O43808 (PM34_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	307 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Transport
Cellular component	Cytoplasm Membrane Peroxisome
Coding sequence diversity	Polymorphism
Domain	Repeat Transmembrane Transmembrane helix
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	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
Cellular_component	integral to peroxisomal membrane Inferred from direct assay PubMed 21153762. Source: UniProtKB mitochondrion Inferred from electronic annotation. Source: Compara
Molecular_function	ADP 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 coenzyme A transmembrane transporter activity Inferred from direct assay Ref.12. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PEX19	P40855	4	EBI-594912,EBI-594747

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 307	307	Peroxisomal membrane protein PMP34		PRO_0000090705
Regions
	Topological domain	1 – 9	9	Cytoplasmic Ref.8 Ref.9
	Transmembrane	10 – 30	21	Helical; Name=1; Potential
	Topological domain	31 – 66	36	Lumenal Potential
	Transmembrane	67 – 87	21	Helical; Name=2; Potential
	Topological domain	88 – 104	17	Cytoplasmic Potential
	Transmembrane	105 – 125	21	Helical; Name=3; Potential
	Topological domain	126 – 160	35	Lumenal Potential
	Transmembrane	161 – 181	21	Helical; Name=4; Potential
	Topological domain	182 – 202	21	Cytoplasmic Potential
	Transmembrane	203 – 223	21	Helical; Name=5; Potential
	Topological domain	224 – 280	57	Lumenal Potential
	Transmembrane	281 – 301	21	Helical; Name=6; Potential
	Topological domain	302 – 307	6	Cytoplasmic Ref.8 Ref.9
	Repeat	7 – 92	86	Solcar 1
	Repeat	99 – 192	94	Solcar 2
	Repeat	200 – 294	95	Solcar 3
	Region	1 – 147	147	Necessary for targeting to peroxisomes and interaction with PEX19
	Region	244 – 307	64	Necessary for targeting to peroxisomes and interaction with PEX19
	Motif	190 – 199	10	Peroxisome localization signal
Natural variations
	Natural variant	98	1	H → R. Corresponds to variant rs12159334 [ dbSNP | Ensembl ].		VAR_050139
Experimental info
	Mutagenesis	190 – 199	10	KRQLLKKRMK → AAQLLAAAMA: Localizes in the cytoplasm. Ref.8
	Mutagenesis	283 – 285	3	LMF → KKK: Impairs interaction with PEX19.
	Mutagenesis	289 – 290	2	EK → LL: Impairs interaction with PEX19.
	Mutagenesis	302 – 303	2	KR → EE: No effect on interaction with PEX19.

Sequences

	Sequence		Length	Mass (Da)
	O43808 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: B7043D82966D47A5	FASTA	307	34,567
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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.

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.
IPI	IPI00014440.
RefSeq	NP_006349.1. NM_006358.2.
UniGene	Hs.474938.
3D structure databases
ProteinModelPortal	O43808.
ModBase	Search...
Protein-protein interaction databases
IntAct	O43808. 1 interaction.
STRING	9606.ENSP00000390722.
Protein family/group databases
TCDB	2.A.29.20.1. mitochondrial carrier (MC) family.
PTM databases
PhosphoSite	O43808.
Proteomic databases
PaxDb	O43808.
PRIDE	O43808.
Protocols and materials databases
DNASU	10478.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000435456; ENSP00000390722; ENSG00000100372.
GeneID	10478.
KEGG	hsa:10478.
UCSC	uc003azc.3. human.
Organism-specific databases
CTD	10478.
GeneCards	GC22M041165.
HGNC	HGNC:10987. SLC25A17.
HPA	HPA052708.
MIM	606795. gene.
neXtProt	NX_O43808.
PharmGKB	PA35863.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG258628.
HOGENOM	HOG000159426.
HOVERGEN	HBG003235.
InParanoid	O43808.
KO	K13354.
OMA	FPVICSL.
PhylomeDB	O43808.
Enzyme and pathway databases
Reactome	REACT_111217. Metabolism.
Gene expression databases
ArrayExpress	O43808.
Bgee	O43808.
CleanEx	HS_SLC25A17.
Genevestigator	O43808.
GermOnline	ENSG00000100372. Homo sapiens.
Family and domain databases
Gene3D	1.50.40.10. 1 hit.
InterPro	IPR002067. Mit_carrier. IPR018108. Mitochondrial_sb/sol_carrier. IPR023395. Mt_carrier_dom. [Graphical view]
Pfam	PF00153. Mito_carr. 3 hits. [Graphical view]
PRINTS	PR00926. MITOCARRIER.
SUPFAM	SSF103506. Mitoch_carrier. 1 hit.
PROSITE	PS50920. SOLCAR. 3 hits. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	10478.
NextBio	39748.
SOURCE	Search...

Entry information

Entry name

PM34_HUMAN

Accession

Primary (citable) accession number: O43808
Secondary accession number(s): A8KA59 , Q5TFL0, Q9UGW8, Q9UGY7

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 24, 2001
Last sequence update:	June 1, 1998
Last modified:	May 1, 2013
This is version 114 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.