TPC1_WHEAT
ID TPC1_WHEAT Reviewed; 742 AA.
AC Q6YLX9;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Two pore calcium channel protein 1;
DE AltName: Full=Voltage-dependent calcium channel protein TPC1;
DE Short=TaTPC1;
GN Name=TPC1;
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Chinese Spring;
RX PubMed=16275671; DOI=10.1093/jxb/eri302;
RA Wang Y.-J., Yu J.-N., Chen T., Zhang Z.-G., Hao Y.-J., Zhang J.-S.,
RA Chen S.-Y.;
RT "Functional analysis of a putative Ca(2+) channel gene TaTPC1 from wheat.";
RL J. Exp. Bot. 56:3051-3060(2005).
CC -!- FUNCTION: Functions as a voltage-gated inward-rectifying Ca(2+) channel
CC (VDCC) across the plasma membrane that mediates sucrose-induced Ca(2+)
CC influx in autotrophically grown leaf cells. Acts as the major ROS-
CC responsive Ca(2+) channel and is the possible target of Al-dependent
CC inhibition. Plays a regulatory role in defense responses.
CC -!- ACTIVITY REGULATION: Inhibited by Al(3+). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:16275671}; Multi-
CC pass membrane protein {ECO:0000269|PubMed:16275671}.
CC -!- INDUCTION: By high salinity, PEG, cold shock, and abscisic acid (ABA).
CC {ECO:0000269|PubMed:16275671}.
CC -!- DOMAIN: Each of the two internal repeats contains five hydrophobic
CC transmembrane segments (S1, S2, S3, S5, S6) and one positively charged
CC transmembrane segment (S4). S4 segments probably represent the voltage-
CC sensor and are characterized by a series of positively charged amino
CC acids (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit (TC
CC 1.A.1.11) family. Two pore calcium channel subfamily. {ECO:0000305}.
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DR EMBL; AY114121; AAM47032.1; -; mRNA.
DR AlphaFoldDB; Q6YLX9; -.
DR SMR; Q6YLX9; -.
DR STRING; 4565.Traes_3DL_A58F69E34.1; -.
DR PRIDE; Q6YLX9; -.
DR eggNOG; KOG2301; Eukaryota.
DR Proteomes; UP000019116; Unplaced.
DR ExpressionAtlas; Q6YLX9; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0000325; C:plant-type vacuole; IBA:GO_Central.
DR GO; GO:0005774; C:vacuolar membrane; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005245; F:voltage-gated calcium channel activity; IBA:GO_Central.
DR GO; GO:0006816; P:calcium ion transport; IBA:GO_Central.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR CDD; cd00051; EFh; 1.
DR Gene3D; 1.20.120.350; -; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR044581; TPC1_plant.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR46988; PTHR46988; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR Pfam; PF00520; Ion_trans; 2.
DR SMART; SM00054; EFh; 2.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS50222; EF_HAND_2; 2.
PE 2: Evidence at transcript level;
KW Calcium; Calcium channel; Calcium transport; Glycoprotein; Ion channel;
KW Ion transport; Membrane; Plant defense; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..742
FT /note="Two pore calcium channel protein 1"
FT /id="PRO_0000343173"
FT TOPO_DOM 1..82
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 83..103
FT /note="Helical; Name=S1 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 104..140
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 141..161
FT /note="Helical; Name=S2 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 162..176
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 177..197
FT /note="Helical; Name=S3 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 198..204
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 205..226
FT /note="Helical; Voltage-sensor; Name=S4 of repeat I"
FT /evidence="ECO:0000255"
FT TRANSMEM 227..247
FT /note="Helical; Name=S5 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 248..258
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT INTRAMEM 259..273
FT /note="Pore-forming; Name=Pore-forming 1"
FT TOPO_DOM 274..296
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 297..317
FT /note="Helical; Name=S6 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 318..446
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 447..467
FT /note="Helical; Name=S1 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 468..480
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 481..501
FT /note="Helical; Name=S2 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 502..510
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 511..531
FT /note="Helical; Name=S3 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 532..540
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 541..558
FT /note="Helical; Voltage-sensor; Name=S4 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 559..582
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 583..603
FT /note="Helical; Name=S5 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 604..627
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT INTRAMEM 628..642
FT /note="Pore-forming; Name=Pore-forming 2"
FT TOPO_DOM 643..663
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 664..684
FT /note="Helical; Name=S6 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 685..742
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 335..370
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 376..411
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 469
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 742 AA; 85647 MW; 0E9DC42C4E445A10 CRC64;
MSEAEAPLIT EEAAERGLAS SGSRRLSDGA GGQGSRKYRR RSDALAYGDR YQKAAALVDL
AEDGVGIPED VLNDTRFGRA MSFYFVYLRL DWLWSLNLFA LILLNFLEKP LWCRKDALQA
YDQRDLYFLG QLPYFSKTES LIYEGLTLVI LVMDIFCPLS YEGLNIFWRS TTNKLKIVLL
FILACDILVF AFSSQPFRLA PYIRVVFLIM TIRELRMCAI TLAGLIGTYL NVLALSLLFL
LFASWLAYVT FEDTPQGKTI FSSYGVTLYQ MFVLFTTSNN PDVWVHAYKI PRWYSLFFIV
YVLLGVYFLT NLILAVIYDS FKEQFAKQLV QVDSIRKNIL QKAFDLIDTN NRGYLDREQC
ISLLNELNKY RSLPKTSRED FELIFAELDR SGDFKVTSEE FADLCNTIAI KFQKEPPPSY
LEKFPFYHSP LCGRLKSFVR SRMFEYIIVF VLLINLVAVI IETTLDIENS SSQETWQEVE
FFLGWIYVAE MALKIFSLGF GAYWMEGQNK FDFVLTWTIF IGETLTFAFP SKLPFLSNGE
WIRYLLLGRV LRLTRILLQV QRFRAFVATF FTLMSSLMPY LGIVFCVLCM YCSIGLQIFG
GIVYAGNPTL EETDLFNNDY LLFNFNDYPS GMVTLFNLLV MGNWQVWMES YWQLTGTSWS
LIYFVSFYLI SILLLLNLIV AFVLEAFFAE MELEKGEEVD IQNPTSGGIK KRRSMRVRSK
GTMVDILLHH MLSNELDGSQ NS
