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Database: UniProt
Entry: D2A6F4_TRICA
LinkDB: D2A6F4_TRICA
Original site: D2A6F4_TRICA 
ID   D2A6F4_TRICA            Unreviewed;       141 AA.
AC   D2A6F4;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   RecName: Full=NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12 {ECO:0000256|RuleBase:RU363103};
GN   Name=AUGUSTUS-3.0.2_15691 {ECO:0000313|EMBL:EFA05745.1};
GN   ORFNames=TcasGA2_TC015691 {ECO:0000313|EMBL:EFA05745.1};
OS   Tribolium castaneum (Red flour beetle).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC   Tenebrionidae; Tenebrionidae incertae sedis; Tribolium.
OX   NCBI_TaxID=7070 {ECO:0000313|EMBL:EFA05745.1, ECO:0000313|Proteomes:UP000007266};
RN   [1] {ECO:0000313|EMBL:EFA05745.1, ECO:0000313|Proteomes:UP000007266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Georgia GA2 {ECO:0000313|EMBL:EFA05745.1,
RC   ECO:0000313|Proteomes:UP000007266};
RX   PubMed=18362917; DOI=10.1038/nature06784;
RG   Tribolium Genome Sequencing Consortium;
RA   Richards S., Gibbs R.A., Weinstock G.M., Brown S.J., Denell R.,
RA   Beeman R.W., Gibbs R., Beeman R.W., Brown S.J., Bucher G., Friedrich M.,
RA   Grimmelikhuijzen C.J., Klingler M., Lorenzen M., Richards S., Roth S.,
RA   Schroder R., Tautz D., Zdobnov E.M., Muzny D., Gibbs R.A., Weinstock G.M.,
RA   Attaway T., Bell S., Buhay C.J., Chandrabose M.N., Chavez D.,
RA   Clerk-Blankenburg K.P., Cree A., Dao M., Davis C., Chacko J., Dinh H.,
RA   Dugan-Rocha S., Fowler G., Garner T.T., Garnes J., Gnirke A., Hawes A.,
RA   Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N., Joshi V.,
RA   Khan Z.M., Jackson L., Kovar C., Kowis A., Lee S., Lewis L.R., Margolis J.,
RA   Morgan M., Nazareth L.V., Nguyen N., Okwuonu G., Parker D., Richards S.,
RA   Ruiz S.J., Santibanez J., Savard J., Scherer S.E., Schneider B.,
RA   Sodergren E., Tautz D., Vattahil S., Villasana D., White C.S., Wright R.,
RA   Park Y., Beeman R.W., Lord J., Oppert B., Lorenzen M., Brown S., Wang L.,
RA   Savard J., Tautz D., Richards S., Weinstock G., Gibbs R.A., Liu Y.,
RA   Worley K., Weinstock G., Elsik C.G., Reese J.T., Elhaik E., Landan G.,
RA   Graur D., Arensburger P., Atkinson P., Beeman R.W., Beidler J., Brown S.J.,
RA   Demuth J.P., Drury D.W., Du Y.Z., Fujiwara H., Lorenzen M., Maselli V.,
RA   Osanai M., Park Y., Robertson H.M., Tu Z., Wang J.J., Wang S., Richards S.,
RA   Song H., Zhang L., Sodergren E., Werner D., Stanke M., Morgenstern B.,
RA   Solovyev V., Kosarev P., Brown G., Chen H.C., Ermolaeva O., Hlavina W.,
RA   Kapustin Y., Kiryutin B., Kitts P., Maglott D., Pruitt K., Sapojnikov V.,
RA   Souvorov A., Mackey A.J., Waterhouse R.M., Wyder S., Zdobnov E.M.,
RA   Zdobnov E.M., Wyder S., Kriventseva E.V., Kadowaki T., Bork P., Aranda M.,
RA   Bao R., Beermann A., Berns N., Bolognesi R., Bonneton F., Bopp D.,
RA   Brown S.J., Bucher G., Butts T., Chaumot A., Denell R.E., Ferrier D.E.,
RA   Friedrich M., Gordon C.M., Jindra M., Klingler M., Lan Q., Lattorff H.M.,
RA   Laudet V., von Levetsow C., Liu Z., Lutz R., Lynch J.A., da Fonseca R.N.,
RA   Posnien N., Reuter R., Roth S., Savard J., Schinko J.B., Schmitt C.,
RA   Schoppmeier M., Schroder R., Shippy T.D., Simonnet F., Marques-Souza H.,
RA   Tautz D., Tomoyasu Y., Trauner J., Van der Zee M., Vervoort M.,
RA   Wittkopp N., Wimmer E.A., Yang X., Jones A.K., Sattelle D.B., Ebert P.R.,
RA   Nelson D., Scott J.G., Beeman R.W., Muthukrishnan S., Kramer K.J.,
RA   Arakane Y., Beeman R.W., Zhu Q., Hogenkamp D., Dixit R., Oppert B.,
RA   Jiang H., Zou Z., Marshall J., Elpidina E., Vinokurov K., Oppert C.,
RA   Zou Z., Evans J., Lu Z., Zhao P., Sumathipala N., Altincicek B.,
RA   Vilcinskas A., Williams M., Hultmark D., Hetru C., Jiang H.,
RA   Grimmelikhuijzen C.J., Hauser F., Cazzamali G., Williamson M., Park Y.,
RA   Li B., Tanaka Y., Predel R., Neupert S., Schachtner J., Verleyen P.,
RA   Raible F., Bork P., Friedrich M., Walden K.K., Robertson H.M., Angeli S.,
RA   Foret S., Bucher G., Schuetz S., Maleszka R., Wimmer E.A., Beeman R.W.,
RA   Lorenzen M., Tomoyasu Y., Miller S.C., Grossmann D., Bucher G.;
RT   "The genome of the model beetle and pest Tribolium castaneum.";
RL   Nature 452:949-955(2008).
RN   [2] {ECO:0000313|EMBL:EFA05745.1, ECO:0000313|Proteomes:UP000007266}
RP   GENOME REANNOTATION.
RC   STRAIN=Georgia GA2 {ECO:0000313|EMBL:EFA05745.1,
RC   ECO:0000313|Proteomes:UP000007266};
RX   PubMed=19820115; DOI=10.1093/nar/gkp807;
RA   Kim H.S., Murphy T., Xia J., Caragea D., Park Y., Beeman R.W.,
RA   Lorenzen M.D., Butcher S., Manak J.R., Brown S.J.;
RT   "BeetleBase in 2010: revisions to provide comprehensive genomic information
RT   for Tribolium castaneum.";
RL   Nucleic Acids Res. 38:D437-D442(2010).
CC   -!- FUNCTION: Accessory subunit of the mitochondrial membrane respiratory
CC       chain NADH dehydrogenase (Complex I), that is believed not to be
CC       involved in catalysis. Complex I functions in the transfer of electrons
CC       from NADH to the respiratory chain. The immediate electron acceptor for
CC       the enzyme is believed to be ubiquinone.
CC       {ECO:0000256|ARBA:ARBA00003195, ECO:0000256|RuleBase:RU363103}.
CC   -!- SUBUNIT: Complex I is composed of 45 different subunits.
CC       {ECO:0000256|RuleBase:RU363103}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000256|RuleBase:RU363103}; Peripheral membrane protein
CC       {ECO:0000256|RuleBase:RU363103}; Matrix side
CC       {ECO:0000256|RuleBase:RU363103}.
CC   -!- SIMILARITY: Belongs to the complex I NDUFA12 subunit family.
CC       {ECO:0000256|ARBA:ARBA00007355, ECO:0000256|RuleBase:RU363103}.
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DR   EMBL; KQ971347; EFA05745.1; -; Genomic_DNA.
DR   RefSeq; XP_969714.1; XM_964621.3.
DR   AlphaFoldDB; D2A6F4; -.
DR   STRING; 7070.D2A6F4; -.
DR   EnsemblMetazoa; TC015691_001; TC015691_001; TC015691.
DR   GeneID; 658213; -.
DR   KEGG; tca:658213; -.
DR   eggNOG; KOG3382; Eukaryota.
DR   HOGENOM; CLU_110455_1_1_1; -.
DR   InParanoid; D2A6F4; -.
DR   OMA; WHGWIHH; -.
DR   OrthoDB; 821at2759; -.
DR   PhylomeDB; D2A6F4; -.
DR   Proteomes; UP000007266; Linkage group 6.
DR   GO; GO:0005747; C:mitochondrial respiratory chain complex I; IBA:GO_Central.
DR   GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; IEA:InterPro.
DR   GO; GO:0006979; P:response to oxidative stress; IBA:GO_Central.
DR   InterPro; IPR007763; NDUFA12.
DR   PANTHER; PTHR12910:SF2; NADH DEHYDROGENASE [UBIQUINONE] 1 ALPHA SUBCOMPLEX SUBUNIT 12; 1.
DR   PANTHER; PTHR12910; NADH-UBIQUINONE OXIDOREDUCTASE SUBUNIT B17.2; 1.
DR   Pfam; PF05071; NDUFA12; 1.
PE   3: Inferred from homology;
KW   Electron transport {ECO:0000256|RuleBase:RU363103};
KW   Membrane {ECO:0000256|RuleBase:RU363103};
KW   Mitochondrion {ECO:0000256|RuleBase:RU363103};
KW   Mitochondrion inner membrane {ECO:0000256|RuleBase:RU363103};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007266};
KW   Respiratory chain {ECO:0000256|RuleBase:RU363103};
KW   Transport {ECO:0000256|RuleBase:RU363103}.
SQ   SEQUENCE   141 AA;  16805 MW;  9FEF6F2096D59375 CRC64;
     MAKFLGIDKV LSVLNIVKEN GGLRASLYKM FRMDELKVGT LVGTDKYGNK YYENKRFFYG
     RNRWIEYAPY YHLDYDGSQV PAEWFGWLHY KTDLPPDQEP FRPKYKWMLD HTENLSGTPG
     QYMPYSTTRP KIEPWIPTKR C
//
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