MAPC1_ARATH
ID MAPC1_ARATH Reviewed; 478 AA.
AC Q9FLS8;
DT 03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Calcium-dependent mitochondrial ATP-magnesium/phosphate carrier protein 1 {ECO:0000303|PubMed:22062157};
DE Short=AtAPC1 {ECO:0000303|PubMed:26140942, ECO:0000303|PubMed:28695448};
DE Short=Mitochondrial ATP-Mg/Pi carrier protein 1 {ECO:0000303|PubMed:22062157, ECO:0000303|PubMed:28695448};
GN Name=APC1 {ECO:0000303|PubMed:21443630, ECO:0000303|PubMed:22062157};
GN OrderedLocusNames=At5g61810 {ECO:0000312|Araport:AT5G61810};
GN ORFNames=MAC9.1 {ECO:0000312|EMBL:BAB10081.1};
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=9628582; DOI=10.1093/dnares/5.1.41;
RA Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT features of the regions of 1,456,315 bp covered by nineteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:41-54(1998).
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;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
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 and, to a lesser extent, other nucleotides (PubMed:26140942,
CC PubMed:26444389). Binds calcium ions Ca(2+) (PubMed:22062157). Mediates
CC also calcium uptake (By similarity). {ECO:0000250|UniProtKB:Q9FI43,
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). 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=0.7 mM for Pi {ECO:0000269|PubMed:26140942};
CC KM=0.32 mM for AMP {ECO:0000269|PubMed:26140942};
CC KM=0.18 mM for ADP {ECO:0000269|PubMed:26140942};
CC KM=0.19 mM for ATP {ECO:0000269|PubMed:26140942};
CC KM=180 uM for ADP (in the absence of calcium ions Ca(2+) but in the
CC presence of ATP) {ECO:0000269|PubMed:26444389};
CC KM=68 uM for ATP (in the absence of calcium ions Ca(2+) but in the
CC presence of Pi) {ECO:0000269|PubMed:26444389};
CC KM=178 uM for ADP (in the presence of calcium ions Ca(2+) and ATP)
CC {ECO:0000269|PubMed:26444389};
CC KM=61 uM for ATP (in the presence of calcium ions Ca(2+) and Pi)
CC {ECO:0000269|PubMed:26444389};
CC Vmax=2078 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=201 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=2455 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=398 nmol/h/mg enzyme with ATP as substrate (in the presence of
CC calcium ions Ca(2+) and Pi) {ECO:0000269|PubMed:26444389};
CC Vmax=100 umol/min/g enzyme with Pi as substrate
CC {ECO:0000269|PubMed:26140942};
CC Vmax=320 umol/min/g enzyme with AMP as substrate
CC {ECO:0000269|PubMed:26140942};
CC Vmax=380 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 -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:22062157}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed at high levels in flowers, leaves, stems,
CC roots and seedlings, mostly in flowers. {ECO:0000269|PubMed:26140942}.
CC -!- DEVELOPMENTAL STAGE: Slightly expressed in vascular tissues, in leaves
CC of both seedlings and mature plants, stamen filaments and developing
CC siliques. {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; AB010069; BAB10081.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97520.1; -; Genomic_DNA.
DR EMBL; AY056219; AAL07068.1; -; mRNA.
DR EMBL; AY091353; AAM14292.1; -; mRNA.
DR RefSeq; NP_568940.1; NM_125575.4.
DR AlphaFoldDB; Q9FLS8; -.
DR SMR; Q9FLS8; -.
DR STRING; 3702.AT5G61810.1; -.
DR PaxDb; Q9FLS8; -.
DR PRIDE; Q9FLS8; -.
DR ProteomicsDB; 177748; -.
DR EnsemblPlants; AT5G61810.1; AT5G61810.1; AT5G61810.
DR GeneID; 836303; -.
DR Gramene; AT5G61810.1; AT5G61810.1; AT5G61810.
DR KEGG; ath:AT5G61810; -.
DR Araport; AT5G61810; -.
DR TAIR; locus:2159168; AT5G61810.
DR eggNOG; KOG0036; Eukaryota.
DR HOGENOM; CLU_015166_2_1_1; -.
DR InParanoid; Q9FLS8; -.
DR OrthoDB; 442523at2759; -.
DR PhylomeDB; Q9FLS8; -.
DR PRO; PR:Q9FLS8; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FLS8; 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 CDD; cd00051; EFh; 1.
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..478
FT /note="Calcium-dependent mitochondrial ATP-
FT magnesium/phosphate carrier protein 1"
FT /id="PRO_0000447461"
FT TOPO_DOM 1..207
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305|PubMed:22062157"
FT TRANSMEM 208..225
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 226..259
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000305|PubMed:22062157"
FT TRANSMEM 260..279
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 280..302
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305|PubMed:22062157"
FT TRANSMEM 303..316
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 317..353
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000305|PubMed:22062157"
FT TRANSMEM 354..373
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 374..396
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305|PubMed:22062157"
FT TRANSMEM 397..414
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 415..448
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000305|PubMed:22062157"
FT TRANSMEM 449..468
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 469..478
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305|PubMed:22062157"
FT DOMAIN 32..67
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 68..103
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 104..134
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 135..170
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REPEAT 202..285
FT /note="Solcar 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00282"
FT REPEAT 293..379
FT /note="Solcar 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00282"
FT REPEAT 391..474
FT /note="Solcar 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00282"
FT BINDING 81
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 83
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
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 92
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 148
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 150
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
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:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 159
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
SQ SEQUENCE 478 AA; 53275 MW; A23632E4B6B2DF3C CRC64;
MEAEKSKQNP GKKPVEATME HVLVALRETK EKREIRIQKL FEFFDNSKLG FLDDTQIEKG
LSSLSIPPKY RYASDFLKVC DSNRDGRVDY QEFRRYMDAK ELELYKIFQA IDIEHNGDIC
PAELWEALDK AGIKIKDEEL ASFMEHVDKD NNGIITFEEW RDFLLLNPHE ATIENIYHHW
ERVCLIDIGE QAVIPDGISA HAQRSKLLLA GGIAGAVSRT ATAPLDRLKV ALQVQRTNLG
VVPTIKKIWR EDKLLGFFRG NGLNVAKVAP ESAIKFAAYE MLKPIIGGAD GDIGTSGRLL
AGGLAGAVAQ TAIYPMDLVK TRLQTFVSEV GTPKLWKLTK DIWIQEGPRA FYRGLCPSLI
GIIPYAGIDL AAYETLKDLS RAHFLHDTAE PGPLIQLGCG MTSGALGASC VYPLQVIRTR
MQADSSKTSM GQEFLKTLRG EGLKGFYRGI FPNFFKVIPS ASISYLVYEA MKKNLALD
