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Q3V132 (ADT4_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ADP/ATP translocase 4
Alternative name(s):
ADP,ATP carrier protein 4
Adenine nucleotide translocator 4
Short name=ANT 4
Solute carrier family 25 member 31
Sperm flagellar energy carrier protein
Gene names
Name:Slc25a31
Synonyms:Aac4, Ant4, Sfec
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length320 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Catalyzes the exchange of cytoplasmic ADP with mitochondrial ATP across the mitochondrial inner membrane. May serve to mediate energy generating and energy consuming processes in the distal flagellum, possibly as a nucleotide shuttle between flagellar glycolysis, protein phosphorylation and mechanisms of motility. Ref.1

Subcellular location

Mitochondrion inner membrane; Multi-pass membrane protein By similarity. Cell projectionciliumflagellum By similarity. Note: In sperm flagellum this protein is located in the fibrous sheath, a non-mitochondrial region By similarity.

Sequence similarities

Belongs to the mitochondrial carrier (TC 2.A.29) family. [View classification]

Contains 3 Solcar repeats.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 320320ADP/ATP translocase 4
PRO_0000297626

Regions

Transmembrane24 – 4421Helical; Name=1; Potential
Transmembrane91 – 11121Helical; Name=2; Potential
Transmembrane125 – 14521Helical; Name=3; Potential
Transmembrane180 – 20021Helical; Name=4; Potential
Transmembrane222 – 24221Helical; Name=5; Potential
Transmembrane286 – 30621Helical; Name=6; Potential
Repeat19 – 11193Solcar 1
Repeat124 – 21491Solcar 2
Repeat221 – 30888Solcar 3

Experimental info

Sequence conflict381A → T in AAT42264. Ref.1
Sequence conflict381A → T in AAH50810. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q3V132 [UniParc].

Last modified October 11, 2005. Version 1.
Checksum: B718DB4AE6C6B2AA

FASTA32035,258
        10         20         30         40         50         60 
MSNESSKKQS SKKALFDPVS FSKDLLAGGV AAAVSKTAVA PIERVKLLLQ VQASSKQISP 

        70         80         90        100        110        120 
EARYKGMLDC LVRIPREQGF LSYWRGNLAN VIRYFPTQAL NFAFKDKYKE LFMSGVNKEK 

       130        140        150        160        170        180 
QFWRWFLANL ASGGAAGATS LCVVYPLDFA RTRLGVDIGK GPEQRQFTGL GDCIMKIAKS 

       190        200        210        220        230        240 
DGLIGLYQGF GVSVQGIIVY RASYFGAYDT VKGLLPKPKE TPFLVSFIIA QIVTTCSGIL 

       250        260        270        280        290        300 
SYPFDTVRRR MMMQSGESDR QYKGTIDCFL KIYRHEGVPA FFRGAFSNIL RGTGGALVLV 

       310        320 
LYDKIKEFLN IDVGGSSSGD 

« Hide

References

« Hide 'large scale' references
[1]"Compartmentalization of a unique ADP/ATP carrier protein SFEC (sperm flagellar energy carrier, AAC4) with glycolytic enzymes in the fibrous sheath of the human sperm flagellar principal piece."
Kim Y.-H., Haidl G., Schaefer M., Egner U., Mandal A., Herr J.C.
Dev. Biol. 302:463-476(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
[2]"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. expand/collapse author list , 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: Testis.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Testis.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY550241 mRNA. Translation: AAT42264.1.
AK132722 mRNA. Translation: BAE21321.1.
BC050810 mRNA. Translation: AAH50810.1.
RefSeqNP_848473.2. NM_178386.3.
UniGeneMm.78691.

3D structure databases

ProteinModelPortalQ3V132.
SMRQ3V132. Positions 19-305.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid215933. 7 interactions.
IntActQ3V132. 1 interaction.

PTM databases

PhosphoSiteQ3V132.

Proteomic databases

PaxDbQ3V132.
PRIDEQ3V132.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000091184; ENSMUSP00000088723; ENSMUSG00000069041.
GeneID73333.
KEGGmmu:73333.
UCSCuc008pbi.2. mouse.

Organism-specific databases

CTD83447.
MGIMGI:1920583. Slc25a31.

Phylogenomic databases

eggNOGNOG238123.
GeneTreeENSGT00390000011543.
HOGENOMHOG000165727.
HOVERGENHBG108348.
InParanoidQ3V132.
KOK05863.
OMARQYKGTI.
OrthoDBEOG7T1RBR.
PhylomeDBQ3V132.
TreeFamTF300743.

Gene expression databases

BgeeQ3V132.
GenevestigatorQ3V132.

Family and domain databases

Gene3D1.50.40.10. 1 hit.
InterProIPR002113. Aden_trnslctor.
IPR002067. Mit_carrier.
IPR018108. Mitochondrial_sb/sol_carrier.
IPR023395. Mt_carrier_dom.
[Graphical view]
PfamPF00153. Mito_carr. 3 hits.
[Graphical view]
PRINTSPR00927. ADPTRNSLCASE.
PR00926. MITOCARRIER.
SUPFAMSSF103506. SSF103506. 1 hit.
PROSITEPS50920. SOLCAR. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio337989.
PROQ3V132.
SOURCESearch...

Entry information

Entry nameADT4_MOUSE
AccessionPrimary (citable) accession number: Q3V132
Secondary accession number(s): Q80W28
Entry history
Integrated into UniProtKB/Swiss-Prot: August 21, 2007
Last sequence update: October 11, 2005
Last modified: April 16, 2014
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot