PMID- 10212238
OWN - NLM
STAT- MEDLINE
DCOM- 19990603
LR  - 20190508
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 18
DP  - 1999 Apr 30
TI  - The peroxin Pex14p. cDNA cloning by functional complementation on a Chinese
      hamster ovary cell mutant, characterization, and functional analysis.
PG  - 12593-604
AB  - Rat cDNA encoding a 376-amino acid peroxin was isolated by functional
      complementation of a peroxisome-deficient Chinese hamster ovary cell mutant,
      ZP110, of complementation group 14 (CG14). The primary sequence showed 28 and 24%
      amino acid identity with the yeast Pex14p from Hansenula polymorpha and
      Saccharomyces cerevisiae, respectively; therefore, we termed this cDNA rat PEX14 
      (RnPEX14). Human and Chinese hamster Pex14p showed 96 and 94% identity to rat
      Pex14p, except that both Pex14p comprised 377 amino acids. Pex14p was
      characterized as an integral membrane protein of peroxisomes, exposing its N- and
      C-terminal parts to the cytosol. Pex14p interacts with both Pex5p and Pex7p, the 
      receptors for peroxisome targeting signal type 1 (PTS1) and PTS2, respectively,
      together with the receptors' cargoes, PTS1 and PTS2 proteins. Mutation in PEX14
      from ZP161, the same CG as ZP110, was determined by reverse transcription-PCR as 
      follows. A 133-base pair deletion at nucleotide residues 37-169 in one allele
      created a termination codon at 40-42; in addition to this mutation, 103 base
      pairs were deleted at positions 385-487, resulting in the second termination
      immediately downstream the second deletion site in the other allele. Neither of
      these two mutant forms of Pex14p restored peroxisome biogenesis in ZP110 and
      ZP161, thereby demonstrating PEX14 to be responsible for peroxisome deficiency in
      CG14.
FAU - Shimizu, N
AU  - Shimizu N
AD  - Department of Biology, Kyushu University Faculty of Science, Fukuoka 812-8581,
      Japan.
FAU - Itoh, R
AU  - Itoh R
FAU - Hirono, Y
AU  - Hirono Y
FAU - Otera, H
AU  - Otera H
FAU - Ghaedi, K
AU  - Ghaedi K
FAU - Tateishi, K
AU  - Tateishi K
FAU - Tamura, S
AU  - Tamura S
FAU - Okumoto, K
AU  - Okumoto K
FAU - Harano, T
AU  - Harano T
FAU - Mukai, S
AU  - Mukai S
FAU - Fujiki, Y
AU  - Fujiki Y
LA  - eng
SI  - GENBANK/AB017544
SI  - GENBANK/AB017545
SI  - GENBANK/AB017546
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Carrier Proteins)
RN  - 0 (DNA, Complementary)
RN  - 0 (Fungal Proteins)
RN  - 0 (Membrane Proteins)
RN  - 0 (Membrane Transport Proteins)
RN  - 0 (PEX14 protein, S cerevisiae)
RN  - 0 (PEX14 protein, human)
RN  - 0 (Peroxins)
RN  - 0 (Pex14 protein, rat)
RN  - 0 (Recombinant Fusion Proteins)
RN  - 0 (Repressor Proteins)
RN  - 0 (Saccharomyces cerevisiae Proteins)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Base Sequence
MH  - Biological Transport
MH  - CHO Cells
MH  - *Carrier Proteins
MH  - Cloning, Molecular
MH  - Cricetinae
MH  - Cricetulus
MH  - DNA, Complementary
MH  - Fungal Proteins/chemistry/*genetics/metabolism
MH  - Genetic Complementation Test
MH  - Humans
MH  - Membrane Proteins/chemistry/*genetics/metabolism
MH  - Membrane Transport Proteins
MH  - Microbodies/metabolism
MH  - Molecular Sequence Data
MH  - Peroxins
MH  - Protein Binding
MH  - Rats
MH  - Recombinant Fusion Proteins/isolation & purification/metabolism
MH  - *Repressor Proteins
MH  - Saccharomyces cerevisiae Proteins
MH  - Sequence Homology, Amino Acid
EDAT- 1999/04/23 00:00
MHDA- 1999/04/23 00:01
CRDT- 1999/04/23 00:00
PHST- 1999/04/23 00:00 [pubmed]
PHST- 1999/04/23 00:01 [medline]
PHST- 1999/04/23 00:00 [entrez]
AID - 10.1074/jbc.274.18.12593 [doi]
PST - ppublish
SO  - J Biol Chem. 1999 Apr 30;274(18):12593-604. doi: 10.1074/jbc.274.18.12593.