TRPC5_MOUSE
ID TRPC5_MOUSE Reviewed; 975 AA.
AC Q9QX29; Q61059; Q9QWT1; Q9R0D4;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Short transient receptor potential channel 5;
DE Short=TrpC5;
DE AltName: Full=Capacitative calcium entry channel 2;
DE Short=CCE2;
DE AltName: Full=Transient receptor protein 5;
DE Short=TRP-5;
DE Short=mTRP5;
DE AltName: Full=Trp-related protein 5;
GN Name=Trpc5; Synonyms=Trp5, Trrp5;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=9553080; DOI=10.1074/jbc.273.17.10279;
RA Okada T., Shimizu S., Wakamori M., Maeda A., Kurosaki T., Takada N.,
RA Imoto K., Mori Y.;
RT "Molecular cloning and functional characterization of a novel receptor-
RT activated TRP Ca2+ channel from mouse brain.";
RL J. Biol. Chem. 273:10279-10287(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Zhu X., Peyton M., Boulay B., Birnbaumer B.;
RT "Molecular cloning and functional expression of mouse TRP5.";
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH SLC9A3R1.
RX PubMed=10980202; DOI=10.1074/jbc.m006635200;
RA Tang Y., Tang J., Chen Z., Trost C., Flockerzi V., Li M., Ramesh V.,
RA Zhu M.X.;
RT "Association of mammalian trp4 and phospholipase C isozymes with a PDZ
RT domain-containing protein, NHERF.";
RL J. Biol. Chem. 275:37559-37564(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-966, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=9687496; DOI=10.1093/emboj/17.15.4274;
RA Philipp S., Hambrecht J., Braslavski L., Schroth G., Freichel M.,
RA Murakami M., Cavalie A., Flockerzi V.;
RT "A novel capacitative calcium entry channel expressed in excitable cells.";
RL EMBO J. 17:4274-4282(1998).
RN [5]
RP PROTEIN SEQUENCE OF 354-361, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 515-637.
RX PubMed=8646775; DOI=10.1016/s0092-8674(00)81233-7;
RA Zhu X., Jiang M., Peyton M., Boulay G., Hurst R., Stefani E.,
RA Birnbaumer L.;
RT "trp, a novel mammalian gene family essential for agonist-activated
RT capacitative Ca2+ entry.";
RL Cell 85:661-671(1996).
RN [7]
RP INTERACTION WITH CABP1.
RX PubMed=15895247; DOI=10.1007/s00424-005-1419-1;
RA Kinoshita-Kawada M., Tang J., Xiao R., Kaneko S., Foskett J.K., Zhu M.X.;
RT "Inhibition of TRPC5 channels by Ca2+-binding protein 1 in Xenopus
RT oocytes.";
RL Pflugers Arch. 450:345-354(2005).
RN [8]
RP INTERACTION WITH TRPC4AP.
RX PubMed=20458742; DOI=10.1002/jcp.22221;
RA Mace K.E., Lussier M.P., Boulay G., Terry-Powers J.L., Parfrey H.,
RA Perraud A.L., Riches D.W.H.;
RT "TRUSS, TNF-R1, and TRPC ion channels synergistically reverse endoplasmic
RT reticulum Ca2+ storage reduction in response to m1 muscarinic acetylcholine
RT receptor signaling.";
RL J. Cell. Physiol. 225:444-453(2010).
RN [9]
RP FUNCTION, AND INTERACTION WITH PLSCR1.
RX PubMed=32110987; DOI=10.3390/cells9030547;
RA Guo J., Li J., Xia L., Wang Y., Zhu J., Du J., Lu Y., Liu G., Yao X.,
RA Shen B.;
RT "Transient Receptor Potential Canonical 5-Scramblase Signaling Complex
RT Mediates Neuronal Phosphatidylserine Externalization and Apoptosis.";
RL Cells 9:0-0(2020).
CC -!- FUNCTION: Thought to form a receptor-activated non-selective calcium
CC permeant cation channel. Probably is operated by a phosphatidylinositol
CC second messenger system activated by receptor tyrosine kinases or G-
CC protein coupled receptors. Has also been shown to be calcium-selective.
CC May also be activated by intracellular calcium store depletion (By
CC similarity). Mediates calcium-dependent phosphatidylserine
CC externalization and apoptosis in neurons via its association with
CC PLSCR1 (PubMed:32110987). {ECO:0000250|UniProtKB:Q9UL62,
CC ECO:0000269|PubMed:32110987}.
CC -!- ACTIVITY REGULATION: Calcium channel activity is enhanced by MYLK, that
CC promotes its subcellular localization at the plasma membrane.
CC {ECO:0000250}.
CC -!- SUBUNIT: Homotetramer and heterotetramer with TRPC1 and/or TRPC4 (By
CC similarity). Interacts (via C-terminus) with CABP1 (PubMed:15895247).
CC Interacts with SLC9A3R1/NHERF (PubMed:10980202). Interacts with MX1 and
CC RNF24 (By similarity). Interacts with SESTD1 (via the spectrin 1
CC repeat) (By similarity). Interacts with TRPC4AP (PubMed:20458742).
CC Interacts with PLSCR1 (PubMed:32110987). {ECO:0000250|UniProtKB:Q9UL62,
CC ECO:0000269|PubMed:10980202, ECO:0000269|PubMed:15895247,
CC ECO:0000269|PubMed:20458742, ECO:0000269|PubMed:32110987}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed almost exclusively in brain, in mitral
CC cells of the olfactory bulb, in lateral cerebellar nuclei and in
CC pyramidal neurons of the hippocampus. Very low levels detected in liver
CC kidney, testis, and uterus. {ECO:0000269|PubMed:9687496}.
CC -!- SIMILARITY: Belongs to the transient receptor (TC 1.A.4) family. STrpC
CC subfamily. TRPC5 sub-subfamily. {ECO:0000305}.
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DR EMBL; AF029983; AAC13550.1; -; mRNA.
DR EMBL; AF060107; AAF02200.1; -; mRNA.
DR EMBL; AJ006204; CAA06912.1; -; mRNA.
DR CCDS; CCDS30457.1; -.
DR RefSeq; NP_033454.1; NM_009428.3.
DR PDB; 6AEI; EM; 2.89 A; A/B/C/D=1-765.
DR PDBsum; 6AEI; -.
DR AlphaFoldDB; Q9QX29; -.
DR SMR; Q9QX29; -.
DR BioGRID; 204331; 2.
DR DIP; DIP-40847N; -.
DR IntAct; Q9QX29; 2.
DR MINT; Q9QX29; -.
DR STRING; 10090.ENSMUSP00000049063; -.
DR BindingDB; Q9QX29; -.
DR ChEMBL; CHEMBL4523481; -.
DR GuidetoPHARMACOLOGY; 490; -.
DR GlyGen; Q9QX29; 1 site.
DR iPTMnet; Q9QX29; -.
DR PhosphoSitePlus; Q9QX29; -.
DR MaxQB; Q9QX29; -.
DR PaxDb; Q9QX29; -.
DR PRIDE; Q9QX29; -.
DR ProteomicsDB; 300017; -.
DR ABCD; Q9QX29; 1 sequenced antibody.
DR Antibodypedia; 356; 306 antibodies from 32 providers.
DR DNASU; 22067; -.
DR Ensembl; ENSMUST00000040184; ENSMUSP00000049063; ENSMUSG00000041710.
DR GeneID; 22067; -.
DR KEGG; mmu:22067; -.
DR UCSC; uc009umv.1; mouse.
DR CTD; 7224; -.
DR MGI; MGI:109524; Trpc5.
DR VEuPathDB; HostDB:ENSMUSG00000041710; -.
DR eggNOG; KOG3609; Eukaryota.
DR GeneTree; ENSGT01050000244831; -.
DR HOGENOM; CLU_005716_4_1_1; -.
DR InParanoid; Q9QX29; -.
DR OMA; ACSQSEM; -.
DR OrthoDB; 824310at2759; -.
DR PhylomeDB; Q9QX29; -.
DR TreeFam; TF313147; -.
DR Reactome; R-MMU-3295583; TRP channels.
DR BioGRID-ORCS; 22067; 0 hits in 72 CRISPR screens.
DR PRO; PR:Q9QX29; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q9QX29; protein.
DR Bgee; ENSMUSG00000041710; Expressed in supraoptic nucleus and 54 other tissues.
DR ExpressionAtlas; Q9QX29; baseline and differential.
DR Genevisible; Q9QX29; MM.
DR GO; GO:0034704; C:calcium channel complex; ISO:MGI.
DR GO; GO:0034703; C:cation channel complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0030426; C:growth cone; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0003779; F:actin binding; ISO:MGI.
DR GO; GO:0042805; F:actinin binding; ISO:MGI.
DR GO; GO:0051117; F:ATPase binding; ISO:MGI.
DR GO; GO:0005262; F:calcium channel activity; ISO:MGI.
DR GO; GO:0030276; F:clathrin binding; ISO:MGI.
DR GO; GO:0070679; F:inositol 1,4,5 trisphosphate binding; IDA:BHF-UCL.
DR GO; GO:0015279; F:store-operated calcium channel activity; IBA:GO_Central.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0006828; P:manganese ion transport; IBA:GO_Central.
DR GO; GO:0050774; P:negative regulation of dendrite morphogenesis; ISO:MGI.
DR GO; GO:0051402; P:neuron apoptotic process; IMP:UniProtKB.
DR GO; GO:0030182; P:neuron differentiation; IEA:Ensembl.
DR GO; GO:0070782; P:phosphatidylserine exposure on apoptotic cell surface; IMP:UniProtKB.
DR GO; GO:0045773; P:positive regulation of axon extension; ISO:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISO:MGI.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; ISO:MGI.
DR GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; ISO:MGI.
DR GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; IBA:GO_Central.
DR GO; GO:1902630; P:regulation of membrane hyperpolarization; ISO:MGI.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR013555; TRP_dom.
DR InterPro; IPR005461; TRPC5_channel.
DR InterPro; IPR002153; TRPC_channel.
DR PANTHER; PTHR10117; PTHR10117; 1.
DR PANTHER; PTHR10117:SF76; PTHR10117:SF76; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR Pfam; PF08344; TRP_2; 1.
DR PRINTS; PR01097; TRNSRECEPTRP.
DR PRINTS; PR01646; TRPCHANNEL5.
DR SMART; SM00248; ANK; 2.
DR SUPFAM; SSF48403; SSF48403; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ANK repeat; Calcium; Calcium channel; Calcium transport;
KW Cell membrane; Direct protein sequencing; Glycoprotein; Ion channel;
KW Ion transport; Membrane; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..975
FT /note="Short transient receptor potential channel 5"
FT /id="PRO_0000215319"
FT TOPO_DOM 1..330
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 331..351
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 352..398
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 399..419
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 420..437
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 438..458
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 459..470
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 471..491
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 492..512
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 513..533
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 534..603
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 604..624
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 625..975
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 31..60
FT /note="ANK 1"
FT REPEAT 69..97
FT /note="ANK 2"
FT REPEAT 98..124
FT /note="ANK 3"
FT REPEAT 141..170
FT /note="ANK 4"
FT REGION 766..795
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 816..838
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 971..973
FT /note="Essential for binding to SLC9A3R1 PDZ domain"
FT /evidence="ECO:0000269|PubMed:10980202"
FT COMPBIAS 767..795
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 461
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT HELIX 31..39
FT /evidence="ECO:0007829|PDB:6AEI"
FT TURN 40..43
FT /evidence="ECO:0007829|PDB:6AEI"
FT HELIX 47..57
FT /evidence="ECO:0007829|PDB:6AEI"
FT STRAND 58..61
FT /evidence="ECO:0007829|PDB:6AEI"
FT HELIX 73..79
FT /evidence="ECO:0007829|PDB:6AEI"
FT HELIX 83..90
FT /evidence="ECO:0007829|PDB:6AEI"
FT HELIX 100..105
FT /evidence="ECO:0007829|PDB:6AEI"
FT HELIX 111..116
FT /evidence="ECO:0007829|PDB:6AEI"
FT HELIX 145..152
FT /evidence="ECO:0007829|PDB:6AEI"
FT HELIX 155..162
FT /evidence="ECO:0007829|PDB:6AEI"
FT TURN 163..165
FT /evidence="ECO:0007829|PDB:6AEI"
FT HELIX 190..203
FT /evidence="ECO:0007829|PDB:6AEI"
FT TURN 206..210
FT /evidence="ECO:0007829|PDB:6AEI"
FT HELIX 216..233
FT /evidence="ECO:0007829|PDB:6AEI"
FT HELIX 238..257
FT /evidence="ECO:0007829|PDB:6AEI"
FT HELIX 262..269
FT /evidence="ECO:0007829|PDB:6AEI"
FT HELIX 288..295
FT /evidence="ECO:0007829|PDB:6AEI"
FT HELIX 299..302
FT /evidence="ECO:0007829|PDB:6AEI"
FT HELIX 305..315
FT /evidence="ECO:0007829|PDB:6AEI"
FT TURN 316..318
FT /evidence="ECO:0007829|PDB:6AEI"
FT HELIX 327..339
FT /evidence="ECO:0007829|PDB:6AEI"
FT HELIX 341..345
FT /evidence="ECO:0007829|PDB:6AEI"
FT TURN 347..349
FT /evidence="ECO:0007829|PDB:6AEI"
FT STRAND 352..354
FT /evidence="ECO:0007829|PDB:6AEI"
FT TURN 355..359
FT /evidence="ECO:0007829|PDB:6AEI"
FT STRAND 360..363
FT /evidence="ECO:0007829|PDB:6AEI"
FT HELIX 364..367
FT /evidence="ECO:0007829|PDB:6AEI"
FT TURN 368..370
FT /evidence="ECO:0007829|PDB:6AEI"
FT HELIX 371..384
FT /evidence="ECO:0007829|PDB:6AEI"
FT STRAND 395..397
FT /evidence="ECO:0007829|PDB:6AEI"
FT HELIX 402..423
FT /evidence="ECO:0007829|PDB:6AEI"
FT HELIX 429..432
FT /evidence="ECO:0007829|PDB:6AEI"
FT HELIX 434..457
FT /evidence="ECO:0007829|PDB:6AEI"
FT HELIX 466..468
FT /evidence="ECO:0007829|PDB:6AEI"
FT HELIX 474..490
FT /evidence="ECO:0007829|PDB:6AEI"
FT HELIX 492..497
FT /evidence="ECO:0007829|PDB:6AEI"
FT TURN 501..503
FT /evidence="ECO:0007829|PDB:6AEI"
FT HELIX 504..539
FT /evidence="ECO:0007829|PDB:6AEI"
FT HELIX 540..542
FT /evidence="ECO:0007829|PDB:6AEI"
FT HELIX 546..548
FT /evidence="ECO:0007829|PDB:6AEI"
FT HELIX 550..552
FT /evidence="ECO:0007829|PDB:6AEI"
FT STRAND 555..560
FT /evidence="ECO:0007829|PDB:6AEI"
FT STRAND 564..567
FT /evidence="ECO:0007829|PDB:6AEI"
FT HELIX 568..577
FT /evidence="ECO:0007829|PDB:6AEI"
FT TURN 578..582
FT /evidence="ECO:0007829|PDB:6AEI"
FT HELIX 585..588
FT /evidence="ECO:0007829|PDB:6AEI"
FT HELIX 595..613
FT /evidence="ECO:0007829|PDB:6AEI"
FT HELIX 616..634
FT /evidence="ECO:0007829|PDB:6AEI"
FT TURN 635..637
FT /evidence="ECO:0007829|PDB:6AEI"
FT HELIX 638..648
FT /evidence="ECO:0007829|PDB:6AEI"
FT STRAND 651..653
FT /evidence="ECO:0007829|PDB:6AEI"
FT TURN 658..662
FT /evidence="ECO:0007829|PDB:6AEI"
FT HELIX 708..735
FT /evidence="ECO:0007829|PDB:6AEI"
FT HELIX 740..760
FT /evidence="ECO:0007829|PDB:6AEI"
SQ SEQUENCE 975 AA; 111458 MW; DF9248168D3D2D62 CRC64;
MAQLYYKKVN YSPYRDRIPL QIVRAETELS AEEKAFLSAV EKGDYATVKQ ALQEAEIYYN
VNINCMDPLG RSALLIAIEN ENLEIMELLL NHSVYVGDAL LYAIRKEVVG AVELLLSYRK
PSGEKQVPTL MMDTQFSEFT PDITPIMLAA HTNNYEIIKL LVQKRVTIPR PHQIRCNCVE
CVSSSEVDSL RHSRSRLNIY KALASPSLIA LSSEDPILTA FRLGWELKEL SKVENEFKAE
YEELSQQCKL FAKDLLDQAR SSRELEIILN HRDDHSEELD PQKYHDLAKL KVAIKYHQKE
FVAQPNCQQL LATLWYDGFP GWRRKHWVVK LLTCMTIGFL FPMLSIAYLI SPRSNLGLFI
KKPFIKFICH TASYLTFLFM LLLASQHIVR TDLHVQGPPP TVVEWMILPW VLGFIWGEIK
EMWDGGFTEY IHDWWNLMDF AMNSLYLATI SLKIVAYVKY NGSRPREEWE MWHPTLIAEA
LFAISNILSS LRLISLFTAN SHLGPLQISL GRMLLDILKF LFIYCLVLLA FANGLNQLYF
YYETRAIDEP NNCKGIRCEK QNNAFSTLFE TLQSLFWSVF GLLNLYVTNV KARHEFTEFV
GATMFGTYNV ISLVVLLNML IAMMNNSYQL IADHADIEWK FARTKLWMSY FDEGGTLPPP
FNIIPSPKSF LYLGNWFNNT FCPKRDPDGR RRRHNLRSFT ERHADSLIQN QHYQEVIRNL
VKRYVAAMIR NSKTNEGLTE ENFKELKQDI SSFRYEVLDL LGNRKHPRRS LSTSSADFSQ
RDDTNDGSGG ARAKSKSVSF NVGCKKKACH GAPLIRTVPR ASGAQGKPKS ESSSKRSFMG
PSFKKLGLFF SKFNGQTSEP TSEPMYTISD GIAQQHCMWQ DIRYSQMEKG KAEACSQSQM
NLGEVELGEI RGAAARSSEC PLACSSSLHC ASGICSSNSK LLDSSEDVFE TWGEACDLLM
HKWGDGQEEQ VTTRL
