ID   NDUB7_PONPY             Reviewed;         137 AA.
AC   Q0MQE2;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 58.
DE   RecName: Full=NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7;
DE   AltName: Full=Complex I-B18;
DE            Short=CI-B18;
DE   AltName: Full=NADH-ubiquinone oxidoreductase B18 subunit;
GN   Name=NDUFB7;
OS   Pongo pygmaeus (Bornean orangutan).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9600;
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:P17568}.
CC   -!- SUBUNIT: Complex I is composed of 45 different subunits.
CC       {ECO:0000250|UniProtKB:P17568}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:P17568}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P17568}. Mitochondrion intermembrane space
CC       {ECO:0000250|UniProtKB:P17568}.
CC   -!- DOMAIN: Contains two 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:P17568}.
CC   -!- SIMILARITY: Belongs to the complex I NDUFB7 subunit family.
CC       {ECO:0000305}.
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; DQ885692; ABH12201.1; -; mRNA.
DR   AlphaFoldDB; Q0MQE2; -.
DR   SMR; Q0MQE2; -.
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:0032981; P:mitochondrial respiratory chain complex I assembly; ISS:UniProtKB.
DR   InterPro; IPR008698; NDUB7.
DR   PANTHER; PTHR20900; PTHR20900; 1.
DR   Pfam; PF05676; NDUF_B7; 1.
DR   PROSITE; PS51808; CHCH; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Electron transport; Lipoprotein; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Myristate; Phosphoprotein; Respiratory chain;
KW   Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..137
FT                   /note="NADH dehydrogenase [ubiquinone] 1 beta subcomplex
FT                   subunit 7"
FT                   /id="PRO_0000251840"
FT   DOMAIN          56..98
FT                   /note="CHCH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   REGION          113..137
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           59..69
FT                   /note="Cx9C motif 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   MOTIF           80..90
FT                   /note="Cx9C motif 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   MOD_RES         73
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CR61"
FT   LIPID           2
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000250"
FT   DISULFID        59..90
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   DISULFID        69..80
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
SQ   SEQUENCE   137 AA;  16428 MW;  3B337170443D9276 CRC64;
     MGAHLVRRYL GDASVEPDPL QMPTFPPDYG FPERKEREMV ATQQEMMDAQ LRLQLRDYCA
     HYLIRLLKCK RDSFPNFLAC KQERHDWDYC EHRDYVMRMK EFERERRLLQ RKKRREKKAA
     ELAKGQGPGE VDPKVAL