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O70579 (PM34_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 105. 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:
Peroxisomal membrane protein PMP34
Alternative name(s):
34 kDa peroxisomal membrane protein
Solute carrier family 25 member 17
Gene names
Name:Slc25a17
Synonyms:Pmp34, Pmp35
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length307 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Peroxisomal transporter for multiple cofactors like coenzyme A (CoA), flavin adenine dinucleotide (FAD), flavin mononucleotide (FMN) and nucleotide adenosine monophosphate (AMP), and to a lesser extend for nicotinamide adenine dinucleotide (NAD+), adenosine diphosphate (ADP) and adenosine 3',5'-diphosphate (PAP). May catalyze the transport of free CoA, FAD and NAD+ from the cytosol into the peroxisomal matrix by a counter-exchange mechanism. Inhibited by pyridoxal 5'-phosphate and bathophenanthroline in vitro By similarity.

Subunit structure

Interacts (via N- and C-terminus peroxisomal targeting regions) with PEX19; the interaction occurs with the newly synthesized SLC25A17 in the cytosol By similarity.

Subcellular location

Cytoplasm By similarity. Peroxisome membrane; Multi-pass membrane protein.

Tissue specificity

Expressed in liver.

Domain

The N- and C-terminal portions are exposed to the cytoplasm. A region between helical transmembrane domains (TM) 4 and 5 and TM1-TM3 or TM4-TM6 are necessary for the peroxisome-targeting activity By similarity. Lacks a typical peroxisomal sorting signal.

Sequence similarities

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

Contains 3 Solcar repeats.

Ontologies

Keywords
   Biological processTransport
   Cellular componentCytoplasm
Membrane
Peroxisome
   DomainRepeat
Transmembrane
Transmembrane helix
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processADP transport

Inferred from sequence or structural similarity. Source: UniProtKB

AMP transport

Inferred from sequence or structural similarity. Source: UniProtKB

FAD transmembrane transport

Inferred from sequence or structural similarity. Source: UniProtKB

NAD transport

Inferred from sequence or structural similarity. Source: UniProtKB

coenzyme A transmembrane transport

Inferred from sequence or structural similarity. Source: UniProtKB

fatty acid beta-oxidation

Inferred from electronic annotation. Source: Ensembl

fatty acid transport

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentintegral component of peroxisomal membrane

Inferred from sequence or structural similarity. Source: UniProtKB

mitochondrion

Inferred from direct assay PubMed 14651853. Source: MGI

peroxisomal membrane

Inferred from direct assay Ref.1. Source: MGI

   Molecular_functionADP transmembrane transporter activity

Inferred from sequence or structural similarity. Source: UniProtKB

AMP transmembrane transporter activity

Inferred from sequence or structural similarity. Source: UniProtKB

ATP transmembrane transporter activity

Inferred from electronic annotation. Source: Ensembl

FAD transmembrane transporter activity

Inferred from sequence or structural similarity. Source: UniProtKB

FMN transmembrane transporter activity

Inferred from sequence or structural similarity. Source: UniProtKB

NAD transporter activity

Inferred from sequence or structural similarity. Source: UniProtKB

coenzyme A transmembrane transporter activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 307307Peroxisomal membrane protein PMP34
PRO_0000090706

Regions

Topological domain1 – 99Cytoplasmic By similarity
Transmembrane10 – 3021Helical; Name=1; Potential
Topological domain31 – 6636Lumenal Potential
Transmembrane67 – 8721Helical; Name=2; Potential
Topological domain88 – 10417Cytoplasmic Potential
Transmembrane105 – 12521Helical; Name=3; Potential
Topological domain126 – 16035Lumenal Potential
Transmembrane161 – 18121Helical; Name=4; Potential
Topological domain182 – 20221Cytoplasmic Potential
Transmembrane203 – 22321Helical; Name=5; Potential
Topological domain224 – 28057Lumenal Potential
Transmembrane281 – 30121Helical; Name=6; Potential
Topological domain302 – 3076Cytoplasmic By similarity
Repeat7 – 9286Solcar 1
Repeat99 – 19294Solcar 2
Repeat200 – 29495Solcar 3
Region1 – 147147Necessary for targeting to peroxisomes and interaction with PEX19 By similarity
Region244 – 30764Necessary for targeting to peroxisomes and interaction with PEX19 By similarity
Motif190 – 19910Peroxisome localization signal By similarity

Sequences

Sequence LengthMass (Da)Tools
O70579 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 8CE406CE66D0EB06

FASTA30734,413
        10         20         30         40         50         60 
MASVLSYESL VHAVAGAVGS VTAMTVFFPL DTARLRLQVD EKRKSKTTHA VLLEIIKEEG 

        70         80         90        100        110        120 
LLAPYRGWFP VISSLCCSNF VYFYTFNSLK AVWVKGQRSS TGKDLVVGFV AGVVNVLLTT 

       130        140        150        160        170        180 
PLWVVNTRLK LQGAKFRNED IIPTNYKGII DAFHQIIRDE GILALWNGTF PSLLLVFNPA 

       190        200        210        220        230        240 
IQFMFYEGLK RQLLKKRMKL SSLDVFIIGA IAKAIATTVT YPMQTVQSIL RFGRHRLNPE 

       250        260        270        280        290        300 
NRTLGSLRNV LSLLHQRVKR FGIMGLYKGL EAKLLQTVLT AALMFLVYEK LTAATFTVMG 


LKSTHKH 

« Hide

References

« Hide 'large scale' references
[1]"Identification and characterization of human PMP34, a protein closely related to the peroxisomal integral membrane protein PMP47 of Candida boidinii."
Wylin T., Baes M., Brees C., Mannaerts G.P., Fransen M., Van Veldhoven P.P.
Eur. J. Biochem. 258:332-338(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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: Kidney.
[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].
Strain: Czech II and FVB/N.
Tissue: Mammary gland.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ006341 mRNA. Translation: CAA06984.1.
AK002388 mRNA. Translation: BAB22062.1.
BC008571 mRNA. Translation: AAH08571.1.
BC011292 mRNA. Translation: AAH11292.1.
RefSeqNP_035529.1. NM_011399.3.
UniGeneMm.222536.

3D structure databases

ProteinModelPortalO70579.
SMRO70579. Positions 11-303.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000023040.

PTM databases

PhosphoSiteO70579.

Proteomic databases

PaxDbO70579.
PRIDEO70579.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000023040; ENSMUSP00000023040; ENSMUSG00000022404.
GeneID20524.
KEGGmmu:20524.
UCSCuc007wwk.1. mouse.

Organism-specific databases

CTD10478.
MGIMGI:1342248. Slc25a17.

Phylogenomic databases

eggNOGNOG258628.
GeneTreeENSGT00600000084419.
HOGENOMHOG000159426.
HOVERGENHBG003235.
InParanoidO70579.
KOK13354.
OMAVWVKGQH.
OrthoDBEOG7Q8CNK.
PhylomeDBO70579.
TreeFamTF324772.

Gene expression databases

BgeeO70579.
GenevestigatorO70579.

Family and domain databases

Gene3D1.50.40.10. 1 hit.
InterProIPR002067. Mit_carrier.
IPR018108. Mitochondrial_sb/sol_carrier.
IPR023395. Mt_carrier_dom.
[Graphical view]
PfamPF00153. Mito_carr. 3 hits.
[Graphical view]
PRINTSPR00926. MITOCARRIER.
SUPFAMSSF103506. SSF103506. 1 hit.
PROSITEPS50920. SOLCAR. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSLC25A17. mouse.
NextBio298759.
PROO70579.
SOURCESearch...

Entry information

Entry namePM34_MOUSE
AccessionPrimary (citable) accession number: O70579
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: August 1, 1998
Last modified: April 16, 2014
This is version 105 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