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Peroxisomal membrane protein PMP34 (34 kDa peroxisomal membrane protein) (Solute carrier family 25 member 17)

 PM34_MOUSE              Reviewed;         307 AA.
O70579;
24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
01-AUG-1998, sequence version 1.
07-NOV-2018, entry version 138.
RecName: Full=Peroxisomal membrane protein PMP34;
AltName: Full=34 kDa peroxisomal membrane protein;
AltName: Full=Solute carrier family 25 member 17;
Name=Slc25a17; Synonyms=Pmp34, Pmp35;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9874197; DOI=10.1046/j.1432-1327.1998.2580332.x;
Wylin T., Baes M., Brees C., Mannaerts G.P., Fransen M.,
Van Veldhoven P.P.;
"Identification and characterization of human PMP34, a protein closely
related to the peroxisomal integral membrane protein PMP47 of Candida
boidinii.";
Eur. J. Biochem. 258:332-338(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Kidney;
PubMed=16141072; DOI=10.1126/science.1112014;
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., 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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Czech II, and FVB/N; TISSUE=Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Kidney, Liver, Lung, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- 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 extent 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). {ECO:0000250}.
-!- SUBUNIT: Interacts (via N- and C-terminus peroxisomal targeting
regions) with PEX19; the interaction occurs with the newly
synthesized SLC25A17 in the cytosol. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. 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. {ECO:0000250}.
-!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29)
family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AJ006341; CAA06984.1; -; mRNA.
EMBL; AK002388; BAB22062.1; -; mRNA.
EMBL; BC008571; AAH08571.1; -; mRNA.
EMBL; BC011292; AAH11292.1; -; mRNA.
CCDS; CCDS27666.1; -.
RefSeq; NP_035529.1; NM_011399.3.
UniGene; Mm.222536; -.
ProteinModelPortal; O70579; -.
SMR; O70579; -.
STRING; 10090.ENSMUSP00000023040; -.
PhosphoSitePlus; O70579; -.
EPD; O70579; -.
MaxQB; O70579; -.
PaxDb; O70579; -.
PeptideAtlas; O70579; -.
PRIDE; O70579; -.
Ensembl; ENSMUST00000023040; ENSMUSP00000023040; ENSMUSG00000022404.
GeneID; 20524; -.
KEGG; mmu:20524; -.
UCSC; uc007wwk.1; mouse.
CTD; 10478; -.
MGI; MGI:1342248; Slc25a17.
eggNOG; KOG0769; Eukaryota.
eggNOG; ENOG410ZNC0; LUCA.
GeneTree; ENSGT00920000149129; -.
HOGENOM; HOG000159426; -.
HOVERGEN; HBG003235; -.
InParanoid; O70579; -.
KO; K13354; -.
OMA; PTNYSGI; -.
OrthoDB; EOG091G0DMQ; -.
PhylomeDB; O70579; -.
TreeFam; TF324772; -.
Reactome; R-MMU-389599; Alpha-oxidation of phytanate.
ChiTaRS; Slc25a17; mouse.
PRO; PR:O70579; -.
Proteomes; UP000000589; Chromosome 15.
Bgee; ENSMUSG00000022404; Expressed in 285 organ(s), highest expression level in adult mammalian kidney.
Genevisible; O70579; MM.
GO; GO:0005779; C:integral component of peroxisomal membrane; ISS:UniProtKB.
GO; GO:0005739; C:mitochondrion; HDA:MGI.
GO; GO:0005778; C:peroxisomal membrane; IDA:MGI.
GO; GO:0005777; C:peroxisome; ISO:MGI.
GO; GO:0015217; F:ADP transmembrane transporter activity; ISS:UniProtKB.
GO; GO:0080122; F:AMP transmembrane transporter activity; ISS:UniProtKB.
GO; GO:0005347; F:ATP transmembrane transporter activity; ISO:MGI.
GO; GO:0051087; F:chaperone binding; ISO:MGI.
GO; GO:0015228; F:coenzyme A transmembrane transporter activity; ISS:UniProtKB.
GO; GO:0015230; F:FAD transmembrane transporter activity; ISS:UniProtKB.
GO; GO:0044610; F:FMN transmembrane transporter activity; ISS:UniProtKB.
GO; GO:0051724; F:NAD transmembrane transporter activity; ISS:UniProtKB.
GO; GO:0015866; P:ADP transport; ISS:UniProtKB.
GO; GO:0080121; P:AMP transport; ISS:UniProtKB.
GO; GO:0015867; P:ATP transport; ISO:MGI.
GO; GO:0035349; P:coenzyme A transmembrane transport; ISS:UniProtKB.
GO; GO:0035350; P:FAD transmembrane transport; ISS:UniProtKB.
GO; GO:0006635; P:fatty acid beta-oxidation; ISO:MGI.
GO; GO:0015908; P:fatty acid transport; ISO:MGI.
GO; GO:0043132; P:NAD transport; ISS:UniProtKB.
Gene3D; 1.50.40.10; -; 2.
InterPro; IPR002067; Mit_carrier.
InterPro; IPR040062; Mitochondrial_carrier_protein.
InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
InterPro; IPR023395; Mt_carrier_dom_sf.
PANTHER; PTHR24089; PTHR24089; 1.
Pfam; PF00153; Mito_carr; 3.
PRINTS; PR00926; MITOCARRIER.
SUPFAM; SSF103506; SSF103506; 1.
PROSITE; PS50920; SOLCAR; 3.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Membrane; Peroxisome;
Reference proteome; Repeat; Transmembrane; Transmembrane helix;
Transport.
CHAIN 1 307 Peroxisomal membrane protein PMP34.
/FTId=PRO_0000090706.
TOPO_DOM 1 9 Cytoplasmic. {ECO:0000250}.
TRANSMEM 10 30 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 31 66 Lumenal. {ECO:0000255}.
TRANSMEM 67 87 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 88 104 Cytoplasmic. {ECO:0000255}.
TRANSMEM 105 125 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 126 160 Lumenal. {ECO:0000255}.
TRANSMEM 161 181 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 182 202 Cytoplasmic. {ECO:0000255}.
TRANSMEM 203 223 Helical; Name=5. {ECO:0000255}.
TOPO_DOM 224 280 Lumenal. {ECO:0000255}.
TRANSMEM 281 301 Helical; Name=6. {ECO:0000255}.
TOPO_DOM 302 307 Cytoplasmic. {ECO:0000250}.
REPEAT 7 92 Solcar 1.
REPEAT 99 192 Solcar 2.
REPEAT 200 294 Solcar 3.
REGION 1 147 Necessary for targeting to peroxisomes
and interaction with PEX19.
{ECO:0000250}.
REGION 244 307 Necessary for targeting to peroxisomes
and interaction with PEX19.
{ECO:0000250}.
MOTIF 190 199 Peroxisome localization signal.
{ECO:0000250}.
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


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