Glycosylationi131N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi132InterchainBy similarity
Disulfide bondi237 ↔ 562By similarity
Glycosylationi262N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi288N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi359 ↔ 396By similarity
Glycosylationi401N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi438 ↔ 450By similarity
Glycosylationi447N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi469N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi489N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi542N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi543 ↔ 563By similarity
Disulfide bondi547 ↔ 566By similarity
Disulfide bondi569 ↔ 583By similarity
Disulfide bondi586 ↔ 599By similarity
Glycosylationi595N-linked (GlcNAc...) asparagineSequence analysis1
<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 residuei921PhosphoserineBy similarity1
Modified residuei1068PhosphoserineBy 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

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

More...
PaxDbi
P35384

PRoteomics IDEntifications database

More...
PRIDEi
P35384

<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
9913.ENSBTAP00000005042

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P35384

<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
P35384

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>Regioni23 – 189Ligand-binding 1 (LB1)By similarityAdd BLAST167
Regioni67 – 71Anion bindingBy similarity5
Regioni190 – 325Ligand-binding 2 (LB2)By similarityAdd BLAST136
Regioni416 – 418Anion bindingBy similarity3
Regioni543 – 613Cysteine-rich (CR)By similarityAdd BLAST71
Regioni881 – 901Interaction 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

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000232092

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P35384

KEGG Orthology (KO)

More...
KOi
K04612

Database of Orthologous Groups

More...
OrthoDBi
327938at2759

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>Sequence (1+)i

<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.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

P35384-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MALYSCCWIL LAFSTWCTSA YGPDQRAQKK GDIILGGLFP IHFGVAVKDQ
60 70 80 90 100
DLKSRPESVE CIRYNFRGFR WLQAMIFAIE EINSSPALLP NMTLGYRIFD
110 120 130 140 150
TCNTVSKALE ATLSFVAQNK IDSLNLDEFC NCSEHIPSTI AVVGATGSGI
160 170 180 190 200
STAVANLLGL FYIPQVSYAS SSRLLSNKNQ FKSFLRTIPN DEHQATAMAD
210 220 230 240 250
IIEYFRWNWV GTIAADDDYG RPGIEKFREE AEERDICIDF SELISQYSDE
260 270 280 290 300
EKIQQVVEVI QNSTAKVIVV FSSGPDLEPL IKEIVRRNIT GRIWLASEAW
310 320 330 340 350
ASSSLIAMPE YFHVVGGTIG FGLKAGQIPG FREFLQKVHP RKSVHNGFAK
360 370 380 390 400
EFWEETFNCH LQEGAKGPLP VDTFLRGHEE GGARLSNSPT AFRPLCTGEE
410 420 430 440 450
NISSVETPYM DYTHLRISYN VYLAVYSIAH ALQDIYTCIP GRGLFTNGSC
460 470 480 490 500
ADIKKVEAWQ VLKHLRHLNF TSNMGEQVTF DECGDLAGNY SIINWHLSPE
510 520 530 540 550
DGSIVFKEVG YYNVYAKKGE RLFINDEKIL WSGFSREVPF SNCSRDCLAG
560 570 580 590 600
TRKGIIEGEP TCCFECVECP DGEYSDETDA SACDKCPDDF WSNENHTSCI
610 620 630 640 650
AKEIEFLSWT EPFGIALTLF AVLGIFLTAF VLGVFIKFRN TPIVKATNRE
660 670 680 690 700
LSYLLLFSLL CCFSSSLFFI GEPQDWTCRL RQPAFGISFV LCISCILVKT
710 720 730 740 750
NRVLLVFEAK IPTSFHRKWW GLNLQFLLVF LCTFMQIVIC AIWLNTAPPS
760 770 780 790 800
SYRNHELEDE IIFITCHEGS LMALGFLIGY TCLLAAICFF FAFKSRKLPE
810 820 830 840 850
NFNEAKFITF SMLIFFIVWI SFIPAYASTY GKFVSAVEVI AILAASFGLL
860 870 880 890 900
ACIFFNKVYI ILFKPSRNTI EEVRCSTAAH AFKVAARATL RRSNVSRQRS
910 920 930 940 950
SSLGGSTGST PSSSISSKSN SEDPFPQQQP KRQKQPQPLA LSPHNAQQPQ
960 970 980 990 1000
PRPPSTPQPQ PQSQQPPRCK QKVIFGSGTV TFSLSFDEPQ KTAVAHRNST
1010 1020 1030 1040 1050
HQTSLEAQKN NDALTKHQAL LPLQCGETDS ELTSQETGLQ GPVGEDHQLE
1060 1070 1080
MEDPEEMSPA LVVSNSRSFV ISGGGSTVTE NMLRS
Length:1,085
Mass (Da):121,171
Last modified:June 1, 1994 - v1
<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:i5D66DE8C9CD13E47
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
F1MDM1F1MDM1_BOVIN
Extracellular calcium-sensing recep...
CASR
1,085Annotation score:

Annotation score:2 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>

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
S67307 mRNA Translation: AAB29171.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S40476

NCBI Reference Sequences

More...
RefSeqi
NP_776427.1, NM_174002.3
XP_005201442.1, XM_005201385.3
XP_010799466.1, XM_010801164.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSBTAT00000005042; ENSBTAP00000005042; ENSBTAG00000003865
ENSBTAT00000084319; ENSBTAP00000059078; ENSBTAG00000003865

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
281038

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
bta:281038

<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
S67307 mRNA Translation: AAB29171.1
PIRiS40476
RefSeqiNP_776427.1, NM_174002.3
XP_005201442.1, XM_005201385.3
XP_010799466.1, XM_010801164.2

3D structure databases

SMRiP35384
ModBaseiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000005042

Chemistry databases

BindingDBiP35384
ChEMBLiCHEMBL1075316

Protein family/group databases

Information system for G protein-coupled receptors (GPCRs)

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GPCRDBi
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Proteomic databases

PaxDbiP35384
PRIDEiP35384

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000005042; ENSBTAP00000005042; ENSBTAG00000003865
ENSBTAT00000084319; ENSBTAP00000059078; ENSBTAG00000003865
GeneIDi281038
KEGGibta:281038

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
846
VGNCiVGNC:26788 CASR

Phylogenomic databases

eggNOGiKOG1056 Eukaryota
ENOG410XR6W LUCA
GeneTreeiENSGT00940000157596
HOGENOMiHOG000232092
InParanoidiP35384
KOiK04612
OrthoDBi327938at2759

Miscellaneous databases

Protein Ontology

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PROi
PR:P35384

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_BOVIN
<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: P35384
<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: June 1, 1994
Last sequence update: June 1, 1994
Last modified: June 5, 2019
This is version 124 of the entry and version 1 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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