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Database: UniProt
Entry: TPC1_WHEAT
LinkDB: TPC1_WHEAT
Original site: 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   25-OCT-2017, entry version 78.
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; Magnoliophyta; 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
RT   wheat.";
RL   J. Exp. Bot. 56:3051-3060(2005).
CC   -!- FUNCTION: Functions as a voltage-gated inward-rectifying Ca(2+)
CC       channel (VDCC) across the plasma membrane that mediates sucrose-
CC       induced Ca(2+) influx in autotrophically grown leaf cells. Acts as
CC       the major ROS-responsive Ca(2+) channel and is the possible target
CC       of Al-dependent inhibition. Plays a regulatory role in defense
CC       responses.
CC   -!- ENZYME REGULATION: Inhibited by Al(3+). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:16275671};
CC       Multi-pass membrane protein {ECO:0000269|PubMed:16275671}.
CC   -!- INDUCTION: By high salinity, PEG, cold shock, and abscisic acid
CC       (ABA). {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
CC       charged transmembrane segment (S4). S4 segments probably represent
CC       the voltage-sensor and are characterized by a series of positively
CC       charged amino 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.
CC       {ECO:0000305}.
DR   EMBL; AY114121; AAM47032.1; -; mRNA.
DR   UniGene; Ta.46666; -.
DR   ProteinModelPortal; Q6YLX9; -.
DR   Proteomes; UP000019116; Unplaced.
DR   ExpressionAtlas; Q6YLX9; baseline.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005245; F:voltage-gated calcium channel activity; IEA:InterPro.
DR   GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR   CDD; cd00051; EFh; 1.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR028801; TPC1.
DR   PANTHER; PTHR10037:SF231; PTHR10037:SF231; 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; Complete proteome;
KW   Glycoprotein; Ion channel; Ion transport; Membrane; Plant defense;
KW   Reference proteome; Repeat; Transmembrane; Transmembrane helix;
KW   Transport; Voltage-gated channel.
FT   CHAIN         1    742       Two pore calcium channel protein 1.
FT                                /FTId=PRO_0000343173.
FT   TOPO_DOM      1     82       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM     83    103       Helical; Name=S1 of repeat I.
FT                                {ECO:0000255}.
FT   TOPO_DOM    104    140       Extracellular. {ECO:0000255}.
FT   TRANSMEM    141    161       Helical; Name=S2 of repeat I.
FT                                {ECO:0000255}.
FT   TOPO_DOM    162    176       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    177    197       Helical; Name=S3 of repeat I.
FT                                {ECO:0000255}.
FT   TOPO_DOM    198    204       Extracellular. {ECO:0000255}.
FT   TRANSMEM    205    226       Helical; Voltage-sensor; Name=S4 of
FT                                repeat I. {ECO:0000255}.
FT   TRANSMEM    227    247       Helical; Name=S5 of repeat I.
FT                                {ECO:0000255}.
FT   TOPO_DOM    248    258       Extracellular. {ECO:0000255}.
FT   INTRAMEM    259    273       Pore-forming; Name=Pore-forming 1.
FT   TOPO_DOM    274    296       Extracellular. {ECO:0000255}.
FT   TRANSMEM    297    317       Helical; Name=S6 of repeat I.
FT                                {ECO:0000255}.
FT   TOPO_DOM    318    446       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    447    467       Helical; Name=S1 of repeat II.
FT                                {ECO:0000255}.
FT   TOPO_DOM    468    480       Extracellular. {ECO:0000255}.
FT   TRANSMEM    481    501       Helical; Name=S2 of repeat II.
FT                                {ECO:0000255}.
FT   TOPO_DOM    502    510       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    511    531       Helical; Name=S3 of repeat II.
FT                                {ECO:0000255}.
FT   TOPO_DOM    532    540       Extracellular. {ECO:0000255}.
FT   TRANSMEM    541    558       Helical; Voltage-sensor; Name=S4 of
FT                                repeat II. {ECO:0000255}.
FT   TOPO_DOM    559    582       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    583    603       Helical; Name=S5 of repeat II.
FT                                {ECO:0000255}.
FT   TOPO_DOM    604    627       Extracellular. {ECO:0000255}.
FT   INTRAMEM    628    642       Pore-forming; Name=Pore-forming 2.
FT   TOPO_DOM    643    663       Extracellular. {ECO:0000255}.
FT   TRANSMEM    664    684       Helical; Name=S6 of repeat II.
FT                                {ECO:0000255}.
FT   TOPO_DOM    685    742       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      335    370       EF-hand 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00448}.
FT   DOMAIN      376    411       EF-hand 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00448}.
FT   COMPBIAS    673    678       Poly-Leu.
FT   CARBOHYD    469    469       N-linked (GlcNAc...) asparagine.
FT                                {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
//
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