TPC1A_TOBAC
ID TPC1A_TOBAC Reviewed; 735 AA.
AC Q75VR1;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=Two pore calcium channel protein 1A;
DE AltName: Full=Voltage-dependent calcium channel protein TPC1A;
DE Short=NtTPC1A;
GN Name=TPC1A;
OS Nicotiana tabacum (Common tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4097;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Bright Yellow 2;
RX PubMed=15081414; DOI=10.1016/j.bbrc.2004.03.114;
RA Kadota Y., Furuichi T., Ogasawara Y., Goh T., Higashi K., Muto S.,
RA Kuchitsu K.;
RT "Identification of putative voltage-dependent Ca(2+)-permeable channels
RT involved in cryptogein-induced Ca(2+) transients and defense responses in
RT tobacco BY-2 cells.";
RL Biochem. Biophys. Res. Commun. 317:823-830(2004).
RN [2]
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=15464979; DOI=10.1016/j.bbrc.2004.09.015;
RA Kawano T., Kadono T., Fumoto K., Lapeyrie F., Kuse M., Isobe M.,
RA Furuichi T., Muto S.;
RT "Aluminum as a specific inhibitor of plant TPC1 Ca(2+) channels.";
RL Biochem. Biophys. Res. Commun. 324:40-45(2004).
RN [3]
RP ACTIVITY REGULATION.
RX PubMed=15913561; DOI=10.1016/j.bbrc.2005.05.030;
RA Lin C., Yu Y., Kadono T., Iwata M., Umemura K., Furuichi T., Kuse M.,
RA Isobe M., Yamamoto Y., Matsumoto H., Yoshizuka K., Kawano T.;
RT "Action of aluminum, novel TPC1-type channel inhibitor, against salicylate-
RT induced and cold-shock-induced calcium influx in tobacco BY-2 cells.";
RL Biochem. Biophys. Res. Commun. 332:823-830(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 {ECO:0000269|PubMed:15464979}.
CC -!- ACTIVITY REGULATION: Inhibited by Al(3+), La(3+) and Gd(3+). Up-
CC regulated by H(2)O(2), cryptogein, salicylic acid (SA) and cold shock.
CC {ECO:0000269|PubMed:15464979, ECO:0000269|PubMed:15913561}.
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 -!- MISCELLANEOUS: Rescues the Ca(2+) uptake activity in yeast mutant cch1.
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; AB124646; BAD15099.1; -; mRNA.
DR RefSeq; NP_001311995.1; NM_001325066.1.
DR RefSeq; XP_016445355.1; XM_016589869.1.
DR AlphaFoldDB; Q75VR1; -.
DR SMR; Q75VR1; -.
DR GeneID; 107770546; -.
DR KEGG; nta:107770546; -.
DR OMA; FTESIEM; -.
DR OrthoDB; 761764at2759; -.
DR Proteomes; UP000084051; Unplaced.
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; 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..735
FT /note="Two pore calcium channel protein 1A"
FT /id="PRO_0000343171"
FT TOPO_DOM 1..67
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 68..88
FT /note="Helical; Name=S1 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 89..125
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..146
FT /note="Helical; Name=S2 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 147..161
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 162..182
FT /note="Helical; Name=S3 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 183
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 184..202
FT /note="Helical; Voltage-sensor; Name=S4 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 203..208
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 209..229
FT /note="Helical; Name=S5 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 230..248
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT INTRAMEM 249..263
FT /note="Pore-forming; Name=Pore-forming 1"
FT TOPO_DOM 264..286
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 287..307
FT /note="Helical; Name=S6 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 308..431
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 432..452
FT /note="Helical; Name=S1 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 453..470
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 471..491
FT /note="Helical; Name=S2 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 492..503
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 504..524
FT /note="Helical; Name=S3 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 525..531
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 532..549
FT /note="Helical; Voltage-sensor; Name=S4 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 550..560
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 561..581
FT /note="Helical; Name=S5 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 582..618
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT INTRAMEM 619..633
FT /note="Pore-forming; Name=Pore-forming 2"
FT TOPO_DOM 634..654
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 655..675
FT /note="Helical; Name=S6 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 676..735
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 325..360
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 366..401
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT CARBOHYD 460
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 735 AA; 84914 MW; FAC54932608E25F9 CRC64;
MEEYLLSGES SNSGRTRRRI GSIFDRRDAI AHGSAYQKAA ALVDLAEDGI GLPEEILEGA
SFEKAAELYF IFTRFDFLWS LNYLALVVLN FFEKPLWCSK HLAESCNNRD YYYLGELPFL
TGAESLIFEG VTLLLLIIHI LFPISYEGFN LYWRSLLNRV KVILLLILVA DIVVYILFLA
DFYYLPFRIA PYLRVVFFIL NIRELRDSFF ILAGMLGTYL NVVALSALFL LFSSWLAYVF
FEDTRQGKTT FTSYGTTLYQ MFVLFTTSNN PDVWIPAYKD SRWYCLFFVL YVLLGVYFVT
NLILAVVYDS FKSELVKQVA DKDRLRLRTL KKAFSLIDEA NNGHLNEKQC TLLFEELNKY
RTLPKISGDD FKSIFSELDD TGDFKINLDE FADLCTAIGL RFQKEDSLPI FEACPNFYHS
PASEKLRGFV RGATFEYIIV FVLLVNLVAV IIETTLDIQN NSGQTFWQKV EFTFGWLYVI
EMALKVYTYG FENYWRDGQN RFDFVVTWVI VIGETATFVA PDGLTFLSNG EWIRYLLIAR
MLRLIRLLMH VERYRAFVAT FFTLIPSLVP YLGTIFCILC FYCSLGLQIF GGIVNTGNPN
LAQTDLAGND YLLFNFNDYP NGMVTLFNIL VMGNWQVWMQ SYKELTGTAW TYAYFVSFYL
ISVLWLLNLI VAFVLEAFQA EVDLEASARC VDGDDKEAKS ERRRNVGTKT RSQRVDFLLH
HMLRSELTEC SNENP
