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Peroxisomal biogenesis factor 19 (33 kDa housekeeping protein) (Peroxin-19) (Peroxisomal farnesylated protein)

 PEX19_HUMAN             Reviewed;         299 AA.
P40855; D3DVE7; Q5QNY4; Q8NI97;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
01-FEB-1995, sequence version 1.
27-SEP-2017, entry version 178.
RecName: Full=Peroxisomal biogenesis factor 19;
AltName: Full=33 kDa housekeeping protein;
AltName: Full=Peroxin-19;
AltName: Full=Peroxisomal farnesylated protein;
Flags: Precursor;
Name=PEX19; Synonyms=HK33, PXF; ORFNames=OK/SW-cl.22;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Ovary, and Placenta;
PubMed=8076834; DOI=10.1016/0378-1119(94)90308-5;
Braun A., Kammerer S., Weissenhorn W., Weiss E.H., Cleve H.;
"Sequence of a putative human housekeeping gene (HK33) localized on
chromosome 1.";
Gene 146:291-295(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING, TISSUE
SPECIFICITY, SUBCELLULAR LOCATION, ISOPRENYLATION AT CYS-296, AND
MUTAGENESIS OF CYS-296.
TISSUE=Leukocyte, and Placenta;
PubMed=9339377; DOI=10.1006/geno.1997.4914;
Kammerer S., Arnold N., Gutensohn W., Mewes H.-W., Kunau W.-H.,
Hoefler G., Roscher A.A., Braun A.;
"Genomic organization and molecular characterization of a gene
encoding HsPXF, a human peroxisomal farnesylated protein.";
Genomics 45:200-210(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ISOPRENYLATION AT CYS-296,
MUTAGENESIS OF CYS-296, SUBCELLULAR LOCATION, FUNCTION, AND
INVOLVEMENT IN PBD12A.
TISSUE=Liver;
PubMed=10051604; DOI=10.1073/pnas.96.5.2116;
Matsuzono Y., Kinoshita N., Tamura S., Shimozawa N., Hamasaki M.,
Ghaedi K., Wanders R.J.A., Suzuki Y., Kondo N., Fujiki Y.;
"Human PEX19: cDNA cloning by functional complementation, mutation
analysis in a patient with Zellweger syndrome, and potential role in
peroxisomal membrane assembly.";
Proc. Natl. Acad. Sci. U.S.A. 96:2116-2121(1999).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
TISSUE=Colon adenocarcinoma;
Shichijo S., Itoh K.;
"Identification of immuno-peptidmics that are recognized by tumor-
reactive CTL generated from TIL of colon cancer patients.";
Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
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).
[9]
INTERACTION WITH ABCD1; ABCD2 AND ABCD3, AND MUTAGENESIS OF CYS-296.
TISSUE=Brain;
PubMed=10777694; DOI=10.1006/bbrc.2000.2572;
Gloeckner C.J., Mayerhofer P.U., Landgraf P., Muntau A.C.,
Holzinger A., Gerber J.-K., Kammerer S., Adamski J., Roscher A.A.;
"Human adrenoleukodystrophy protein and related peroxisomal ABC
transporters interact with the peroxisomal assembly protein PEX19p.";
Biochem. Biophys. Res. Commun. 271:144-150(2000).
[10]
FUNCTION, MUTAGENESIS OF CYS-296, SUBCELLULAR LOCATION, AND
INTERACTION WITH ABCD1; ABCD2; ABCD3; PEX3; PEX10; PEX11A; PEX11B;
PEX12; PEX13; PEX14; PEX16; PXMP2; PXMP4 AND SLC25A17.
PubMed=10704444; DOI=10.1083/jcb.148.5.931;
Sacksteder K.A., Jones J.M., South S.T., Li X., Liu Y., Gould S.J.;
"PEX19 binds multiple peroxisomal membrane proteins, is predominantly
cytoplasmic, and is required for peroxisome membrane synthesis.";
J. Cell Biol. 148:931-944(2000).
[11]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CDKN2A.
TISSUE=Testis;
PubMed=11259404; DOI=10.1074/jbc.C100011200;
Sugihara T., Kaul S.C., Kato J.-Y., Reddel R.R., Nomura H., Wadhwa R.;
"Pex19p dampens the p19ARF-p53-p21WAF1 tumor suppressor pathway.";
J. Biol. Chem. 276:18649-18652(2001).
[12]
INTERACTION WITH PEX3; PEX10; PEX11B; PEX12; PEX13 AND PEX16, AND
MUTAGENESIS OF 296-CYS--MET-299.
PubMed=11390669; DOI=10.1128/MCB.21.13.4413-4424.2001;
Fransen M., Wylin T., Brees C., Mannaerts G.P., Van Veldhoven P.P.;
"Human pex19p binds peroxisomal integral membrane proteins at regions
distinct from their sorting sequences.";
Mol. Cell. Biol. 21:4413-4424(2001).
[13]
FUNCTION, AND INTERACTION WITH ABCD1; ABCD2; ABCD3 AND PEX3.
PubMed=11883941; DOI=10.1006/bbrc.2002.6568;
Mayerhofer P.U., Kattenfeld T., Roscher A.A., Muntau A.C.;
"Two splice variants of human PEX19 exhibit distinct functions in
peroxisomal assembly.";
Biochem. Biophys. Res. Commun. 291:1180-1186(2002).
[14]
FUNCTION, INTERACTION WITH PEX3, AND SUBCELLULAR LOCATION.
PubMed=15007061; DOI=10.1083/jcb.200311131;
Fang Y., Morrell J.C., Jones J.M., Gould S.J.;
"PEX3 functions as a PEX19 docking factor in the import of class I
peroxisomal membrane proteins.";
J. Cell Biol. 164:863-875(2004).
[15]
FUNCTION, AND INTERACTION WITH PEX11B; PEX16; PXMP2; PXMP4; SLC25A17
AND ABCD3.
PubMed=14709540; DOI=10.1083/jcb.200304111;
Jones J.M., Morrell J.C., Gould S.J.;
"PEX19 is a predominantly cytosolic chaperone and import receptor for
class 1 peroxisomal membrane proteins.";
J. Cell Biol. 164:57-67(2004).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[17]
INVOLVEMENT IN PBD-CG14.
PubMed=20683989; DOI=10.1002/ajmg.a.33560;
Mohamed S., El-Meleagy E., Nasr A., Ebberink M.S., Wanders R.J.,
Waterham H.R.;
"A mutation in PEX19 causes a severe clinical phenotype in a patient
with peroxisomal biogenesis disorder.";
Am. J. Med. Genet. A 152:2318-2321(2010).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[19]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35 AND SER-54, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[22]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[23]
STRUCTURE BY NMR OF 66-77 IN COMPLEX WITH PEX14.
PubMed=19197237; DOI=10.1038/emboj.2009.7;
Neufeld C., Filipp F.V., Simon B., Neuhaus A., Schueller N., David C.,
Kooshapur H., Madl T., Erdmann R., Schliebs W., Wilmanns M.,
Sattler M.;
"Structural basis for competitive interactions of Pex14 with the
import receptors Pex5 and Pex19.";
EMBO J. 28:745-754(2009).
[24]
X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 1-44 IN COMPLEX WITH PEX3,
AND SUBUNIT.
PubMed=21102411; DOI=10.1038/emboj.2010.293;
Sato Y., Shibata H., Nakatsu T., Nakano H., Kashiwayama Y.,
Imanaka T., Kato H.;
"Structural basis for docking of peroxisomal membrane protein carrier
Pex19p onto its receptor Pex3p.";
EMBO J. 29:4083-4093(2010).
[25]
X-RAY CRYSTALLOGRAPHY (2.42 ANGSTROMS) OF 13-33 IN COMPLEX WITH PEX3,
SUBUNIT, AND MUTAGENESIS OF PHE-29.
PubMed=20554521; DOI=10.1074/jbc.M110.138503;
Schmidt F., Treiber N., Zocher G., Bjelic S., Steinmetz M.O.,
Kalbacher H., Stehle T., Dodt G.;
"Insights into peroxisome function from the structure of PEX3 in
complex with a soluble fragment of PEX19.";
J. Biol. Chem. 285:25410-25417(2010).
-!- FUNCTION: Necessary for early peroxisomal biogenesis. Acts both as
a cytosolic chaperone and as an import receptor for peroxisomal
membrane proteins (PMPs). Binds and stabilizes newly synthesized
PMPs in the cytoplasm by interacting with their hydrophobic
membrane-spanning domains, and targets them to the peroxisome
membrane by binding to the integral membrane protein PEX3.
Excludes CDKN2A from the nucleus and prevents its interaction with
MDM2, which results in active degradation of TP53.
{ECO:0000269|PubMed:10051604, ECO:0000269|PubMed:10704444,
ECO:0000269|PubMed:11259404, ECO:0000269|PubMed:11883941,
ECO:0000269|PubMed:14709540, ECO:0000269|PubMed:15007061}.
-!- SUBUNIT: Interacts with a broad range of peroxisomal membrane
proteins, including PEX3, PEX10, PEX11A, PEX11B, PEX12, PEX13,
PEX14 and PEX16, PXMP2/PMP22, PXMP4/PMP24, SLC25A17/PMP34,
ABCD1/ALDP, ABCD2/ALDRP, and ABCD3/PMP70. Also interacts with the
tumor suppressor CDKN2A/p19ARF. {ECO:0000269|PubMed:10704444,
ECO:0000269|PubMed:10777694, ECO:0000269|PubMed:11259404,
ECO:0000269|PubMed:11390669, ECO:0000269|PubMed:11883941,
ECO:0000269|PubMed:14709540, ECO:0000269|PubMed:15007061,
ECO:0000269|PubMed:19197237, ECO:0000269|PubMed:20554521,
ECO:0000269|PubMed:21102411}.
-!- INTERACTION:
P33897:ABCD1; NbExp=3; IntAct=EBI-594747, EBI-81045;
P28288:ABCD3; NbExp=4; IntAct=EBI-594747, EBI-80992;
Q9Y680:FKBP7; NbExp=3; IntAct=EBI-594747, EBI-3918971;
Q9NPF7:IL23A; NbExp=5; IntAct=EBI-594747, EBI-2481154;
Q8N9F0:NAT8L; NbExp=4; IntAct=EBI-594747, EBI-14384265;
O96011:PEX11B; NbExp=12; IntAct=EBI-594747, EBI-594824;
O00623:PEX12; NbExp=2; IntAct=EBI-594747, EBI-594836;
Q92968:PEX13; NbExp=12; IntAct=EBI-594747, EBI-594849;
O75381:PEX14; NbExp=15; IntAct=EBI-594747, EBI-594898;
Q9Y5Y5:PEX16; NbExp=7; IntAct=EBI-594747, EBI-981985;
P28328:PEX2; NbExp=3; IntAct=EBI-594747, EBI-713978;
Q7Z412:PEX26; NbExp=8; IntAct=EBI-594747, EBI-752057;
P56589:PEX3; NbExp=27; IntAct=EBI-594747, EBI-594885;
P23284:PPIB; NbExp=5; IntAct=EBI-594747, EBI-359252;
Q9NR77:PXMP2; NbExp=2; IntAct=EBI-594747, EBI-1392944;
O43808:SLC25A17; NbExp=4; IntAct=EBI-594747, EBI-594912;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10704444,
ECO:0000269|PubMed:11259404, ECO:0000269|PubMed:15007061}.
Peroxisome membrane {ECO:0000269|PubMed:10051604,
ECO:0000269|PubMed:10704444, ECO:0000269|PubMed:15007061,
ECO:0000269|PubMed:9339377}; Lipid-anchor
{ECO:0000269|PubMed:10051604, ECO:0000269|PubMed:9339377};
Cytoplasmic side {ECO:0000269|PubMed:10051604,
ECO:0000269|PubMed:9339377}. Note=Mainly cytoplasmic. Some
fraction membrane-associated to the outer surface of peroxisomes.
{ECO:0000269|PubMed:10704444, ECO:0000269|PubMed:15007061}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Comment=Experimental confirmation may be lacking for some
isoforms.;
Name=1; Synonyms=PXF-all;
IsoId=P40855-1; Sequence=Displayed;
Note=The two main transcripts are PXF-all and PXF-delta-2.;
Name=2; Synonyms=PXF-delta-2, PXF lacking exon 2;
IsoId=P40855-2; Sequence=Not described;
Note=The two main transcripts are PXF-all and PXF-delta-2.;
Name=3; Synonyms=PXF-delta-4, PXF lacking exon 4;
IsoId=P40855-3; Sequence=Not described;
Name=4; Synonyms=PXF-delta-8, PXF lacking part of exon 8;
IsoId=P40855-4; Sequence=Not described;
Name=5;
IsoId=P40855-5; Sequence=VSP_012649;
Note=Incomplete sequence.;
-!- TISSUE SPECIFICITY: Ubiquitously expressed. Isoform 1 is strongly
predominant in all tissues except in utero where isoform 2 is the
main form. {ECO:0000269|PubMed:9339377}.
-!- DISEASE: Peroxisome biogenesis disorder complementation group 14
(PBD-CG14) [MIM:614886]: A peroxisomal disorder arising from a
failure of protein import into the peroxisomal membrane or matrix.
The peroxisome biogenesis disorders (PBD group) are genetically
heterogeneous with at least 14 distinct genetic groups as
concluded from complementation studies. Include disorders are:
Zellweger syndrome (ZWS), neonatal adrenoleukodystrophy (NALD),
infantile Refsum disease (IRD), and classical rhizomelic
chondrodysplasia punctata (RCDP). ZWS, NALD and IRD are distinct
from RCDP and constitute a clinical continuum of overlapping
phenotypes known as the Zellweger spectrum (PBD-ZSS).
{ECO:0000269|PubMed:20683989}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Peroxisome biogenesis disorder 12A (PBD12A) [MIM:614886]:
A fatal peroxisome biogenesis disorder belonging to the Zellweger
disease spectrum and clinically characterized by severe neurologic
dysfunction with profound psychomotor retardation, severe
hypotonia and neonatal seizures, craniofacial abnormalities, liver
dysfunction, and biochemically by the absence of peroxisomes.
Additional features include cardiovascular and skeletal defects,
renal cysts, ocular abnormalities, and hearing impairment. Most
severely affected individuals with the classic form of the disease
(classic Zellweger syndrome) die within the first year of life.
{ECO:0000269|PubMed:10051604}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the peroxin-19 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAB93469.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; X75535; CAA53225.1; -; mRNA.
EMBL; Y09048; CAA70257.1; -; Genomic_DNA.
EMBL; AB018541; BAA76291.1; -; mRNA.
EMBL; AB062286; BAB93469.1; ALT_INIT; mRNA.
EMBL; BT006879; AAP35525.1; -; mRNA.
EMBL; AL513282; CAI12457.1; -; Genomic_DNA.
EMBL; CH471121; EAW52728.1; -; Genomic_DNA.
EMBL; CH471121; EAW52729.1; -; Genomic_DNA.
EMBL; BC000496; AAH00496.1; -; mRNA.
CCDS; CCDS1201.1; -. [P40855-1]
PIR; I37468; I37468.
RefSeq; NP_001180573.1; NM_001193644.1.
RefSeq; NP_002848.1; NM_002857.3. [P40855-1]
UniGene; Hs.517232; -.
PDB; 2W85; NMR; -; B=66-77.
PDB; 2WL8; X-ray; 2.05 A; A/B/C/D=161-283.
PDB; 3AJB; X-ray; 2.50 A; B=1-44.
PDB; 3MK4; X-ray; 2.42 A; B=14-33.
PDB; 5LNF; NMR; -; A=161-299.
PDBsum; 2W85; -.
PDBsum; 2WL8; -.
PDBsum; 3AJB; -.
PDBsum; 3MK4; -.
PDBsum; 5LNF; -.
ProteinModelPortal; P40855; -.
SMR; P40855; -.
BioGrid; 111782; 124.
DIP; DIP-24172N; -.
ELM; P40855; -.
IntAct; P40855; 43.
MINT; MINT-241394; -.
STRING; 9606.ENSP00000357051; -.
TCDB; 9.A.17.1.2; the integral membrane peroxisomal protein importer-2 (ppi2) family.
iPTMnet; P40855; -.
PhosphoSitePlus; P40855; -.
BioMuta; PEX19; -.
DMDM; 729723; -.
EPD; P40855; -.
PaxDb; P40855; -.
PeptideAtlas; P40855; -.
PRIDE; P40855; -.
DNASU; 5824; -.
Ensembl; ENST00000368072; ENSP00000357051; ENSG00000162735. [P40855-1]
GeneID; 5824; -.
KEGG; hsa:5824; -.
UCSC; uc001fvs.3; human. [P40855-1]
CTD; 5824; -.
DisGeNET; 5824; -.
EuPathDB; HostDB:ENSG00000162735.18; -.
GeneCards; PEX19; -.
GeneReviews; PEX19; -.
HGNC; HGNC:9713; PEX19.
HPA; HPA044837; -.
HPA; HPA051966; -.
MalaCards; PEX19; -.
MIM; 600279; gene.
MIM; 614886; phenotype.
neXtProt; NX_P40855; -.
OpenTargets; ENSG00000162735; -.
Orphanet; 772; Infantile Refsum disease.
Orphanet; 44; Neonatal adrenoleukodystrophy.
Orphanet; 912; Zellweger syndrome.
PharmGKB; PA34058; -.
eggNOG; KOG3133; Eukaryota.
eggNOG; ENOG4111QGU; LUCA.
GeneTree; ENSGT00390000010993; -.
HOGENOM; HOG000038537; -.
HOVERGEN; HBG053573; -.
InParanoid; P40855; -.
KO; K13337; -.
OMA; LQDYGQP; -.
OrthoDB; EOG091G0IMB; -.
PhylomeDB; P40855; -.
TreeFam; TF315082; -.
Reactome; R-HSA-1369062; ABC transporters in lipid homeostasis.
SIGNOR; P40855; -.
EvolutionaryTrace; P40855; -.
GeneWiki; PEX19; -.
GenomeRNAi; 5824; -.
PRO; PR:P40855; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000162735; -.
CleanEx; HS_PEX19; -.
ExpressionAtlas; P40855; baseline and differential.
Genevisible; P40855; HS.
GO; GO:0031526; C:brush border membrane; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IMP:UniProtKB.
GO; GO:0005778; C:peroxisomal membrane; IDA:UniProtKB.
GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; IDA:UniProtKB.
GO; GO:0051117; F:ATPase binding; IPI:UniProtKB.
GO; GO:0036105; F:peroxisome membrane class-1 targeting sequence binding; IDA:UniProtKB.
GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB.
GO; GO:0061077; P:chaperone-mediated protein folding; IDA:UniProtKB.
GO; GO:0072321; P:chaperone-mediated protein transport; IDA:UniProtKB.
GO; GO:0072663; P:establishment of protein localization to peroxisome; IMP:UniProtKB.
GO; GO:1900131; P:negative regulation of lipid binding; IDA:UniProtKB.
GO; GO:0016559; P:peroxisome fission; IMP:UniProtKB.
GO; GO:0016557; P:peroxisome membrane biogenesis; IDA:UniProtKB.
GO; GO:0007031; P:peroxisome organization; IMP:UniProtKB.
GO; GO:0045046; P:protein import into peroxisome membrane; IDA:UniProtKB.
GO; GO:0050821; P:protein stabilization; IDA:UniProtKB.
GO; GO:0006625; P:protein targeting to peroxisome; IDA:UniProtKB.
GO; GO:0055085; P:transmembrane transport; TAS:Reactome.
InterPro; IPR006708; Pex19.
PANTHER; PTHR12774; PTHR12774; 1.
Pfam; PF04614; Pex19; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Cytoplasm; Lipoprotein; Membrane; Methylation; Peroxisome;
Peroxisome biogenesis; Peroxisome biogenesis disorder; Phosphoprotein;
Prenylation; Reference proteome; Zellweger syndrome.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22814378,
ECO:0000244|PubMed:25944712}.
CHAIN 2 296 Peroxisomal biogenesis factor 19.
/FTId=PRO_0000218759.
PROPEP 297 299 Removed in mature form. {ECO:0000305}.
/FTId=PRO_0000393944.
REGION 2 91 Necessary for PEX19 function on
peroxisome biogenesis.
REGION 2 56 Docking to the peroxisome membrane and
binding to PEX3.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:22814378,
ECO:0000244|PubMed:25944712}.
MOD_RES 35 35 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 54 54 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 66 66 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QYU1}.
MOD_RES 236 236 Phosphothreonine.
{ECO:0000250|UniProtKB:Q8VCI5}.
MOD_RES 296 296 Cysteine methyl ester. {ECO:0000305}.
LIPID 296 296 S-farnesyl cysteine.
{ECO:0000269|PubMed:10051604,
ECO:0000269|PubMed:9339377}.
VAR_SEQ 1 59 MAAAEEGCSVGAEADRELEELLESALDDFDKAKPSPAPPST
TTAPDASGPQKRSPGDTA -> PPLRKAVVSGPKRTGNWRS
FW (in isoform 5). {ECO:0000303|Ref.4}.
/FTId=VSP_012649.
MUTAGEN 29 29 F->A: Abolishes binding to PEX3.
{ECO:0000269|PubMed:20554521}.
MUTAGEN 296 299 Missing: Abolishes binding to PEX10,
PEX11B, PEX12 and PEX13. Does not affect
binding to PEX3 and PEX16.
{ECO:0000269|PubMed:11390669}.
MUTAGEN 296 296 C->A: Slightly inhibits PEX19 function on
peroxisome biogenesis.
{ECO:0000269|PubMed:10051604,
ECO:0000269|PubMed:10704444,
ECO:0000269|PubMed:10777694,
ECO:0000269|PubMed:9339377}.
MUTAGEN 296 296 C->S: Abolishes farnesylation. Abolishes
PEX19 function on peroxisome biogenesis.
Does not affect binding to ABCD1, ABCD2
and ABCD3. {ECO:0000269|PubMed:10051604,
ECO:0000269|PubMed:10704444,
ECO:0000269|PubMed:10777694,
ECO:0000269|PubMed:9339377}.
HELIX 16 27 {ECO:0000244|PDB:3MK4}.
HELIX 28 31 {ECO:0000244|PDB:3AJB}.
HELIX 67 76 {ECO:0000244|PDB:2W85}.
HELIX 172 182 {ECO:0000244|PDB:2WL8}.
HELIX 185 196 {ECO:0000244|PDB:2WL8}.
HELIX 199 206 {ECO:0000244|PDB:2WL8}.
HELIX 207 209 {ECO:0000244|PDB:2WL8}.
HELIX 212 234 {ECO:0000244|PDB:2WL8}.
HELIX 241 260 {ECO:0000244|PDB:2WL8}.
HELIX 266 268 {ECO:0000244|PDB:2WL8}.
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


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