MAPC3_ARATH
ID MAPC3_ARATH Reviewed; 479 AA.
AC Q9LY28;
DT 03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Calcium-dependent mitochondrial ATP-magnesium/phosphate carrier protein 3 {ECO:0000303|PubMed:22062157};
DE Short=AtAPC3 {ECO:0000303|PubMed:26140942, ECO:0000303|PubMed:28695448};
DE Short=Mitochondrial ATP-Mg/Pi carrier protein 3 {ECO:0000303|PubMed:22062157, ECO:0000303|PubMed:28695448};
GN Name=APC3 {ECO:0000303|PubMed:21443630, ECO:0000303|PubMed:22062157};
GN OrderedLocusNames=At5g07320 {ECO:0000312|Araport:AT5G07320};
GN ORFNames=T2I1.30 {ECO:0000312|EMBL:CAB87921.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP GENE FAMILY.
RX PubMed=12372144; DOI=10.1186/gb-2002-3-10-research0056;
RA Day I.S., Reddy V.S., Shad Ali G., Reddy A.S.;
RT "Analysis of EF-hand-containing proteins in Arabidopsis.";
RL Genome Biol. 3:RESEARCH0056.1-RESEARCH0056.24(2002).
RN [5]
RP REVIEW, AND GENE FAMILY.
RX PubMed=15003237; DOI=10.1016/j.tplants.2004.01.007;
RA Picault N., Hodges M., Palmieri L., Palmieri F.;
RT "The growing family of mitochondrial carriers in Arabidopsis.";
RL Trends Plant Sci. 9:138-146(2004).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=22062157; DOI=10.1016/j.febslet.2011.10.039;
RA Stael S., Rocha A.G., Robinson A.J., Kmiecik P., Vothknecht U.C., Teige M.;
RT "Arabidopsis calcium-binding mitochondrial carrier proteins as potential
RT facilitators of mitochondrial ATP-import and plastid SAM-import.";
RL FEBS Lett. 585:3935-3940(2011).
RN [7]
RP GENE FAMILY.
RX PubMed=21443630; DOI=10.1111/j.1365-313x.2011.04516.x;
RA Palmieri F., Pierri C.L., De Grassi A., Nunes-Nesi A., Fernie A.R.;
RT "Evolution, structure and function of mitochondrial carriers: a review with
RT new insights.";
RL Plant J. 66:161-181(2011).
RN [8]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, INDUCTION BY STRESS CONDITIONS, AND ACTIVITY REGULATION.
RC STRAIN=cv. Columbia;
RX PubMed=26140942; DOI=10.1016/j.bbabio.2015.06.015;
RA Monne M., Miniero D.V., Obata T., Daddabbo L., Palmieri L., Vozza A.,
RA Nicolardi M.C., Fernie A.R., Palmieri F.;
RT "Functional characterization and organ distribution of three mitochondrial
RT ATP-Mg/Pi carriers in Arabidopsis thaliana.";
RL Biochim. Biophys. Acta 1847:1220-1230(2015).
RN [9]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION.
RX PubMed=26444389; DOI=10.1186/s12870-015-0616-0;
RA Lorenz A., Lorenz M., Vothknecht U.C., Niopek-Witz S., Neuhaus H.E.,
RA Haferkamp I.;
RT "In vitro analyses of mitochondrial ATP/phosphate carriers from Arabidopsis
RT thaliana revealed unexpected Ca(2+)-effects.";
RL BMC Plant Biol. 15:238-238(2015).
RN [10]
RP REVIEW.
RX PubMed=27033520; DOI=10.1016/j.bbamcr.2016.03.024;
RA Del Arco A., Contreras L., Pardo B., Satrustegui J.;
RT "Calcium regulation of mitochondrial carriers.";
RL Biochim. Biophys. Acta 1863:2413-2421(2016).
RN [11]
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=28695448; DOI=10.1007/s10863-017-9721-0;
RA Monne M., Daddabbo L., Giannossa L.C., Nicolardi M.C., Palmieri L.,
RA Miniero D.V., Mangone A., Palmieri F.;
RT "Mitochondrial ATP-Mg/phosphate carriers transport divalent inorganic
RT cations in complex with ATP.";
RL J. Bioenerg. Biomembr. 49:369-380(2017).
CC -!- FUNCTION: Calcium-dependent mitochondrial carrier protein that
CC catalyzes the import of ATP co-transported with metal divalent cations
CC across the mitochondrial inner membrane in exchange for phosphate (Pi)
CC (PubMed:22062157, PubMed:28695448, PubMed:26140942, PubMed:26444389).
CC Can transport phosphate, AMP, ADP, ATP, adenosine 5'-phosphosulfate,
CC sulfate and thiosulfate, and, to a lesser extent, other nucleotides
CC (PubMed:26140942, PubMed:26444389). Binds calcium ions Ca(2+)
CC (PubMed:22062157). Mediates also calcium uptake (By similarity).
CC {ECO:0000250|UniProtKB:Q9FI43, ECO:0000269|PubMed:22062157,
CC ECO:0000269|PubMed:26140942, ECO:0000269|PubMed:26444389,
CC ECO:0000269|PubMed:28695448}.
CC -!- ACTIVITY REGULATION: Counter-exchange transport activity is saturable
CC and inhibited by pyridoxal-5'-phosphate, EDTA and EGTA
CC (PubMed:26140942). Activated by calcium Ca(2+) and manganese Mn(2+)
CC ions, and slightly by iron Fe(2+) and zinc Zn(2+) ions
CC (PubMed:26140942, PubMed:28695448). Repressed by copper ions Cu(2+) and
CC slightly by magnesium Mg(2+) ions (PubMed:28695448). Magnesium Mg(2+)
CC ions promotes slightly ATP uptake, ATP-Mg(2+) being exchanged with
CC ATP(4-) (PubMed:26444389). {ECO:0000269|PubMed:26140942,
CC ECO:0000269|PubMed:26444389, ECO:0000269|PubMed:28695448}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.6 mM for Pi {ECO:0000269|PubMed:26140942};
CC KM=0.25 mM for AMP {ECO:0000269|PubMed:26140942};
CC KM=0.17 mM for ADP {ECO:0000269|PubMed:26140942};
CC KM=0.14 mM for ATP {ECO:0000269|PubMed:26140942};
CC KM=72 uM for ADP (in the absence of calcium ions Ca(2+) but in the
CC presence of ATP) {ECO:0000269|PubMed:26444389};
CC KM=113 uM for ATP (in the absence of calcium ions Ca(2+) but in the
CC presence of Pi) {ECO:0000269|PubMed:26444389};
CC KM=140 uM for ADP (in the presence of calcium ions Ca(2+) and ATP)
CC {ECO:0000269|PubMed:26444389};
CC KM=58 uM for ATP (in the presence of calcium ions Ca(2+) and Pi)
CC {ECO:0000269|PubMed:26444389};
CC Vmax=330 umol/min/g enzyme with Pi as substrate
CC {ECO:0000269|PubMed:26140942};
CC Vmax=300 umol/min/g enzyme with AMP as substrate
CC {ECO:0000269|PubMed:26140942};
CC Vmax=410 umol/min/g enzyme with ADP as substrate
CC {ECO:0000269|PubMed:26140942};
CC Vmax=330 umol/min/g enzyme with ATP as substrate
CC {ECO:0000269|PubMed:26140942};
CC Vmax=770 nmol/h/mg enzyme with ADP as substrate (in the absence of
CC calcium ions Ca(2+) but in the presence of ATP)
CC {ECO:0000269|PubMed:26444389};
CC Vmax=282 nmol/h/mg enzyme with ATP as substrate (in the absence of
CC calcium ions Ca(2+) but in the presence of Pi)
CC {ECO:0000269|PubMed:26444389};
CC Vmax=1025 nmol/h/mg enzyme with ADP as substrate (in the presence of
CC calcium ions Ca(2+) and ATP) {ECO:0000269|PubMed:26444389};
CC Vmax=646 nmol/h/mg enzyme with ATP as substrate (in the presence of
CC calcium ions Ca(2+) and Pi) {ECO:0000269|PubMed:26444389};
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:22062157}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in flowers, leaves, stems, roots and
CC seedlings, mostly in seedlings. {ECO:0000269|PubMed:26140942}.
CC -!- DEVELOPMENTAL STAGE: Slightly expressed in seedling leaves.
CC {ECO:0000269|PubMed:26140942}.
CC -!- INDUCTION: By stress conditions. {ECO:0000269|PubMed:26140942}.
CC -!- DOMAIN: The N-terminal domain can bind calcium.
CC {ECO:0000269|PubMed:22062157}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000305}.
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DR EMBL; AL163912; CAB87921.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91136.1; -; Genomic_DNA.
DR EMBL; AK175228; BAD42991.1; -; mRNA.
DR PIR; T49871; T49871.
DR RefSeq; NP_196349.1; NM_120814.3.
DR AlphaFoldDB; Q9LY28; -.
DR SMR; Q9LY28; -.
DR IntAct; Q9LY28; 1.
DR STRING; 3702.AT5G07320.1; -.
DR PaxDb; Q9LY28; -.
DR PRIDE; Q9LY28; -.
DR ProteomicsDB; 187418; -.
DR EnsemblPlants; AT5G07320.1; AT5G07320.1; AT5G07320.
DR GeneID; 830623; -.
DR Gramene; AT5G07320.1; AT5G07320.1; AT5G07320.
DR KEGG; ath:AT5G07320; -.
DR Araport; AT5G07320; -.
DR TAIR; locus:2183314; AT5G07320.
DR eggNOG; KOG0036; Eukaryota.
DR HOGENOM; CLU_015166_2_1_1; -.
DR InParanoid; Q9LY28; -.
DR OMA; LGIFPYA; -.
DR OrthoDB; 442523at2759; -.
DR PhylomeDB; Q9LY28; -.
DR PRO; PR:Q9LY28; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LY28; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0015217; F:ADP transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0080122; F:AMP transmembrane transporter activity; IDA:TAIR.
DR GO; GO:0005347; F:ATP transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IDA:TAIR.
DR GO; GO:0015085; F:calcium ion transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0015114; F:phosphate ion transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0015866; P:ADP transport; IDA:UniProtKB.
DR GO; GO:0080121; P:AMP transport; IDA:TAIR.
DR GO; GO:0015867; P:ATP transport; IDA:UniProtKB.
DR GO; GO:0070588; P:calcium ion transmembrane transport; ISS:UniProtKB.
DR GO; GO:0035435; P:phosphate ion transmembrane transport; IDA:UniProtKB.
DR Gene3D; 1.50.40.10; -; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR002067; Mit_carrier.
DR InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR InterPro; IPR023395; Mt_carrier_dom_sf.
DR Pfam; PF13202; EF-hand_5; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR Pfam; PF00153; Mito_carr; 3.
DR PRINTS; PR00926; MITOCARRIER.
DR SMART; SM00054; EFh; 4.
DR SUPFAM; SSF103506; SSF103506; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 4.
DR PROSITE; PS50920; SOLCAR; 3.
PE 1: Evidence at protein level;
KW Calcium; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..479
FT /note="Calcium-dependent mitochondrial ATP-
FT magnesium/phosphate carrier protein 3"
FT /id="PRO_0000447463"
FT TOPO_DOM 1..208
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305|PubMed:22062157"
FT TRANSMEM 209..226
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 227..260
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000305|PubMed:22062157"
FT TRANSMEM 261..280
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 281..303
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305|PubMed:22062157"
FT TRANSMEM 304..317
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 318..355
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000305|PubMed:22062157"
FT TRANSMEM 356..375
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 376..397
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305|PubMed:22062157"
FT TRANSMEM 398..415
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 416..449
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000305|PubMed:22062157"
FT TRANSMEM 450..469
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 470..479
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305|PubMed:22062157"
FT DOMAIN 33..68
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 69..104
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 105..135
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 136..171
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REPEAT 203..286
FT /note="Solcar 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00282"
FT REPEAT 294..381
FT /note="Solcar 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00282"
FT REPEAT 392..475
FT /note="Solcar 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00282"
FT BINDING 82
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 84
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 86
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 88
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 93
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 149
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 151
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 153
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 155
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 160
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
SQ SEQUENCE 479 AA; 53970 MW; 38D58E1395316D6E CRC64;
MESSKPKNRN PMKKPVSITM EHVLLALRET MDEREIRIRS LFDFFDNSNL GFLDYAQIEK
GLASLQIPPE YKYARDLFRV CDANRDGRVD YQEFRRYIDA KELELYRIFQ AIDVEHNGCI
LPEELWEALV KAGIEIDDEE LARFVEHVDK DNNGTITFEE WRDFLLLYPH EATLENIYHH
WERVCLIDIG EQAVIPDGIS KHVKRSRLLL AGGLAGAVSR TATAPLDRLK VVLQVQRAHA
GVLPTIKKIW REDKLMGFFR GNGLNVMKVA PESAIKFCAY EMLKPMIGGE DGDIGTSGRL
MAGGMAGALA QTAIYPMDLV KTRLQTCVSE GGKAPKLWKL TKDIWVREGP RAFYKGLFPS
LLGIVPYAGI DLAAYETLKD LSRTYILQDT EPGPLIQLSC GMTSGALGAS CVYPLQVVRT
RMQADSSKTT MKQEFMNTMK GEGLRGFYRG LLPNLLKVVP AASITYIVYE AMKKNMALD
