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Q9JMI9

- TRPC3_RAT

UniProt

Q9JMI9 - TRPC3_RAT

Protein

Short transient receptor potential channel 3

Gene

Trpc3

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 3 (26 May 2009)
      Previous versions | rss
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    Functioni

    Thought to form a receptor-activated non-selective calcium permeant cation channel. Probably is operated by a phosphatidylinositol second messenger system activated by receptor tyrosine kinases or G-protein coupled receptors. Activated by diacylglycerol (DAG) in a membrane-delimited fashion, independently of protein kinase C, and by inositol 1,4,5-triphosphate receptors (ITPR) with bound IP3 By similarity. May also be activated by internal calcium store depletion.By similarity

    GO - Molecular functioni

    1. calcium activated cation channel activity Source: RGD
    2. calcium channel activity Source: UniProtKB-KW

    Keywords - Molecular functioni

    Calcium channel, Ion channel

    Keywords - Biological processi

    Calcium transport, Ion transport, Transport

    Keywords - Ligandi

    Calcium

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Short transient receptor potential channel 3
    Short name:
    TrpC3
    Alternative name(s):
    Trp-related protein 3
    Gene namesi
    Name:Trpc3
    Synonyms:Trrp3
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi61973. Trpc3.

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 836836Short transient receptor potential channel 3PRO_0000215312Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi404 – 4041N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    PRIDEiQ9JMI9.

    PTM databases

    PhosphoSiteiQ9JMI9.

    Expressioni

    Gene expression databases

    GenevestigatoriQ9JMI9.

    Interactioni

    Subunit structurei

    Interacts with TRPC1, ITPR1, ITPR3, MX1 and RNF24. Interacts with JPH2; the interaction is involved in maintaining Ca2+ homeostasis in skeletal muscle and is mediated by JPH2 'Ser-165' phosphorylation By similarity.By similarity

    Protein-protein interaction databases

    DIPiDIP-59688N.

    Structurei

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 369369CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini391 – 41828ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini440 – 45112CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini473 – 52351ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini545 – 56723CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini589 – 63749ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini659 – 836178CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei370 – 39021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei419 – 43921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei452 – 47221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei524 – 54421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei568 – 58821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei638 – 65821HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati26 – 5530ANK 1Add
    BLAST
    Repeati61 – 9030ANK 2Add
    BLAST
    Repeati92 – 11827ANK 3Add
    BLAST
    Repeati147 – 17630ANK 4Add
    BLAST

    Sequence similaritiesi

    Contains 4 ANK repeats.Curated

    Keywords - Domaini

    ANK repeat, Repeat, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG254238.
    HOGENOMiHOG000020590.
    HOVERGENiHBG068337.
    PhylomeDBiQ9JMI9.

    Family and domain databases

    Gene3Di1.25.40.20. 1 hit.
    InterProiIPR002110. Ankyrin_rpt.
    IPR020683. Ankyrin_rpt-contain_dom.
    IPR005821. Ion_trans_dom.
    IPR004729. TRP_channel.
    IPR013555. TRP_dom.
    IPR005459. TRPC3_channel.
    IPR002153. TRPC_channel.
    [Graphical view]
    PANTHERiPTHR10117. PTHR10117. 1 hit.
    PTHR10117:SF8. PTHR10117:SF8. 1 hit.
    PfamiPF12796. Ank_2. 1 hit.
    PF00520. Ion_trans. 1 hit.
    PF08344. TRP_2. 1 hit.
    [Graphical view]
    PRINTSiPR01097. TRNSRECEPTRP.
    PR01644. TRPCHANNEL3.
    SMARTiSM00248. ANK. 3 hits.
    [Graphical view]
    SUPFAMiSSF48403. SSF48403. 1 hit.
    TIGRFAMsiTIGR00870. trp. 1 hit.
    PROSITEiPS50297. ANK_REP_REGION. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9JMI9-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MRDKGRRQAV RGPAFMFGAR GPSLTAEEER FLDAAEYGNI PVVRKMLEES    50
    RTLNVNCVDY MGQNALQLAV GNEHLEVTEL LLKKENLARI GDALLLAISK 100
    GYVRIVEAIL GHPGFAASRR LTLSPCEQEL RDDDFYAYDE DGTRFSPDIT 150
    PIILAAHCHK YEVVHLLLLK GARIERPHDY FCRCADCAEK QRLDAFSHSR 200
    SRINAYKGLA SPAYLSLSSE DPVLTALELS NELAKLANIE KEFKNDYRKL 250
    SMQCKDFVVG VLDLCRDSEE VEAILNGDLE SVEPLERHGH KASLSRVKLA 300
    IKYEVKKFVA HPNCQQQLLT IWYENLSGLR EQTIAIKCLV VLVVALGLPF 350
    LAIGYWIAPC SRLGKILRSP FMKFVAHAAS FIIFLGLLVF NASDRFEGIT 400
    TLPNITVIDY PKQIFRVKTT QFTWTEMLIM VWVLGMMWSE CKELWLEGPR 450
    EYIVQLWNVL DFGMLSIFIA AFTARFLAFL QATKAQQYVD SHVQESDLSE 500
    VTLPPEVQYF TYARDKWLPS DPQIISEGLY AIAVVLSFSR IAYILPANES 550
    FGPLQISLGR TVKDIFKFMV LFIMVFLAFM IGMFILYSYY LGAKVNPAFT 600
    TVEESFKTLF WSIFGLSEVT SVVLKYDHKF IENIGYVLYG IYNVTMVVVL 650
    LNMLIAMINS SYQEIEDDSD VEWKFARSKL WLSYFDDGKT LPPPFSLVPS 700
    PKSFVYFIMR ITNFSKCRRR RLQKDLELGM GNSKSRLNLF TQSNSRVFES 750
    HSFNSILNQP TRYQQIMKRL IKRYVLKAQV DKENDEVNEG ELKEIKQDIS 800
    SLRYELLEDK SQATEELAIL IHKLSEKLNP SALRCE 836
    Length:836
    Mass (Da):95,682
    Last modified:May 26, 2009 - v3
    Checksum:iE405FBFC9285613F
    GO
    Isoform 2 (identifier: Q9JMI9-2)

    Also known as: Trp3SV

    Sequence is not available

    Note: No experimental confirmation available.

    Length:
    Mass (Da):

    Sequence cautioni

    The sequence BAA93434.1 differs from that shown. Reason: Chimeric cDNA.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti335 – 3351A → S in BAA93434. (PubMed:10984475)Curated
    Sequence conflicti361 – 3611S → T in BAA93434. (PubMed:10984475)Curated
    Sequence conflicti394 – 3941D → H in BAA93434. (PubMed:10984475)Curated
    Sequence conflicti486 – 4861Q → H in BAA93434. (PubMed:10984475)Curated
    Sequence conflicti506 – 5061E → K in BAA93434. (PubMed:10984475)Curated
    Sequence conflicti563 – 5631K → E in BAA93434. (PubMed:10984475)Curated
    Sequence conflicti567 – 5671K → Q in BAA93434. (PubMed:10984475)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AABR03013307 Genomic DNA. No translation available.
    AABR03015957 Genomic DNA. No translation available.
    AB022331 mRNA. Translation: BAA93434.1. Sequence problems.
    UniGeneiRn.45385.

    Genome annotation databases

    UCSCiRGD:61973. rat. [Q9JMI9-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AABR03013307 Genomic DNA. No translation available.
    AABR03015957 Genomic DNA. No translation available.
    AB022331 mRNA. Translation: BAA93434.1 . Sequence problems.
    UniGenei Rn.45385.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-59688N.

    PTM databases

    PhosphoSitei Q9JMI9.

    Proteomic databases

    PRIDEi Q9JMI9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    UCSCi RGD:61973. rat. [Q9JMI9-1 ]

    Organism-specific databases

    RGDi 61973. Trpc3.

    Phylogenomic databases

    eggNOGi NOG254238.
    HOGENOMi HOG000020590.
    HOVERGENi HBG068337.
    PhylomeDBi Q9JMI9.

    Miscellaneous databases

    PROi Q9JMI9.

    Gene expression databases

    Genevestigatori Q9JMI9.

    Family and domain databases

    Gene3Di 1.25.40.20. 1 hit.
    InterProi IPR002110. Ankyrin_rpt.
    IPR020683. Ankyrin_rpt-contain_dom.
    IPR005821. Ion_trans_dom.
    IPR004729. TRP_channel.
    IPR013555. TRP_dom.
    IPR005459. TRPC3_channel.
    IPR002153. TRPC_channel.
    [Graphical view ]
    PANTHERi PTHR10117. PTHR10117. 1 hit.
    PTHR10117:SF8. PTHR10117:SF8. 1 hit.
    Pfami PF12796. Ank_2. 1 hit.
    PF00520. Ion_trans. 1 hit.
    PF08344. TRP_2. 1 hit.
    [Graphical view ]
    PRINTSi PR01097. TRNSRECEPTRP.
    PR01644. TRPCHANNEL3.
    SMARTi SM00248. ANK. 3 hits.
    [Graphical view ]
    SUPFAMi SSF48403. SSF48403. 1 hit.
    TIGRFAMsi TIGR00870. trp. 1 hit.
    PROSITEi PS50297. ANK_REP_REGION. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
      Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
      , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
      Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Brown Norway.
    2. "A calcium-activated cation current by an alternatively spliced form of Trp3 in the heart."
      Ohki G., Miyoshi T., Murata M., Ishibashi K., Imai M., Suzuki M.
      J. Biol. Chem. 275:39055-39060(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 133-836.
      Tissue: Heart.

    Entry informationi

    Entry nameiTRPC3_RAT
    AccessioniPrimary (citable) accession number: Q9JMI9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 20, 2001
    Last sequence update: May 26, 2009
    Last modified: October 1, 2014
    This is version 109 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3