NDUA8_PANTR
ID NDUA8_PANTR Reviewed; 172 AA.
AC Q0MQB1;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8;
DE AltName: Full=Complex I-19kD;
DE Short=CI-19kD;
DE AltName: Full=NADH-ubiquinone oxidoreductase 19 kDa subunit;
GN Name=NDUFA8;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=16828987; DOI=10.1016/j.gene.2006.03.015;
RA Mishmar D., Ruiz-Pesini E., Mondragon-Palomino M., Procaccio V., Gaut B.,
RA Wallace D.C.;
RT "Adaptive selection of mitochondrial complex I subunits during primate
RT radiation.";
RL Gene 378:11-18(2006).
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:0000250|UniProtKB:P51970}.
CC -!- SUBUNIT: Complex I is composed of 45 different subunits.
CC {ECO:0000250|UniProtKB:P51970}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P51970}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P51970}. Mitochondrion intermembrane space
CC {ECO:0000250|UniProtKB:P51970}. Mitochondrion
CC {ECO:0000250|UniProtKB:P51970}.
CC -!- DOMAIN: Contains four C-X9-C motifs that are predicted to form a helix-
CC coil-helix structure, permitting the formation of intramolecular
CC disulfide bonds. {ECO:0000250|UniProtKB:P51970}.
CC -!- SIMILARITY: Belongs to the complex I NDUFA8 subunit family.
CC {ECO:0000305}.
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DR EMBL; DQ885723; ABH12232.1; -; mRNA.
DR RefSeq; NP_001065268.1; NM_001071800.1.
DR AlphaFoldDB; Q0MQB1; -.
DR SMR; Q0MQB1; -.
DR STRING; 9598.ENSPTRP00000036436; -.
DR PaxDb; Q0MQB1; -.
DR Ensembl; ENSPTRT00000039432; ENSPTRP00000036436; ENSPTRG00000021319.
DR GeneID; 464897; -.
DR KEGG; ptr:464897; -.
DR CTD; 4702; -.
DR VGNC; VGNC:4799; NDUFA8.
DR eggNOG; KOG3458; Eukaryota.
DR GeneTree; ENSGT00390000008938; -.
DR HOGENOM; CLU_081931_2_1_1; -.
DR InParanoid; Q0MQB1; -.
DR OMA; DRPNKEF; -.
DR OrthoDB; 1526152at2759; -.
DR TreeFam; TF105633; -.
DR Proteomes; UP000002277; Chromosome 9.
DR Bgee; ENSPTRG00000021319; Expressed in heart and 21 other tissues.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; IEA:InterPro.
DR GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; ISS:UniProtKB.
DR InterPro; IPR010625; CHCH.
DR InterPro; IPR016680; NDUFA8.
DR PANTHER; PTHR13344; PTHR13344; 1.
DR Pfam; PF06747; CHCH; 1.
DR PIRSF; PIRSF017016; NDUA8; 1.
DR PROSITE; PS51808; CHCH; 2.
PE 2: Evidence at transcript level;
KW Disulfide bond; Electron transport; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Repeat;
KW Respiratory chain; Transport.
FT CHAIN 1..172
FT /note="NADH dehydrogenase [ubiquinone] 1 alpha subcomplex
FT subunit 8"
FT /id="PRO_0000251809"
FT DOMAIN 33..74
FT /note="CHCH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT DOMAIN 75..118
FT /note="CHCH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT REGION 133..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 36..46
FT /note="Cx9C motif 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT MOTIF 56..66
FT /note="Cx9C motif 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT MOTIF 78..88
FT /note="Cx9C motif 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT MOTIF 100..110
FT /note="Cx9C motif 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT COMPBIAS 133..152
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 36..66
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT DISULFID 46..56
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT DISULFID 78..110
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT DISULFID 88..100
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
SQ SEQUENCE 172 AA; 20105 MW; E1647472B69E1149 CRC64;
MPGIVELPTL EELKVDEVKI SSAVLKAAAH HYGAQCDKPN KEFMLCRWEE KDPRRCLEEG
KLVNKCALDF FRQIKRHCAE PFTEYWTCID YTGQQLFRHC RKQQAKFDEC VLDKLGWVRP
DLGELSKVTK VKTDRPLPEN PYHSRPRPDP SPEIEGDLQP ATHGSRFYFW TK
