NDUS4_BOVIN
ID NDUS4_BOVIN Reviewed; 175 AA.
AC Q02375;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial;
DE AltName: Full=Complex I-18 kDa;
DE Short=CI-18 kDa;
DE AltName: Full=Complex I-AQDQ;
DE Short=CI-AQDQ;
DE AltName: Full=NADH-ubiquinone oxidoreductase 18 kDa subunit;
DE Flags: Precursor;
GN Name=NDUFS4;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Heart;
RX PubMed=1518044; DOI=10.1016/0022-2836(92)91052-q;
RA Walker J.E., Arizmendi J.M., Dupuis A., Fearnley I.M., Finel M., Medd S.M.,
RA Pilkington S.J., Runswick M.J., Skehel J.M.;
RT "Sequences of 20 subunits of NADH:ubiquinone oxidoreductase from bovine
RT heart mitochondria. Application of a novel strategy for sequencing proteins
RT using the polymerase chain reaction.";
RL J. Mol. Biol. 226:1051-1072(1992).
RN [2]
RP PHOSPHORYLATION.
RX PubMed=8603710; DOI=10.1016/0014-5793(95)01532-9;
RA Papa S., Sardanelli A.M., Cocco T., Speranza F., Scacco S.C.,
RA Technikova-Dobrova Z.;
RT "The nuclear-encoded 18 kDa (IP) AQDQ subunit of bovine heart complex I is
RT phosphorylated by the mitochondrial cAMP-dependent protein kinase.";
RL FEBS Lett. 379:299-301(1996).
RN [3]
RP PARTIAL PROTEIN SEQUENCE, FUNCTION, SUBUNIT, AND IDENTIFICATION IN COMPLEX
RP I.
RX PubMed=10852722; DOI=10.1021/bi000335t;
RA Sazanov L.A., Peak-Chew S.Y., Fearnley I.M., Walker J.E.;
RT "Resolution of the membrane domain of bovine complex I into subcomplexes:
RT implications for the structural organization of the enzyme.";
RL Biochemistry 39:7229-7235(2000).
RN [4]
RP SUBUNIT, IDENTIFICATION IN COMPLEX I, AND FUNCTION.
RX PubMed=18721790; DOI=10.1016/j.ab.2008.07.029;
RA Lemma-Gray P., Valusova E., Carroll C.A., Weintraub S.T., Musatov A.,
RA Robinson N.C.;
RT "Subunit analysis of bovine heart complex I by reversed-phase high-
RT performance liquid chromatography, electrospray ionization-tandem mass
RT spectrometry, and matrix-assisted laser desorption/ionization-time-of-
RT flight mass spectrometry.";
RL Anal. Biochem. 382:116-121(2008).
RN [5]
RP PHOSPHORYLATION AT SER-173.
RX PubMed=20433953; DOI=10.1016/j.mito.2010.04.005;
RA De Rasmo D., Palmisano G., Scacco S., Technikova-Dobrova Z., Panelli D.,
RA Cocco T., Sardanelli A.M., Gnoni A., Micelli L., Trani A., Di Luccia A.,
RA Papa S.;
RT "Phosphorylation pattern of the NDUFS4 subunit of complex I of the
RT mammalian respiratory chain.";
RL Mitochondrion 10:464-471(2010).
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. {ECO:0000269|PubMed:10852722,
CC ECO:0000269|PubMed:18721790}.
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 (PubMed:10852722, PubMed:18721790). Interacts with BCAP31 and TOMM40;
CC the interaction mediates its translocation to the mitochondria; the
CC interaction with BCAP31 is direct (By similarity).
CC {ECO:0000250|UniProtKB:O43181, ECO:0000269|PubMed:10852722,
CC ECO:0000269|PubMed:18721790}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:10852722, ECO:0000269|PubMed:18721790}; Peripheral
CC membrane protein {ECO:0000269|PubMed:10852722,
CC ECO:0000269|PubMed:18721790}; Matrix side {ECO:0000269|PubMed:10852722,
CC ECO:0000269|PubMed:18721790}. Note=The interaction with BCAP31 mediates
CC mitochondria localization. {ECO:0000250|UniProtKB:O43181}.
CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:8603710}.
CC -!- SIMILARITY: Belongs to the complex I NDUFS4 subunit family.
CC {ECO:0000305}.
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DR EMBL; X63215; CAA44900.1; -; mRNA.
DR PIR; S28240; S28240.
DR RefSeq; NP_786994.1; NM_175800.2.
DR PDB; 5O31; EM; 4.13 A; Q=43-175.
DR PDB; 7QSD; EM; 3.10 A; Q=1-175.
DR PDBsum; 5O31; -.
DR PDBsum; 7QSD; -.
DR AlphaFoldDB; Q02375; -.
DR SMR; Q02375; -.
DR CORUM; Q02375; -.
DR DIP; DIP-38808N; -.
DR IntAct; Q02375; 3.
DR STRING; 9913.ENSBTAP00000044670; -.
DR TCDB; 3.D.1.6.1; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR iPTMnet; Q02375; -.
DR PaxDb; Q02375; -.
DR PeptideAtlas; Q02375; -.
DR PRIDE; Q02375; -.
DR Ensembl; ENSBTAT00000047463; ENSBTAP00000044670; ENSBTAG00000003728.
DR GeneID; 327680; -.
DR KEGG; bta:327680; -.
DR CTD; 4724; -.
DR VEuPathDB; HostDB:ENSBTAG00000003728; -.
DR VGNC; VGNC:50229; NDUFS4.
DR eggNOG; KOG3389; Eukaryota.
DR GeneTree; ENSGT00390000013835; -.
DR HOGENOM; CLU_077196_3_0_1; -.
DR InParanoid; Q02375; -.
DR OMA; GTIMKFD; -.
DR OrthoDB; 1507807at2759; -.
DR TreeFam; TF105619; -.
DR Proteomes; UP000009136; Chromosome 20.
DR Bgee; ENSBTAG00000003728; Expressed in tongue muscle and 105 other tissues.
DR ExpressionAtlas; Q02375; baseline and differential.
DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; IDA:UniProtKB.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; ISS:AgBase.
DR GO; GO:0007420; P:brain development; ISS:AgBase.
DR GO; GO:0045333; P:cellular respiration; ISS:AgBase.
DR GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; ISS:AgBase.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; ISS:AgBase.
DR GO; GO:0072593; P:reactive oxygen species metabolic process; ISS:AgBase.
DR GO; GO:0001932; P:regulation of protein phosphorylation; IEA:Ensembl.
DR GO; GO:0051591; P:response to cAMP; ISS:AgBase.
DR Gene3D; 3.30.160.190; -; 1.
DR InterPro; IPR006885; NADH_UbQ_FeS_4_mit.
DR InterPro; IPR038532; NDUFS4-like_sf.
DR PANTHER; PTHR12219; PTHR12219; 1.
DR Pfam; PF04800; ETC_C1_NDUFA4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Electron transport; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Phosphoprotein;
KW Reference proteome; Respiratory chain; Transit peptide; Transport.
FT TRANSIT 1..42
FT /note="Mitochondrion"
FT CHAIN 43..175
FT /note="NADH dehydrogenase [ubiquinone] iron-sulfur protein
FT 4, mitochondrial"
FT /id="PRO_0000020037"
FT REGION 149..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 173
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:20433953"
SQ SEQUENCE 175 AA; 19812 MW; C77BE67FE6E5A407 CRC64;
MAAVSMSVAL RQALWGRRVA TVAAVSVSKV STRSLSTSTW RLAQDQTRDT QLITVDEKLD
ITTITGVPEE HIKTRKARIF VPARNNMQSG VNNTKKWKME FDTRERWENP LMGWASTADP
LSNLVLTFST KEDAVAFAEK NGWSYDVEER KVPKPKSKSY GANFSWNKRT RVSTK
