Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-10090-00902
Entry Name
UniProt Accession
Theoretical PI
5.62
Molecular Weight
117303.86
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Leucyl-cystinyl aminopeptidase
Protein Synonyms/Alias
Cystinyl aminopeptidase; 3.4.11.3; Oxytocinase; OTase;
Gene Name
Lnpep
Gene Synonyms/Alias
Created Date
20-FEB-2007
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
134
Canonical
VIYLLPRCTFTKEGC
[1]
S-Palmitoylation
Organism
Mus musculus (Mouse)
NCBI Taxa ID
10090
Reference
[1] Predicted from GPS-Lipid
Functional Description
Release of an N-terminal amino acid, cleave 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 (By similarity).
Sequence Annotation
Topological domain: 1 109 Cytoplasmic.
Transmembrane: 110 131 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: 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)
MESFTNDRLQ LPRNMIENSM FEEEPDVVDL AKEPCLHPLE PDEVEYEPRG SRLLVRGLGE  60
HEMDEDEEDY ESSAKLLGMS FMNRSSGLRN SAAGYRQSPD GTCSLPSART LVICVFVIVV  120
AVSVIMVIYL LPRCTFTKEG CHKTNQSAEL IQPVATNGKV FPWAQIRLPT AIIPLCYELS  180
LHPNLTSMTF RGSVTISLQA LQDTRDIILH STGHNISRVT FMSAVSSQEK QVEILEYPYH  240
EQIAVVAPEP LLTGHNYTLK IEYSANISNS YYGFYGITYT DKSNEKKYFA ATQFEPLAAR  300
SAFPCFDEPA FKATFIIKIT RNEHHTALSN MPKKSSVPAE EGLIQDEFSE SVKMSTYLVA  360
FIVGEMRNLS QDVNGTLVSV YAVPEKIGQV HHALDTTIKL LEFYQTYFEI QYPLKKLDLV  420
AIPDFEAGAM ENWGLLTFRE ETLLYDNATS SVADRKLVTK IIAHELAHQW FGNLVTMQWW  480
NDLWLNEGFA TFMEYFSVEK IFKELNSYED FLDARFKTMR KDSLNSSHPI SSSVQSSEQI  540
EEMFDSLSYF KGASLLLMLK SYLSEDVFRH AVILYLHNHS YAAIQSDDLW DSFNEVTDKT  600
LDVKKMMKTW TLQKGFPLVT VQRKGTELLL QQERFFLRMQ PESQPSDTSH LWHIPISYVT  660
DGRNYSEYRS VSLLDKKSDV INLTEQVQWV KVNSNMTGYY IVHYAHDDWT ALINQLKRNP  720
YVLSDKDRAN LINNIFELAG LGKVPLRMAF DLIDYLKNET HTAPITEALF QTNLIYNLLE  780
KLGHMDLSSR LVARVHKLLQ NQIQQQTWTD EGTPSMRELR SALLEFACAH SLENCTTMAT  840
NLFDSWMASN GTQSLPTDVM VTVFKVGART EKGWLFLFSM YSSMGSEAEK NKILEALASS  900
EDVHKLYWLM KSSLDGDIIR TQKLSLIIRT VGRHFPGHLL AWDFVKENWN KLVHKFHLGS  960
YTIQSIVAGS THLFSTKTHL SEVQAFFENQ SEATLKLRCV QEALEVIQLN IQWMVRNLKT  1020
LSQWL                                                              1025
FASTA
(Canonical)
>LipidDB-10090-00902|Q8C129
MESFTNDRLQLPRNMIENSMFEEEPDVVDLAKEPCLHPLEPDEVEYEPRGSRLLVRGLGE
HEMDEDEEDYESSAKLLGMSFMNRSSGLRNSAAGYRQSPDGTCSLPSARTLVICVFVIVV
AVSVIMVIYLLPRCTFTKEGCHKTNQSAELIQPVATNGKVFPWAQIRLPTAIIPLCYELS
LHPNLTSMTFRGSVTISLQALQDTRDIILHSTGHNISRVTFMSAVSSQEKQVEILEYPYH
EQIAVVAPEPLLTGHNYTLKIEYSANISNSYYGFYGITYTDKSNEKKYFAATQFEPLAAR
SAFPCFDEPAFKATFIIKITRNEHHTALSNMPKKSSVPAEEGLIQDEFSESVKMSTYLVA
FIVGEMRNLSQDVNGTLVSVYAVPEKIGQVHHALDTTIKLLEFYQTYFEIQYPLKKLDLV
AIPDFEAGAMENWGLLTFREETLLYDNATSSVADRKLVTKIIAHELAHQWFGNLVTMQWW
NDLWLNEGFATFMEYFSVEKIFKELNSYEDFLDARFKTMRKDSLNSSHPISSSVQSSEQI
EEMFDSLSYFKGASLLLMLKSYLSEDVFRHAVILYLHNHSYAAIQSDDLWDSFNEVTDKT
LDVKKMMKTWTLQKGFPLVTVQRKGTELLLQQERFFLRMQPESQPSDTSHLWHIPISYVT
DGRNYSEYRSVSLLDKKSDVINLTEQVQWVKVNSNMTGYYIVHYAHDDWTALINQLKRNP
YVLSDKDRANLINNIFELAGLGKVPLRMAFDLIDYLKNETHTAPITEALFQTNLIYNLLE
KLGHMDLSSRLVARVHKLLQNQIQQQTWTDEGTPSMRELRSALLEFACAHSLENCTTMAT
NLFDSWMASNGTQSLPTDVMVTVFKVGARTEKGWLFLFSMYSSMGSEAEKNKILEALASS
EDVHKLYWLMKSSLDGDIIRTQKLSLIIRTVGRHFPGHLLAWDFVKENWNKLVHKFHLGS
YTIQSIVAGSTHLFSTKTHLSEVQAFFENQSEATLKLRCVQEALEVIQLNIQWMVRNLKT
LSQWL
Gene Ontology
GO:0030659; C:cytoplasmic vesicle membrane; TAS:Reactome
GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW
GO:0005765; C:lysosomal membrane; IEA:Ensembl
GO:0016020; C:membrane; IMP:MGI
GO:0048471; C:perinuclear region of cytoplasm; IDA:MGI
GO:0005886; C:plasma membrane; IDA:MGI
GO:0004177; F:aminopeptidase activity; IMP:MGI
GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW
GO:0008270; F:zinc ion binding; IEA:InterPro
GO:0030163; P:protein catabolic process; IMP:MGI
GO:0060395; P:SMAD protein signal transduction; IDA:MGI
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;