ID AOX2_ARATH Reviewed; 353 AA. AC O22049; Q4PS98; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 27-MAY-2002, sequence version 2. DT 14-DEC-2011, entry version 92. DE RecName: Full=Alternative oxidase 2, mitochondrial; DE EC=1.-.-.-; DE Flags: Precursor; GN Name=AOX2; OrderedLocusNames=At5g64210; ORFNames=MSJ1.5; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=cv. Columbia; TISSUE=Leaf, and Stem; RX MEDLINE=98009993; PubMed=9349280; DOI=10.1023/A:1005818507743; RA Saisho D., Nambara E., Naito S., Tsutsumi N., Hirai A., Nakazono M.; RT "Characterization of the gene family for alternative oxidase from RT Arabidopsis thaliana."; RL Plant Mol. Biol. 35:585-596(1997). RN [2] RP SEQUENCE REVISION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, RP DEVELOPMENTAL STAGE, AND INDUCTION. RX MEDLINE=21327317; PubMed=11434463; DOI=10.1266/ggs.76.89; RA Saisho D., Nakazono M., Lee K.-H., Tsutsumi N., Akita S., Hirai A.; RT "The gene for alternative oxidase-2 (AOX2) from Arabidopsis thaliana RT consists of five exons unlike other AOX genes and is transcribed at an RT early stage during germination."; RL Genes Genet. Syst. 76:89-97(2001). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX MEDLINE=98162728; PubMed=9501997; DOI=10.1093/dnares/4.6.401; RA Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N., RA Tabata S.; RT "Structural analysis of Arabidopsis thaliana chromosome 5. III. RT Sequence features of the regions of 1,191,918 bp covered by seventeen RT physically assigned P1 clones."; RL DNA Res. 4:401-414(1997). RN [4] RP GENOME REANNOTATION. RC STRAIN=cv. Columbia; RG The Arabidopsis Information Resource (TAIR); RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RA Underwood B.A., Xiao Y.-L., Moskal W.A. Jr., Monaghan E.L., Wang W., RA Redman J.C., Wu H.C., Utterback T., Town C.D.; RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP IRON-BINDING SITES. RX MEDLINE=99239925; PubMed=10225419; DOI=10.1016/S0014-5793(99)00376-2; RA Andersson M.E., Nordlund P.; RT "A revised model of the active site of alternative oxidase."; RL FEBS Lett. 449:17-22(1999). CC -!- FUNCTION: Catalyzes cyanide-resistant oxygen consumption. May CC increase respiration when the cytochrome respiratory pathway is CC restricted, or in response to low temperatures (By similarity). CC -!- COFACTOR: Binds 2 iron ions per subunit. CC -!- SUBUNIT: Homodimer; disulfide-linked (Probable). CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass CC membrane protein (Probable). Note=Mitochondrial, possibly in the CC inner surface of the inner mitochondrial membrane. CC -!- TISSUE SPECIFICITY: Maximally expressed in dry seeds. CC -!- DEVELOPMENTAL STAGE: Found predominantly during early stages of CC germination with maximum level at 12 hours after imbibition. CC -!- INDUCTION: Antimycin A has no effect on expression. CC -!- SIMILARITY: Belongs to the alternative oxidase family. CC -!- SEQUENCE CAUTION: CC Sequence=BAB09852.1; Type=Erroneous gene model prediction; 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; AB003176; BAA22636.2; -; Genomic_DNA. DR EMBL; AB008268; BAB09852.1; ALT_SEQ; Genomic_DNA. DR EMBL; CP002688; AED97855.1; -; Genomic_DNA. DR EMBL; DQ056738; AAY78882.1; -; mRNA. DR IPI; IPI00542540; -. DR RefSeq; NP_201226.2; NM_125817.2. DR UniGene; At.55697; -. DR STRING; O22049; -. DR PRIDE; O22049; -. DR EnsemblPlants; AT5G64210.1; AT5G64210.1; AT5G64210. DR GeneID; 836542; -. DR GenomeReviews; BA000015_GR; AT5G64210. DR KEGG; ath:AT5G64210; -. DR NMPDR; fig|3702.1.peg.28479; -. DR GeneFarm; 1754; 131. DR TAIR; At5g64210; -. DR eggNOG; euNOG04325; -. DR GeneTree; EPGT00050000014563; -. DR HOGENOM; HBG597538; -. DR InParanoid; O22049; -. DR OMA; KVAYRIV; -. DR PhylomeDB; O22049; -. DR ProtClustDB; PLN02478; -. DR ArrayExpress; O22049; -. DR Genevestigator; O22049; -. DR GermOnline; AT5G64210; Arabidopsis thaliana. DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell. DR GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW. DR GO; GO:0007585; P:respiratory gaseous exchange; IEA:InterPro. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR InterPro; IPR002680; AOX. DR KO; K00540; -. DR Pfam; PF01786; AOX; 1. DR PIRSF; PIRSF005229; AOX; 1. PE 1: Evidence at protein level; KW Complete proteome; Disulfide bond; Electron transport; Iron; Membrane; KW Metal-binding; Mitochondrion; Mitochondrion inner membrane; KW Oxidoreductase; Reference proteome; Respiratory chain; KW Transit peptide; Transmembrane; Transmembrane helix; Transport. FT TRANSIT 1 21 Mitochondrion (Potential). FT CHAIN 22 353 Alternative oxidase 2, mitochondrial. FT /FTId=PRO_0000001734. FT TRANSMEM 178 198 Helical; (Potential). FT TRANSMEM 240 260 Helical; (Potential). FT METAL 182 182 Iron (Potential). FT METAL 221 221 Iron (Potential). FT METAL 224 224 Iron (Potential). FT METAL 273 273 Iron (Potential). FT METAL 323 323 Iron (Potential). FT METAL 326 326 Iron (Potential). FT DISULFID 126 126 Interchain (Potential). SQ SEQUENCE 353 AA; 40087 MW; DF7ACB113E57A133 CRC64; MSQLITKAAL RVLLVCGRGN CNMFVSSVSS TSVMKSPYEI TAPMRIHDWC GGFGDFKIGS KHVQGNFNLR WMGMSSASAM EKKDENLTVK KGQNGGGSVA VPSYWGIETA KMKITRKDGS DWPWNCFMPW ETYQANLSID LKKHHVPKNI ADKVAYRIVK LLRIPTDIFF QRRYGCRAMM LETVAAVPGM VGGMLLHLKS IRKFEHSGGW IKALLEEAEN ERMHLMTMME LVKPKWYERL LVMLVQGIFF NSFFVCYVIS PRLAHRVVGY LEEEAIHSYT EFLKDIDNGK IENVAAPAIA IDYWRLPKDA TLKDVVTVIR ADEAHHRDVN HFASDIRNQG KELREAAAPI GYH //