ID TRPC5_RABIT Reviewed; 974 AA.
AC O62852;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 24-JAN-2024, entry version 141.
DE RecName: Full=Short transient receptor potential channel 5;
DE Short=Rtrp5;
DE Short=TrpC5;
DE AltName: Full=Capacitative calcium entry channel 2;
DE Short=CCE2;
GN Name=TRPC5; Synonyms=TRP5;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], 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).
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 (By similarity). {ECO:0000250|UniProtKB:Q9QX29,
CC ECO:0000250|UniProtKB:Q9UL62}.
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 with NHERF1 (By similarity). Interacts with MX1
CC and RNF24 (By similarity). Interacts (via C-terminus) with CABP1 (By
CC similarity). Interacts with SESTD1 (via the spectrin 1 repeat) (By
CC similarity). Interacts with TRPC4AP (By similarity). Interacts with
CC PLSCR1 (By similarity). {ECO:0000250|UniProtKB:Q9QX29,
CC ECO:0000250|UniProtKB:Q9UL62}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in brain. {ECO:0000269|PubMed:9687496}.
CC -!- SIMILARITY: Belongs to the transient receptor (TC 1.A.4) family. STrpC
CC subfamily. TRPC5 sub-subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ006203; CAA06911.1; -; mRNA.
DR RefSeq; NP_001076248.1; NM_001082779.1.
DR AlphaFoldDB; O62852; -.
DR SMR; O62852; -.
DR STRING; 9986.ENSOCUP00000007983; -.
DR GlyCosmos; O62852; 1 site, No reported glycans.
DR PaxDb; 9986-ENSOCUP00000007983; -.
DR Ensembl; ENSOCUT00000009246.2; ENSOCUP00000007983.2; ENSOCUG00000009245.2.
DR GeneID; 100009574; -.
DR KEGG; ocu:100009574; -.
DR CTD; 7224; -.
DR eggNOG; KOG3609; Eukaryota.
DR GeneTree; ENSGT01060000248594; -.
DR HOGENOM; CLU_005716_4_1_1; -.
DR InParanoid; O62852; -.
DR OMA; LCKWIHK; -.
DR OrthoDB; 5406916at2759; -.
DR TreeFam; TF313147; -.
DR Proteomes; UP000001811; Chromosome X.
DR Bgee; ENSOCUG00000009245; Expressed in kidney and 4 other cell types or tissues.
DR GO; GO:0034704; C:calcium channel complex; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005262; F:calcium channel activity; IEA:UniProtKB-KW.
DR GO; GO:0070679; F:inositol 1,4,5 trisphosphate binding; IEA:Ensembl.
DR GO; GO:0051402; P:neuron apoptotic process; ISS:UniProtKB.
DR GO; GO:0070782; P:phosphatidylserine exposure on apoptotic cell surface; ISS:UniProtKB.
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.
PE 2: Evidence at transcript level;
KW ANK repeat; Calcium; Calcium channel; Calcium transport; Cell membrane;
KW Glycoprotein; Ion channel; Ion transport; Membrane; Reference proteome;
KW Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..974
FT /note="Short transient receptor potential channel 5"
FT /id="PRO_0000215320"
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..974
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 811..838
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 972..974
FT /note="Essential for binding to NHERF1 PDZ domain"
FT /evidence="ECO:0000250|UniProtKB:Q9QX29"
FT CARBOHYD 461
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 974 AA; 111537 MW; 94256E0F2B925316 CRC64;
MAQLYYKKVN YSPYRDRIPL QIVRAETELS AEEKAFLNAV 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 LGNRKQPRRS LSTSSTELSQ
RDDTNDGSGG ARAKSKSVSF NLGCKKKACH GPPLIRTMPR ASGAQGKSKA ESSSKRSFMG
PSLKKLGLLF SKFNGHMSEP SSEPMYTISD GIVQQHYMWQ DIRYSQMEKG KAEACSQSEI
NLSEVELGEV RGAAQSSECP LTCSSSLHCA SSICSSNSKL LDSSEDVFET WGEACDLLMH
KWGDGQEEQV TTRL
//
