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Database: UniProt
Entry: H2ZMN3_CIOSA
LinkDB: H2ZMN3_CIOSA
Original site: H2ZMN3_CIOSA 
ID   H2ZMN3_CIOSA            Unreviewed;       302 AA.
AC   H2ZMN3;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   RecName: Full=Mitochondrial 2-oxoglutarate/malate carrier protein {ECO:0000256|ARBA:ARBA00040264};
DE   AltName: Full=Solute carrier family 25 member 11 {ECO:0000256|ARBA:ARBA00041881};
OS   Ciona savignyi (Pacific transparent sea squirt).
OC   Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Phlebobranchia;
OC   Cionidae; Ciona.
OX   NCBI_TaxID=51511 {ECO:0000313|Ensembl:ENSCSAVP00000018849.1, ECO:0000313|Proteomes:UP000007875};
RN   [1] {ECO:0000313|Proteomes:UP000007875}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Birren B., Nusbaum C., Abebe A., Abouelleil A., Adekoya E., Ait-zahra M.,
RA   Allen N., Allen T., An P., Anderson M., Anderson S., Arachchi H.,
RA   Armbruster J., Bachantsang P., Baldwin J., Barry A., Bayul T.,
RA   Blitshsteyn B., Bloom T., Blye J., Boguslavskiy L., Borowsky M.,
RA   Boukhgalter B., Brunache A., Butler J., Calixte N., Calvo S., Camarata J.,
RA   Campo K., Chang J., Cheshatsang Y., Citroen M., Collymore A., Considine T.,
RA   Cook A., Cooke P., Corum B., Cuomo C., David R., Dawoe T., Degray S.,
RA   Dodge S., Dooley K., Dorje P., Dorjee K., Dorris L., Duffey N., Dupes A.,
RA   Elkins T., Engels R., Erickson J., Farina A., Faro S., Ferreira P.,
RA   Fischer H., Fitzgerald M., Foley K., Gage D., Galagan J., Gearin G.,
RA   Gnerre S., Gnirke A., Goyette A., Graham J., Grandbois E., Gyaltsen K.,
RA   Hafez N., Hagopian D., Hagos B., Hall J., Hatcher B., Heller A.,
RA   Higgins H., Honan T., Horn A., Houde N., Hughes L., Hulme W., Husby E.,
RA   Iliev I., Jaffe D., Jones C., Kamal M., Kamat A., Kamvysselis M.,
RA   Karlsson E., Kells C., Kieu A., Kisner P., Kodira C., Kulbokas E.,
RA   Labutti K., Lama D., Landers T., Leger J., Levine S., Lewis D., Lewis T.,
RA   Lindblad-toh K., Liu X., Lokyitsang T., Lokyitsang Y., Lucien O., Lui A.,
RA   Ma L.J., Mabbitt R., Macdonald J., Maclean C., Major J., Manning J.,
RA   Marabella R., Maru K., Matthews C., Mauceli E., Mccarthy M., Mcdonough S.,
RA   Mcghee T., Meldrim J., Meneus L., Mesirov J., Mihalev A., Mihova T.,
RA   Mikkelsen T., Mlenga V., Moru K., Mozes J., Mulrain L., Munson G.,
RA   Naylor J., Newes C., Nguyen C., Nguyen N., Nguyen T., Nicol R., Nielsen C.,
RA   Nizzari M., Norbu C., Norbu N., O'donnell P., Okoawo O., O'leary S.,
RA   Omotosho B., O'neill K., Osman S., Parker S., Perrin D., Phunkhang P.,
RA   Piqani B., Purcell S., Rachupka T., Ramasamy U., Rameau R., Ray V.,
RA   Raymond C., Retta R., Richardson S., Rise C., Rodriguez J., Rogers J.,
RA   Rogov P., Rutman M., Schupbach R., Seaman C., Settipalli S., Sharpe T.,
RA   Sheridan J., Sherpa N., Shi J., Smirnov S., Smith C., Sougnez C.,
RA   Spencer B., Stalker J., Stange-thomann N., Stavropoulos S., Stetson K.,
RA   Stone C., Stone S., Stubbs M., Talamas J., Tchuinga P., Tenzing P.,
RA   Tesfaye S., Theodore J., Thoulutsang Y., Topham K., Towey S., Tsamla T.,
RA   Tsomo N., Vallee D., Vassiliev H., Venkataraman V., Vinson J., Vo A.,
RA   Wade C., Wang S., Wangchuk T., Wangdi T., Whittaker C., Wilkinson J.,
RA   Wu Y., Wyman D., Yadav S., Yang S., Yang X., Yeager S., Yee E., Young G.,
RA   Zainoun J., Zembeck L., Zimmer A., Zody M., Lander E.;
RL   Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSCSAVP00000018849.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-malate(in) + 2-oxoglutarate(out) = (S)-malate(out) + 2-
CC         oxoglutarate(in); Xref=Rhea:RHEA:71587, ChEBI:CHEBI:15589,
CC         ChEBI:CHEBI:16810; Evidence={ECO:0000256|ARBA:ARBA00036491};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate(out) + maleate(in) = 2-oxoglutarate(in) +
CC         maleate(out); Xref=Rhea:RHEA:71599, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:30780; Evidence={ECO:0000256|ARBA:ARBA00036076};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate(out) + malonate(in) = 2-oxoglutarate(in) +
CC         malonate(out); Xref=Rhea:RHEA:71591, ChEBI:CHEBI:15792,
CC         ChEBI:CHEBI:16810; Evidence={ECO:0000256|ARBA:ARBA00036366};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate(out) + oxaloacetate(in) = 2-oxoglutarate(in) +
CC         oxaloacetate(out); Xref=Rhea:RHEA:71603, ChEBI:CHEBI:16452,
CC         ChEBI:CHEBI:16810; Evidence={ECO:0000256|ARBA:ARBA00036462};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate(out) + succinate(in) = 2-oxoglutarate(in) +
CC         succinate(out); Xref=Rhea:RHEA:71595, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:30031; Evidence={ECO:0000256|ARBA:ARBA00036084};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC       {ECO:0000256|ARBA:ARBA00006375, ECO:0000256|RuleBase:RU000488}.
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DR   AlphaFoldDB; H2ZMN3; -.
DR   STRING; 51511.ENSCSAVP00000018849; -.
DR   Ensembl; ENSCSAVT00000019055.1; ENSCSAVP00000018849.1; ENSCSAVG00000011076.1.
DR   eggNOG; KOG0759; Eukaryota.
DR   GeneTree; ENSGT00940000158465; -.
DR   HOGENOM; CLU_015166_14_1_1; -.
DR   InParanoid; H2ZMN3; -.
DR   OMA; TLWRGAI; -.
DR   TreeFam; TF354262; -.
DR   Proteomes; UP000007875; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015297; F:antiporter activity; IEA:UniProtKB-KW.
DR   GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR   Gene3D; 1.50.40.10; Mitochondrial carrier domain; 1.
DR   InterPro; IPR002067; Mit_carrier.
DR   InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR   InterPro; IPR023395; Mt_carrier_dom_sf.
DR   PANTHER; PTHR45618:SF9; MITOCHONDRIAL 2-OXOGLUTARATE_MALATE CARRIER PROTEIN; 1.
DR   PANTHER; PTHR45618; MITOCHONDRIAL DICARBOXYLATE CARRIER-RELATED; 1.
DR   Pfam; PF00153; Mito_carr; 3.
DR   PRINTS; PR00784; MTUNCOUPLING.
DR   SUPFAM; SSF103506; Mitochondrial carrier; 1.
DR   PROSITE; PS50920; SOLCAR; 3.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PROSITE-
KW   ProRule:PRU00282}; Reference proteome {ECO:0000313|Proteomes:UP000007875};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|PROSITE-
KW   ProRule:PRU00282}; Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU000488}.
FT   REPEAT          12..97
FT                   /note="Solcar"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT   REPEAT          106..197
FT                   /note="Solcar"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT   REPEAT          206..295
FT                   /note="Solcar"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
SQ   SEQUENCE   302 AA;  33226 MW;  BED12E0D7AB78012 CRC64;
     MSDTRKVLPN GVKFLFGGTA GMGATLFVQP LDLVKNRLQL SGAGGQEKLY KNSFDAISQI
     LRNEGIVGIY NGLSAGLLRQ ATYTTTRLGV YTILLDKFSD PDGTPPNFFQ KAALGMTAGA
     CGAFIGTPAE VSLIRMTADG RLPADQRRGY TSVFNALSRM VREEGLFTLW RGCIPTMGRA
     VVVNAAQLAS YSQAKQMLLS TDYFQDNIFC HFVASMISGL ITTCASMPVD IAKTRIQNMK
     TINGVPEYKG AIDVLGKVVR NEGFFSLWKG FTPYYFRLGP HTVLTFIFLE QMNIMYKRTF
     MS
//
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