Any feedback?
Please rate this page
(sequences.php)
(0/150)

BRENDA support

Sequence of LYPA1_RAT

EC Number:3.1.2.22

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
palmitoyl[protein] hydrolase
P70470
Rattus norvegicus
230
24709
Reaction
palmitoyl[protein] + H2O = palmitate + protein
Other sequences found for EC No. 3.1.2.22

General information:

Sequence
show sequence in fasta format
  0 MCGNNMSAPM PAVVPAARKA TAAVIFLHGL GDTGHGWAEA FAGIKSSHIK YICPHAPVMP
 60 VTLNMSMMMP SWFDIIGLSP DSQEDESGIK QAAETVKALI DQEVKNGIPS NRIILGGFSQ
120 GGALSLYTAL TTQQKLAGVT ALSCWLPLRA SFSQGPINSA NRDISVLQCH GDCDPLVPLM
180 FGSLTVERLK GLVNPANVTF KVYEGMMHSS CQQEMMDVKY FIDKLLPPID
Download this sequence
in fasta format
Download all sequences for 3.1.2.22
in fasta format
in csv (Excel, OpenOffice) format
Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
439409
Sugimoto H.,Hayashi H.,Yamashita S.
Purification, cDNA cloning, and regulation of lysophospholipase from rat liver.
J. Biol. Chem.
271
7705-7711
1996
439410
Portilla D.,Crew M.D.,Grant D.,Serrero G.,Bates L.M.,Dai G.,Sasner M.,Cheng J.,Buonanno A.
cDNA cloning and expression of a novel family of enzymes with calcium-independent phospholipase A2 and lysophospholipase activities.
J. Am. Soc. Nephrol.
9
1178-1186
1998
439411
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Genome Res.
14
2121-2127
2004
439412
Duncan J.A.,Gilman A.G.
A cytoplasmic acyl-protein thioesterase that removes palmitate from G protein alpha subunits and p21(RAS).
J. Biol. Chem.
273
15830-15837
1998