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Q9CXZ1

- NDUS4_MOUSE

UniProt

Q9CXZ1 - NDUS4_MOUSE

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Protein

NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial

Gene

Ndufs4

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.

GO - Molecular functioni

  1. NADH dehydrogenase (ubiquinone) activity Source: MGI

GO - Biological processi

  1. electron transport chain Source: InterPro
  2. regulation of protein phosphorylation Source: MGI
Complete GO annotation...

Keywords - Biological processi

Electron transport, Respiratory chain, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial
Alternative name(s):
Complex I-18 kDa
Short name:
CI-18 kDa
Complex I-AQDQ
Short name:
CI-AQDQ
NADH-ubiquinone oxidoreductase 18 kDa subunit
Gene namesi
Name:Ndufs4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Unplaced

Organism-specific databases

MGIiMGI:1343135. Ndufs4.

Subcellular locationi

Mitochondrion inner membrane By similarity; Peripheral membrane protein By similarity; Matrix side By similarity

GO - Cellular componenti

  1. mitochondrial respiratory chain complex I Source: MGI
  2. mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4242MitochondrionBy similarityAdd
BLAST
Chaini43 – 175133NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrialPRO_0000020039Add
BLAST

Proteomic databases

MaxQBiQ9CXZ1.
PaxDbiQ9CXZ1.
PRIDEiQ9CXZ1.

PTM databases

PhosphoSiteiQ9CXZ1.

Expressioni

Gene expression databases

CleanExiMM_NDUFS4.
GenevestigatoriQ9CXZ1.

Interactioni

Subunit structurei

Mammalian complex I is composed of 45 different subunits. This is a component of the iron-sulfur (IP) fragment of the enzyme By similarity.By similarity

Protein-protein interaction databases

BioGridi201718. 1 interaction.
IntActiQ9CXZ1. 2 interactions.
MINTiMINT-4104504.

Structurei

3D structure databases

ProteinModelPortaliQ9CXZ1.
SMRiQ9CXZ1. Positions 78-147.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the complex I NDUFS4 subunit family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiNOG79671.
HOGENOMiHOG000140414.
HOVERGENiHBG003007.
InParanoidiQ9CXZ1.
KOiK03937.
PhylomeDBiQ9CXZ1.

Family and domain databases

InterProiIPR006885. NADH_UbQ_FeS_4_mit.
[Graphical view]
PANTHERiPTHR12219. PTHR12219. 1 hit.
PfamiPF04800. ETC_C1_NDUFA4. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9CXZ1-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAAVSISVSL RQAMLGRRAM ATAAVSVCRV PSRLLSTSTW KLADNQTRDT
60 70 80 90 100
QLITVDEKLD ITTLTGVPEE HIKTRKVRIF VPARNNMQSG VNNTKKWKME
110 120 130 140 150
FDTRERWENP LMGWASTADP LSNMVLTFSA KEDAIAFAEK NGWSYDVEEK
160 170
KVPKPKSKSY GANFSWNKRT RVSTK
Length:175
Mass (Da):19,785
Last modified:May 10, 2004 - v3
Checksum:i33D565B204D1C7A2
GO

Sequence cautioni

The sequence AAD30474.1 differs from that shown. Reason: Erroneous initiation.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti68 – 681P → Q in BAB27417. (PubMed:16141072)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK011124 mRNA. Translation: BAB27417.2.
AF124785 mRNA. Translation: AAD30474.1. Different initiation.
CCDSiCCDS49368.1.
RefSeqiNP_035017.2. NM_010887.2.
UniGeneiMm.253142.

Genome annotation databases

GeneIDi17993.
KEGGimmu:17993.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK011124 mRNA. Translation: BAB27417.2 .
AF124785 mRNA. Translation: AAD30474.1 . Different initiation.
CCDSi CCDS49368.1.
RefSeqi NP_035017.2. NM_010887.2.
UniGenei Mm.253142.

3D structure databases

ProteinModelPortali Q9CXZ1.
SMRi Q9CXZ1. Positions 78-147.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 201718. 1 interaction.
IntActi Q9CXZ1. 2 interactions.
MINTi MINT-4104504.

PTM databases

PhosphoSitei Q9CXZ1.

Proteomic databases

MaxQBi Q9CXZ1.
PaxDbi Q9CXZ1.
PRIDEi Q9CXZ1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 17993.
KEGGi mmu:17993.

Organism-specific databases

CTDi 4724.
MGIi MGI:1343135. Ndufs4.

Phylogenomic databases

eggNOGi NOG79671.
HOGENOMi HOG000140414.
HOVERGENi HBG003007.
InParanoidi Q9CXZ1.
KOi K03937.
PhylomeDBi Q9CXZ1.

Miscellaneous databases

NextBioi 292975.
PROi Q9CXZ1.
SOURCEi Search...

Gene expression databases

CleanExi MM_NDUFS4.
Genevestigatori Q9CXZ1.

Family and domain databases

InterProi IPR006885. NADH_UbQ_FeS_4_mit.
[Graphical view ]
PANTHERi PTHR12219. PTHR12219. 1 hit.
Pfami PF04800. ETC_C1_NDUFA4. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Liver.
  2. "Up-regulation of nuclear and mitochondrial genes in the skeletal muscle of mice lacking the heart/muscle isoform of the adenine nucleotide translocator."
    Murdock D.G., Boone B.E., Esposito L.A., Wallace D.C.
    J. Biol. Chem. 274:14429-14433(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 7-175.
    Strain: BALB/c.
    Tissue: Skeletal muscle.
  3. Lubec G., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 49-73; 132-150 AND 159-168, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6.
    Tissue: Brain.

Entry informationi

Entry nameiNDUS4_MOUSE
AccessioniPrimary (citable) accession number: Q9CXZ1
Secondary accession number(s): Q9WUB1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: May 10, 2004
Last modified: October 1, 2014
This is version 96 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3