PEX19_MOUSE
ID PEX19_MOUSE Reviewed; 299 AA.
AC Q8VCI5; Q4FJU7; Q8CEE1; Q921H0; Q9CZC1; Q9QUQ1;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Peroxisomal biogenesis factor 19;
DE AltName: Full=Peroxin-19;
DE AltName: Full=Peroxisomal farnesylated protein;
DE Short=PxF;
DE Flags: Precursor;
GN Name=Pex19; Synonyms=Pxf;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
RC STRAIN=129/SvJ, and BALB/cJ; TISSUE=Liver, and Lung;
RA Kammerer S.;
RL Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Embryo, Head, and Skin;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J.,
RA Wiemann S., Schick M., Korn B.;
RT "Cloning of mouse full open reading frames in Gateway(R) system entry
RT vector (pDONR201).";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Eye, and Mammary tumor;
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 [5]
RP PROTEIN SEQUENCE OF 218-227, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-236, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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:0000250|UniProtKB:P40855}.
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 (By
CC similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q8VCI5; Q64364-1: Cdkn2a; NbExp=4; IntAct=EBI-1810767, EBI-1202306;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P40855}.
CC Peroxisome membrane {ECO:0000250|UniProtKB:P40855}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P40855}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P40855}. Note=Mainly cytoplasmic, some fraction
CC membrane-associated to the outer surface of peroxisomes.
CC {ECO:0000250|UniProtKB:P40855}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8VCI5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8VCI5-2; Sequence=VSP_012652;
CC -!- SIMILARITY: Belongs to the peroxin-19 family. {ECO:0000305}.
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DR EMBL; Y09046; CAA70255.1; -; mRNA.
DR EMBL; Y09047; CAA70256.1; -; Genomic_DNA.
DR EMBL; AK012785; BAB28468.1; -; mRNA.
DR EMBL; AK028449; BAC25957.1; -; mRNA.
DR EMBL; AK029368; BAC26421.1; -; mRNA.
DR EMBL; CT010305; CAJ18513.1; -; mRNA.
DR EMBL; BC012517; AAH12517.1; -; mRNA.
DR EMBL; BC019767; AAH19767.1; -; mRNA.
DR CCDS; CCDS15508.1; -. [Q8VCI5-1]
DR CCDS; CCDS48445.1; -. [Q8VCI5-2]
DR RefSeq; NP_001152997.1; NM_001159525.1. [Q8VCI5-2]
DR RefSeq; NP_075528.3; NM_023041.3. [Q8VCI5-1]
DR AlphaFoldDB; Q8VCI5; -.
DR SMR; Q8VCI5; -.
DR BioGRID; 202520; 7.
DR IntAct; Q8VCI5; 1.
DR STRING; 10090.ENSMUSP00000075289; -.
DR iPTMnet; Q8VCI5; -.
DR PhosphoSitePlus; Q8VCI5; -.
DR EPD; Q8VCI5; -.
DR jPOST; Q8VCI5; -.
DR MaxQB; Q8VCI5; -.
DR PaxDb; Q8VCI5; -.
DR PeptideAtlas; Q8VCI5; -.
DR PRIDE; Q8VCI5; -.
DR ProteomicsDB; 288037; -. [Q8VCI5-1]
DR ProteomicsDB; 288038; -. [Q8VCI5-2]
DR Antibodypedia; 34274; 376 antibodies from 30 providers.
DR DNASU; 19298; -.
DR Ensembl; ENSMUST00000075895; ENSMUSP00000075289; ENSMUSG00000003464. [Q8VCI5-1]
DR Ensembl; ENSMUST00000111252; ENSMUSP00000106883; ENSMUSG00000003464. [Q8VCI5-2]
DR GeneID; 19298; -.
DR KEGG; mmu:19298; -.
DR UCSC; uc007dpq.2; mouse. [Q8VCI5-1]
DR UCSC; uc011wwj.1; mouse. [Q8VCI5-2]
DR CTD; 5824; -.
DR MGI; MGI:1334458; Pex19.
DR VEuPathDB; HostDB:ENSMUSG00000003464; -.
DR eggNOG; KOG3133; Eukaryota.
DR GeneTree; ENSGT00390000010993; -.
DR HOGENOM; CLU_043063_3_0_1; -.
DR InParanoid; Q8VCI5; -.
DR OMA; NPQCPTM; -.
DR OrthoDB; 1282367at2759; -.
DR PhylomeDB; Q8VCI5; -.
DR TreeFam; TF315082; -.
DR Reactome; R-MMU-1369062; ABC transporters in lipid homeostasis.
DR Reactome; R-MMU-9603798; Class I peroxisomal membrane protein import.
DR BioGRID-ORCS; 19298; 8 hits in 74 CRISPR screens.
DR ChiTaRS; Pex19; mouse.
DR PRO; PR:Q8VCI5; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8VCI5; protein.
DR Bgee; ENSMUSG00000003464; Expressed in embryonic brain and 261 other tissues.
DR Genevisible; Q8VCI5; MM.
DR GO; GO:0031526; C:brush border membrane; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005778; C:peroxisomal membrane; ISO:MGI.
DR GO; GO:0005777; C:peroxisome; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0051117; F:ATPase binding; ISO:MGI.
DR GO; GO:0036105; F:peroxisome membrane class-1 targeting sequence binding; ISO:MGI.
DR GO; GO:0033328; F:peroxisome membrane targeting sequence binding; IBA:GO_Central.
DR GO; GO:0140597; F:protein carrier chaperone; ISO:MGI.
DR GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
DR GO; GO:0061077; P:chaperone-mediated protein folding; ISO:MGI.
DR GO; GO:0072663; P:establishment of protein localization to peroxisome; ISO:MGI.
DR GO; GO:1900131; P:negative regulation of lipid binding; ISO:MGI.
DR GO; GO:0016559; P:peroxisome fission; ISO:MGI.
DR GO; GO:0016557; P:peroxisome membrane biogenesis; ISO:MGI.
DR GO; GO:0007031; P:peroxisome organization; ISO:MGI.
DR GO; GO:0045046; P:protein import into peroxisome membrane; ISO:MGI.
DR GO; GO:0050821; P:protein stabilization; ISO:MGI.
DR GO; GO:0006625; P:protein targeting to peroxisome; ISO:MGI.
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 Acetylation; Alternative splicing; Cytoplasm; Direct protein sequencing;
KW Lipoprotein; Membrane; Methylation; Peroxisome; Peroxisome biogenesis;
KW Phosphoprotein; Prenylation; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P40855"
FT CHAIN 2..296
FT /note="Peroxisomal biogenesis factor 19"
FT /id="PRO_0000218760"
FT PROPEP 297..299
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000396701"
FT REGION 1..61
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 /evidence="ECO:0000250"
FT REGION 2..56
FT /note="Docking to the peroxisome membrane and binding to
FT PEX3"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P40855"
FT MOD_RES 35
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYU1"
FT MOD_RES 236
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 296
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 296
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 25..116
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_012652"
FT CONFLICT 31
FT /note="K -> E (in Ref. 2; BAB28468)"
FT /evidence="ECO:0000305"
FT CONFLICT 55
FT /note="P -> S (in Ref. 1; CAA70255/CAA70256 and 3;
FT AAH12517)"
FT /evidence="ECO:0000305"
FT CONFLICT 110
FT /note="E -> K (in Ref. 2; BAB28468)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 299 AA; 32733 MW; 530A3A0C29370E51 CRC64;
MAAAEEGCGV GVEDDRELEE LLESALDDFD KAKPSPEHAP TISAPDASGP QKRAPGDTAK
DALFASQEKF FQELFDSELA SQATAEFEKA MKELAEEEPH LVEQFQKLSE AAGRVGSDAS
SQQEFTSCLK ETLSGLAKNA TELQNSGMSE EELMKAMEGL GMDEGDGEAS ILPIMQSIMQ
NLLSKDVLYP SLKEITEKYP EWLQSHQDST PPEQFEKYQQ QHSVMVKICE QFEAETPTDS
EATQRARFEA MLDLMQQLQA LGHPPKELAG EMPPGLNFDL DALNLSGPPG ANGEQCLIM
