NDUB7_PANTR
ID NDUB7_PANTR Reviewed; 137 AA.
AC Q0MQE4;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 29-SEP-2021, entry version 67.
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 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: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}.
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DR EMBL; DQ885690; ABH12199.1; -; mRNA.
DR RefSeq; NP_001065270.1; NM_001071802.1.
DR STRING; 9598.ENSPTRP00000018081; -.
DR PaxDb; Q0MQE4; -.
DR GeneID; 468748; -.
DR KEGG; ptr:468748; -.
DR CTD; 4713; -.
DR eggNOG; KOG3468; Eukaryota.
DR InParanoid; Q0MQE4; -.
DR OrthoDB; 1570033at2759; -.
DR Proteomes; UP000002277; Unplaced.
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;
KW Reference proteome; Respiratory chain; 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_0000251839"
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; 16426 MW; 3B337164503D8662 CRC64;
MGAHLVRRYL GDASVEPDPL QMPTFPPDYG FPERKEREMV ATQQEMMDAQ LRLQLRDYCA
HYLIRLLKCK RDSFPNFXAC KQERHDWDYC EHRDYVMRMK EFERERRLLQ RKKRREKKAA
ELAKGQGPGE VDPKVAL