Inositol 1,4,5-trisphosphate receptor type 3

<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

<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

• calcium ion binding Source: RGD <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ
  • "Protein kinase C decreases the apparent affinity of the inositol 1,4,5-trisphosphate receptor type 3 in RINm5F cells."
    Caron A.Z., Chaloux B., Arguin G., Guillemette G.
    Cell Calcium 42:323-331(2007) [PubMed] [Europe PMC] [Abstract]
  • "Protein kinase A increases the binding affinity and the Ca2+ release activity of the inositol 1,4,5-trisphosphate receptor type 3 in RINm5F cells."
    Chaloux B., Caron A.Z., Guillemette G.
    Biol. Cell 99:379-388(2007) [PubMed] [Europe PMC] [Abstract]
• calcium ion transmembrane transporter activity Source: RGD <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#tas">GO evidence code guide</a></p> Traceable author statementⁱ
  • "Intracellular signal transduction during gastrin-induced histamine secretion in rat gastric ECL cells."
    Zanner R., Hapfelmeier G., Gratzl M., Prinz C.
    Am. J. Physiol., Cell Physiol. 282:C374-82(2002) [PubMed] [Europe PMC] [Abstract]
• calcium-release channel activity Source: UniProtKB
• identical protein binding Source: RGD <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ipi">GO evidence code guide</a></p> Inferred from physical interactionⁱ
  • "Single-channel properties in endoplasmic reticulum membrane of recombinant type 3 inositol trisphosphate receptor."
    Mak D.O., McBride S., Raghuram V., Yue Y., Joseph S.K., Foskett J.K.
    J. Gen. Physiol. 115:241-256(2000) [PubMed] [Europe PMC] [Abstract]
• inositol 1,3,4,5 tetrakisphosphate binding Source: RGDInferred from direct assayⁱ
  • Ref.1

    "Sequence and functional characterization of a third inositol trisphosphate receptor subtype, IP3R-3, expressed in pancreatic islets, kidney, gastrointestinal tract, and other tissues."
    Blondel O., Takeda J., Janssen H., Seino S., Bell G.I.
    J. Biol. Chem. 268:11356-11363(1993) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
• inositol 1,4,5 trisphosphate binding Source: RGDInferred from direct assayⁱ
  • "Protein kinase C decreases the apparent affinity of the inositol 1,4,5-trisphosphate receptor type 3 in RINm5F cells."
    Caron A.Z., Chaloux B., Arguin G., Guillemette G.
    Cell Calcium 42:323-331(2007) [PubMed] [Europe PMC] [Abstract]
  • "Protein kinase A increases the binding affinity and the Ca2+ release activity of the inositol 1,4,5-trisphosphate receptor type 3 in RINm5F cells."
    Chaloux B., Caron A.Z., Guillemette G.
    Biol. Cell 99:379-388(2007) [PubMed] [Europe PMC] [Abstract]
• inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity Source: RGDInferred from direct assayⁱ
  • "Single-channel properties in endoplasmic reticulum membrane of recombinant type 3 inositol trisphosphate receptor."
    Mak D.O., McBride S., Raghuram V., Yue Y., Joseph S.K., Foskett J.K.
    J. Gen. Physiol. 115:241-256(2000) [PubMed] [Europe PMC] [Abstract]
  • "Functional characterization of mammalian inositol 1,4,5-trisphosphate receptor isoforms."
    Tu H., Wang Z., Nosyreva E., De Smedt H., Bezprozvanny I.
    Biophys. J. 88:1046-1055(2005) [PubMed] [Europe PMC] [Abstract]
  • "Protein kinase C decreases the apparent affinity of the inositol 1,4,5-trisphosphate receptor type 3 in RINm5F cells."
    Caron A.Z., Chaloux B., Arguin G., Guillemette G.
    Cell Calcium 42:323-331(2007) [PubMed] [Europe PMC] [Abstract]
  • "Protein kinase A increases the binding affinity and the Ca2+ release activity of the inositol 1,4,5-trisphosphate receptor type 3 in RINm5F cells."
    Chaloux B., Caron A.Z., Guillemette G.
    Biol. Cell 99:379-388(2007) [PubMed] [Europe PMC] [Abstract]
• inositol hexakisphosphate binding Source: RGDInferred from direct assayⁱ
  • Ref.1

    "Sequence and functional characterization of a third inositol trisphosphate receptor subtype, IP3R-3, expressed in pancreatic islets, kidney, gastrointestinal tract, and other tissues."
    Blondel O., Takeda J., Janssen H., Seino S., Bell G.I.
    J. Biol. Chem. 268:11356-11363(1993) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
• phosphatidylinositol binding Source: RGDInferred from sequence orthologyⁱ
  • "Molecular basis of the isoform-specific ligand-binding affinity of inositol 1,4,5-trisphosphate receptors."
    Iwai M., Michikawa T., Bosanac I., Ikura M., Mikoshiba K.
    J. Biol. Chem. 282:12755-12764(2007) [PubMed] [Europe PMC] [Abstract]
• protein-containing complex binding Source: RGDInferred from direct assayⁱ
  • "Single-channel properties in endoplasmic reticulum membrane of recombinant type 3 inositol trisphosphate receptor."
    Mak D.O., McBride S., Raghuram V., Yue Y., Joseph S.K., Foskett J.K.
    J. Gen. Physiol. 115:241-256(2000) [PubMed] [Europe PMC] [Abstract]

GO - Biological processⁱ

• calcium ion transport Source: RGDInferred from sequence orthologyⁱ
  • "The Pro335 --> Leu polymorphism of type 3 inositol 1,4,5-trisphosphate receptor found in mouse inbred lines results in functional change."
    Kim S., Ahn T., Park C.
    J. Biol. Chem. 280:26024-26031(2005) [PubMed] [Europe PMC] [Abstract]
  • "Nuclear inositol 1,4,5-trisphosphate receptors regulate local Ca2+ transients and modulate cAMP response element binding protein phosphorylation."
    Cardenas C., Liberona J.L., Molgo J., Colasante C., Mignery G.A., Jaimovich E.
    J. Cell. Sci. 118:3131-3140(2005) [PubMed] [Europe PMC] [Abstract]
• calcium ion transport into cytosol Source: UniProtKB
• cellular response to cAMP Source: RGDInferred from direct assayⁱ
  • "Regulation of inositol 1,4,5-trisphosphate receptors by cAMP independent of cAMP-dependent protein kinase."
    Tovey S.C., Dedos S.G., Rahman T., Taylor E.J., Pantazaka E., Taylor C.W.
    J. Biol. Chem. 285:12979-12989(2010) [PubMed] [Europe PMC] [Abstract]
• G protein-coupled receptor signaling pathway Source: RGDInferred from direct assayⁱ
  • "Intracellular signal transduction during gastrin-induced histamine secretion in rat gastric ECL cells."
    Zanner R., Hapfelmeier G., Gratzl M., Prinz C.
    Am. J. Physiol., Cell Physiol. 282:C374-82(2002) [PubMed] [Europe PMC] [Abstract]
• long-term synaptic potentiation Source: RGDInferred from sequence orthologyⁱ
  • "Impaired fear memory, altered object memory and modified hippocampal synaptic plasticity in split-brain mice."
    MacPherson P., McGaffigan R., Wahlsten D., Nguyen P.V.
    Brain Res. 1210:179-188(2008) [PubMed] [Europe PMC] [Abstract]
• memory Source: RGDInferred from sequence orthologyⁱ
  • "Impaired fear memory, altered object memory and modified hippocampal synaptic plasticity in split-brain mice."
    MacPherson P., McGaffigan R., Wahlsten D., Nguyen P.V.
    Brain Res. 1210:179-188(2008) [PubMed] [Europe PMC] [Abstract]
• positive regulation of cytosolic calcium ion concentration Source: RGDInferred from direct assayⁱ
  • "Intracellular signal transduction during gastrin-induced histamine secretion in rat gastric ECL cells."
    Zanner R., Hapfelmeier G., Gratzl M., Prinz C.
    Am. J. Physiol., Cell Physiol. 282:C374-82(2002) [PubMed] [Europe PMC] [Abstract]
  • "Protein kinase C decreases the apparent affinity of the inositol 1,4,5-trisphosphate receptor type 3 in RINm5F cells."
    Caron A.Z., Chaloux B., Arguin G., Guillemette G.
    Cell Calcium 42:323-331(2007) [PubMed] [Europe PMC] [Abstract]
  • "Protein kinase A increases the binding affinity and the Ca2+ release activity of the inositol 1,4,5-trisphosphate receptor type 3 in RINm5F cells."
    Chaloux B., Caron A.Z., Guillemette G.
    Biol. Cell 99:379-388(2007) [PubMed] [Europe PMC] [Abstract]
• release of sequestered calcium ion into cytosol Source: GO_Central <p>Inferred from Biological aspect of Ancestor</p> <p>A type of phylogenetic evidence whereby an aspect of a descendent is inferred through the characterization of an aspect of a ancestral gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#iba">GO evidence code guide</a></p> Inferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief. Bioinformatics 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• response to calcium ion Source: RGDInferred from sequence orthologyⁱ
  • "Caveolin-1 scaffold domain interacts with TRPC1 and IP3R3 to regulate Ca2+ store release-induced Ca2+ entry in endothelial cells."
    Sundivakkam P.C., Kwiatek A.M., Sharma T.T., Minshall R.D., Malik A.B., Tiruppathi C.
    Am. J. Physiol., Cell Physiol. 296:C403-13(2009) [PubMed] [Europe PMC] [Abstract]
• sensory perception of bitter taste Source: RGDInferred from sequence orthologyⁱ
  • "Abnormal taste perception in mice lacking the type 3 inositol 1,4,5-trisphosphate receptor."
    Hisatsune C., Yasumatsu K., Takahashi-Iwanaga H., Ogawa N., Kuroda Y., Yoshida R., Ninomiya Y., Mikoshiba K.
    J. Biol. Chem. 282:37225-37231(2007) [PubMed] [Europe PMC] [Abstract]
• sensory perception of sweet taste Source: RGDInferred from sequence orthologyⁱ
  • "Abnormal taste perception in mice lacking the type 3 inositol 1,4,5-trisphosphate receptor."
    Hisatsune C., Yasumatsu K., Takahashi-Iwanaga H., Ogawa N., Kuroda Y., Yoshida R., Ninomiya Y., Mikoshiba K.
    J. Biol. Chem. 282:37225-37231(2007) [PubMed] [Europe PMC] [Abstract]
• sensory perception of umami taste Source: RGDInferred from sequence orthologyⁱ
  • "Abnormal taste perception in mice lacking the type 3 inositol 1,4,5-trisphosphate receptor."
    Hisatsune C., Yasumatsu K., Takahashi-Iwanaga H., Ogawa N., Kuroda Y., Yoshida R., Ninomiya Y., Mikoshiba K.
    J. Biol. Chem. 282:37225-37231(2007) [PubMed] [Europe PMC] [Abstract]

<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

Enzyme and pathway databases

Protein family/group databases

<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

Organism-specific databases

<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

Topology

Keywords - Cellular componentⁱ

<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

<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

Amino acid modifications

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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

Keywords - PTMⁱ

Proteomic databases

PTM databases

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structureⁱ

GO - Molecular functionⁱ

• identical protein binding Source: RGDInferred from physical interactionⁱ
  • "Single-channel properties in endoplasmic reticulum membrane of recombinant type 3 inositol trisphosphate receptor."
    Mak D.O., McBride S., Raghuram V., Yue Y., Joseph S.K., Foskett J.K.
    J. Gen. Physiol. 115:241-256(2000) [PubMed] [Europe PMC] [Abstract]

Protein-protein interaction databases

<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

<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

Domains and Repeats

Region

<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

<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

Phylogenomic databases

Family and domain databases

<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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

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

        10         20         30         40         50
MNEMSSFLHI GDIVSLYAEG SVNGFISTLG LVDDRCVVEP AAGDLDNPPK 
        60         70         80         90        100
KFRDCLFKVC PMNRYSAQKQ YWKAKQTKQD KEKIADVVLL QKLQHAAQME 
       110        120        130        140        150
QKQNDTENKK VHGDVVKYGS VIQLLHMKSN KYLTVNKRLP ALLEKNAMRV 
       160        170        180        190        200
TLDATGNEGS WLFIQPFWKL RSNGDNVVVG DKVILNPVNA GQPLHASNYE 
       210        220        230        240        250
LSDNVGCKEV NSVNCNTSWK INLFMQFRDH LEEVLKGGDV VRLFHAEQEK 
       260        270        280        290        300
FLTCDEYRGK LQVFLRTTLR QSATSATSSN ALWEVEVVHH DPCRGGAGHW 
       310        320        330        340        350
NGLYRFKHLA TGNYLAAEEN PSYKGDVSDP KAAGPGAQSR TGRRNAGEKI 
       360        370        380        390        400
KYRLVAVPHG NDIASLFELD PTTLQKTDSF VPRNSYVRLR HLCTNTWIQS 
       410        420        430        440        450
TNAPIDVEEE RPIRLMLGTC PTKEDKEAFA IVSVPVSEIR DLDFANDASS 
       460        470        480        490        500
MLASAVEKLN EGFISQNDRR FVIQLLEDLV FFVSDVPNNG QNVLDIMVTK 
       510        520        530        540        550
PNRERQKLMR DENILKQIFG ILKAPFRDKG GEGPLVRLEE LSDQKNAPYQ 
       560        570        580        590        600
YMFRLCYRVL RHSQEDYRKN QEHIAKQFGM MQSQIGYDIL AEDTITALLH 
       610        620        630        640        650
NNRKLLEKHI TKTEVETFVS LVRKNREPRF LDYLSDLCVS NRIAIPVTQE 
       660        670        680        690        700
LICKCVLDPK NSDILIQTEL RPVKEMAQSH EYLSIEYSEE EVWLTWTDRN 
       710        720        730        740        750
NEHHEKSVRQ LAQEARAGNA HDENVLSYYR YQLKLFARMC LDRQYLAIDE 
       760        770        780        790        800
ISKQLGVELL FLCMADEMLP FDLRASFCHL MLHVHVDRDP QELVTPVKFA 
       810        820        830        840        850
RLWTEIPTAI TIKDYDSNLN ASRDDKKNKF ASTMEFVEDY LNNVVGEAVP 
       860        870        880        890        900
FANDEKNILT FEVVSLAHNL IYFGFYSFSE LLRLTRTLLG IIDCIQAPAA 
       910        920        930        940        950
VLQAYEEPGG KNVRRSIQGV GHMMSTMVLS RKQSVFGASS LPTGVGVPEQ 
       960        970        980        990       1000
LDRSKFEDNE HTVVMETKLK ILEILQFILN VRLDYRISYL LSVFKKEFVE 
      1010       1020       1030       1040       1050
VFPMQDSGAD GTAPAFDSST ANMNLDRIGE QAEAMFGVGK TSSMLEVDDE 
      1060       1070       1080       1090       1100
GGRMFLRVLL HLTMHDYPPL VSGALQLLFK HFSQRQEAMH TFKQVQLLIS 
      1110       1120       1130       1140       1150
AQDVENYKVI KSELDRLRTM VEKSELWVDK KGSVKGEEGE AGASKDKKER 
      1160       1170       1180       1190       1200
PSDEEGFLQP HGEKSSENYQ IVKGILERLN KMCGVGEQMR KKQQRLLKNM 
      1210       1220       1230       1240       1250
DAHKVMLDLL QIPYDKNDNK MMEILRYTHQ FLQKFCAGNP GNQALLHKHL 
      1260       1270       1280       1290       1300
QLFLTPGLLE AETMQHIFLN NYQLCSEISE PVLQHFVHCW PTHGRHVQYL 
      1310       1320       1330       1340       1350
DFLHTVIKAE GKYVKKCQDM IMTELTNAGD DVVVFYNDKA SLAHLLDMMK 
      1360       1370       1380       1390       1400
AARDGVEDHS PLMYHISLVD LLAACAEGKN VYTEIKCTSL LPLEDVVSVV 
      1410       1420       1430       1440       1450
THEDCITEVK MAYVNFVNHC YVDTEVEMKE IYTSNHIWTL FENFTLDMAL 
      1460       1470       1480       1490       1500
VCNKREKRLS DPTLEKYVLT VVLDTISAFF SSPFSENSTS LQTHQTIVVQ 
      1510       1520       1530       1540       1550
LLQSTTRLLE CPWLQQQHKG SVEACVRTLA MVAKSRAILL PMDLDAHMSA 
      1560       1570       1580       1590       1600
LLSSGGSCSA AAQRSAANYK TATRTFPRVI PTANQWDYKN IIEKLQDIIT 
      1610       1620       1630       1640       1650
ALEERLKPLV QAELSVLVDM LHWPELLFLE GSEAYQRCES GGFLSKLIRH 
      1660       1670       1680       1690       1700
TKGLMESEEK LCVKVLRTLQ QMLQKKSKYG DRGNQLRKML LQNYLQNRKS 
      1710       1720       1730       1740       1750
GPRGELTDPT GSGVDQDWSA IAATQCRLDK EGATKLVCDL ITSTKNEKIF 
      1760       1770       1780       1790       1800
QESIGLAIRL LDGGNTEIQK SFYNLMTSDK KSERFFKVLH DRMKRAQQET 
      1810       1820       1830       1840       1850
KSTVAVNMSD LGSQPREDRE PADPTTKGRV SSFSMPSSSR YSLGPGLHRG 
      1860       1870       1880       1890       1900
HDVSERAQNN EMGTSVLIMR PILRFLQLLC ENHNRDLQNF LRCQNNKTNY 
      1910       1920       1930       1940       1950
NLVCETLQFL DIMCGSTTGG LGLLGLYINE DNVGLVIQTL ETLTEYCQGP 
      1960       1970       1980       1990       2000
CHENQTCIVT HESNGIDIIT ALILNDISPL CKYRMDLVLQ LKDNASKLLL 
      2010       2020       2030       2040       2050
ALMESRHDSE NAERILISLR PQELVDVIKK AYLQEEEREN SEVSPREVGH 
      2060       2070       2080       2090       2100
NIYILALQLS RHNKQLQHLL KPVKRIQEEE AEGISSMLSL NNKQLSQMLK 
      2110       2120       2130       2140       2150
SSAPAQEEEE DPLAYYENHT SQIEIVRQDR SMEQIVFPVP AICQFLTEET 
      2160       2170       2180       2190       2200
KHRLFTTTEQ DEQGSKVSDF FDQSSFLHNE MEWQRRLRSM PLIYWFSRRM 
      2210       2220       2230       2240       2250
TLWGSISFNL AVFINIIIAF FYPYVEGAST GVLGSPLISL LFWILICFSI 
      2260       2270       2280       2290       2300
AALFTKHYSV RPLIVALVLR SIYYLGIGPT LNILGALNLT NKIVFVVSFV 
      2310       2320       2330       2340       2350
GNRGTFIRGY KAMVMDMEFL YHVGYILTSV LGLFAHELFY SILLFDLIYR 
      2360       2370       2380       2390       2400
EETLFNVIKS VTRNGRSILL TALLALILVY LFSIVGFLFL KDDFILEVDR 
      2410       2420       2430       2440       2450
LPGNHSRAST LGMPHGAATF MGTCSGDKMD CVSEVSVPEI LEEDEELDST 
      2460       2470       2480       2490       2500
ERACDTLLMC IVTVMNHGLR NGGGVGDILR KPSKDESLFP ARVVYDLLFF 
      2510       2520       2530       2540       2550
FIVIIIVLNL IFGVIIDTFA DLRSEKQKKE EILKTTCFIC GLERDKFDNK 
      2560       2570       2580       2590       2600
TVSFEEHIKL EHNMWNYLYF IVLVRVKNKT DYTGPESYVA QMIKNKNLDW 
      2610       2620       2630       2640       2650
FPRMRAMSLV SGEGEGEQNE IRILQEKLGS TMKLVSHLTA QLNELKEQMT 
      2660       2670
EQRKRRQRLG FVDVQNCMSR                                  

Sequence databases

Genome annotation databases

<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

• 90% Identity
• 50% Identity

<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

3D structure databases

Protein-protein interaction databases

Chemistry databases

Protein family/group databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<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 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

Documents

1. SIMILARITY comments
   Index of protein domains and families