TPC1_HORVU
ID TPC1_HORVU Reviewed; 742 AA.
AC Q6S5H8;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=Two pore calcium channel protein 1;
DE AltName: Full=Voltage-dependent calcium channel protein TPC1;
DE Short=HvTPC1;
GN Name=TPC1;
OS Hordeum vulgare (Barley).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX NCBI_TaxID=4513;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Zhang Z., Qiu J.-L., Lindhart U., Thordal-Christensen H.;
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
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 (By
CC similarity). {ECO:0000250}.
CC -!- ACTIVITY REGULATION: Inhibited by Al(3+). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
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; AY465119; AAR27998.1; -; mRNA.
DR AlphaFoldDB; Q6S5H8; -.
DR SMR; Q6S5H8; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0000325; C:plant-type vacuole; IEA:EnsemblPlants.
DR GO; GO:0005774; C:vacuolar membrane; IEA:EnsemblPlants.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IEA:EnsemblPlants.
DR GO; GO:0005245; F:voltage-gated calcium channel activity; IEA:InterPro.
DR GO; GO:0019722; P:calcium-mediated signaling; IEA:EnsemblPlants.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0080141; P:regulation of jasmonic acid biosynthetic process; IEA:EnsemblPlants.
DR GO; GO:0010119; P:regulation of stomatal movement; IEA:EnsemblPlants.
DR GO; GO:0009845; P:seed germination; IEA:EnsemblPlants.
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; 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; Repeat; Transmembrane;
KW Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..742
FT /note="Two pore calcium channel protein 1"
FT /id="PRO_0000343170"
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 /evidence="ECO:0000250"
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 /evidence="ECO:0000250"
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..44
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; 85432 MW; C88CABCA58C5E6A0 CRC64;
MSEAQAPLIT EEAAERGLAS SGSRRLSDGG GGQGSRKYRR RSDALAHGDR YQKAAALVDL
AEDGVGIPED VLNDTRFGRA MSFYFVYLRL DWLWSLNIFA LILLNFLEKP LWCRKDALHA
CDQRDMYFLG QLPYFSKTES LIYEGLTLVI LVMEILCPLS YEGLNIFWRS TTNKLKILLL
FILACDILVF AFSSQPFRLA PYIRVVFLIM TIRELRMCAI TLAGLIGTYL NVLALSLLFL
LFASWLAYVT FEDTPQGKTI FSSYGVTLYQ MFVLFTTSNN PDVWVPAYKI SRWYSLFFIV
YVLLGVYFLT NLILAVIYDS FKEQFAKQLV QVDAIRKNIL QKAFELIDTN TRGYLDREQC
ISLLNELNKY RSLPKTSRED FELIFAELDR SGDFKVTSEE FADLCNTIAI KFQKEPPPSY
LEKFPFYHSP VCGRLKSFVR SRTFEYIIVF VLLINLVAVI IETTLDIENS SSQETWQEVE
FFLGWIYVAE MALKIFSLGF GAYWMEGQNK FDFVLTWTIF IGETLTFAFP SKLPFLSNGE
WIRYLLLGRV LRLTRILLQV QRFRVFVATF FTLMSSLMPY LGIVFCILCM YCSLGLQIFG
GIVYAGNPTL EETDLFSNDY LLFNFNDYPS GMVTLFNLLV MGNWQVWMES YWQLTGSSWS
LIYFVSFYLI SILLLLNLIV AFVLEAFFAE MELEKGEEVD IQSPTSGGIK KRRSMRVRSK
GTMVDILLHH MLSNELDGSQ NS
