ID PEX19_HUMAN Reviewed; 299 AA. AC P40855; D3DVE7; E9PPB4; G3V3G9; Q5QNY4; Q8NI97; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 1. DT 27-MAR-2024, entry version 220. DE RecName: Full=Peroxisomal biogenesis factor 19 {ECO:0000305}; DE AltName: Full=33 kDa housekeeping protein; DE AltName: Full=Peroxin-19; DE AltName: Full=Peroxisomal farnesylated protein; DE Flags: Precursor; GN Name=PEX19 {ECO:0000312|HGNC:HGNC:9713}; Synonyms=HK33, PXF; GN ORFNames=OK/SW-cl.22; 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] (ISOFORM 1). RC TISSUE=Ovary, and Placenta; RX PubMed=8076834; DOI=10.1016/0378-1119(94)90308-5; RA Braun A., Kammerer S., Weissenhorn W., Weiss E.H., Cleve H.; RT "Sequence of a putative human housekeeping gene (HK33) localized on RT chromosome 1."; RL Gene 146:291-295(1994). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING, TISSUE RP SPECIFICITY, SUBCELLULAR LOCATION, ISOPRENYLATION AT CYS-296, AND RP MUTAGENESIS OF CYS-296. RC TISSUE=Leukocyte, and Placenta; RX PubMed=9339377; DOI=10.1006/geno.1997.4914; RA Kammerer S., Arnold N., Gutensohn W., Mewes H.-W., Kunau W.-H., Hoefler G., RA Roscher A.A., Braun A.; RT "Genomic organization and molecular characterization of a gene encoding RT HsPXF, a human peroxisomal farnesylated protein."; RL Genomics 45:200-210(1997). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ISOPRENYLATION AT CYS-296, RP MUTAGENESIS OF CYS-296, SUBCELLULAR LOCATION, FUNCTION, AND INVOLVEMENT IN RP PBD12A. RC TISSUE=Liver; RX PubMed=10051604; DOI=10.1073/pnas.96.5.2116; RA Matsuzono Y., Kinoshita N., Tamura S., Shimozawa N., Hamasaki M., RA Ghaedi K., Wanders R.J.A., Suzuki Y., Kondo N., Fujiki Y.; RT "Human PEX19: cDNA cloning by functional complementation, mutation analysis RT in a patient with Zellweger syndrome, and potential role in peroxisomal RT membrane assembly."; RL Proc. Natl. Acad. Sci. U.S.A. 96:2116-2121(1999). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6). RX PubMed=26871637; DOI=10.1016/j.cell.2016.01.029; RA Yang X., Coulombe-Huntington J., Kang S., Sheynkman G.M., Hao T., RA Richardson A., Sun S., Yang F., Shen Y.A., Murray R., Spirohn K., RA Begg B.E., Duran-Frigola M., MacWilliams A., Pevzner S.J., Zhong Q., RA Trigg S.A., Tam S., Ghamsari L., Sahni N., Yi S., Rodriguez M.D., RA Balcha D., Tan G., Costanzo M., Andrews B., Boone C., Zhou X.J., RA Salehi-Ashtiani K., Charloteaux B., Chen A., Calderwood M.A., Aloy P., RA Roth F.P., Hill D.E., Iakoucheva L.M., Xia Y., Vidal M.; RT "Widespread Expansion of Protein Interaction Capabilities by Alternative RT Splicing."; RL Cell 164:805-817(2016). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [7] 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Lung; 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 [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-39 (ISOFORM 6). RC TISSUE=Colon adenocarcinoma; RA Shichijo S., Itoh K.; RT "Identification of immuno-peptidmics that are recognized by tumor-reactive RT CTL generated from TIL of colon cancer patients."; RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases. RN [10] RP INTERACTION WITH ABCD1; ABCD2 AND ABCD3, AND MUTAGENESIS OF CYS-296. RC TISSUE=Brain; RX PubMed=10777694; DOI=10.1006/bbrc.2000.2572; RA Gloeckner C.J., Mayerhofer P.U., Landgraf P., Muntau A.C., Holzinger A., RA Gerber J.-K., Kammerer S., Adamski J., Roscher A.A.; RT "Human adrenoleukodystrophy protein and related peroxisomal ABC RT transporters interact with the peroxisomal assembly protein PEX19p."; RL Biochem. Biophys. Res. Commun. 271:144-150(2000). RN [11] RP FUNCTION, MUTAGENESIS OF CYS-296, SUBCELLULAR LOCATION, AND INTERACTION RP WITH ABCD1; ABCD2; ABCD3; PEX3; PEX10; PEX11A; PEX11B; PEX12; PEX13; PEX14; RP PEX16; PXMP2; PXMP4 AND SLC25A17. 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 [12] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CDKN2A. RC TISSUE=Testis; RX PubMed=11259404; DOI=10.1074/jbc.c100011200; RA Sugihara T., Kaul S.C., Kato J.-Y., Reddel R.R., Nomura H., Wadhwa R.; RT "Pex19p dampens the p19ARF-p53-p21WAF1 tumor suppressor pathway."; RL J. Biol. Chem. 276:18649-18652(2001). RN [13] RP INTERACTION WITH PEX3; PEX10; PEX11B; PEX12; PEX13 AND PEX16, AND RP MUTAGENESIS OF 296-CYS--MET-299. RX PubMed=11390669; DOI=10.1128/mcb.21.13.4413-4424.2001; RA Fransen M., Wylin T., Brees C., Mannaerts G.P., Van Veldhoven P.P.; RT "Human pex19p binds peroxisomal integral membrane proteins at regions RT distinct from their sorting sequences."; RL Mol. Cell. Biol. 21:4413-4424(2001). RN [14] RP FUNCTION, AND INTERACTION WITH ABCD1; ABCD2; ABCD3 AND PEX3. RX PubMed=11883941; DOI=10.1006/bbrc.2002.6568; RA Mayerhofer P.U., Kattenfeld T., Roscher A.A., Muntau A.C.; RT "Two splice variants of human PEX19 exhibit distinct functions in RT peroxisomal assembly."; RL Biochem. Biophys. Res. Commun. 291:1180-1186(2002). RN [15] RP FUNCTION, INTERACTION WITH PEX3, AND SUBCELLULAR LOCATION. RX PubMed=15007061; DOI=10.1083/jcb.200311131; RA Fang Y., Morrell J.C., Jones J.M., Gould S.J.; RT "PEX3 functions as a PEX19 docking factor in the import of class I RT peroxisomal membrane proteins."; RL J. Cell Biol. 164:863-875(2004). RN [16] RP FUNCTION, AND INTERACTION WITH PEX11B; PEX16; PXMP2; PXMP4; SLC25A17 AND RP ABCD3. 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 [17] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [18] RP INVOLVEMENT IN PBD-CG14. RX PubMed=20683989; DOI=10.1002/ajmg.a.33560; RA Mohamed S., El-Meleagy E., Nasr A., Ebberink M.S., Wanders R.J., RA Waterham H.R.; RT "A mutation in PEX19 causes a severe clinical phenotype in a patient with RT peroxisomal biogenesis disorder."; RL Am. J. Med. Genet. A 152:2318-2321(2010). RN [19] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [20] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35 AND SER-54, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [22] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [23] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [24] RP SUBCELLULAR LOCATION, AND INTERACTION WITH HUMAN CYTOMEGALOVIRUS PROTEIN RP UL37 (MICROBIAL INFECTION). RX PubMed=27181750; DOI=10.1038/srep26028; RA Magalhaes A.C., Ferreira A.R., Gomes S., Vieira M., Gouveia A., Valenca I., RA Islinger M., Nascimento R., Schrader M., Kagan J.C., Ribeiro D.; RT "Peroxisomes are platforms for cytomegalovirus' evasion from the cellular RT immune response."; RL Sci. Rep. 6:26028-26028(2016). RN [25] RP STRUCTURE BY NMR OF 66-77 IN COMPLEX WITH PEX14. RX PubMed=19197237; DOI=10.1038/emboj.2009.7; RA Neufeld C., Filipp F.V., Simon B., Neuhaus A., Schueller N., David C., RA Kooshapur H., Madl T., Erdmann R., Schliebs W., Wilmanns M., Sattler M.; RT "Structural basis for competitive interactions of Pex14 with the import RT receptors Pex5 and Pex19."; RL EMBO J. 28:745-754(2009). RN [26] RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 1-44 IN COMPLEX WITH PEX3, AND RP SUBUNIT. RX PubMed=21102411; DOI=10.1038/emboj.2010.293; RA Sato Y., Shibata H., Nakatsu T., Nakano H., Kashiwayama Y., Imanaka T., RA Kato H.; RT "Structural basis for docking of peroxisomal membrane protein carrier RT Pex19p onto its receptor Pex3p."; RL EMBO J. 29:4083-4093(2010). RN [27] RP X-RAY CRYSTALLOGRAPHY (2.42 ANGSTROMS) OF 13-33 IN COMPLEX WITH PEX3, RP SUBUNIT, AND MUTAGENESIS OF PHE-29. RX PubMed=20554521; DOI=10.1074/jbc.m110.138503; RA Schmidt F., Treiber N., Zocher G., Bjelic S., Steinmetz M.O., Kalbacher H., RA Stehle T., Dodt G.; RT "Insights into peroxisome function from the structure of PEX3 in complex RT with a soluble fragment of PEX19."; RL J. Biol. Chem. 285:25410-25417(2010). RN [28] RP VARIANT VAL-85. RX PubMed=33798445; DOI=10.1016/j.ajhg.2021.03.013; RA Courage C., Oliver K.L., Park E.J., Cameron J.M., Grabinska K.A., Muona M., RA Canafoglia L., Gambardella A., Said E., Afawi Z., Baykan B., Brandt C., RA di Bonaventura C., Chew H.B., Criscuolo C., Dibbens L.M., Castellotti B., RA Riguzzi P., Labate A., Filla A., Giallonardo A.T., Berecki G., RA Jackson C.B., Joensuu T., Damiano J.A., Kivity S., Korczyn A., Palotie A., RA Striano P., Uccellini D., Giuliano L., Andermann E., Scheffer I.E., RA Michelucci R., Bahlo M., Franceschetti S., Sessa W.C., Berkovic S.F., RA Lehesjoki A.E.; RT "Progressive myoclonus epilepsies-Residual unsolved cases have marked RT genetic heterogeneity including dolichol-dependent protein glycosylation RT pathway genes."; RL Am. J. Hum. Genet. 108:722-738(2021). CC -!- FUNCTION: Necessary for early peroxisomal biogenesis. Acts both as a CC cytosolic chaperone and as an import receptor for peroxisomal membrane CC proteins (PMPs). Binds and stabilizes newly synthesized PMPs in the CC cytoplasm by interacting with their hydrophobic membrane-spanning CC domains, and targets them to the peroxisome membrane by binding to the CC integral membrane protein PEX3. Excludes CDKN2A from the nucleus and CC prevents its interaction with MDM2, which results in active degradation CC of TP53. {ECO:0000269|PubMed:10051604, ECO:0000269|PubMed:10704444, CC ECO:0000269|PubMed:11259404, ECO:0000269|PubMed:11883941, CC ECO:0000269|PubMed:14709540, ECO:0000269|PubMed:15007061}. CC -!- SUBUNIT: Interacts with a broad range of peroxisomal membrane proteins, CC including PEX3, PEX10, PEX11A, PEX11B, PEX12, PEX13, PEX14 and PEX16, CC PXMP2/PMP22, PXMP4/PMP24, SLC25A17/PMP34, ABCD1/ALDP, ABCD2/ALDRP, and CC ABCD3/PMP70. Also interacts with the tumor suppressor CDKN2A/p19ARF. CC {ECO:0000269|PubMed:10704444, ECO:0000269|PubMed:10777694, CC ECO:0000269|PubMed:11259404, ECO:0000269|PubMed:11390669, CC ECO:0000269|PubMed:11883941, ECO:0000269|PubMed:14709540, CC ECO:0000269|PubMed:15007061, ECO:0000269|PubMed:19197237, CC ECO:0000269|PubMed:20554521, ECO:0000269|PubMed:21102411}. CC -!- SUBUNIT: (Microbial infection) Interacts with human cytomegalovirus CC protein UL37 isoform vMIA; this interaction inhibits the peroxisomal- CC dependent antiviral signaling. {ECO:0000269|PubMed:27181750}. CC -!- INTERACTION: CC P40855; P33897: ABCD1; NbExp=3; IntAct=EBI-594747, EBI-81045; CC P40855; P28288: ABCD3; NbExp=4; IntAct=EBI-594747, EBI-80992; CC P40855; O43521: BCL2L11; NbExp=3; IntAct=EBI-594747, EBI-526406; CC P40855; Q9Y680: FKBP7; NbExp=3; IntAct=EBI-594747, EBI-3918971; CC P40855; P01574: IFNB1; NbExp=3; IntAct=EBI-594747, EBI-12383562; CC P40855; Q9NPF7: IL23A; NbExp=6; IntAct=EBI-594747, EBI-2481154; CC P40855; Q8N9F0: NAT8L; NbExp=3; IntAct=EBI-594747, EBI-14384265; CC P40855; O96011: PEX11B; NbExp=22; IntAct=EBI-594747, EBI-594824; CC P40855; O00623: PEX12; NbExp=2; IntAct=EBI-594747, EBI-594836; CC P40855; Q92968: PEX13; NbExp=12; IntAct=EBI-594747, EBI-594849; CC P40855; O75381: PEX14; NbExp=26; IntAct=EBI-594747, EBI-594898; CC P40855; Q9Y5Y5: PEX16; NbExp=20; IntAct=EBI-594747, EBI-981985; CC P40855; P28328: PEX2; NbExp=3; IntAct=EBI-594747, EBI-713978; CC P40855; Q7Z412: PEX26; NbExp=9; IntAct=EBI-594747, EBI-752057; CC P40855; P56589: PEX3; NbExp=47; IntAct=EBI-594747, EBI-594885; CC P40855; P23284: PPIB; NbExp=6; IntAct=EBI-594747, EBI-359252; CC P40855; Q9UIG4: PSORS1C2; NbExp=5; IntAct=EBI-594747, EBI-11974061; CC P40855; Q9NR77: PXMP2; NbExp=3; IntAct=EBI-594747, EBI-1392944; CC P40855; O43808: SLC25A17; NbExp=4; IntAct=EBI-594747, EBI-594912; CC P40855; P51687: SUOX; NbExp=3; IntAct=EBI-594747, EBI-3921347; CC P40855; Q99757: TXN2; NbExp=3; IntAct=EBI-594747, EBI-2932492; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10704444, CC ECO:0000269|PubMed:11259404, ECO:0000269|PubMed:15007061}. Peroxisome CC membrane {ECO:0000269|PubMed:10051604, ECO:0000269|PubMed:10704444, CC ECO:0000269|PubMed:15007061, ECO:0000269|PubMed:27181750, CC ECO:0000269|PubMed:9339377}; Lipid-anchor {ECO:0000269|PubMed:10051604, CC ECO:0000269|PubMed:9339377}; Cytoplasmic side CC {ECO:0000269|PubMed:10051604, ECO:0000269|PubMed:9339377}. Note=Mainly CC cytoplasmic. Some fraction membrane-associated to the outer surface of CC peroxisomes. {ECO:0000269|PubMed:10704444, CC ECO:0000269|PubMed:15007061}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Comment=Experimental confirmation may be lacking for some isoforms.; CC Name=1; Synonyms=PXF-all; CC IsoId=P40855-1; Sequence=Displayed; CC Name=2; Synonyms=PXF-delta-2, PXF lacking exon 2; CC IsoId=P40855-2; Sequence=Not described; CC Name=3; Synonyms=PXF-delta-4, PXF lacking exon 4; CC IsoId=P40855-3; Sequence=Not described; CC Name=4; Synonyms=PXF-delta-8, PXF lacking part of exon 8; CC IsoId=P40855-4; Sequence=Not described; CC Name=6; CC IsoId=P40855-6; Sequence=VSP_061572, VSP_061573; CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Isoform 1 is strongly CC predominant in all tissues except in utero where isoform 2 is the main CC form. {ECO:0000269|PubMed:9339377}. CC -!- DISEASE: Peroxisome biogenesis disorder complementation group 14 (PBD- CC CG14) [MIM:614886]: A peroxisomal disorder arising from a failure of CC protein import into the peroxisomal membrane or matrix. The peroxisome CC biogenesis disorders (PBD group) are genetically heterogeneous with at CC least 14 distinct genetic groups as concluded from complementation CC studies. Include disorders are: Zellweger syndrome (ZWS), neonatal CC adrenoleukodystrophy (NALD), infantile Refsum disease (IRD), and CC classical rhizomelic chondrodysplasia punctata (RCDP). ZWS, NALD and CC IRD are distinct from RCDP and constitute a clinical continuum of CC overlapping phenotypes known as the Zellweger spectrum (PBD-ZSS). CC {ECO:0000269|PubMed:20683989}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Peroxisome biogenesis disorder 12A (PBD12A) [MIM:614886]: A CC fatal peroxisome biogenesis disorder belonging to the Zellweger disease CC spectrum and clinically characterized by severe neurologic dysfunction CC with profound psychomotor retardation, severe hypotonia and neonatal CC seizures, craniofacial abnormalities, liver dysfunction, and CC biochemically by the absence of peroxisomes. Additional features CC include cardiovascular and skeletal defects, renal cysts, ocular CC abnormalities, and hearing impairment. Most severely affected CC individuals with the classic form of the disease (classic Zellweger CC syndrome) die within the first year of life. CC {ECO:0000269|PubMed:10051604}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- MISCELLANEOUS: [Isoform 1]: The two main transcripts are PXF-all and CC PXF-delta-2. CC -!- MISCELLANEOUS: [Isoform 2]: The two main transcripts are PXF-all and CC PXF-delta-2. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 6]: May be produced at very low levels due to a CC premature stop CC codon in the mRNA, leading to nonsense-mediated mRNA CC decay. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the peroxin-19 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAB93469.1; Type=Erroneous translation; Note=Wrong choice of frame.; Evidence={ECO:0000305}; 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; X75535; CAA53225.1; -; mRNA. DR EMBL; Y09048; CAA70257.1; -; Genomic_DNA. DR EMBL; AB018541; BAA76291.1; -; mRNA. DR EMBL; BT006879; AAP35525.1; -; mRNA. DR EMBL; KU178291; ALQ33749.1; -; mRNA. DR EMBL; AL139011; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL513282; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471121; EAW52728.1; -; Genomic_DNA. DR EMBL; CH471121; EAW52729.1; -; Genomic_DNA. DR EMBL; BC000496; AAH00496.1; -; mRNA. DR EMBL; AB062286; BAB93469.1; ALT_SEQ; mRNA. DR CCDS; CCDS1201.1; -. [P40855-1] DR PIR; I37468; I37468. DR RefSeq; NP_001180573.1; NM_001193644.1. DR RefSeq; NP_002848.1; NM_002857.3. [P40855-1] DR PDB; 2W85; NMR; -; B=66-77. DR PDB; 2WL8; X-ray; 2.05 A; A/B/C/D=161-283. DR PDB; 3AJB; X-ray; 2.50 A; B=1-44. DR PDB; 3MK4; X-ray; 2.42 A; B=14-33. DR PDB; 5LNF; NMR; -; A=161-299. DR PDBsum; 2W85; -. DR PDBsum; 2WL8; -. DR PDBsum; 3AJB; -. DR PDBsum; 3MK4; -. DR PDBsum; 5LNF; -. DR AlphaFoldDB; P40855; -. DR SMR; P40855; -. DR BioGRID; 111782; 204. DR DIP; DIP-24172N; -. DR ELM; P40855; -. DR IntAct; P40855; 116. DR MINT; P40855; -. DR STRING; 9606.ENSP00000357051; -. DR TCDB; 9.A.17.1.2; the integral membrane peroxisomal protein importer-2 (ppi2) family. DR GlyCosmos; P40855; 1 site, 1 glycan. DR GlyGen; P40855; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; P40855; -. DR MetOSite; P40855; -. DR PhosphoSitePlus; P40855; -. DR BioMuta; ENSG00000258465; -. DR BioMuta; PEX19; -. DR DMDM; 729723; -. DR EPD; P40855; -. DR jPOST; P40855; -. DR MassIVE; P40855; -. DR MaxQB; P40855; -. DR PaxDb; 9606-ENSP00000357051; -. DR PeptideAtlas; P40855; -. DR ProteomicsDB; 22668; -. DR ProteomicsDB; 32939; -. DR ProteomicsDB; 55381; -. [P40855-1] DR Pumba; P40855; -. DR Antibodypedia; 34274; 409 antibodies from 30 providers. DR DNASU; 5824; -. DR Ensembl; ENST00000368072.10; ENSP00000357051.5; ENSG00000162735.19. [P40855-1] DR Ensembl; ENST00000472750.5; ENSP00000434633.1; ENSG00000162735.19. [P40855-6] DR GeneID; 5824; -. DR KEGG; hsa:5824; -. DR MANE-Select; ENST00000368072.10; ENSP00000357051.5; NM_002857.4; NP_002848.1. DR UCSC; uc001fvs.3; human. [P40855-1] DR UCSC; uc010pjc.2; human. DR AGR; HGNC:9713; -. DR CTD; 5824; -. DR DisGeNET; 5824; -. DR GeneCards; PEX19; -. DR GeneReviews; PEX19; -. DR HGNC; HGNC:9713; PEX19. DR HPA; ENSG00000162735; Low tissue specificity. DR MalaCards; PEX19; -. DR MIM; 600279; gene. DR MIM; 614886; phenotype. DR neXtProt; NX_P40855; -. DR OpenTargets; ENSG00000162735; -. DR OpenTargets; ENSG00000258465; -. DR Orphanet; 772; Infantile Refsum disease. DR Orphanet; 44; Neonatal adrenoleukodystrophy. DR Orphanet; 912; Zellweger syndrome. DR PharmGKB; PA34058; -. DR VEuPathDB; HostDB:ENSG00000162735; -. DR VEuPathDB; HostDB:ENSG00000258465; -. DR eggNOG; KOG3133; Eukaryota. DR GeneTree; ENSGT00390000010993; -. DR HOGENOM; CLU_043063_3_0_1; -. DR InParanoid; P40855; -. DR OMA; YEPMKEM; -. DR OrthoDB; 1708793at2759; -. DR PhylomeDB; P40855; -. DR TreeFam; TF315082; -. DR TreeFam; TF326071; -. DR PathwayCommons; P40855; -. DR Reactome; R-HSA-1369062; ABC transporters in lipid homeostasis. DR Reactome; R-HSA-9603798; Class I peroxisomal membrane protein import. DR SignaLink; P40855; -. DR SIGNOR; P40855; -. DR BioGRID-ORCS; 5824; 32 hits in 1146 CRISPR screens. DR ChiTaRS; PEX19; human. DR EvolutionaryTrace; P40855; -. DR GeneWiki; PEX19; -. DR GenomeRNAi; 5824; -. DR Pharos; P40855; Tbio. DR PRO; PR:P40855; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; P40855; Protein. DR Bgee; ENSG00000162735; Expressed in hindlimb stylopod muscle and 198 other cell types or tissues. DR ExpressionAtlas; P40855; baseline and differential. DR GO; GO:0031526; C:brush border membrane; ISS:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:UniProtKB. DR GO; GO:0016020; C:membrane; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IMP:UniProtKB. DR GO; GO:0005778; C:peroxisomal membrane; IDA:UniProtKB. DR GO; GO:0005777; C:peroxisome; IDA:HPA. DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB. DR GO; GO:0051117; F:ATPase binding; IPI:UniProtKB. DR GO; GO:0036105; F:peroxisome membrane class-1 targeting sequence binding; IDA:UniProtKB. DR GO; GO:0033328; F:peroxisome membrane targeting sequence binding; IBA:GO_Central. DR GO; GO:0140597; F:protein carrier chaperone; IDA:UniProtKB. DR GO; GO:0061077; P:chaperone-mediated protein folding; IDA:UniProtKB. DR GO; GO:0072663; P:establishment of protein localization to peroxisome; IMP:UniProtKB. DR GO; GO:1900131; P:negative regulation of lipid binding; IDA:UniProtKB. DR GO; GO:0016559; P:peroxisome fission; IMP:UniProtKB. DR GO; GO:0016557; P:peroxisome membrane biogenesis; IDA:UniProtKB. DR GO; GO:0007031; P:peroxisome organization; IMP:UniProtKB. DR GO; GO:0045046; P:protein import into peroxisome membrane; IDA:UniProtKB. DR GO; GO:0050821; P:protein stabilization; IDA:UniProtKB. DR GO; GO:0006625; P:protein targeting to peroxisome; IDA:UniProtKB. DR DisProt; DP01805; -. DR Gene3D; 1.20.120.900; Pex19, mPTS binding domain; 1. DR InterPro; IPR006708; Pex19. DR InterPro; IPR038322; Pex19_C_sf. DR PANTHER; PTHR12774; PEROXISOMAL BIOGENESIS FACTOR 19; 1. DR PANTHER; PTHR12774:SF2; PEROXISOMAL BIOGENESIS FACTOR 19; 1. DR Pfam; PF04614; Pex19; 1. DR Genevisible; P40855; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm; KW Host-virus interaction; Lipoprotein; Membrane; Methylation; Peroxisome; KW Peroxisome biogenesis; Peroxisome biogenesis disorder; Phosphoprotein; KW Prenylation; Reference proteome; Zellweger syndrome. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:22814378, FT ECO:0007744|PubMed:25944712" FT CHAIN 2..296 FT /note="Peroxisomal biogenesis factor 19" FT /id="PRO_0000218759" FT PROPEP 297..299 FT /note="Removed in mature form" FT /evidence="ECO:0000305" FT /id="PRO_0000393944" FT REGION 1..63 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2..91 FT /note="Necessary for PEX19 function on peroxisome FT biogenesis" FT REGION 2..56 FT /note="Docking to the peroxisome membrane and binding to FT PEX3" FT COMPBIAS 10..30 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0007744|PubMed:22814378, FT ECO:0007744|PubMed:25944712" FT MOD_RES 35 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 54 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 66 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9QYU1" FT MOD_RES 236 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q8VCI5" FT MOD_RES 296 FT /note="Cysteine methyl ester" FT /evidence="ECO:0000305" FT LIPID 296 FT /note="S-farnesyl cysteine" FT /evidence="ECO:0000269|PubMed:10051604, FT ECO:0000269|PubMed:9339377" FT VAR_SEQ 24..40 FT /note="SALDDFDKAKPSPAPPS -> RCPLRFPREVFPGTIRQ (in isoform FT 6)" FT /id="VSP_061572" FT VAR_SEQ 41..299 FT /note="Missing (in isoform 6)" FT /id="VSP_061573" FT VARIANT 85 FT /note="A -> V (found in patients with progressive myoclonus FT epilepsy and dementia; uncertain significance; FT dbSNP:rs11550119)" FT /evidence="ECO:0000269|PubMed:33798445" FT /id="VAR_085044" FT MUTAGEN 29 FT /note="F->A: Abolishes binding to PEX3." FT /evidence="ECO:0000269|PubMed:20554521" FT MUTAGEN 296..299 FT /note="Missing: Abolishes binding to PEX10, PEX11B, PEX12 FT and PEX13. Does not affect binding to PEX3 and PEX16." FT /evidence="ECO:0000269|PubMed:11390669" FT MUTAGEN 296 FT /note="C->A: Slightly inhibits PEX19 function on peroxisome FT biogenesis." FT /evidence="ECO:0000269|PubMed:10051604, FT ECO:0000269|PubMed:10704444, ECO:0000269|PubMed:10777694, FT ECO:0000269|PubMed:9339377" FT MUTAGEN 296 FT /note="C->S: Abolishes farnesylation. Abolishes PEX19 FT function on peroxisome biogenesis. Does not affect binding FT to ABCD1, ABCD2 and ABCD3." FT /evidence="ECO:0000269|PubMed:10051604, FT ECO:0000269|PubMed:10704444, ECO:0000269|PubMed:10777694, FT ECO:0000269|PubMed:9339377" FT HELIX 16..27 FT /evidence="ECO:0007829|PDB:3MK4" FT HELIX 28..31 FT /evidence="ECO:0007829|PDB:3AJB" FT HELIX 67..76 FT /evidence="ECO:0007829|PDB:2W85" FT HELIX 172..182 FT /evidence="ECO:0007829|PDB:2WL8" FT HELIX 185..196 FT /evidence="ECO:0007829|PDB:2WL8" FT HELIX 199..206 FT /evidence="ECO:0007829|PDB:2WL8" FT HELIX 207..209 FT /evidence="ECO:0007829|PDB:2WL8" FT HELIX 212..234 FT /evidence="ECO:0007829|PDB:2WL8" FT HELIX 241..260 FT /evidence="ECO:0007829|PDB:2WL8" FT HELIX 266..268 FT /evidence="ECO:0007829|PDB:2WL8" FT HELIX 280..283 FT /evidence="ECO:0007829|PDB:5LNF" SQ SEQUENCE 299 AA; 32807 MW; 399AF6B79F219100 CRC64; MAAAEEGCSV GAEADRELEE LLESALDDFD KAKPSPAPPS TTTAPDASGP QKRSPGDTAK DALFASQEKF FQELFDSELA SQATAEFEKA MKELAEEEPH LVEQFQKLSE AAGRVGSDMT SQQEFTSCLK ETLSGLAKNA TDLQNSSMSE EELTKAMEGL GMDEGDGEGN ILPIMQSIMQ NLLSKDVLYP SLKEITEKYP EWLQSHRESL PPEQFEKYQE QHSVMCKICE QFEAETPTDS ETTQKARFEM VLDLMQQLQD LGHPPKELAG EMPPGLNFDL DALNLSGPPG ASGEQCLIM //