Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

O43808 (PM34_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length307 AA.
Sequence statusComplete.
Protein existenceEvidence at protein 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. Ref.10 Ref.12

Subunit structure

Interacts (via N- and C-terminus peroxisomal targeting regions) with PEX19; the interaction occurs with the newly synthesized SLC25A17 in the cytosol. Ref.7 Ref.9 Ref.11

Subcellular location

Cytoplasm. Peroxisome membrane; Multi-pass membrane protein Ref.8 Ref.9 Ref.11.

Tissue specificity

Ubiquitous. Expressed in liver. Ref.12

Domain

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

Sequence similarities

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

Contains 3 Solcar repeats.

Caution

Was first identified as a peroxisomal ATP transporter (Ref.10). However, later experiments showed that it acts as a peroxisomal transporter for multiple cofactors (Ref.12).

Ontologies

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

Inferred from direct assay Ref.12. Source: GOC

AMP transport

Inferred from direct assay Ref.12. Source: GOC

ATP transport

Inferred from genetic interaction Ref.10. Source: BHF-UCL

FAD transmembrane transport

Inferred from direct assay Ref.12. Source: GOC

NAD transport

Inferred from direct assay Ref.12. Source: GOC

cellular lipid metabolic process

Traceable author statement. Source: Reactome

coenzyme A transmembrane transport

Inferred from direct assay Ref.12. Source: GOC

fatty acid alpha-oxidation

Traceable author statement. Source: Reactome

fatty acid beta-oxidation

Inferred from genetic interaction Ref.10. Source: BHF-UCL

fatty acid transport

Inferred from genetic interaction Ref.10. Source: BHF-UCL

nucleotide transmembrane transport

Inferred from direct assay Ref.12. Source: GOC

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentintegral component of peroxisomal membrane

Inferred from direct assay PubMed 21153762. Source: UniProtKB

intracellular membrane-bounded organelle

Inferred from direct assay. Source: HPA

mitochondrion

Inferred from electronic annotation. Source: Ensembl

peroxisomal membrane

Inferred from direct assay Ref.9Ref.11. Source: UniProtKB

peroxisome

Inferred from direct assay Ref.1. Source: BHF-UCL

   Molecular_functionADP transmembrane transporter activity

Inferred from direct assay Ref.12. Source: UniProtKB

AMP transmembrane transporter activity

Inferred from direct assay Ref.12. Source: UniProtKB

ATP transmembrane transporter activity

Inferred from genetic interaction Ref.10. Source: BHF-UCL

FAD transmembrane transporter activity

Inferred from direct assay Ref.12. Source: UniProtKB

FMN transmembrane transporter activity

Inferred from direct assay Ref.12. Source: UniProtKB

NAD transporter activity

Inferred from direct assay Ref.12. Source: UniProtKB

chaperone binding

Inferred from physical interaction Ref.9. Source: BHF-UCL

coenzyme A transmembrane transporter activity

Inferred from direct assay Ref.12. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PEX19P408554EBI-594912,EBI-594747

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 307307Peroxisomal membrane protein PMP34
PRO_0000090705

Regions

Topological domain1 – 99Cytoplasmic Ref.8 Ref.9
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 Ref.8 Ref.9
Repeat7 – 9286Solcar 1
Repeat99 – 19294Solcar 2
Repeat200 – 29495Solcar 3
Region1 – 147147Necessary for targeting to peroxisomes and interaction with PEX19
Region244 – 30764Necessary for targeting to peroxisomes and interaction with PEX19
Motif190 – 19910Peroxisome localization signal

Natural variations

Natural variant981H → R.
Corresponds to variant rs12159334 [ dbSNP | Ensembl ].
VAR_050139

Experimental info

Mutagenesis190 – 19910KRQLLKKRMK → AAQLLAAAMA: Localizes in the cytoplasm. Ref.8
Mutagenesis283 – 2853LMF → KKK: Impairs interaction with PEX19.
Mutagenesis289 – 2902EK → LL: Impairs interaction with PEX19.
Mutagenesis302 – 3032KR → EE: No effect on interaction with PEX19.

Sequences

Sequence LengthMass (Da)Tools
O43808 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: B7043D82966D47A5

FASTA30734,567
        10         20         30         40         50         60 
MASVLSYESL VHAVAGAVGS VTAMTVFFPL DTARLRLQVD EKRKSKTTHM VLLEIIKEEG 

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

       130        140        150        160        170        180 
PLWVVNTRLK LQGAKFRNED IVPTNYKGII DAFHQIIRDE GISALWNGTF PSLLLVFNPA 

       190        200        210        220        230        240 
IQFMFYEGLK RQLLKKRMKL SSLDVFIIGA VAKAIATTVT YPLQTVQSIL RFGRHRLNPE 

       250        260        270        280        290        300 
NRTLGSLRNI LYLLHQRVRR FGIMGLYKGL EAKLLQTVLT AALMFLVYEK LTAATFTVMG 


LKRAHQH 

« 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].
Tissue: Liver.
[2]"A genome annotation-driven approach to cloning the human ORFeome."
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I.
Genome Biol. 5:R84.1-R84.11(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Trachea.
[4]"The DNA sequence of human chromosome 22."
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. expand/collapse author list , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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: Skin and Uterus.
[7]"PEX19 binds multiple peroxisomal membrane proteins, is predominantly cytoplasmic, and is required for peroxisome membrane synthesis."
Sacksteder K.A., Jones J.M., South S.T., Li X., Liu Y., Gould S.J.
J. Cell Biol. 148:931-944(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PEX19.
[8]"Topogenesis of peroxisomal membrane protein requires a short, positively charged intervening-loop sequence and flanking hydrophobic segments: study using human membrane protein PMP34."
Honsho M., Fujiki Y.
J. Biol. Chem. 276:9375-9382(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, TOPOLOGY, MUTAGENESIS OF 190-LYS--LYS-199.
[9]"Multiple distinct targeting signals in integral peroxisomal membrane proteins."
Jones J.M., Morrell J.C., Gould S.J.
J. Cell Biol. 153:1141-1150(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PEX19, TOPOLOGY, SUBCELLULAR LOCATION, PEROXISOMAL TARGETING.
[10]"Identification of human PMP34 as a peroxisomal ATP transporter."
Visser W.F., van Roermund C.W., Waterham H.R., Wanders R.J.
Biochem. Biophys. Res. Commun. 299:494-497(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[11]"PEX19 is a predominantly cytosolic chaperone and import receptor for class 1 peroxisomal membrane proteins."
Jones J.M., Morrell J.C., Gould S.J.
J. Cell Biol. 164:57-67(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PEX19, SUBCELLULAR LOCATION, MUTAGENESIS OF 283-LEU--PHE-285; 289-GLU-LYS-290 AND 302-LYS-GLU-303.
[12]"The human gene SLC25A17 encodes a peroxisomal transporter of coenzyme A, FAD and NAD+."
Agrimi G., Russo A., Scarcia P., Palmieri F.
Biochem. J. 443:241-247(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y12860 mRNA. Translation: CAA73367.1.
CR456577 mRNA. Translation: CAG30463.1.
AK292924 mRNA. Translation: BAF85613.1.
AL049764, Z98048 Genomic DNA. Translation: CAI20333.1.
Z98048, AL049764 Genomic DNA. Translation: CAI20491.1.
CH471095 Genomic DNA. Translation: EAW60390.1.
BC005957 mRNA. Translation: AAH05957.1.
BC012998 mRNA. Translation: AAH12998.1.
RefSeqNP_001269656.1. NM_001282727.1.
NP_006349.1. NM_006358.3.
UniGeneHs.474938.

3D structure databases

ProteinModelPortalO43808.
SMRO43808. Positions 11-302.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115741. 11 interactions.
IntActO43808. 1 interaction.
STRING9606.ENSP00000390722.

Protein family/group databases

TCDB2.A.29.20.1. the mitochondrial carrier (mc) family.

PTM databases

PhosphoSiteO43808.

Proteomic databases

PaxDbO43808.
PRIDEO43808.

Protocols and materials databases

DNASU10478.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000435456; ENSP00000390722; ENSG00000100372.
GeneID10478.
KEGGhsa:10478.
UCSCuc003azc.3. human.

Organism-specific databases

CTD10478.
GeneCardsGC22M041165.
HGNCHGNC:10987. SLC25A17.
HPAHPA052708.
MIM606795. gene.
neXtProtNX_O43808.
PharmGKBPA35863.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG258628.
HOGENOMHOG000159426.
HOVERGENHBG003235.
InParanoidO43808.
KOK13354.
OMAVWVKGQH.
PhylomeDBO43808.
TreeFamTF324772.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressO43808.
BgeeO43808.
CleanExHS_SLC25A17.
GenevestigatorO43808.

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

GeneWikiSLC25A17.
GenomeRNAi10478.
NextBio39748.
PROO43808.
SOURCESearch...

Entry information

Entry namePM34_HUMAN
AccessionPrimary (citable) accession number: O43808
Secondary accession number(s): A8KA59 expand/collapse secondary AC list , Q5TFL0, Q9UGW8, Q9UGY7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: June 1, 1998
Last modified: April 16, 2014
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 22

Human chromosome 22: entries, gene names and cross-references to MIM