TPC1_ORYSJ
ID TPC1_ORYSJ Reviewed; 757 AA.
AC Q5QM84; B9EYL2; Q0JKF6; Q5QM85; Q7XB54; Q7XXT1;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Two pore calcium channel protein 1;
DE AltName: Full=OsTPC1;
DE AltName: Full=Voltage-dependent calcium channel protein TPC1;
GN Name=TPC1; OrderedLocusNames=Os01g0678500, LOC_Os01g48680;
GN ORFNames=B1144G04.26-1, OsJ_03004 {ECO:0000312|EMBL:EEE55175.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=15111725; DOI=10.1093/pcp/pch053;
RA Hashimoto K., Saito M., Matsuoka H., Iida K., Iida H.;
RT "Functional analysis of a rice putative voltage-dependent Ca2+ channel,
RT OsTPC1, expressed in yeast cells lacking its homologous gene CCH1.";
RL Plant Cell Physiol. 45:496-500(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ACTIVITY REGULATION, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15215504; DOI=10.1093/pcp/pch082;
RA Kurusu T., Sakurai Y., Miyao A., Hirochika H., Kuchitsu K.;
RT "Identification of a putative voltage-gated Ca2+ -permeable channel
RT (OsTPC1) involved in Ca2+ influx and regulation of growth and development
RT in rice.";
RL Plant Cell Physiol. 45:693-702(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12447438; DOI=10.1038/nature01184;
RA Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y.,
RA Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H.,
RA Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M.,
RA Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M.,
RA Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T.,
RA Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S.,
RA Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H.,
RA Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y.,
RA Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S.,
RA Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y.,
RA Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S.,
RA Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H.,
RA Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T.;
RT "The genome sequence and structure of rice chromosome 1.";
RL Nature 420:312-316(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [6]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15941394; DOI=10.1111/j.1365-313x.2005.02415.x;
RA Kurusu T., Yagala T., Miyao A., Hirochika H., Kuchitsu K.;
RT "Identification of a putative voltage-gated Ca2+ channel as a key regulator
RT of elicitor-induced hypersensitive cell death and mitogen-activated protein
RT kinase activation in rice.";
RL Plant J. 42:798-809(2005).
CC -!- FUNCTION: May function as one of the major voltage-gated Ca(2+) channel
CC (VDCC) across the plasma membrane. May be involved in the regulation of
CC cytosolic Ca(2+) and in growth and development. Acts as the major ROS-
CC responsive Ca(2+) channel and is the possible target of Al-dependent
CC inhibition. Determines sensitivity to T.viride xylanase elicitor. Plays
CC a regulatory role in elicitor-induced defense responses and
CC hypersensitive cell death. {ECO:0000269|PubMed:15111725,
CC ECO:0000269|PubMed:15215504, ECO:0000269|PubMed:15941394}.
CC -!- ACTIVITY REGULATION: Inhibited by the VDCC blocker verapamil in yeast
CC cells. Channel activity may be down-regulated by cytosolic Ca(2+) in
CC rice cells. Inhibited by Al(3+) (By similarity). {ECO:0000250}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=47.5 uM for Ca(2+) (at 30 degrees Celsius)
CC {ECO:0000269|PubMed:15111725};
CC Note=Measured in yeast knockout mutant cch1.;
CC -!- SUBUNIT: Homodimer. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:15111725,
CC ECO:0000269|PubMed:15215504, ECO:0000269|PubMed:15941394}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:15111725,
CC ECO:0000269|PubMed:15215504, ECO:0000269|PubMed:15941394}.
CC -!- TISSUE SPECIFICITY: Expressed in shoot, mature leaf, cultured cells,
CC and at lower level in roots. {ECO:0000269|PubMed:15215504}.
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 Plants overexpressing TPC1 display reduced growth rate and dwarf
CC phenotype, and seedlings show greening of roots under light conditions.
CC The highest overexpressor line shows most severe phenotype including a
CC death symptom, possibily due to Ca(2+) accumulation to toxic level.
CC -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit (TC
CC 1.A.1.11) family. Two pore calcium channel subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD73470.1; Type=Erroneous gene model prediction; Evidence={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; AB100696; BAC80148.1; -; mRNA.
DR EMBL; AB071014; BAC78525.1; -; mRNA.
DR EMBL; AP003335; BAD73469.1; -; Genomic_DNA.
DR EMBL; AP003335; BAD73470.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP008207; BAF05772.1; -; Genomic_DNA.
DR EMBL; AP014957; BAS73676.1; -; Genomic_DNA.
DR EMBL; CM000138; EEE55175.1; -; Genomic_DNA.
DR RefSeq; XP_015621659.1; XM_015766173.1.
DR AlphaFoldDB; Q5QM84; -.
DR SMR; Q5QM84; -.
DR STRING; 4530.OS01T0678500-02; -.
DR TCDB; 1.A.1.11.13; the voltage-gated ion channel (vic) superfamily.
DR PaxDb; Q5QM84; -.
DR PRIDE; Q5QM84; -.
DR EnsemblPlants; Os01t0678500-01; Os01t0678500-01; Os01g0678500.
DR EnsemblPlants; Os01t0678500-02; Os01t0678500-02; Os01g0678500.
DR GeneID; 4325272; -.
DR Gramene; Os01t0678500-01; Os01t0678500-01; Os01g0678500.
DR Gramene; Os01t0678500-02; Os01t0678500-02; Os01g0678500.
DR KEGG; osa:4325272; -.
DR eggNOG; KOG2301; Eukaryota.
DR HOGENOM; CLU_426053_0_0_1; -.
DR InParanoid; Q5QM84; -.
DR OMA; QHACDQR; -.
DR OrthoDB; 761764at2759; -.
DR Proteomes; UP000000763; Chromosome 1.
DR Proteomes; UP000007752; Chromosome 1.
DR Proteomes; UP000059680; Chromosome 1.
DR Genevisible; Q5QM84; OS.
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:0042802; F:identical protein binding; IEA:EnsemblPlants.
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: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 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 1: Evidence at protein 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..757
FT /note="Two pore calcium channel protein 1"
FT /id="PRO_0000053962"
FT TOPO_DOM 1..94
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 95..115
FT /note="Helical; Name=S1 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 116..152
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 153..173
FT /note="Helical; Name=S2 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 174..188
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 189..209
FT /note="Helical; Name=S3 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 210
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 211..228
FT /note="Helical; Voltage-sensor; Name=S4 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 229..233
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 234..254
FT /note="Helical; Name=S5 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 255..270
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT INTRAMEM 271..285
FT /note="Pore-forming; Name=Pore-forming 1"
FT TOPO_DOM 286..308
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 309..329
FT /note="Helical; Name=S6 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 330..453
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 454..474
FT /note="Helical; Name=S1 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 475..493
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 494..514
FT /note="Helical; Name=S2 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 515..523
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 524..544
FT /note="Helical; Name=S3 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 545..553
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 554..571
FT /note="Helical; Voltage-sensor; Name=S4 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 572..595
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 596..616
FT /note="Helical; Name=S5 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 617..640
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT INTRAMEM 641..655
FT /note="Pore-forming; Name=Pore-forming 2"
FT TOPO_DOM 656..676
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 677..697
FT /note="Helical; Name=S6 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 698..757
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 347..382
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 388..423
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 24..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 482
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 554
FT /note="W -> L (in Ref. 1; BAC80148)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 757 AA; 87069 MW; E12332F4E1A493BC CRC64;
MRERGEMREA KAPLIAEAAE HISHSHGSGS SGTGSHTSGG GGGWRGSRQY QRRSDALAYG
NRYQKAAALV DLAEDGVGIP EDVLNDTRFE RAMRFYFVYL RLDWLWSLNL FALILLNFLE
KPLWCRGYSQ HACDQRDLYF LGQLPYLSKT ESLIYEGLTL VILVMDIFYP LSYEGLNLFW
KNTINKLKVL LLFILACDIL VFAFSPQPFR VAPYIRVAFL IMNIRELRMC AVTLVGMVGT
YLNVLALSLL FLLFASWLAY VTFEDTPQGK TVFSSYGTTL YQMFILFTTS NNPDVWVPAY
KSSRWSSLFF IVYVLLGVYF LTNLILAVIY DSFKEQLAKQ VSQADCTRKS ILEKAFGIID
ATGQGYLNKE QCLSLLDELN KYRSLPKTSR EDFELIFAEL DQSGDFKVTS EEFATLCNTI
AIKFQKEPPP SYLEKYPSFY HSALCEWLKS FVRSPLFEYI VIFVLLMNLV AVIIETTLDI
ENSSSQKVWQ EVEFVFGWIY VIEMALKIFS LGFGAYWMEG QNKFDFVLTW TIFIGETLTF
AFPSKLSFLS NGEWIRYLLL GRMLRLTRIL LQVRRFRAFV ATFFTLMSSL MPYLGIVFCT
LCIYCSLGLQ IFGGIVYAGN PTLEETDLFS NDYLLFNFND YPSGMVTLFN LLVMGNWQAW
MESYRQLTGS YWSLIYFVSF YLISVLLLLN LIVAFVLEAF FAEMELEKDG EADIQDPTLE
GRNRRRSVRV RTKGTMVDIL LHHMLSNELD GSQNRDQ
