Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-00031
Entry Name
UniProt Accession
Theoretical PI
5.5
Molecular Weight
117349.11
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Leucyl-cystinyl aminopeptidase, pregnancy serum form
Protein Synonyms/Alias
Cystinyl aminopeptidase; 3.4.11.3; Insulin-regulated membrane aminopeptidase; Insulin-responsive aminopeptidase; IRAP; Oxytocinase; OTase; Placental leucine aminopeptidase; P-LAP;
Gene Name
LNPEP
Gene Synonyms/Alias
OTASE;
Created Date
27-MAR-2002
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
134
Canonical
VIYLLPRCTFTKEGC
[1]
S-Palmitoylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Predicted from GPS-Lipid
Functional Description
Release of an N-terminal amino acid, cleaves before cysteine, leucine as well as other amino acids. Degrades peptide hormones such as oxytocin, vasopressin and angiotensin III, and plays a role in maintaining homeostasis during pregnancy. May be involved in the inactivation of neuronal peptides in the brain. Cleaves Met-enkephalin and dynorphin. Binds angiotensin IV and may be the angiotensin IV receptor in the brain.
Sequence Annotation
Topological domain: 1 110 Cytoplasmic.
Transmembrane: 111 131 Helical; Signal-anchor for type IImembrane protein.
Topological domain: 132 1025 Extracellular.
Region: 96 101 Tankyrase binding.
Region: 428 432 Substrate binding.
Motif: 53 54 Dileucine internalization motif.
Motif: 76 77 Dileucine internalization motif.
Active site: 465 465 Proton acceptor.
Metal binding site: 464 464 Zinc; catalytic.
Metal binding site: 468 468 Zinc; catalytic.
Metal binding site: 487 487 Zinc; catalytic.
Binding site: 295 295 Substrate.
Functional site: 154 155 Cleavage; to produce pregnancy serumform.
Functional site: 549 549 Transition state stabilizer.
Modified residue: 1 1 N-acetylmethionine.
Modified residue: 70 70 Phosphotyrosine.
Modified residue: 80 80 Phosphoserine.
Modified residue: 91 91 Phosphoserine.
Protein Length
1025 AA.
Protein Sequence
(Canonical)
MEPFTNDRLQ LPRNMIENSM FEEEPDVVDL AKEPCLHPLE PDEVEYEPRG SRLLVRGLGE  60
HEMEEDEEDY ESSAKLLGMS FMNRSSGLRN SATGYRQSPD GACSVPSART MVVCAFVIVV  120
AVSVIMVIYL LPRCTFTKEG CHKKNQSIGL IQPFATNGKL FPWAQIRLPT AVVPLRYELS  180
LHPNLTSMTF RGSVTISVQA LQVTWNIILH STGHNISRVT FMSAVSSQEK QAEILEYAYH  240
GQIAIVAPEA LLAGHNYTLK IEYSANISSS YYGFYGFSYT DESNEKKYFA ATQFEPLAAR  300
SAFPCFDEPA FKATFIIKII RDEQYTALSN MPKKSSVVLD DGLVQDEFSE SVKMSTYLVA  360
FIVGEMKNLS QDVNGTLVSI YAVPEKIGQV HYALETTVKL LEFFQNYFEI QYPLKKLDLV  420
AIPDFEAGAM ENWGLLTFRE ETLLYDSNTS SMADRKLVTK IIAHELAHQW FGNLVTMKWW  480
NDLWLNEGFA TFMEYFSLEK IFKELSSYED FLDARFKTMK KDSLNSSHPI SSSVQSSEQI  540
EEMFDSLSYF KGSSLLLMLK TYLSEDVFQH AVVLYLHNHS YASIQSDDLW DSFNEVTNQT  600
LDVKRMMKTW TLQKGFPLVT VQKKGKELFI QQERFFLNMK PEIQPSDTSY LWHIPLSYVT  660
EGRNYSKYQS VSLLDKKSGV INLTEEVLWV KVNINMNGYY IVHYADDDWE ALIHQLKINP  720
YVLSDKDRAN LINNIFELAG LGKVPLKRAF DLINYLGNEN HTAPITEALF QTDLIYNLLE  780
KLGYMDLASR LVTRVFKLLQ NQIQQQTWTD EGTPSMRELR SALLEFACTH NLGNCSTTAM  840
KLFDDWMASN GTQSLPTDVM TTVFKVGAKT DKGWSFLLGK YISIGSEAEK NKILEALASS  900
EDVRKLYWLM KSSLNGDNFR TQKLSFIIRT VGRHFPGHLL AWDFVKENWN KLVQKFPLGS  960
YTIQNIVAGS TYLFSTKTHL SEVQAFFENQ SEATFRLRCV QEALEVIQLN IQWMEKNLKS  1020
LTWWL                                                              1025
FASTA
(Canonical)
>LipidDB-9606-00031|Q9UIQ6
MEPFTNDRLQLPRNMIENSMFEEEPDVVDLAKEPCLHPLEPDEVEYEPRGSRLLVRGLGE
HEMEEDEEDYESSAKLLGMSFMNRSSGLRNSATGYRQSPDGACSVPSARTMVVCAFVIVV
AVSVIMVIYLLPRCTFTKEGCHKKNQSIGLIQPFATNGKLFPWAQIRLPTAVVPLRYELS
LHPNLTSMTFRGSVTISVQALQVTWNIILHSTGHNISRVTFMSAVSSQEKQAEILEYAYH
GQIAIVAPEALLAGHNYTLKIEYSANISSSYYGFYGFSYTDESNEKKYFAATQFEPLAAR
SAFPCFDEPAFKATFIIKIIRDEQYTALSNMPKKSSVVLDDGLVQDEFSESVKMSTYLVA
FIVGEMKNLSQDVNGTLVSIYAVPEKIGQVHYALETTVKLLEFFQNYFEIQYPLKKLDLV
AIPDFEAGAMENWGLLTFREETLLYDSNTSSMADRKLVTKIIAHELAHQWFGNLVTMKWW
NDLWLNEGFATFMEYFSLEKIFKELSSYEDFLDARFKTMKKDSLNSSHPISSSVQSSEQI
EEMFDSLSYFKGSSLLLMLKTYLSEDVFQHAVVLYLHNHSYASIQSDDLWDSFNEVTNQT
LDVKRMMKTWTLQKGFPLVTVQKKGKELFIQQERFFLNMKPEIQPSDTSYLWHIPLSYVT
EGRNYSKYQSVSLLDKKSGVINLTEEVLWVKVNINMNGYYIVHYADDDWEALIHQLKINP
YVLSDKDRANLINNIFELAGLGKVPLKRAFDLINYLGNENHTAPITEALFQTDLIYNLLE
KLGYMDLASRLVTRVFKLLQNQIQQQTWTDEGTPSMRELRSALLEFACTHNLGNCSTTAM
KLFDDWMASNGTQSLPTDVMTTVFKVGAKTDKGWSFLLGKYISIGSEAEKNKILEALASS
EDVRKLYWLMKSSLNGDNFRTQKLSFIIRTVGRHFPGHLLAWDFVKENWNKLVQKFPLGS
YTIQNIVAGSTYLFSTKTHLSEVQAFFENQSEATFRLRCVQEALEVIQLNIQWMEKNLKS
LTWWL
Gene Ontology
GO:0030659; C:cytoplasmic vesicle membrane; TAS:Reactome
GO:0005829; C:cytosol; TAS:Reactome
GO:0031905; C:early endosome lumen; TAS:Reactome
GO:0005576; C:extracellular region; IEA:UniProtKB-KW
GO:0005887; C:integral component of plasma membrane; TAS:ProtInc
GO:0005622; C:intracellular; IDA:HGNC
GO:0005765; C:lysosomal membrane; IDA:UniProtKB
GO:0016020; C:membrane; IDA:UniProtKB
GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl
GO:0005886; C:plasma membrane; TAS:ProtInc
GO:0004177; F:aminopeptidase activity; TAS:HGNC
GO:0008237; F:metallopeptidase activity; TAS:ProtInc
GO:0008270; F:zinc ion binding; TAS:ProtInc
GO:0042590; P:antigen processing and presentation of exogenous peptide antigen via MHC class I; TAS:Reactome
GO:0002480; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-independent; TAS:Reactome
GO:0002474; P:antigen processing and presentation of peptide antigen via MHC class I; TAS:Reactome
GO:0007267; P:cell-cell signaling; TAS:ProtInc
GO:0007565; P:female pregnancy; TAS:ProtInc
GO:0061024; P:membrane organization; TAS:Reactome
GO:0030163; P:protein catabolic process; IEA:Ensembl
GO:0000209; P:protein polyubiquitination; TAS:Reactome
GO:0006508; P:proteolysis; TAS:ProtInc
Interpro
InterPro; IPR024571; ERAP1-like_C_dom
InterPro; IPR001930; Peptidase_M1
InterPro; IPR014782; Peptidase_M1_N
Pfam
Pfam; PF11838; ERAP1_C;
Pfam; PF01433; Peptidase_M1;
SMART
PROSITE
PROSITE; PS00142; ZINC_PROTEASE;
PRINTS
PRINTS; PR00756; ALADIPTASE;