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Q9Z329 (ITPR2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Inositol 1,4,5-trisphosphate receptor type 2
Alternative name(s):
IP3 receptor isoform 2
Short name=IP3R 2
Short name=InsP3R2
Inositol 1,4,5-trisphosphate type V receptor
Type 2 inositol 1,4,5-trisphosphate receptor
Short name=Type 2 InsP3 receptor
Gene names
Name:Itpr2
Synonyms:Itpr5
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length2701 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Receptor for inositol 1,4,5-trisphosphate, a second messenger that mediates the release of intracellular calcium. This release is regulated by cAMP both dependently and independently of PKA. Ref.1 Ref.3 Ref.10

Isoform 3 has neither inositol 1,4,5-trisphosphate binding activity nor calcium releasing activity. Ref.1 Ref.3 Ref.10

Subunit structure

Homotetramer By similarity. Interacts with CABP1 By similarity.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein Ref.1.

Tissue specificity

Isoforms 1 and 3 are widely expressed. Isoform 2 is found in skeletal muscle and heart. Ref.1

Domain

The receptor contains a calcium channel in its C-terminal extremity. Its large N-terminal cytoplasmic region has the ligand-binding site in the N-terminus and modulatory sites in the middle portion immediately upstream of the channel region.

Post-translational modification

Phosphorylation by cAMP-dependent PKA on Ser-937 increases calcium release.

Sequence similarities

Belongs to the InsP3 receptor family.

Contains 5 MIR domains.

Ontologies

Keywords
   Biological processCalcium transport
Ion transport
Transport
   Cellular componentEndoplasmic reticulum
Membrane
   Coding sequence diversityAlternative splicing
   DomainRepeat
Transmembrane
Transmembrane helix
   LigandCalcium
   Molecular functionCalcium channel
Ion channel
Ligand-gated ion channel
Receptor
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcalcium ion transport

Inferred from direct assay Ref.7. Source: MGI

cellular response to cAMP

Inferred from direct assay Ref.3. Source: UniProtKB

cellular response to ethanol

Inferred from mutant phenotype PubMed 21436055. Source: MGI

inositol phosphate-mediated signaling

Inferred from direct assay PubMed 17327232Ref.7. Source: GOC

response to hypoxia

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcell cortex

Inferred from direct assay PubMed 9858485. Source: MGI

cytoplasm

Inferred from direct assay PubMed 9858485. Source: MGI

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from electronic annotation. Source: Ensembl

receptor complex

Inferred from sequence orthology PubMed 23382219. Source: MGI

sarcoplasmic reticulum

Inferred from direct assay PubMed 16014380. Source: MGI

sarcoplasmic reticulum membrane

Inferred from electronic annotation. Source: Ensembl

   Molecular_functioncalcium-release channel activity

Inferred from direct assay Ref.7. Source: MGI

inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity

Inferred from direct assay PubMed 17327232Ref.7. Source: MGI

phosphatidylinositol binding

Inferred from direct assay PubMed 17327232Ref.7. Source: MGI

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9Z329-1)

Also known as: Long;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9Z329-2)

Also known as: Short; TIPR;

The sequence of this isoform differs from the canonical sequence as follows:
     175-175: N → NDMGAVI
     176-1281: Missing.
Isoform 3 (identifier: Q9Z329-3)

Also known as: Itpr2v;

The sequence of this isoform differs from the canonical sequence as follows:
     176-208: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 27012701Inositol 1,4,5-trisphosphate receptor type 2
PRO_0000153925

Regions

Topological domain1 – 22272227Cytoplasmic Potential
Transmembrane2228 – 224821Helical; Potential
Topological domain2249 – 226012Extracellular Potential
Transmembrane2261 – 228121Helical; Potential
Topological domain2282 – 230726Cytoplasmic Potential
Transmembrane2308 – 232821Helical; Potential
Topological domain2329 – 235123Extracellular Potential
Transmembrane2352 – 237221Helical; Potential
Topological domain2373 – 239422Cytoplasmic Potential
Transmembrane2395 – 241521Helical; Potential
Topological domain2416 – 2520105Extracellular Potential
Transmembrane2521 – 254121Helical; Potential
Topological domain2542 – 2701160Cytoplasmic Potential
Domain112 – 16655MIR 1
Domain173 – 22351MIR 2
Domain231 – 28757MIR 3
Domain294 – 37279MIR 4
Domain378 – 43457MIR 5
Region265 – 2695Inositol 1,4,5-trisphosphate binding By similarity
Region507 – 5104Inositol 1,4,5-trisphosphate binding By similarity
Region567 – 5693Inositol 1,4,5-trisphosphate binding By similarity

Amino acid modifications

Modified residue9371Phosphoserine; by PKA Ref.9 Ref.10
Modified residue11601Phosphoserine By similarity
Modified residue26071Phosphotyrosine Potential

Natural variations

Alternative sequence1751N → NDMGAVI in isoform 2.
VSP_002701
Alternative sequence176 – 12811106Missing in isoform 2.
VSP_002702
Alternative sequence176 – 20833Missing in isoform 3.
VSP_016026

Experimental info

Mutagenesis5071K → A: Loss of binding activity. Ref.1
Mutagenesis5101R → A: Loss of binding activity. Ref.1
Mutagenesis9371S → A: Abolishes PKA-mediated phosphorylation. No enhanced calcium release. Abolishes PKA-mediated phosphorylation: When associated with A-990; A-1190; A-1351 and A-1581. Ref.10
Mutagenesis9901S → A: No effect on PKA-mediated phosphorylation. Abolishes PKA-mediated phosphorylation: When associated with A-937; A-1190; A-1351 and A-1581. Ref.10
Mutagenesis11901S → A: No effect on PKA-mediated phosphorylation. Abolishes PKA-mediated phosphorylation: When associated with A-937; A-990; A-1351 and A-1581. Ref.10
Mutagenesis13511S → A: No effect on PKA-mediated phosphorylation. Abolishes PKA-mediated phosphorylation: When associated with A-937; A-990; A-1190 and A-1581. Ref.10
Mutagenesis15811S → A: No effect on PKA-mediated phosphorylation. Abolishes PKA-mediated phosphorylation: When associated with A-937; A-990; A-1190 and A-1351. Ref.10
Mutagenesis26331S → A: No effect on PKA-mediated phosphorylation. Enhanced calcium release on PKA activation. Ref.10
Sequence conflict17101I → V in AAH25805. Ref.6
Sequence conflict17291S → G in AAH25805. Ref.6
Sequence conflict17381K → T in AAH25805. Ref.6
Sequence conflict21961F → L in CAA94861. Ref.7
Sequence conflict22231S → P in AAH25805. Ref.6
Sequence conflict22651V → A in AAH25805. Ref.6
Sequence conflict22651V → A in CAA94861. Ref.7
Sequence conflict22651V → A in CAA83957. Ref.8

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Long) [UniParc].

Last modified July 27, 2011. Version 4.
Checksum: E7853104F0BD9B08

FASTA2,701307,475
        10         20         30         40         50         60 
MSDKMSSFLY IGDIVSLYAE GSVNGFISTL GLVDDRCVVH PEAGDLANPP KKFRDCLFKV 

        70         80         90        100        110        120 
CPMNRYSAQK QYWKAKQAKQ GNHTEAALLK KLQHAAELEQ KQNESENRKL LGEIVKYSNV 

       130        140        150        160        170        180 
IQLLHIKSNK YLTVNKRLPA LLEKNAMRVS LDAAGNEGSW FYIHPFWKLR SEGDNIVVGD 

       190        200        210        220        230        240 
KVVLMPVNAG QPLHASNVEL LDNPGCKEVN AVNCNTSWKI TLFMKFSSYR EDVLKGGDVV 

       250        260        270        280        290        300 
RLFHAEQEKF LTCDDYEKKQ HIFLRTTLRQ SATSATSSKA LWEIEVVHHD PCRGGAGQWN 

       310        320        330        340        350        360 
SLFRFKHLAT GNYLAAELNP DYRDAQNEGK NVKDGEIPTP KKKRQAGEKI MYTLVSVPHG 

       370        380        390        400        410        420 
NDIASLFELD ATTLQRADCL VPRNSYVRLR HLCTNTWVTS TTIPIDTEEE RPVMLKIGTC 

       430        440        450        460        470        480 
QTKEDKEAFA IVCVPLSEVR DLDFANDANK VLATTVKKLE NGSITQNERR FVTKLLEDLI 

       490        500        510        520        530        540 
FFVADVTNNG QDVLDVVITK PNRERQKLMR EQNILAQVFG ILKAPFKEKA GEGSMLRLED 

       550        560        570        580        590        600 
LGDQRYAPYK YVLRLCYRVL RHSQQDYRKN QEYIAKNFCV MQSQIGYDIL AEDTITALLH 

       610        620        630        640        650        660 
NNRKLLEKHI TAKEIETFVS LLRRNREPRF LDYLSDLCVS NSTAIPVTQE LICKFMLSPG 

       670        680        690        700        710        720 
NADILIQTKL VSMQVENPME SSILPDDIDD EEVWLYWIDS NKEPHGKAIR HLAQEAREGT 

       730        740        750        760        770        780 
KADLEVLTYY RYQLNLFARM CLDRQYLAIN QISTQLSVDL ILRCVSDESL PFDLRASFCR 

       790        800        810        820        830        840 
LMLHMHVDRD PQESVVPVRY ARLWTEIPTK ITIHEYDSIT DSSRNDMKRK FALTMEFVEE 

       850        860        870        880        890        900 
YLKEVVNQPF PFGDKEKNKL TFEVVHLARN LIYFGFYSFS ELLRLTRTLL AILDIVQAPM 

       910        920        930        940        950        960 
SSYFERLSKF QDGSNNVMRT IHGVGEMMTQ MVLSRGSIFP VSVPDAQPIV HPSKQASPGE 

       970        980        990       1000       1010       1020 
QEDVTVMDTK LKVIEILQFI LSVRLDYRIS YMLSIYKKEF GDNNDNGDPS ASGTPDTLLP 

      1030       1040       1050       1060       1070       1080 
SALVPDIDEI AAQAETMFAG RKEKTPVQLD DEGGRTFLRV LIHLIMHDYA PLLSGALQLL 

      1090       1100       1110       1120       1130       1140 
FKHFSQRAEV LQAFKQVQLL VSNQDVDNYK QIKADLDQLR LTVEKSELWV EKSGSYENGD 

      1150       1160       1170       1180       1190       1200 
VGEGQAKGGE EANEESNLLS PVQDGAKTPQ IDSNKGNNYR IVKEILIRLS KLCVQNKKCR 

      1210       1220       1230       1240       1250       1260 
NQHQRLLKNM GAHSVVLDLL QIPYEKTDEK MNEVMDLAHT FLQNFCRGNP QNQVLLHKHL 

      1270       1280       1290       1300       1310       1320 
NLFLTPGLLE AETMRHIFMN NYHLCNEISE RVVQHFVHCI ETHGRHVEYL RFLQTIVKAD 

      1330       1340       1350       1360       1370       1380 
GKYVKKCQDM VMTELINGGE DVLIFYNDRA SFPILLNMMC SERARGDESG PLAYHITLVE 

      1390       1400       1410       1420       1430       1440 
LLAACTEGKN VYTEIKCNSL LPLDDIVRVV THDDCIPEVK IAYVNFVNHC YVDTEVEMKE 

      1450       1460       1470       1480       1490       1500 
IYTSNHIWKL FENFLVDMAR VCNTTTDRKH ADTFLERCVT ESVMNIVSGF FNSPFSDNST 

      1510       1520       1530       1540       1550       1560 
SLQTHQPVFI QLLQSAFRIY NCTWPNPAQK ASVESCIRAL AEVAKNRGIA IPVDLDSQVN 

      1570       1580       1590       1600       1610       1620 
TLFMKNHSST VQRAAMGWRL SARSGPRFKE ALGGPAWDYR NIIEKLQDVV ASLEQQFSPM 

      1630       1640       1650       1660       1670       1680 
MQAEFSVLVD VLYSPELLFP EGSDARIRCG AFMSKLINHT KKLMEKEEKL CIKILQTLRE 

      1690       1700       1710       1720       1730       1740 
MLEKKDSFME EGSTLRRILL NRYFKGDHSI SVNGPLSGAY AKTAQVGGSF SGQDSDKKGI 

      1750       1760       1770       1780       1790       1800 
SMSDIQCLLD KEGASELVID VIVNTKNDRI FSEGILLGIA LLEGGNTQTQ YSFYQQLHEQ 

      1810       1820       1830       1840       1850       1860 
KKSEKFFKVL YDRMKAAQKE IRSTVTVNTI DLGSKKREED SDVMALGPRM RVRDSSLHLR 

      1870       1880       1890       1900       1910       1920 
EGMKGQLTEA SSATSKAYCV YRREMDPEID TMCPGQEAGS AEEKSAEEVT MSPAITIMRP 

      1930       1940       1950       1960       1970       1980 
ILRFLQLLCE NHNRELQNFL RNQNNKTNYN LVCETLQFLD CICGSTTGGL GLLGLYINER 

      1990       2000       2010       2020       2030       2040 
NVALVNQTLE SLTEYCQGPC HENQTCIATH ESNGIDIIIA LILNDINPLG KYRMDLVLQL 

      2050       2060       2070       2080       2090       2100 
KNNASKLLLA IMESRHDSEN AERILFNMRP RELVDVMKNA YNQGLECDHG DEEGGDDGVS 

      2110       2120       2130       2140       2150       2160 
PKDVGHNIYI LAHQLARHNK LLQQMLKPGS DPEEGDEALK YYANHTAQIE IVRHDRTMEQ 

      2170       2180       2190       2200       2210       2220 
IVFPVPNICE FLTRESKYRV FNTTERDEQG SKVNDFFQQT EDLYNEMKWQ KKIRNNPALF 

      2230       2240       2250       2260       2270       2280 
WFSRHISLWG SISFNLAVFI NLAVALFYPF GDDGDEGTLS PMFSVLLWVA VAICTSMLFF 

      2290       2300       2310       2320       2330       2340 
FSKPVGIRPF LVSVMLRSIY TIGLGPTLIL LGAANLCNKI VFLVSFVGNR GTFTRGYRAV 

      2350       2360       2370       2380       2390       2400 
ILDMAFLYHV AYVLVCMLGL FVHEFFYSFL LFDLVYREET LLNVIKSVTR NGRSIILTAV 

      2410       2420       2430       2440       2450       2460 
LALILVYLFS IIGFLFLKDD FTMEVDRLKN RTPVTGNHGV PTMTLSSMME TCQKENCSPT 

      2470       2480       2490       2500       2510       2520 
IPSSNTAGEE GEDGIERTCD TLLMCIVTVL NQGLRNGGGV GDVLRRPSKD EPLFAARVVY 

      2530       2540       2550       2560       2570       2580 
DLLFFFIVII IVLNLIFGVI IDTFADLRSE KQKKEEILKT TCFICGLERD KFDNKTVSFE 

      2590       2600       2610       2620       2630       2640 
EHIKSEHNMW HYLYFIVLVK VKDPTEYTGP ESYVAQMITE KNLDWFPRMR AMSLVSNEGD 

      2650       2660       2670       2680       2690       2700 
SEQNEIRNLQ EKLESTMSLV KQLSGQLAEL KEQMTEQRKN KQRLGFLGSN TPHVNHHMPP 


H 

« Hide

Isoform 2 (Short) (TIPR) [UniParc].

Checksum: 1E28137D334C60D4
Show »

FASTA1,601181,743
Isoform 3 (Itpr2v) [UniParc].

Checksum: 79912954DF5F5F17
Show »

FASTA2,668304,036

References

« Hide 'large scale' references
[1]"Molecular cloning of mouse type 2 and type 3 inositol 1,4,5-trisphosphate receptors and identification of a novel type 2 receptor splice variant."
Iwai M., Tateishi Y., Hattori M., Mizutani A., Nakamura T., Futatsugi A., Inoue T., Furuichi T., Michikawa T., Mikoshiba K.
J. Biol. Chem. 280:10305-10317(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-507 AND ARG-510.
Strain: C57BL/6J.
Tissue: Lung.
[2]"Muscle-specific mRNA isoform encodes a protein composed mainly of the N-terminal 175 residues of type 2 Ins(1,4,5)P3 receptor."
Futatsugi A., Kuwajima G., Mikoshiba K.
Biochem. J. 334:559-563(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Heart.
[3]"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]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
[4]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[5]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1290-2701.
Strain: Czech II.
Tissue: Mammary tumor.
[7]"Determination of relative amounts of inositol trisphosphate receptor mRNA isoforms by ratio polymerase chain reaction."
De Smedt H., Missiaen L., Parys J.B., Bootman M.D., Mertens L., Van Den Bosch L., Casteels R.
J. Biol. Chem. 269:21691-21698(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1693-2701 (ISOFORM 1).
Strain: C3H.
Tissue: Embryo.
[8]"Isoform diversity of the inositol trisphosphate receptor in cell types of mouse origin."
De Smedt H., Missiaen L., Parys J.B., Henning R.H., Sienaert I., Vanlingen S., Gijsens A., Himpens B., Casteels R.
Biochem. J. 322:575-583(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2238-2646 (ISOFORM 1).
Strain: C3H.
Tissue: Embryo.
[9]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-937, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[10]"Protein kinase A increases type-2 inositol 1,4,5-trisphosphate receptor activity by phosphorylation of serine 937."
Betzenhauser M.J., Fike J.L., Wagner L.E. II, Yule D.I.
J. Biol. Chem. 284:25116-25125(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-937, FUNCTION, MUTAGENESIS OF SER-937; SER-990; SER-1190; SER-1351; SER-1581 AND SER-2633.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB182288 mRNA. Translation: BAD90682.1.
AB182290 mRNA. Translation: BAD90684.1.
AB012393 mRNA. Translation: BAA33960.1.
GU980658 mRNA. Translation: ADG01867.1.
CU207333, CU207302, CU207317 Genomic DNA. Translation: CAQ51734.1.
CU207302, CU207317, CU207333 Genomic DNA. Translation: CAQ51929.1.
CU207317, CU207302, CU207333 Genomic DNA. Translation: CAQ52319.1.
CH466572 Genomic DNA. Translation: EDL10703.1.
BC025805 mRNA. Translation: AAH25805.1.
Z71173 mRNA. Translation: CAA94861.1.
Z33908 mRNA. Translation: CAA83957.1.
PIRI48607.
RefSeqNP_034716.1. NM_010586.2.
NP_064307.2. NM_019923.4.
UniGeneMm.7800.

3D structure databases

ProteinModelPortalQ9Z329.
SMRQ9Z329. Positions 5-578.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBQ9Z329.

PTM databases

PhosphoSiteQ9Z329.

Proteomic databases

PaxDbQ9Z329.
PRIDEQ9Z329.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000053273; ENSMUSP00000049584; ENSMUSG00000030287. [Q9Z329-1]
ENSMUST00000079573; ENSMUSP00000078526; ENSMUSG00000030287. [Q9Z329-3]
GeneID16439.
KEGGmmu:16439.
UCSCuc009erw.1. mouse. [Q9Z329-1]

Organism-specific databases

CTD3709.
MGIMGI:99418. Itpr2.

Phylogenomic databases

eggNOGNOG280601.
GeneTreeENSGT00690000102000.
HOVERGENHBG052158.
InParanoidB2KF91.
KOK04959.
OMAQSAFRIY.
OrthoDBEOG76HQ0M.
TreeFamTF312815.

Gene expression databases

ArrayExpressQ9Z329.
BgeeQ9Z329.
CleanExMM_ITPR2.
GenevestigatorQ9Z329.

Family and domain databases

Gene3D1.25.10.30. 2 hits.
InterProIPR016024. ARM-type_fold.
IPR014821. Ins145_P3_rcpt.
IPR000493. InsP3_rcpt-bd.
IPR005821. Ion_trans_dom.
IPR016093. MIR_motif.
IPR013662. RIH_assoc-dom.
IPR000699. RIH_dom.
IPR015925. Ryanodine_recept-rel.
[Graphical view]
PANTHERPTHR13715. PTHR13715. 1 hit.
PfamPF08709. Ins145_P3_rec. 1 hit.
PF00520. Ion_trans. 1 hit.
PF02815. MIR. 1 hit.
PF08454. RIH_assoc. 1 hit.
PF01365. RYDR_ITPR. 2 hits.
[Graphical view]
PRINTSPR00779. INSP3RECEPTR.
SMARTSM00472. MIR. 4 hits.
[Graphical view]
SUPFAMSSF100909. SSF100909. 2 hits.
SSF48371. SSF48371. 3 hits.
SSF82109. SSF82109. 2 hits.
PROSITEPS50919. MIR. 5 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSITPR2. mouse.
NextBio289685.
PROQ9Z329.
SOURCESearch...

Entry information

Entry nameITPR2_MOUSE
AccessionPrimary (citable) accession number: Q9Z329
Secondary accession number(s): B2KF91 expand/collapse secondary AC list , P70226, Q5DWM3, Q5DWM5, Q61744, Q8R3B0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 2, 2001
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 124 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot