PEX19_HUMAN
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 03-AUG-2022, entry version 211.
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 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 [25]
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 [26]
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 [27]
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 -!- 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:9339377}; Lipid-anchor
CC {ECO:0000269|PubMed:10051604, ECO:0000269|PubMed:9339377}; Cytoplasmic
CC side {ECO:0000269|PubMed:10051604, ECO:0000269|PubMed:9339377}.
CC Note=Mainly cytoplasmic. Some fraction membrane-associated to the outer
CC surface of 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};
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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; 199.
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 GlyGen; P40855; 1 site, 1 O-linked glycan (1 site).
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; P40855; -.
DR PeptideAtlas; P40855; -.
DR PRIDE; P40855; -.
DR ProteomicsDB; 55381; -. [P40855-1]
DR Antibodypedia; 34274; 376 antibodies from 30 providers.
DR DNASU; 5824; -.
DR Ensembl; ENST00000368072.10; ENSP00000357051.5; ENSG00000162735.19. [P40855-1]
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 CTD; 5824; -.
DR DisGeNET; 5824; -.
DR GeneCards; ENSG00000258465; -.
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 Orphanet; 772; Infantile Refsum disease.
DR Orphanet; 44; Neonatal adrenoleukodystrophy.
DR Orphanet; 912; Zellweger syndrome.
DR PharmGKB; PA34058; -.
DR VEuPathDB; HostDB:ENSG00000162735; -.
DR eggNOG; KOG3133; Eukaryota.
DR GeneTree; ENSGT00390000010993; -.
DR HOGENOM; CLU_043063_3_0_1; -.
DR InParanoid; P40855; -.
DR OMA; NPQCPTM; -.
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; 30 hits in 1068 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 196 other tissues.
DR ExpressionAtlas; P40855; baseline and differential.
DR Genevisible; P40855; HS.
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:0016021; C:integral component of 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:UniProtKB.
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:0047485; F:protein N-terminus binding; IPI: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; -; 1.
DR InterPro; IPR006708; Pex19.
DR InterPro; IPR038322; Pex19_C_sf.
DR PANTHER; PTHR12774; PTHR12774; 1.
DR Pfam; PF04614; Pex19; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm; Lipoprotein;
KW Membrane; Methylation; Peroxisome; Peroxisome biogenesis;
KW Peroxisome biogenesis disorder; Phosphoprotein; Prenylation;
KW 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; unknown pathological 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
