ID   NDUS5_PONPY             Reviewed;         106 AA.
AC   P0CB88; Q5R7L6;
DT   24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-NOV-2009, sequence version 1.
DT   25-MAY-2022, entry version 33.
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;
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: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; DQ885662; ABH12171.1; -; mRNA.
DR   AlphaFoldDB; P0CB88; -.
DR   SMR; P0CB88; -.
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; Respiratory chain; Transport.
FT   CHAIN           1..106
FT                   /note="NADH dehydrogenase [ubiquinone] iron-sulfur protein
FT                   5"
FT                   /id="PRO_0000389250"
FT   DOMAIN          30..74
FT                   /note="CHCH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   REGION          78..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;  12594 MW;  26529409D2F1ADFA CRC64;
     MPFLDIQKRF GLNIDRWLTT QSAEQPYKMA SRCHAFEKEW IECAHGIGYT RAEKECKIEY
     DDFIECLLRQ KTMRRTGTIR KQRDKLIKEG KYTPPPHHIG KGEPRP