ID   PM34_MOUSE              Reviewed;         307 AA.
AC   O70579;
DT   24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   24-JAN-2024, entry version 162.
DE   RecName: Full=Peroxisomal membrane protein PMP34;
DE   AltName: Full=34 kDa peroxisomal membrane protein;
DE   AltName: Full=Solute carrier family 25 member 17;
GN   Name=Slc25a17; Synonyms=Pmp34, Pmp35;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX   PubMed=9874197; DOI=10.1046/j.1432-1327.1998.2580332.x;
RA   Wylin T., Baes M., Brees C., Mannaerts G.P., Fransen M.,
RA   Van Veldhoven P.P.;
RT   "Identification and characterization of human PMP34, a protein closely
RT   related to the peroxisomal integral membrane protein PMP47 of Candida
RT   boidinii.";
RL   Eur. J. Biochem. 258:332-338(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Kidney;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II, and FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Kidney, Liver, Lung, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Peroxisomal transporter for multiple cofactors like coenzyme
CC       A (CoA), flavin adenine dinucleotide (FAD), flavin mononucleotide (FMN)
CC       and nucleotide adenosine monophosphate (AMP), and to a lesser extent
CC       for nicotinamide adenine dinucleotide (NAD(+)), adenosine diphosphate
CC       (ADP) and adenosine 3',5'-diphosphate (PAP). May catalyze the transport
CC       of free CoA, FAD and NAD(+) from the cytosol into the peroxisomal
CC       matrix by a counter-exchange mechanism. {ECO:0000250|UniProtKB:O43808}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=AMP(out) + CoA(in) = AMP(in) + CoA(out); Xref=Rhea:RHEA:73095,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:456215;
CC         Evidence={ECO:0000250|UniProtKB:O43808};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3'-dephospho-CoA(in) + AMP(out) = 3'-dephospho-CoA(out) +
CC         AMP(in); Xref=Rhea:RHEA:73099, ChEBI:CHEBI:57328, ChEBI:CHEBI:456215;
CC         Evidence={ECO:0000250|UniProtKB:O43808};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA(in) + AMP(out) = acetyl-CoA(out) + AMP(in);
CC         Xref=Rhea:RHEA:73447, ChEBI:CHEBI:57288, ChEBI:CHEBI:456215;
CC         Evidence={ECO:0000250|UniProtKB:O43808};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=AMP(in) + NAD(+)(out) = AMP(out) + NAD(+)(in);
CC         Xref=Rhea:RHEA:65424, ChEBI:CHEBI:57540, ChEBI:CHEBI:456215;
CC         Evidence={ECO:0000250|UniProtKB:O43808};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=AMP(out) + FAD(in) = AMP(in) + FAD(out); Xref=Rhea:RHEA:73087,
CC         ChEBI:CHEBI:57692, ChEBI:CHEBI:456215;
CC         Evidence={ECO:0000250|UniProtKB:O43808};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=AMP(out) + FMN(in) = AMP(in) + FMN(out); Xref=Rhea:RHEA:73091,
CC         ChEBI:CHEBI:58210, ChEBI:CHEBI:456215;
CC         Evidence={ECO:0000250|UniProtKB:O43808};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ADP(out) + AMP(in) = ADP(in) + AMP(out); Xref=Rhea:RHEA:72851,
CC         ChEBI:CHEBI:456215, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000250|UniProtKB:O43808};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosine 3',5'-bisphosphate(in) + AMP(out) = adenosine 3',5'-
CC         bisphosphate(out) + AMP(in); Xref=Rhea:RHEA:73451, ChEBI:CHEBI:58343,
CC         ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:O43808};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=CoA(out) + FAD(in) = CoA(in) + FAD(out); Xref=Rhea:RHEA:73143,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:O43808};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosine 3',5'-bisphosphate(out) + FAD(in) = adenosine 3',5'-
CC         bisphosphate(in) + FAD(out); Xref=Rhea:RHEA:73147, ChEBI:CHEBI:57692,
CC         ChEBI:CHEBI:58343; Evidence={ECO:0000250|UniProtKB:O43808};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=CoA(out) + FMN(in) = CoA(in) + FMN(out); Xref=Rhea:RHEA:73151,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000250|UniProtKB:O43808};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosine 3',5'-bisphosphate(out) + FMN(in) = adenosine 3',5'-
CC         bisphosphate(in) + FMN(out); Xref=Rhea:RHEA:73155, ChEBI:CHEBI:58210,
CC         ChEBI:CHEBI:58343; Evidence={ECO:0000250|UniProtKB:O43808};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=FAD(out) + NAD(+)(in) = FAD(in) + NAD(+)(out);
CC         Xref=Rhea:RHEA:73163, ChEBI:CHEBI:57540, ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:O43808};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=FMN(out) + NAD(+)(in) = FMN(in) + NAD(+)(out);
CC         Xref=Rhea:RHEA:73159, ChEBI:CHEBI:57540, ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000250|UniProtKB:O43808};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=CoA(out) + NAD(+)(in) = CoA(in) + NAD(+)(out);
CC         Xref=Rhea:RHEA:73167, ChEBI:CHEBI:57287, ChEBI:CHEBI:57540;
CC         Evidence={ECO:0000250|UniProtKB:O43808};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosine 3',5'-bisphosphate(out) + NAD(+)(in) = adenosine
CC         3',5'-bisphosphate(in) + NAD(+)(out); Xref=Rhea:RHEA:73171,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:58343;
CC         Evidence={ECO:0000250|UniProtKB:O43808};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ADP(in) + FMN(out) = ADP(out) + FMN(in); Xref=Rhea:RHEA:73175,
CC         ChEBI:CHEBI:58210, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000250|UniProtKB:O43808};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ADP(in) + FAD(out) = ADP(out) + FAD(in); Xref=Rhea:RHEA:73183,
CC         ChEBI:CHEBI:57692, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000250|UniProtKB:O43808};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ADP(out) + CoA(in) = ADP(in) + CoA(out); Xref=Rhea:RHEA:72839,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000250|UniProtKB:O43808};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosine 3',5'-bisphosphate(in) + ADP(out) = adenosine 3',5'-
CC         bisphosphate(out) + ADP(in); Xref=Rhea:RHEA:72847, ChEBI:CHEBI:58343,
CC         ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O43808};
CC   -!- SUBUNIT: Interacts (via N- and C-terminus peroxisomal targeting
CC       regions) with PEX19; the interaction occurs with the newly synthesized
CC       SLC25A17 in the cytosol. {ECO:0000250|UniProtKB:O43808}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O43808}.
CC       Peroxisome membrane {ECO:0000250|UniProtKB:O43808}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Expressed in liver, kidney, heart, spleen, muscle
CC       and lung. {ECO:0000269|PubMed:9874197}.
CC   -!- DOMAIN: The N- and C-terminal portions are exposed to the cytoplasm.
CC       Lacks a typical peroxisomal sorting signal. A region between helical
CC       transmembrane domains (TM) 4 and 5 and TM1-TM3 or TM4-TM6 are necessary
CC       for the peroxisome-targeting activity. {ECO:0000250|UniProtKB:O43808}.
CC   -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC       {ECO:0000305}.
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DR   EMBL; AJ006341; CAA06984.1; -; mRNA.
DR   EMBL; AK002388; BAB22062.1; -; mRNA.
DR   EMBL; BC008571; AAH08571.1; -; mRNA.
DR   EMBL; BC011292; AAH11292.1; -; mRNA.
DR   CCDS; CCDS27666.1; -.
DR   RefSeq; NP_035529.1; NM_011399.3.
DR   AlphaFoldDB; O70579; -.
DR   SMR; O70579; -.
DR   BioGRID; 203303; 6.
DR   STRING; 10090.ENSMUSP00000023040; -.
DR   PhosphoSitePlus; O70579; -.
DR   EPD; O70579; -.
DR   jPOST; O70579; -.
DR   MaxQB; O70579; -.
DR   PaxDb; 10090-ENSMUSP00000023040; -.
DR   PeptideAtlas; O70579; -.
DR   ProteomicsDB; 289633; -.
DR   Pumba; O70579; -.
DR   Antibodypedia; 26801; 125 antibodies from 23 providers.
DR   DNASU; 20524; -.
DR   Ensembl; ENSMUST00000023040.9; ENSMUSP00000023040.8; ENSMUSG00000022404.9.
DR   GeneID; 20524; -.
DR   KEGG; mmu:20524; -.
DR   UCSC; uc007wwk.1; mouse.
DR   AGR; MGI:1342248; -.
DR   CTD; 10478; -.
DR   MGI; MGI:1342248; Slc25a17.
DR   VEuPathDB; HostDB:ENSMUSG00000022404; -.
DR   eggNOG; KOG0769; Eukaryota.
DR   GeneTree; ENSGT00920000149129; -.
DR   HOGENOM; CLU_015166_6_3_1; -.
DR   InParanoid; O70579; -.
DR   OMA; QFMMYEL; -.
DR   OrthoDB; 3670854at2759; -.
DR   PhylomeDB; O70579; -.
DR   TreeFam; TF324772; -.
DR   Reactome; R-MMU-389599; Alpha-oxidation of phytanate.
DR   Reactome; R-MMU-9603798; Class I peroxisomal membrane protein import.
DR   BioGRID-ORCS; 20524; 3 hits in 79 CRISPR screens.
DR   ChiTaRS; Slc25a17; mouse.
DR   PRO; PR:O70579; -.
DR   Proteomes; UP000000589; Chromosome 15.
DR   RNAct; O70579; Protein.
DR   Bgee; ENSMUSG00000022404; Expressed in right kidney and 269 other cell types or tissues.
DR   ExpressionAtlas; O70579; baseline and differential.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR   GO; GO:0005778; C:peroxisomal membrane; IDA:MGI.
DR   GO; GO:0005777; C:peroxisome; ISO:MGI.
DR   GO; GO:0015217; F:ADP transmembrane transporter activity; ISS:UniProtKB.
DR   GO; GO:0080122; F:AMP transmembrane transporter activity; ISS:UniProtKB.
DR   GO; GO:0015297; F:antiporter activity; IEA:UniProtKB-KW.
DR   GO; GO:0005347; F:ATP transmembrane transporter activity; ISO:MGI.
DR   GO; GO:0015228; F:coenzyme A transmembrane transporter activity; ISS:UniProtKB.
DR   GO; GO:0015230; F:FAD transmembrane transporter activity; ISS:UniProtKB.
DR   GO; GO:0044610; F:FMN transmembrane transporter activity; ISS:UniProtKB.
DR   GO; GO:0051724; F:NAD transmembrane transporter activity; ISS:UniProtKB.
DR   GO; GO:0051087; F:protein-folding chaperone binding; ISO:MGI.
DR   GO; GO:0015866; P:ADP transport; ISS:UniProtKB.
DR   GO; GO:0080121; P:AMP transport; ISS:UniProtKB.
DR   GO; GO:0015867; P:ATP transport; ISO:MGI.
DR   GO; GO:0035349; P:coenzyme A transmembrane transport; ISS:UniProtKB.
DR   GO; GO:0035350; P:FAD transmembrane transport; ISS:UniProtKB.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; ISO:MGI.
DR   GO; GO:0015908; P:fatty acid transport; ISO:MGI.
DR   GO; GO:0043132; P:NAD transport; ISS:UniProtKB.
DR   Gene3D; 1.50.40.10; Mitochondrial carrier domain; 2.
DR   InterPro; IPR002067; Mit_carrier.
DR   InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR   InterPro; IPR023395; Mt_carrier_dom_sf.
DR   PANTHER; PTHR45939:SF5; PEROXISOMAL MEMBRANE PROTEIN PMP34; 1.
DR   PANTHER; PTHR45939; PEROXISOMAL MEMBRANE PROTEIN PMP34-RELATED; 1.
DR   Pfam; PF00153; Mito_carr; 3.
DR   PRINTS; PR00926; MITOCARRIER.
DR   SUPFAM; SSF103506; Mitochondrial carrier; 1.
DR   PROSITE; PS50920; SOLCAR; 3.
DR   Genevisible; O70579; MM.
PE   1: Evidence at protein level;
KW   Antiport; Cytoplasm; Membrane; Peroxisome; Reference proteome; Repeat;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..307
FT                   /note="Peroxisomal membrane protein PMP34"
FT                   /id="PRO_0000090706"
FT   TOPO_DOM        1..9
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        10..30
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        31..66
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        67..87
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        88..104
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        105..125
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        126..160
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        161..181
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        182..202
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        203..223
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        224..280
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        281..301
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        302..307
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   REPEAT          7..92
FT                   /note="Solcar 1"
FT   REPEAT          99..192
FT                   /note="Solcar 2"
FT   REPEAT          200..294
FT                   /note="Solcar 3"
FT   REGION          1..147
FT                   /note="Necessary for targeting to peroxisomes and
FT                   interaction with PEX19"
FT                   /evidence="ECO:0000250|UniProtKB:O43808"
FT   REGION          244..307
FT                   /note="Necessary for targeting to peroxisomes and
FT                   interaction with PEX19"
FT                   /evidence="ECO:0000250|UniProtKB:O43808"
FT   MOTIF           190..199
FT                   /note="Peroxisome localization signal"
FT                   /evidence="ECO:0000250|UniProtKB:O43808"
SQ   SEQUENCE   307 AA;  34413 MW;  8CE406CE66D0EB06 CRC64;
     MASVLSYESL VHAVAGAVGS VTAMTVFFPL DTARLRLQVD EKRKSKTTHA VLLEIIKEEG
     LLAPYRGWFP VISSLCCSNF VYFYTFNSLK AVWVKGQRSS TGKDLVVGFV AGVVNVLLTT
     PLWVVNTRLK LQGAKFRNED IIPTNYKGII DAFHQIIRDE GILALWNGTF PSLLLVFNPA
     IQFMFYEGLK RQLLKKRMKL SSLDVFIIGA IAKAIATTVT YPMQTVQSIL RFGRHRLNPE
     NRTLGSLRNV LSLLHQRVKR FGIMGLYKGL EAKLLQTVLT AALMFLVYEK LTAATFTVMG
     LKSTHKH
//