CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-011735
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Leukotriene A-4 hydrolase homolog 
Protein Synonyms/Alias
 LTA-4 hydrolase; Leucine aminopeptidase 2; Leukotriene A(4) hydrolase 
Gene Name
 LAP2 
Gene Synonyms/Alias
 YNL045W; N2535 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
178SKQTKGGKPYVFSQLacetylation[1]
228IRIEDTSKDTNIYRFubiquitination[2]
Reference
 [1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919]
 [2] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, Villén J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301] 
Functional Description
 Aminopeptidase that preferentially cleaves tripeptides. Also has low epoxide hydrolase activity (in vitro). Can hydrolyze an epoxide moiety of LTA(4) to form LTB(4) (in vitro). 
Sequence Annotation
 REGION 184 186 Substrate binding.
 REGION 311 316 Substrate binding.
 ACT_SITE 341 341 Proton acceptor.
 ACT_SITE 429 429 Proton donor.
 METAL 340 340 Zinc; catalytic.
 METAL 344 344 Zinc; catalytic.
 METAL 363 363 Zinc; catalytic.  
Keyword
 3D-structure; Complete proteome; Cytoplasm; Hydrolase; Leukotriene biosynthesis; Metal-binding; Metalloprotease; Nucleus; Protease; Reference proteome; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 671 AA 
Protein Sequence
MFLLPFVIRH SSSIYLPTLR FRGLLTVISR NIHISTPHKM LPLSIEQRRP SRSPEYDQST 60
LSNYKDFAVL HTDLNLSVSF EKSAISGSVT FQLKKLHEGK NKSDELHLDT SYLDVQEVHI 120
DGSKADFQIE QRKEPLGSRL VINNASCNDN FTLNIQFRTT DKCTALQWLN SKQTKGGKPY 180
VFSQLEAIHA RSLFPCFDTP SVKSTFTASI ESPLPVVFSG IRIEDTSKDT NIYRFEQKVP 240
IPAYLIGIAS GDLSSAPIGP RSTVYTEPFR LKDCQWEFEN DVEKFIQTAE KIIFEYEWGT 300
YDILVNVDSY PYGGMESPNM TFATPTLIAH DRSNIDVIAH ELAHSWSGNL VTNCSWNHFW 360
LNEGWTVYLE RRIIGAIHGE PTRHFSALIG WSDLQNSIDS MKDPERFSTL VQNLNDNTDP 420
DDAFSTVPYE KGFNLLFHLE TILGGKAEFD PFIRHYFKKF AKKSLDTFQF LDTLYEFYPE 480
KKEILDSVDW ETWLYKPGMP PRPHFITALA DNVYQLADKW VEMAQHLKTT EDFRSEFNAI 540
DIKDFNSNQL VLFLETLTQN GHSNKKPKDF DWAKFPVASR ALLDIYQDNI VKSQNAEVVF 600
KMFKFQIFAK LQEEYKHLAD WLGTVGRMKF VRPGYRLLNS VDRRLALATF DKFKDTYHPI 660
CKALVKQDLG L 671 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:SGD.
 GO:0005634; C:nucleus; IDA:SGD.
 GO:0004177; F:aminopeptidase activity; IDA:SGD.
 GO:0004301; F:epoxide hydrolase activity; IDA:SGD.
 GO:0004463; F:leukotriene-A4 hydrolase activity; ISS:SGD.
 GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
 GO:0008270; F:zinc ion binding; ISS:UniProtKB.
 GO:0044255; P:cellular lipid metabolic process; IDA:SGD.
 GO:0019370; P:leukotriene biosynthetic process; IEA:UniProtKB-KW.
 GO:0043171; P:peptide catabolic process; ISS:UniProtKB.
 GO:0030163; P:protein catabolic process; IDA:SGD.
 GO:0006508; P:proteolysis; IEA:UniProtKB-KW. 
Interpro
 IPR016024; ARM-type_fold.
 IPR012777; Leukotriene_A4_hydrolase.
 IPR001930; Peptidase_M1.
 IPR015211; Peptidase_M1_C.
 IPR014782; Peptidase_M1_N. 
Pfam
 PF09127; Leuk-A4-hydro_C
 PF01433; Peptidase_M1 
SMART
  
PROSITE
 PS00142; ZINC_PROTEASE 
PRINTS
 PR00756; ALADIPTASE.