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Peroxisome assembly protein 12 (Peroxin-12) (Peroxisome assembly factor 3) (PAF-3)

 PEX12_HUMAN             Reviewed;         359 AA.
O00623; B2R6M2;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
01-JUL-1997, sequence version 1.
27-SEP-2017, entry version 151.
RecName: Full=Peroxisome assembly protein 12;
AltName: Full=Peroxin-12;
AltName: Full=Peroxisome assembly factor 3;
Short=PAF-3;
Name=PEX12; Synonyms=PAF3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND INVOLVEMENT IN PBD3A.
TISSUE=Fetal brain;
PubMed=9090384; DOI=10.1038/ng0497-385;
Chang C.-C., Lee W.-H., Moser H., Valle D., Gould S.J.;
"Isolation of the human PEX12 gene, mutated in group 3 of the
peroxisome biogenesis disorders.";
Nat. Genet. 15:385-388(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=9632816; DOI=10.1128/MCB.18.7.4324;
Okumoto K., Shimozawa N., Kawai A., Tamura S., Tsukamoto T., Osumi T.,
Moser H., Wanders R.J.A., Suzuki Y., Kondo N., Fujiki Y.;
"PEX12, the pathogenic gene of group III Zellweger syndrome: cDNA
cloning by functional complementation on a CHO cell mutant, patient
analysis, and characterization of PEX12p.";
Mol. Cell. Biol. 18:4324-4336(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
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.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Testis;
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).
[6]
INTERACTION WITH PEX19.
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).
[7]
INTERACTION WITH PEX19, AND MUTAGENESIS OF CYS-304 AND CYS-307.
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).
[8]
VARIANT PBD3B PHE-320, CHARACTERIZATION OF VARIANT PBD3B PHE-320, AND
INTERACTION WITH PEX5 AND PEX10.
PubMed=10562279; DOI=10.1083/jcb.147.4.761;
Chang C.C., Warren D.S., Sacksteder K.A., Gould S.J.;
"PEX12 interacts with PEX5 and PEX10 and acts downstream of receptor
docking in peroxisomal matrix protein import.";
J. Cell Biol. 147:761-774(1999).
[9]
VARIANTS PBD-CG3 SER-34; GLN-178 DEL AND GLN-349 DEL, VARIANT PBD3B
PHE-320, AND VARIANT ILE-245.
PubMed=19105186; DOI=10.1002/humu.20932;
Yik W.Y., Steinberg S.J., Moser A.B., Moser H.W., Hacia J.G.;
"Identification of novel mutations and sequence variation in the
Zellweger syndrome spectrum of peroxisome biogenesis disorders.";
Hum. Mutat. 30:E467-E480(2009).
-!- FUNCTION: Required for protein import into peroxisomes.
{ECO:0000269|PubMed:9632816}.
-!- SUBUNIT: Interacts with PEX5 and PEX10. Interacts with PEX19 via
its cytoplasmic domain. {ECO:0000269|PubMed:10562279,
ECO:0000269|PubMed:10704444, ECO:0000269|PubMed:11390669}.
-!- INTERACTION:
P40855:PEX19; NbExp=2; IntAct=EBI-594836, EBI-594747;
P50542:PEX5; NbExp=4; IntAct=EBI-594836, EBI-597835;
-!- SUBCELLULAR LOCATION: Peroxisome membrane
{ECO:0000269|PubMed:9632816}; Multi-pass membrane protein
{ECO:0000269|PubMed:9632816}.
-!- DISEASE: Peroxisome biogenesis disorder complementation group 3
(PBD-CG3) [MIM:614859]: 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:19105186}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Peroxisome biogenesis disorder 3A (PBD3A) [MIM:614859]: 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:9090384}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Peroxisome biogenesis disorder 3B (PBD3B) [MIM:266510]: A
peroxisome biogenesis disorder that includes neonatal
adrenoleukodystrophy (NALD) and infantile Refsum disease (IRD),
two milder manifestations of the Zellweger disease spectrum. The
clinical course of patients with the NALD and IRD presentation is
variable and may include developmental delay, hypotonia, liver
dysfunction, sensorineural hearing loss, retinal dystrophy and
vision impairment. Children with the NALD presentation may reach
their teens, while patients with the IRD presentation may reach
adulthood. The clinical conditions are often slowly progressive in
particular with respect to loss of hearing and vision. The
biochemical abnormalities include accumulation of phytanic acid,
very long chain fatty acids (VLCFA), di- and
trihydroxycholestanoic acid and pipecolic acid. Note=The disease
is caused by mutations affecting the gene represented in this
entry. {ECO:0000269|PubMed:10562279, ECO:0000269|PubMed:19105186}.
-!- SIMILARITY: Belongs to the pex2/pex10/pex12 family. {ECO:0000305}.
-!- WEB RESOURCE: Name=dbPEX, PEX Gene Database;
URL="http://www.dbpex.org/home.php?select_db=PEX12";
-----------------------------------------------------------------------
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EMBL; U91521; AAC68812.1; -; mRNA.
EMBL; U91522; AAC68813.1; -; Genomic_DNA.
EMBL; AB004546; BAA31559.1; -; mRNA.
EMBL; AK312635; BAG35519.1; -; mRNA.
EMBL; CH471147; EAW80143.1; -; Genomic_DNA.
EMBL; BC031085; AAH31085.1; -; mRNA.
CCDS; CCDS11296.1; -.
RefSeq; NP_000277.1; NM_000286.2.
UniGene; Hs.591190; -.
ProteinModelPortal; O00623; -.
BioGrid; 111216; 4.
IntAct; O00623; 3.
MINT; MINT-241654; -.
STRING; 9606.ENSP00000225873; -.
TCDB; 3.A.20.1.1; the peroxisomal protein importer (ppi) family.
iPTMnet; O00623; -.
PhosphoSitePlus; O00623; -.
BioMuta; PEX12; -.
EPD; O00623; -.
MaxQB; O00623; -.
PaxDb; O00623; -.
PeptideAtlas; O00623; -.
PRIDE; O00623; -.
DNASU; 5193; -.
Ensembl; ENST00000225873; ENSP00000225873; ENSG00000108733.
Ensembl; ENST00000613219; ENSP00000482609; ENSG00000108733.
GeneID; 5193; -.
KEGG; hsa:5193; -.
UCSC; uc002hjp.4; human.
CTD; 5193; -.
DisGeNET; 5193; -.
EuPathDB; HostDB:ENSG00000108733.9; -.
GeneCards; PEX12; -.
GeneReviews; PEX12; -.
HGNC; HGNC:8854; PEX12.
HPA; HPA069386; -.
MalaCards; PEX12; -.
MIM; 266510; phenotype.
MIM; 601758; gene.
MIM; 614859; phenotype.
neXtProt; NX_O00623; -.
OpenTargets; ENSG00000108733; -.
Orphanet; 772; Infantile Refsum disease.
Orphanet; 44; Neonatal adrenoleukodystrophy.
Orphanet; 912; Zellweger syndrome.
PharmGKB; PA33196; -.
eggNOG; KOG0826; Eukaryota.
eggNOG; ENOG410Y4Q2; LUCA.
GeneTree; ENSGT00390000016209; -.
HOGENOM; HOG000038427; -.
HOVERGEN; HBG053569; -.
InParanoid; O00623; -.
KO; K13345; -.
OMA; WWYSSEN; -.
OrthoDB; EOG091G0BN4; -.
PhylomeDB; O00623; -.
TreeFam; TF314511; -.
Reactome; R-HSA-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
SIGNOR; O00623; -.
GeneWiki; PEX12; -.
GenomeRNAi; 5193; -.
PRO; PR:O00623; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000108733; -.
CleanEx; HS_PEX12; -.
ExpressionAtlas; O00623; baseline and differential.
Genevisible; O00623; HS.
GO; GO:0005779; C:integral component of peroxisomal membrane; IDA:UniProtKB.
GO; GO:1990429; C:peroxisomal importomer complex; IBA:GO_Central.
GO; GO:0005778; C:peroxisomal membrane; IDA:UniProtKB.
GO; GO:0005777; C:peroxisome; IDA:MGI.
GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IBA:GO_Central.
GO; GO:0008270; F:zinc ion binding; IMP:UniProtKB.
GO; GO:0007031; P:peroxisome organization; IMP:UniProtKB.
GO; GO:0016558; P:protein import into peroxisome matrix; IMP:UniProtKB.
GO; GO:0006513; P:protein monoubiquitination; IBA:GO_Central.
GO; GO:0006625; P:protein targeting to peroxisome; NAS:UniProtKB.
GO; GO:0016567; P:protein ubiquitination; TAS:Reactome.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR017375; PEX12.
InterPro; IPR006845; Pex_N.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
PANTHER; PTHR12888; PTHR12888; 1.
Pfam; PF04757; Pex2_Pex12; 1.
PIRSF; PIRSF038074; Peroxisome_assembly_p12; 1.
1: Evidence at protein level;
Complete proteome; Disease mutation; Membrane; Metal-binding;
Peroxisome; Peroxisome biogenesis disorder; Polymorphism;
Reference proteome; Transmembrane; Transmembrane helix;
Zellweger syndrome; Zinc; Zinc-finger.
CHAIN 1 359 Peroxisome assembly protein 12.
/FTId=PRO_0000218610.
TOPO_DOM 1 158 Cytoplasmic. {ECO:0000255}.
TRANSMEM 159 179 Helical. {ECO:0000255}.
TOPO_DOM 180 239 Peroxisomal matrix. {ECO:0000255}.
TRANSMEM 240 260 Helical. {ECO:0000255}.
TOPO_DOM 261 359 Cytoplasmic. {ECO:0000255}.
ZN_FING 304 343 RING-type; degenerate.
COMPBIAS 280 285 Poly-Pro.
VARIANT 34 34 R -> S (in PBD-CG3; dbSNP:rs147530802).
{ECO:0000269|PubMed:19105186}.
/FTId=VAR_058389.
VARIANT 178 178 Missing (in PBD-CG3).
{ECO:0000269|PubMed:19105186}.
/FTId=VAR_058390.
VARIANT 245 245 L -> I (in dbSNP:rs12941376).
{ECO:0000269|PubMed:19105186}.
/FTId=VAR_050495.
VARIANT 320 320 S -> F (in PBD3B; attenuates interaction
with PEX10 and decreases peroxisomal
protein import; dbSNP:rs28936697).
{ECO:0000269|PubMed:10562279,
ECO:0000269|PubMed:19105186}.
/FTId=VAR_031998.
VARIANT 349 349 Missing (in PBD-CG3).
{ECO:0000269|PubMed:19105186}.
/FTId=VAR_058391.
MUTAGEN 304 304 C->W: Abolishes interaction with PEX19;
when associated with Q-307.
{ECO:0000269|PubMed:11390669}.
MUTAGEN 307 307 C->Q: Abolishes interaction with PEX19;
when associated with W-304.
{ECO:0000269|PubMed:11390669}.
SEQUENCE 359 AA; 40797 MW; 1AF0BE6416422109 CRC64;
MAEHGAHFTA ASVADDQPSI FEVVAQDSLM TAVRPALQHV VKVLAESNPT HYGFLWRWFD
EIFTLLDLLL QQHYLSRTSA SFSENFYGLK RIVMGDTHKS QRLASAGLPK QQLWKSIMFL
VLLPYLKVKL EKLVSSLREE DEYSIHPPSS RWKRFYRAFL AAYPFVNMAW EGWFLVQQLR
YILGKAQHHS PLLRLAGVQL GRLTVQDIQA LEHKPAKASM MQQPARSVSE KINSALKKAV
GGVALSLSTG LSVGVFFLQF LDWWYSSENQ ETIKSLTALP TPPPPVHLDY NSDSPLLPKM
KTVCPLCRKT RVNDTVLATS GYVFCYRCVF HYVRSHQACP ITGYPTEVQH LIKLYSPEN


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