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   24-JAN-2024, entry version 196.
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 NHERF1.
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   EMDB; EMD-9615; -.
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   GlyCosmos; Q9QX29; 1 site, No reported glycans.
DR   GlyGen; Q9QX29; 1 site.
DR   iPTMnet; Q9QX29; -.
DR   PhosphoSitePlus; Q9QX29; -.
DR   MaxQB; Q9QX29; -.
DR   PaxDb; 10090-ENSMUSP00000049063; -.
DR   ProteomicsDB; 300017; -.
DR   ABCD; Q9QX29; 1 sequenced antibody.
DR   Antibodypedia; 356; 337 antibodies from 32 providers.
DR   DNASU; 22067; -.
DR   Ensembl; ENSMUST00000040184.4; ENSMUSP00000049063.4; ENSMUSG00000041710.5.
DR   GeneID; 22067; -.
DR   KEGG; mmu:22067; -.
DR   UCSC; uc009umv.1; mouse.
DR   AGR; MGI:109524; -.
DR   CTD; 7224; -.
DR   MGI; MGI:109524; Trpc5.
DR   VEuPathDB; HostDB:ENSMUSG00000041710; -.
DR   eggNOG; KOG3609; Eukaryota.
DR   GeneTree; ENSGT01060000248594; -.
DR   HOGENOM; CLU_005716_4_1_1; -.
DR   InParanoid; Q9QX29; -.
DR   OMA; LCKWIHK; -.
DR   OrthoDB; 5406916at2759; -.
DR   PhylomeDB; Q9QX29; -.
DR   TreeFam; TF313147; -.
DR   Reactome; R-MMU-3295583; TRP channels.
DR   BioGRID-ORCS; 22067; 0 hits in 77 CRISPR screens.
DR   PRO; PR:Q9QX29; -.
DR   Proteomes; UP000000589; Chromosome X.
DR   RNAct; Q9QX29; Protein.
DR   Bgee; ENSMUSG00000041710; Expressed in supraoptic nucleus and 55 other cell types or tissues.
DR   ExpressionAtlas; Q9QX29; baseline and differential.
DR   GO; GO:0034704; C:calcium channel complex; ISO:MGI.
DR   GO; GO:0034703; C:cation channel complex; IBA:GO_Central.
DR   GO; GO:0030425; C:dendrite; ISO:MGI.
DR   GO; GO:0030426; C:growth cone; ISO:MGI.
DR   GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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: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; Ankyrin repeat-containing domain; 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   NCBIfam; TIGR00870; trp; 1.
DR   PANTHER; PTHR10117:SF76; SHORT TRANSIENT RECEPTOR POTENTIAL CHANNEL 5; 1.
DR   PANTHER; PTHR10117; TRANSIENT RECEPTOR POTENTIAL CHANNEL; 1.
DR   Pfam; PF00023; Ank; 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   SMART; SM01420; TRP_2; 1.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   Genevisible; Q9QX29; MM.
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 NHERF1 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
//