Gene/Proteome Database (LMPD)
Proteins
| Lap2p | |
|---|---|
| Refseq ID | NP_014353 |
| Protein GI | 6324283 |
| UniProt ID | Q10740 |
| mRNA ID | NM_001182884 |
| Length | 671 |
| RefSeq Status | PROVISIONAL |
| MFLLPFVIRHSSSIYLPTLRFRGLLTVISRNIHISTPHKMLPLSIEQRRPSRSPEYDQSTLSNYKDFAVLHTDLNLSVSFEKSAISGSVTFQLKKLHEGKNKSDELHLDTSYLDVQEVHIDGSKADFQIEQRKEPLGSRLVINNASCNDNFTLNIQFRTTDKCTALQWLNSKQTKGGKPYVFSQLEAIHARSLFPCFDTPSVKSTFTASIESPLPVVFSGIRIEDTSKDTNIYRFEQKVPIPAYLIGIASGDLSSAPIGPRSTVYTEPFRLKDCQWEFENDVEKFIQTAEKIIFEYEWGTYDILVNVDSYPYGGMESPNMTFATPTLIAHDRSNIDVIAHELAHSWSGNLVTNCSWNHFWLNEGWTVYLERRIIGAIHGEPTRHFSALIGWSDLQNSIDSMKDPERFSTLVQNLNDNTDPDDAFSTVPYEKGFNLLFHLETILGGKAEFDPFIRHYFKKFAKKSLDTFQFLDTLYEFYPEKKEILDSVDWETWLYKPGMPPRPHFITALADNVYQLADKWVEMAQHLKTTEDFRSEFNAIDIKDFNSNQLVLFLETLTQNGHSNKKPKDFDWAKFPVASRALLDIYQDNIVKSQNAEVVFKMFKFQIFAKLQEEYKHLADWLGTVGRMKFVRPGYRLLNSVDRRLALATFDKFKDTYHPICKALVKQDLGL | |
Gene Information
Gene Ontology (GO Annotations)
| GO ID | Source | Type | Description |
|---|---|---|---|
| GO:0005737 | IEA:UniProtKB-KW | C | cytoplasm |
| GO:0005634 | IEA:UniProtKB-KW | C | nucleus |
| GO:0004177 | IDA:SGD | F | aminopeptidase activity |
| GO:0004301 | IDA:SGD | F | epoxide hydrolase activity |
| GO:0004463 | ISS:SGD | F | leukotriene-A4 hydrolase activity |
| GO:0008237 | IEA:UniProtKB-KW | F | metallopeptidase activity |
| GO:0008270 | ISS:UniProtKB | F | zinc ion binding |
| GO:0044255 | IDA:SGD | P | cellular lipid metabolic process |
| GO:0019370 | IEA:UniProtKB-KW | P | leukotriene biosynthetic process |
| GO:0043171 | ISS:UniProtKB | P | peptide catabolic process |
| GO:0030163 | IDA:SGD | P | protein catabolic process |
KEGG Pathway Links
REACTOME Pathway Links
Domain Information
InterPro Annotations
| Accession | Description |
|---|---|
| IPR016024 | Armadillo-type fold |
| IPR012777 | Leukotriene A4 hydrolase |
| IPR001930 | Peptidase M1, alanine aminopeptidase/leukotriene A4 hydrolase |
| IPR015211 | Peptidase M1, leukotriene A4 hydrolase, aminopeptidase C-terminal |
| IPR014782 | Peptidase M1, membrane alanine aminopeptidase, N-terminal |
UniProt Annotations
Entry Information
Comments
| Comment Type | Description |
|---|---|
| Biophysicochemical Properties | Kinetic parameters: KM=1.5 mM for Leu-p-nitroanilide {ECO:0000269|PubMed:10574934, ECO:0000269|PubMed:11601994, ECO:0000269|PubMed:16597475}; KM=1.8 mM for Met-p-nitroanilide {ECO:0000269|PubMed:10574934, ECO:0000269|PubMed:11601994, ECO:0000269|PubMed:16597475}; KM=2.0 mM for Ala-p-nitroanilide {ECO:0000269|PubMed:10574934, ECO:0000269|PubMed:11601994, ECO:0000269|PubMed:16597475}; Vmax=520 nmol/min/mg enzyme with Leu-p-nitroanilide as substrate {ECO:0000269|PubMed:10574934, ECO:0000269|PubMed:11601994, ECO:0000269|PubMed:16597475}; Vmax=360 nmol/min/mg enzyme with Met-p-nitroanilide as substrate {ECO:0000269|PubMed:10574934, ECO:0000269|PubMed:11601994, ECO:0000269|PubMed:16597475}; Vmax=170 nmol/min/mg enzyme with Ala-p-nitroanilide as substrate {ECO:0000269|PubMed:10574934, ECO:0000269|PubMed:11601994, ECO:0000269|PubMed:16597475}; pH dependence: Optimum pH is about 7.3. {ECO:0000269|PubMed:10574934, ECO:0000269|PubMed:11601994, ECO:0000269|PubMed:16597475}; |
| Catalytic Activity | (7E,9E,11Z,14Z)-(5S,6S)-5,6-epoxyicosa- 7,9,11,14-tetraenoate + H(2)O = (6Z,8E,10E,14Z)-(5S,12R)-5,12- dihydroxyicosa-6,8,10,14-tetraenoate. {ECO:0000269|PubMed:21146536}. |
| Cofactor | Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:21146536}; Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:21146536}; |
| Enzyme Regulation | Inhibited 3-(4-benzyloxyphenyl)-2-(R)-amino-1- propanethiol (thioamine) and N-hydroxy-N-(2-(S)-amino-3-(4- benzyloxyphenyl)propyl)-5-carboxypen-tanamide (hydroxamic acid). The aminopeptidase activity is stimulated by LTA(4). {ECO:0000269|PubMed:10574934, ECO:0000269|PubMed:16024909}. |
| Function | 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). {ECO:0000269|PubMed:10574934, ECO:0000269|PubMed:11601994, ECO:0000269|PubMed:16024909, ECO:0000269|PubMed:16597475, ECO:0000269|PubMed:21146536}. |
| Miscellaneous | Present with 5590 molecules/cell in log phase SD medium. {ECO:0000269|PubMed:14562106}. |
| Pathway | Lipid metabolism; leukotriene B4 biosynthesis. |
| Similarity | Belongs to the peptidase M1 family. {ECO:0000305}. |
| Subcellular Location | Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}. |
Identical and Related Proteins
Unique RefSeq proteins for LMP007272 (as displayed in Record Overview)
Identical Sequences to LMP007272 proteins
| Reference | Database | Accession | Length | Protein Name |
|---|---|---|---|---|
| GI:6324283 | DBBJ | GAA26050.1 | 671 | K7_Ynl045wp [Saccharomyces cerevisiae Kyokai no. 7] |
| GI:6324283 | GenBank | EDN62765.1 | 671 | conserved protein [Saccharomyces cerevisiae YJM789] |
| GI:6324283 | GenBank | ABZ28049.1 | 671 | Sequence 1987 from patent US 7314974 |
| GI:6324283 | GenBank | EIW08047.1 | 671 | Lap2p [Saccharomyces cerevisiae CEN.PK113-7D] |
| GI:6324283 | SwissProt | A6ZS33.1 | 671 | RecName: Full=Leukotriene A-4 hydrolase homolog; Short=LTA-4 hydrolase; AltName: Full=Leukotriene A(4) hydrolase [Saccharomyces cerevisiae YJM789] |
| GI:6324283 | Third Party Genbank | DAA10500.1 | 671 | TPA: Lap2p [Saccharomyces cerevisiae S288c] |
Related Sequences to LMP007272 proteins
| Reference | Database | Accession | Length | Protein Name |
|---|---|---|---|---|
| GI:6324283 | EMBL | CAY82556.1 | 671 | EC1118_1N9_3268p [Saccharomyces cerevisiae EC1118] |
| GI:6324283 | GenBank | EDV12302.1 | 671 | hypothetical protein SCRG_03182 [Saccharomyces cerevisiae RM11-1a] |
| GI:6324283 | GenBank | EEU08214.1 | 671 | YNL045W-like protein [Saccharomyces cerevisiae JAY291] |
| GI:6324283 | GenBank | EWG83793.1 | 671 | hypothetical protein R008_N11721 [Saccharomyces cerevisiae R008] |
| GI:6324283 | GenBank | EWG93842.1 | 671 | hypothetical protein R103_N21191 [Saccharomyces cerevisiae R103] |
| GI:6324283 | GenBank | EWH16206.1 | 671 | hypothetical protein P283_N20421 [Saccharomyces cerevisiae P283] |