PM34_MOUSE
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 03-AUG-2022, entry version 154.
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].
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. Inhibited by pyridoxal 5'-
CC phosphate and bathophenanthroline in vitro (By similarity).
CC {ECO:0000250}.
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}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Peroxisome membrane;
CC Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed in liver.
CC -!- DOMAIN: The N- and C-terminal portions are exposed to the cytoplasm. A
CC region between helical transmembrane domains (TM) 4 and 5 and TM1-TM3
CC or TM4-TM6 are necessary for the peroxisome-targeting activity (By
CC similarity). Lacks a typical peroxisomal sorting signal. {ECO:0000250}.
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; 5.
DR STRING; 10090.ENSMUSP00000023040; -.
DR PhosphoSitePlus; O70579; -.
DR EPD; O70579; -.
DR jPOST; O70579; -.
DR MaxQB; O70579; -.
DR PaxDb; O70579; -.
DR PeptideAtlas; O70579; -.
DR PRIDE; O70579; -.
DR ProteomicsDB; 289633; -.
DR Antibodypedia; 26801; 105 antibodies from 23 providers.
DR DNASU; 20524; -.
DR Ensembl; ENSMUST00000023040; ENSMUSP00000023040; ENSMUSG00000022404.
DR GeneID; 20524; -.
DR KEGG; mmu:20524; -.
DR UCSC; uc007wwk.1; mouse.
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; YEWTRSF; -.
DR OrthoDB; 1186395at2759; -.
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 74 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 265 other tissues.
DR ExpressionAtlas; O70579; baseline and differential.
DR Genevisible; O70579; MM.
DR GO; GO:0005779; C:integral component of peroxisomal membrane; ISS:UniProtKB.
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:0005347; F:ATP transmembrane transporter activity; ISO:MGI.
DR GO; GO:0051087; F:chaperone binding; 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: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; -; 2.
DR InterPro; IPR002067; Mit_carrier.
DR InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR InterPro; IPR023395; Mt_carrier_dom_sf.
DR Pfam; PF00153; Mito_carr; 3.
DR PRINTS; PR00926; MITOCARRIER.
DR SUPFAM; SSF103506; SSF103506; 1.
DR PROSITE; PS50920; SOLCAR; 3.
PE 1: Evidence at protein level;
KW Cytoplasm; Membrane; Peroxisome; Reference proteome; Repeat; Transmembrane;
KW 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"
FT REGION 244..307
FT /note="Necessary for targeting to peroxisomes and
FT interaction with PEX19"
FT /evidence="ECO:0000250"
FT MOTIF 190..199
FT /note="Peroxisome localization signal"
FT /evidence="ECO:0000250"
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
