MAPC2_ARATH
ID MAPC2_ARATH Reviewed; 487 AA.
AC Q9FI43; F4KBU1;
DT 03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Calcium-dependent mitochondrial ATP-magnesium/phosphate carrier protein 2 {ECO:0000303|PubMed:22062157};
DE Short=AtAPC2 {ECO:0000303|PubMed:26140942, ECO:0000303|PubMed:28695448};
DE Short=Mitochondrial ATP-Mg/Pi carrier protein 2 {ECO:0000303|PubMed:22062157, ECO:0000303|PubMed:28695448};
GN Name=APC2 {ECO:0000303|PubMed:21443630, ECO:0000303|PubMed:22062157};
GN OrderedLocusNames=At5g51050 {ECO:0000312|Araport:AT5G51050};
GN ORFNames=K3K7.23 {ECO:0000312|EMBL:AED96027.2};
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=10470850; DOI=10.1093/dnares/6.3.183;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IX. Sequence
RT features of the regions of 1,011,550 bp covered by seventeen P1 and TAC
RT clones.";
RL DNA Res. 6:183-195(1999).
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 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 [4]
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 [5]
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 [6]
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 [7]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, 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 [8]
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 [9]
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 [10]
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 (PubMed:26444389).
CC {ECO:0000269|PubMed:22062157, ECO:0000269|PubMed:26140942,
CC ECO:0000269|PubMed:26444389, 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, PubMed:26444389). Activated by calcium Ca(2+) and
CC manganese Mn(2+) ions, and slightly by iron Fe(2+) and zinc Zn(2+) ions
CC (PubMed:26140942, PubMed:28695448, PubMed:26444389). Repressed by
CC copper ions Cu(2+) and slightly by magnesium Mg(2+) ions
CC (PubMed:28695448). Magnesium Mg(2+) ions promotes slightly ATP uptake,
CC ATP-Mg(2+) being exchanged with ATP(4-) (PubMed:26444389).
CC {ECO:0000269|PubMed:26140942, ECO:0000269|PubMed:26444389,
CC ECO:0000269|PubMed:28695448}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.74 mM for Pi {ECO:0000269|PubMed:26140942};
CC KM=0.25 mM for AMP {ECO:0000269|PubMed:26140942};
CC KM=0.16 mM for ADP {ECO:0000269|PubMed:26140942};
CC KM=0.08 mM for ATP {ECO:0000269|PubMed:26140942};
CC KM=374 uM for ADP (in the absence of calcium ions Ca(2+) but in the
CC presence of ATP) {ECO:0000269|PubMed:26444389};
CC KM=95 uM for ATP (in the absence of calcium ions Ca(2+) but in the
CC presence of Pi) {ECO:0000269|PubMed:26444389};
CC KM=508 uM for ADP (in the presence of calcium ions Ca(2+) and ATP)
CC {ECO:0000269|PubMed:26444389};
CC KM=59 uM for ATP (in the presence of calcium ions Ca(2+) and Pi)
CC {ECO:0000269|PubMed:26444389};
CC Vmax=380 umol/min/g enzyme with Pi as substrate
CC {ECO:0000269|PubMed:26140942};
CC Vmax=150 umol/min/g enzyme with AMP as substrate
CC {ECO:0000269|PubMed:26140942};
CC Vmax=350 umol/min/g enzyme with ADP as substrate
CC {ECO:0000269|PubMed:26140942};
CC Vmax=54 umol/min/g enzyme with ATP as substrate
CC {ECO:0000269|PubMed:26140942};
CC Vmax=778 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=212 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=1169 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=523 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 aerial parts. {ECO:0000269|PubMed:26140942}.
CC -!- DEVELOPMENTAL STAGE: Slightly expressed in flower petals.
CC {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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AED96027.2; Type=Erroneous initiation; Note=Extended N-terminus.; 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; AB017063; BAB08751.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96027.2; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_199918.2; NM_124484.2.
DR AlphaFoldDB; Q9FI43; -.
DR SMR; Q9FI43; -.
DR STRING; 3702.AT5G51050.1; -.
DR PaxDb; Q9FI43; -.
DR PeptideAtlas; Q9FI43; -.
DR PRIDE; Q9FI43; -.
DR ProteomicsDB; 214332; -.
DR EnsemblPlants; AT5G51050.1; AT5G51050.1; AT5G51050.
DR GeneID; 835178; -.
DR Gramene; AT5G51050.1; AT5G51050.1; AT5G51050.
DR KEGG; ath:AT5G51050; -.
DR Araport; AT5G51050; -.
DR TAIR; locus:2157423; AT5G51050.
DR eggNOG; KOG0036; Eukaryota.
DR HOGENOM; CLU_015166_2_1_1; -.
DR InParanoid; Q9FI43; -.
DR OrthoDB; 442523at2759; -.
DR PhylomeDB; Q9FI43; -.
DR PRO; PR:Q9FI43; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FI43; 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; IDA: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; IDA: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; PF13833; EF-hand_8; 1.
DR Pfam; PF00153; Mito_carr; 3.
DR PRINTS; PR00926; MITOCARRIER.
DR SMART; SM00054; EFh; 2.
DR SUPFAM; SSF103506; SSF103506; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
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..487
FT /note="Calcium-dependent mitochondrial ATP-
FT magnesium/phosphate carrier protein 2"
FT /id="PRO_0000447462"
FT TOPO_DOM 1..211
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305|PubMed:22062157"
FT TRANSMEM 212..229
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 230..263
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000305|PubMed:22062157"
FT TRANSMEM 264..283
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 284..310
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305|PubMed:22062157"
FT TRANSMEM 311..324
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 325..363
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000305|PubMed:22062157"
FT TRANSMEM 364..383
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 384..405
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305|PubMed:22062157"
FT TRANSMEM 406..423
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 424..457
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000305|PubMed:22062157"
FT TRANSMEM 458..477
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 478..487
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305|PubMed:22062157"
FT DOMAIN 36..71
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 72..107
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 108..138
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 139..174
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REPEAT 206..289
FT /note="Solcar 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00282"
FT REPEAT 301..389
FT /note="Solcar 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00282"
FT REPEAT 400..483
FT /note="Solcar 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00282"
FT BINDING 85
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 87
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 89
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 91
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 96
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 152
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 154
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 156
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 163
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
SQ SEQUENCE 487 AA; 54506 MW; 2268B650C8841537 CRC64;
MEATKSSKQN CCNPVKKPGP VSIDHVLLAL RETREERDLR IRSLFSFFDS ENVGYLDCAQ
IEKGLCALQI PSGYKYAKEL FRVCDANRDG RVDYHEFRRY MDDKELELYR IFQAIDVEHN
GCISPEGLWD SLVKAGIEIK DEELARFVEH VDKDNDGIIM FEEWRDFLLL YPHEATIENI
YHHWERVCLV DIGEQAVIPE GISKHIKRSN YFIAGGIAGA ASRTATAPLD RLKVLLQIQK
TDARIREAIK LIWKQGGVRG FFRGNGLNIV KVAPESAIKF YAYELFKNAI GENMGEDKAD
IGTTVRLFAG GMAGAVAQAS IYPLDLVKTR LQTYTSQAGV AVPRLGTLTK DILVHEGPRA
FYKGLFPSLL GIIPYAGIDL AAYETLKDLS RTYILQDAEP GPLVQLGCGT ISGALGATCV
YPLQVVRTRM QAERARTSMS GVFRRTISEE GYRALYKGLL PNLLKVVPAA SITYMVYEAM
KKSLELD
