NDUS5_MACFA
ID NDUS5_MACFA Reviewed; 106 AA.
AC Q4R3M6;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=NADH dehydrogenase [ubiquinone] iron-sulfur protein 5;
DE AltName: Full=Complex I-15 kDa;
DE Short=CI-15 kDa;
DE AltName: Full=NADH-ubiquinone oxidoreductase 15 kDa subunit;
GN Name=NDUFS5; ORFNames=QtsA-15861;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
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:O43920}.
CC -!- SUBUNIT: Mammalian complex I is composed of 45 different subunits. This
CC is a component of the iron-sulfur (IP) fragment of the enzyme.
CC {ECO:0000250|UniProtKB:O43920}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:O43920}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:O43920}. Mitochondrion intermembrane space
CC {ECO:0000250|UniProtKB:O43920}.
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:O43920}.
CC -!- SIMILARITY: Belongs to the complex I NDUFS5 subunit family.
CC {ECO:0000305}.
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DR EMBL; AB179240; BAE02291.1; -; mRNA.
DR RefSeq; NP_001271006.1; NM_001284077.1.
DR AlphaFoldDB; Q4R3M6; -.
DR SMR; Q4R3M6; -.
DR STRING; 9541.XP_005543960.1; -.
DR PRIDE; Q4R3M6; -.
DR GeneID; 101867140; -.
DR CTD; 4725; -.
DR VEuPathDB; HostDB:ENSMFAG00000027526; -.
DR eggNOG; KOG4110; Eukaryota.
DR OMA; CAHGIGQ; -.
DR OrthoDB; 1549192at2759; -.
DR Proteomes; UP000233100; Chromosome 1.
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:0032981; P:mitochondrial respiratory chain complex I assembly; ISS:UniProtKB.
DR InterPro; IPR019342; NADH_UbQ_OxRdtase_FeS-su5.
DR PANTHER; PTHR15224; PTHR15224; 1.
DR Pfam; PF10200; Ndufs5; 1.
DR PROSITE; PS51808; CHCH; 1.
PE 3: Inferred from homology;
KW Disulfide bond; Electron transport; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Respiratory chain;
KW Transport.
FT CHAIN 1..106
FT /note="NADH dehydrogenase [ubiquinone] iron-sulfur protein
FT 5"
FT /id="PRO_0000251865"
FT DOMAIN 30..74
FT /note="CHCH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT REGION 87..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 33..43
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 DISULFID 33..66
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT DISULFID 43..56
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
SQ SEQUENCE 106 AA; 12644 MW; 241F614369658305 CRC64;
MPFLDIQKRF GLNIDRWWTI QSAEQPYKLA PRCHAFEKEW IECAHGIGAI RAEKECKIEY
DDFIECLLRQ KTMRRVNAIR RQRDKLIKEG KYTPPPHHIG KGEPRP