ID PM34_HUMAN Reviewed; 307 AA. AC O43808; A8KA59; Q5TFL0; Q9UGW8; Q9UGY7; DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 1. DT 24-JAN-2024, entry version 185. 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 {ECO:0000303|PubMed:22185573, GN ECO:0000312|HGNC:HGNC:10987}; GN Synonyms=PMP34 {ECO:0000303|PubMed:9874197}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RC TISSUE=Liver; 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]. RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84; RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., RA Beare D.M., Dunham I.; RT "A genome annotation-driven approach to cloning the human ORFeome."; RL Genome Biol. 5:R84.1-R84.11(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Trachea; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=10591208; DOI=10.1038/990031; RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C., RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., RA Wright H.; RT "The DNA sequence of human chromosome 22."; RL Nature 402:489-495(1999). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Skin, and Uterus; 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 [7] RP INTERACTION WITH PEX19, AND REGION. RX PubMed=10704444; DOI=10.1083/jcb.148.5.931; RA Sacksteder K.A., Jones J.M., South S.T., Li X., Liu Y., Gould S.J.; RT "PEX19 binds multiple peroxisomal membrane proteins, is predominantly RT cytoplasmic, and is required for peroxisome membrane synthesis."; RL J. Cell Biol. 148:931-944(2000). RN [8] RP SUBCELLULAR LOCATION, TOPOLOGY, MUTAGENESIS OF 190-LYS--LYS-199, AND RP DOMAIN. RX PubMed=11121399; DOI=10.1074/jbc.m003304200; RA Honsho M., Fujiki Y.; RT "Topogenesis of peroxisomal membrane protein requires a short, positively RT charged intervening-loop sequence and flanking hydrophobic segments: study RT using human membrane protein PMP34."; RL J. Biol. Chem. 276:9375-9382(2001). RN [9] RP INTERACTION WITH PEX19, TOPOLOGY, SUBCELLULAR LOCATION, AND PEROXISOMAL RP TARGETING. RX PubMed=11402059; DOI=10.1083/jcb.153.6.1141; RA Jones J.M., Morrell J.C., Gould S.J.; RT "Multiple distinct targeting signals in integral peroxisomal membrane RT proteins."; RL J. Cell Biol. 153:1141-1150(2001). RN [10] RP CAUTION. RX PubMed=12445829; DOI=10.1016/s0006-291x(02)02663-3; RA Visser W.F., van Roermund C.W., Waterham H.R., Wanders R.J.; RT "Identification of human PMP34 as a peroxisomal ATP transporter."; RL Biochem. Biophys. Res. Commun. 299:494-497(2002). RN [11] RP INTERACTION WITH PEX19, SUBCELLULAR LOCATION, AND MUTAGENESIS OF RP 283-LEU--PHE-285; 289-GLU-LYS-290 AND 302-LYS-GLU-303. RX PubMed=14709540; DOI=10.1083/jcb.200304111; RA Jones J.M., Morrell J.C., Gould S.J.; RT "PEX19 is a predominantly cytosolic chaperone and import receptor for class RT 1 peroxisomal membrane proteins."; RL J. Cell Biol. 164:57-67(2004). RN [12] RP FUNCTION, TRANSPORT ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL RP PROPERTIES, TISSUE SPECIFICITY, AND CAUTION. RX PubMed=22185573; DOI=10.1042/bj20111420; RA Agrimi G., Russo A., Scarcia P., Palmieri F.; RT "The human gene SLC25A17 encodes a peroxisomal transporter of coenzyme A, RT FAD and NAD+."; RL Biochem. J. 443:241-247(2012). 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:0000269|PubMed:22185573}. 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:0000269|PubMed:22185573}; 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:0000269|PubMed:22185573}; 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:0000269|PubMed:22185573}; 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:0000269|PubMed:22185573}; 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:0000269|PubMed:22185573}; 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:0000269|PubMed:22185573}; 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:0000269|PubMed:22185573}; 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:0000269|PubMed:22185573}; 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:0000269|PubMed:22185573}; 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:0000269|PubMed:22185573}; 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:0000269|PubMed:22185573}; 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:0000269|PubMed:22185573}; 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:0000269|PubMed:22185573}; 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:0000269|PubMed:22185573}; 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:0000269|PubMed:22185573}; 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:0000269|PubMed:22185573}; 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:0000269|PubMed:22185573}; 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:0000269|PubMed:22185573}; 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:0000269|PubMed:22185573}; 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:0000269|PubMed:22185573}; CC -!- ACTIVITY REGULATION: Inhibited by pyridoxal 5'-phosphate and CC bathophenanthroline. {ECO:0000269|PubMed:22185573}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.19 mM for AMP {ECO:0000269|PubMed:22185573}; CC Vmax=74 umol/min/g enzyme toward AMP {ECO:0000269|PubMed:22185573}; 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:0000269|PubMed:10704444, CC ECO:0000269|PubMed:11402059, ECO:0000269|PubMed:14709540}. CC -!- INTERACTION: CC O43808; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-594912, EBI-16439278; CC O43808; P40855: PEX19; NbExp=4; IntAct=EBI-594912, EBI-594747; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14709540}. CC Peroxisome membrane {ECO:0000269|PubMed:11121399, CC ECO:0000269|PubMed:11402059, ECO:0000269|PubMed:14709540, CC ECO:0000269|PubMed:9874197}; Multi-pass membrane protein {ECO:0000255}. CC -!- TISSUE SPECIFICITY: Ubiquitous. Expressed in liver. CC {ECO:0000269|PubMed:22185573, 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:0000269|PubMed:11121399}. CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family. CC {ECO:0000305}. CC -!- CAUTION: Was first identified as a peroxisomal ATP transporter CC (PubMed:12445829). However, later experiments showed that it acts as a CC peroxisomal transporter for multiple cofactors (PubMed:22185573). CC {ECO:0000305|PubMed:12445829, ECO:0000305|PubMed:22185573}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Y12860; CAA73367.1; -; mRNA. DR EMBL; CR456577; CAG30463.1; -; mRNA. DR EMBL; AK292924; BAF85613.1; -; mRNA. DR EMBL; AL049764; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; Z98048; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471095; EAW60390.1; -; Genomic_DNA. DR EMBL; BC005957; AAH05957.1; -; mRNA. DR EMBL; BC012998; AAH12998.1; -; mRNA. DR CCDS; CCDS14005.1; -. DR RefSeq; NP_001269656.1; NM_001282727.1. DR RefSeq; NP_006349.1; NM_006358.3. DR AlphaFoldDB; O43808; -. DR SMR; O43808; -. DR BioGRID; 115741; 71. DR IntAct; O43808; 15. DR STRING; 9606.ENSP00000390722; -. DR TCDB; 2.A.29.20.1; the mitochondrial carrier (mc) family. DR GlyGen; O43808; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; O43808; -. DR PhosphoSitePlus; O43808; -. DR SwissPalm; O43808; -. DR BioMuta; SLC25A17; -. DR EPD; O43808; -. DR jPOST; O43808; -. DR MassIVE; O43808; -. DR MaxQB; O43808; -. DR PaxDb; 9606-ENSP00000390722; -. DR PeptideAtlas; O43808; -. DR ProteomicsDB; 49175; -. DR Pumba; O43808; -. DR Antibodypedia; 26801; 125 antibodies from 23 providers. DR DNASU; 10478; -. DR Ensembl; ENST00000435456.7; ENSP00000390722.2; ENSG00000100372.15. DR GeneID; 10478; -. DR KEGG; hsa:10478; -. DR MANE-Select; ENST00000435456.7; ENSP00000390722.2; NM_006358.4; NP_006349.1. DR UCSC; uc003azc.5; human. DR AGR; HGNC:10987; -. DR CTD; 10478; -. DR DisGeNET; 10478; -. DR GeneCards; SLC25A17; -. DR HGNC; HGNC:10987; SLC25A17. DR HPA; ENSG00000100372; Low tissue specificity. DR MIM; 606795; gene. DR neXtProt; NX_O43808; -. DR OpenTargets; ENSG00000100372; -. DR PharmGKB; PA35863; -. DR VEuPathDB; HostDB:ENSG00000100372; -. DR eggNOG; KOG0769; Eukaryota. DR GeneTree; ENSGT00920000149129; -. DR InParanoid; O43808; -. DR OMA; QFMMYEL; -. DR OrthoDB; 3670854at2759; -. DR PhylomeDB; O43808; -. DR TreeFam; TF324772; -. DR PathwayCommons; O43808; -. DR Reactome; R-HSA-389599; Alpha-oxidation of phytanate. DR Reactome; R-HSA-9603798; Class I peroxisomal membrane protein import. DR SignaLink; O43808; -. DR BioGRID-ORCS; 10478; 11 hits in 1158 CRISPR screens. DR ChiTaRS; SLC25A17; human. DR GeneWiki; SLC25A17; -. DR GenomeRNAi; 10478; -. DR Pharos; O43808; Tbio. DR PRO; PR:O43808; -. DR Proteomes; UP000005640; Chromosome 22. DR RNAct; O43808; Protein. DR Bgee; ENSG00000100372; Expressed in left ovary and 186 other cell types or tissues. DR ExpressionAtlas; O43808; baseline and differential. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005778; C:peroxisomal membrane; IDA:UniProtKB. DR GO; GO:0005777; C:peroxisome; IDA:BHF-UCL. DR GO; GO:0000295; F:adenine nucleotide transmembrane transporter activity; TAS:Reactome. DR GO; GO:0015217; F:ADP transmembrane transporter activity; IDA:UniProtKB. DR GO; GO:0080122; F:AMP transmembrane transporter activity; IDA:UniProtKB. DR GO; GO:0015297; F:antiporter activity; IEA:UniProtKB-KW. DR GO; GO:0005347; F:ATP transmembrane transporter activity; IGI:BHF-UCL. DR GO; GO:0015228; F:coenzyme A transmembrane transporter activity; IDA:UniProtKB. DR GO; GO:0015230; F:FAD transmembrane transporter activity; IDA:UniProtKB. DR GO; GO:0044610; F:FMN transmembrane transporter activity; IDA:UniProtKB. DR GO; GO:0051724; F:NAD transmembrane transporter activity; IDA:UniProtKB. DR GO; GO:0051087; F:protein-folding chaperone binding; IPI:BHF-UCL. DR GO; GO:0015867; P:ATP transport; IGI:BHF-UCL. DR GO; GO:0001561; P:fatty acid alpha-oxidation; TAS:Reactome. DR GO; GO:0006635; P:fatty acid beta-oxidation; IGI:BHF-UCL. DR GO; GO:0015908; P:fatty acid transport; IGI:BHF-UCL. 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; O43808; HS. 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_0000090705" FT TOPO_DOM 1..9 FT /note="Cytoplasmic" 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 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:0000269|PubMed:10704444" FT REGION 244..307 FT /note="Necessary for targeting to peroxisomes and FT interaction with PEX19" FT /evidence="ECO:0000269|PubMed:11402059" FT MOTIF 190..199 FT /note="Peroxisome localization signal" FT /evidence="ECO:0000269|PubMed:11121399" FT VARIANT 98 FT /note="H -> R (in dbSNP:rs12159334)" FT /id="VAR_050139" FT MUTAGEN 190..199 FT /note="KRQLLKKRMK->AAQLLAAAMA: Localizes in the cytoplasm." FT /evidence="ECO:0000269|PubMed:11121399" FT MUTAGEN 283..285 FT /note="LMF->KKK: Impairs interaction with PEX19." FT /evidence="ECO:0000269|PubMed:14709540" FT MUTAGEN 289..290 FT /note="EK->LL: Impairs interaction with PEX19." FT /evidence="ECO:0000269|PubMed:14709540" FT MUTAGEN 302..303 FT /note="KR->EE: No effect on interaction with PEX19." FT /evidence="ECO:0000269|PubMed:14709540" SQ SEQUENCE 307 AA; 34567 MW; B7043D82966D47A5 CRC64; MASVLSYESL VHAVAGAVGS VTAMTVFFPL DTARLRLQVD EKRKSKTTHM VLLEIIKEEG LLAPYRGWFP VISSLCCSNF VYFYTFNSLK ALWVKGQHST TGKDLVVGFV AGVVNVLLTT PLWVVNTRLK LQGAKFRNED IVPTNYKGII DAFHQIIRDE GISALWNGTF PSLLLVFNPA IQFMFYEGLK RQLLKKRMKL SSLDVFIIGA VAKAIATTVT YPLQTVQSIL RFGRHRLNPE NRTLGSLRNI LYLLHQRVRR FGIMGLYKGL EAKLLQTVLT AALMFLVYEK LTAATFTVMG LKRAHQH //