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Q9QX29 (TRPC5_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Short transient receptor potential channel 5

Short name=TrpC5
Alternative name(s):
Capacitative calcium entry channel 2
Short name=CCE2
Transient receptor protein 5
Short name=TRP-5
Short name=mTRP5
Trp-related protein 5
Gene names
Name:Trpc5
Synonyms:Trp5, Trrp5
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length975 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Has also been shown to be calcium-selective. May also be activated by intracellular calcium store depletion.

Enzyme regulation

Calcium channel activity is enhanced by MYLK, that promotes its subcellular localization at the plasma membrane By similarity.

Subunit structure

Homotetramer and heterotetramer with TRPC1 and/or TRPC4 By similarity. Interacts (via C-terminus) with CABP1. Interacts with NHERF By similarity. Interacts with MX1 and RNF24 By similarity. Interacts with SESTD1 (via the spectrin 1 repeat) By similarity. Interacts with TRPC4AP. Ref.7 Ref.8

Subcellular location

Cell membrane; Multi-pass membrane protein By similarity.

Tissue specificity

Expressed almost exclusively in brain, in mitral cells of the olfactory bulb, in lateral cerebellar nuclei and in pyramidal neurons of the hippocampus. Very low levels detected in liver kidney, testis, and uterus. Ref.4

Sequence similarities

Belongs to the transient receptor (TC 1.A.4) family. STrpC subfamily. TRPC5 sub-subfamily. [View classification]

Contains 4 ANK repeats.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 975975Short transient receptor potential channel 5
PRO_0000215319

Regions

Topological domain1 – 330330Cytoplasmic Potential
Transmembrane331 – 35121Helical; Potential
Topological domain352 – 39847Extracellular Potential
Transmembrane399 – 41921Helical; Potential
Topological domain420 – 43718Cytoplasmic Potential
Transmembrane438 – 45821Helical; Potential
Topological domain459 – 47012Extracellular Potential
Transmembrane471 – 49121Helical; Potential
Topological domain492 – 51221Cytoplasmic Potential
Transmembrane513 – 53321Helical; Potential
Topological domain534 – 60370Extracellular Potential
Transmembrane604 – 62421Helical; Potential
Topological domain625 – 975351Cytoplasmic Potential
Repeat31 – 6030ANK 1
Repeat69 – 9729ANK 2
Repeat98 – 12427ANK 3
Repeat141 – 17030ANK 4
Region971 – 9733Essential for binding to NHERF PDZ domain By similarity
Compositional bias690 – 6934Poly-Arg

Amino acid modifications

Glycosylation4611N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q9QX29 [UniParc].

Last modified June 20, 2001. Version 2.
Checksum: DF9248168D3D2D62

FASTA975111,458
        10         20         30         40         50         60 
MAQLYYKKVN YSPYRDRIPL QIVRAETELS AEEKAFLSAV EKGDYATVKQ ALQEAEIYYN 

        70         80         90        100        110        120 
VNINCMDPLG RSALLIAIEN ENLEIMELLL NHSVYVGDAL LYAIRKEVVG AVELLLSYRK 

       130        140        150        160        170        180 
PSGEKQVPTL MMDTQFSEFT PDITPIMLAA HTNNYEIIKL LVQKRVTIPR PHQIRCNCVE 

       190        200        210        220        230        240 
CVSSSEVDSL RHSRSRLNIY KALASPSLIA LSSEDPILTA FRLGWELKEL SKVENEFKAE 

       250        260        270        280        290        300 
YEELSQQCKL FAKDLLDQAR SSRELEIILN HRDDHSEELD PQKYHDLAKL KVAIKYHQKE 

       310        320        330        340        350        360 
FVAQPNCQQL LATLWYDGFP GWRRKHWVVK LLTCMTIGFL FPMLSIAYLI SPRSNLGLFI 

       370        380        390        400        410        420 
KKPFIKFICH TASYLTFLFM LLLASQHIVR TDLHVQGPPP TVVEWMILPW VLGFIWGEIK 

       430        440        450        460        470        480 
EMWDGGFTEY IHDWWNLMDF AMNSLYLATI SLKIVAYVKY NGSRPREEWE MWHPTLIAEA 

       490        500        510        520        530        540 
LFAISNILSS LRLISLFTAN SHLGPLQISL GRMLLDILKF LFIYCLVLLA FANGLNQLYF 

       550        560        570        580        590        600 
YYETRAIDEP NNCKGIRCEK QNNAFSTLFE TLQSLFWSVF GLLNLYVTNV KARHEFTEFV 

       610        620        630        640        650        660 
GATMFGTYNV ISLVVLLNML IAMMNNSYQL IADHADIEWK FARTKLWMSY FDEGGTLPPP 

       670        680        690        700        710        720 
FNIIPSPKSF LYLGNWFNNT FCPKRDPDGR RRRHNLRSFT ERHADSLIQN QHYQEVIRNL 

       730        740        750        760        770        780 
VKRYVAAMIR NSKTNEGLTE ENFKELKQDI SSFRYEVLDL LGNRKHPRRS LSTSSADFSQ 

       790        800        810        820        830        840 
RDDTNDGSGG ARAKSKSVSF NVGCKKKACH GAPLIRTVPR ASGAQGKPKS ESSSKRSFMG 

       850        860        870        880        890        900 
PSFKKLGLFF SKFNGQTSEP TSEPMYTISD GIAQQHCMWQ DIRYSQMEKG KAEACSQSQM 

       910        920        930        940        950        960 
NLGEVELGEI RGAAARSSEC PLACSSSLHC ASGICSSNSK LLDSSEDVFE TWGEACDLLM 

       970 
HKWGDGQEEQ VTTRL 

« Hide

References

[1]"Molecular cloning and functional characterization of a novel receptor-activated TRP Ca2+ channel from mouse brain."
Okada T., Shimizu S., Wakamori M., Maeda A., Kurosaki T., Takada N., Imoto K., Mori Y.
J. Biol. Chem. 273:10279-10287(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[2]"Molecular cloning and functional expression of mouse TRP5."
Zhu X., Peyton M., Boulay B., Birnbaumer B.
Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Association of mammalian trp4 and phospholipase C isozymes with a PDZ domain-containing protein, NHERF."
Tang Y., Tang J., Chen Z., Trost C., Flockerzi V., Li M., Ramesh V., Zhu M.X.
J. Biol. Chem. 275:37559-37564(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"A novel capacitative calcium entry channel expressed in excitable cells."
Philipp S., Hambrecht J., Braslavski L., Schroth G., Freichel M., Murakami M., Cavalie A., Flockerzi V.
EMBO J. 17:4274-4282(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-966, TISSUE SPECIFICITY.
Tissue: Brain.
[5]Lubec G., Sunyer B., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 354-361, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: OF1.
Tissue: Hippocampus.
[6]"trp, a novel mammalian gene family essential for agonist-activated capacitative Ca2+ entry."
Zhu X., Jiang M., Peyton M., Boulay G., Hurst R., Stefani E., Birnbaumer L.
Cell 85:661-671(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 515-637.
[7]"Inhibition of TRPC5 channels by Ca2+-binding protein 1 in Xenopus oocytes."
Kinoshita-Kawada M., Tang J., Xiao R., Kaneko S., Foskett J.K., Zhu M.X.
Pflugers Arch. 450:345-354(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CABP1.
[8]"TRUSS, TNF-R1, and TRPC ion channels synergistically reverse endoplasmic reticulum Ca2+ storage reduction in response to m1 muscarinic acetylcholine receptor signaling."
Mace K.E., Lussier M.P., Boulay G., Terry-Powers J.L., Parfrey H., Perraud A.L., Riches D.W.H.
J. Cell. Physiol. 225:444-453(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TRPC4AP.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF029983 mRNA. Translation: AAC13550.1.
AF060107 mRNA. Translation: AAF02200.1.
AJ006204 mRNA. Translation: CAA06912.1.
CCDSCCDS30457.1.
RefSeqNP_033454.1. NM_009428.2.
UniGeneMm.328378.

3D structure databases

ProteinModelPortalQ9QX29.
SMRQ9QX29. Positions 35-169.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204331. 1 interaction.
MINTMINT-144678.

Chemistry

GuidetoPHARMACOLOGY490.

PTM databases

PhosphoSiteQ9QX29.

Proteomic databases

PRIDEQ9QX29.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000040184; ENSMUSP00000049063; ENSMUSG00000041710.
GeneID22067.
KEGGmmu:22067.
UCSCuc009umv.1. mouse.

Organism-specific databases

CTD7224.
MGIMGI:109524. Trpc5.

Phylogenomic databases

eggNOGNOG254238.
GeneTreeENSGT00680000099866.
HOGENOMHOG000020589.
HOVERGENHBG068337.
InParanoidQ9QX29.
KOK04968.
OMAPPLIRTM.
OrthoDBEOG72G17P.
PhylomeDBQ9QX29.
TreeFamTF313147.

Gene expression databases

BgeeQ9QX29.
GenevestigatorQ9QX29.

Family and domain databases

Gene3D1.25.40.20. 1 hit.
InterProIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR005821. Ion_trans_dom.
IPR004729. TRP_channel.
IPR013555. TRP_dom.
IPR005461. TRPC5_channel.
IPR002153. TRPC_channel.
[Graphical view]
PANTHERPTHR10117. PTHR10117. 1 hit.
PTHR10117:SF24. PTHR10117:SF24. 1 hit.
PfamPF00023. Ank. 1 hit.
PF12796. Ank_2. 1 hit.
PF00520. Ion_trans. 1 hit.
PF08344. TRP_2. 1 hit.
[Graphical view]
PRINTSPR01097. TRNSRECEPTRP.
PR01646. TRPCHANNEL5.
SMARTSM00248. ANK. 2 hits.
[Graphical view]
SUPFAMSSF48403. SSF48403. 1 hit.
TIGRFAMsTIGR00870. trp. 1 hit.
ProtoNetSearch...

Other

NextBio301888.
PROQ9QX29.
SOURCESearch...

Entry information

Entry nameTRPC5_MOUSE
AccessionPrimary (citable) accession number: Q9QX29
Secondary accession number(s): Q61059, Q9QWT1, Q9R0D4
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: June 20, 2001
Last modified: July 9, 2014
This is version 124 of the entry and version 2 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