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P97629 (LCAP_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Leucyl-cystinyl aminopeptidase

Short name=Cystinyl aminopeptidase
EC=3.4.11.3
Alternative name(s):
GP160
Insulin-regulated membrane aminopeptidase
Insulin-responsive aminopeptidase
Short name=IRAP
Oxytocinase
Short name=OTase
Placental leucine aminopeptidase
Short name=P-LAP
Vesicle protein of 165 kDa
Short name=Vp165
Gene names
Name:Lnpep
Synonyms:Irap, Otase
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length1025 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Catalytic activity

Release of an N-terminal amino acid, Cys-|-Xaa-, in which the half-cystine residue is involved in a disulfide loop, notably in oxytocin or vasopressin. Hydrolysis rates on a range of aminoacyl arylamides exceed that for the cystinyl derivative, however.

Cofactor

Binds 1 zinc ion per subunit By similarity.

Subunit structure

Homodimer. Binds tankyrases 1 and 2 By similarity.

Subcellular location

Cell membrane; Single-pass type II membrane protein. Endomembrane system; Single-pass type II membrane protein. Note: Localized mainly in intracellular vesicles together with GLUT4. Relocalizes to the plasma membrane in response to insulin. The dileucine internalization motif and/or the interaction with tankyrases may be involved in intracellular sequestration.

Tissue specificity

Highly expressed in heart, brain, spleen, lung, kidney and white adipose tissue. Detected at lower levels in skeletal muscle and liver.

Post-translational modification

N-glycosylated.

Sequence similarities

Belongs to the peptidase M1 family.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
   DomainSignal-anchor
Transmembrane
Transmembrane helix
   LigandMetal-binding
Zinc
   Molecular functionAminopeptidase
Hydrolase
Metalloprotease
Protease
   PTMAcetylation
Glycoprotein
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processangiotensin-activated signaling pathway

Inferred from mutant phenotype PubMed 11282364. Source: GOC

neuropeptide catabolic process

Inferred from mutant phenotype PubMed 16771832. Source: RGD

peptide catabolic process

Inferred from direct assay Ref.1. Source: RGD

positive regulation of blood pressure

Inferred from mutant phenotype PubMed 11390024. Source: RGD

regulation of long-term neuronal synaptic plasticity

Inferred from mutant phenotype PubMed 11282364. Source: RGD

response to hormone

Inferred from direct assay PubMed 12709058. Source: RGD

   Cellular_componentcell surface

Inferred from direct assay PubMed 16967782. Source: RGD

cytoplasm

Inferred from direct assay PubMed 16420524. Source: RGD

insulin-responsive compartment

Inferred from direct assay Ref.1PubMed 9271094. Source: RGD

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

intracellular membrane-bounded organelle

Inferred from direct assay Ref.1PubMed 9224710. Source: RGD

intracellular organelle

Inferred from direct assay PubMed 11489215. Source: RGD

neuronal cell body

Inferred from direct assay PubMed 15906313. Source: RGD

perinuclear region of cytoplasm

Inferred from direct assay PubMed 9271094. Source: RGD

plasma membrane

Inferred from direct assay PubMed 11489215PubMed 16870704PubMed 9224710. Source: RGD

vesicle

Inferred from direct assay PubMed 12709058. Source: RGD

   Molecular_functionaminopeptidase activity

Inferred from direct assay PubMed 16619500Ref.1. Source: RGD

angiotensin receptor activity

Inferred from mutant phenotype PubMed 11282364. Source: RGD

metallopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

peptide hormone binding

Inferred from mutant phenotype PubMed 11282364. Source: RGD

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10251025Leucyl-cystinyl aminopeptidase
PRO_0000095115

Regions

Topological domain1 – 109109Cytoplasmic Potential
Transmembrane110 – 13122Helical; Signal-anchor for type II membrane protein; Potential
Topological domain132 – 1025894Extracellular Potential
Region96 – 1016Tankyrase binding By similarity
Region428 – 4325Substrate binding By similarity
Motif53 – 542Dileucine internalization motif Potential
Motif76 – 772Dileucine internalization motif Potential

Sites

Active site4651Proton acceptor By similarity
Metal binding4641Zinc; catalytic By similarity
Metal binding4681Zinc; catalytic By similarity
Metal binding4871Zinc; catalytic By similarity
Binding site2951Substrate By similarity
Site5491Transition state stabilizer By similarity

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue701Phosphotyrosine By similarity
Modified residue801Phosphoserine; by PKC/PRKCZ; in vitro Ref.3
Modified residue911Phosphoserine; by PKC/PRKCZ; in vitro Ref.3
Glycosylation1451N-linked (GlcNAc...) Potential
Glycosylation1841N-linked (GlcNAc...) Potential
Glycosylation2151N-linked (GlcNAc...) Potential
Glycosylation2561N-linked (GlcNAc...) Potential
Glycosylation2661N-linked (GlcNAc...) Potential
Glycosylation3681N-linked (GlcNAc...) Potential
Glycosylation3741N-linked (GlcNAc...) Potential
Glycosylation4471N-linked (GlcNAc...) Potential
Glycosylation5251N-linked (GlcNAc...) Potential
Glycosylation5781N-linked (GlcNAc...) Potential
Glycosylation6641N-linked (GlcNAc...) Potential
Glycosylation6821N-linked (GlcNAc...) Potential
Glycosylation6951N-linked (GlcNAc...) Potential
Glycosylation7581N-linked (GlcNAc...) Potential
Glycosylation8341N-linked (GlcNAc...) Potential
Glycosylation8501N-linked (GlcNAc...) Potential
Glycosylation9891N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict909 – 9168LMKSSLDG → YGTTQRAW in AAB38021. Ref.1
Sequence conflict916 – 1025110Missing in AAB38021. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P97629 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: 8AD3BA3A446FB5EF

FASTA1,025117,201
        10         20         30         40         50         60 
METFTNDRLQ LPRNMIENSM FEEEPDVVDL AKEPCLHPLE PDEVEYEPRG SRLLVRGLGE 

        70         80         90        100        110        120 
HEMDEDEEDY ESSAKLLGMS FMNRSSGLRN SATGYRQSPD GTCSVPSART LVICVFVIVV 

       130        140        150        160        170        180 
AVSVIMVIYL LPRCTFTKEG CHKTNQSAEL IQPIATNGKV FPWAQIRLPT AIIPQRYELS 

       190        200        210        220        230        240 
LHPNLTSMTF RGSVTISLQA LQDTRDIILH STGHNISSVT FMSAVSSQEK QVEILEYPYH 

       250        260        270        280        290        300 
EQIAVVAPES LLTGHNYTLK IEYSANISNS YYGFYGITYT DKSNEKKNFA ATQFEPLAAR 

       310        320        330        340        350        360 
SAFPCFDEPA FKATFIIKIT RDEHHTALSN MPKKSSVPTE EGLIQDEFSE SVKMSTYLVA 

       370        380        390        400        410        420 
FIVGEMRNLS QDVNGTLVSV YAVPEKIDQV YHALDTTVKL LEFYQNYFEI QYPLKKLDLV 

       430        440        450        460        470        480 
AIPDFEAGAM ENWGLLTFRE ETLLYDNATS SVADRKLVTK IIAHELAHQW FGNLVTMQWW 

       490        500        510        520        530        540 
NDLWLNEGFA TFMEYFSVEK IFKELNSYED FLDARFKTMR KDSLNSSHPI SSSVQSSEQI 

       550        560        570        580        590        600 
EEMFDSLSYF KGASLLLMLK SYLSEDVFQH AIILYLHNHS YAAIQSDDLW DSFNEVTGKT 

       610        620        630        640        650        660 
LDVKKMMKTW TLQKGFPLVT VQRKGTELLL QQERFFPSMQ PEIQDSDTSH LWHIPISYVT 

       670        680        690        700        710        720 
DGRNYSEYRS VSLLDKKSDV INLTEQVQWV KVNTNMTGYY IVHYAHDGWA ALINQLKRNP 

       730        740        750        760        770        780 
YVLSDKDRAN LINNIFELAG LGKVPLQMAF DLIDYLRNET HTAPITEALF QTDLIYNLLE 

       790        800        810        820        830        840 
KLGHMDLSSR LVTRVHKLLQ NQIQQQTWTD EGTPSMRELR SALLEFACAH SLENCTTMAT 

       850        860        870        880        890        900 
KLFDGWMASN GTQSLPTDVM TTVFKVGART EKGWLFLFSM YSSMGSEAEK DKILEALASS 

       910        920        930        940        950        960 
ADAHKLYWLM KSSLDGDIIR TQKLSLIIRT VGRQFPGHLL AWDFVKENWN KLVHKFHLGS 

       970        980        990       1000       1010       1020 
YTIQSIVAGS THLFSTKTHL SEVQEFFENQ SEATLQLRCV QEAFEVIELN IQWMARNLKT 


LTLWL 

« Hide

References

[1]"Cloning and characterization of a novel insulin-regulated membrane aminopeptidase from Glut4 vesicles."
Keller S.R., Scott H.M., Mastick C.C., Aebersold R., Lienhard G.E.
J. Biol. Chem. 270:23612-23618(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
Strain: Sprague-Dawley.
Tissue: Adipocyte.
[2]"Characterization of a major protein in GLUT4 vesicles. Concentration in the vesicles and insulin-stimulated translocation to the plasma membrane."
Mastick C.C., Aebersold R., Lienhard G.E.
J. Biol. Chem. 269:6089-6092(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 168-176; 387-399; 731-740 AND 893-905.
[3]"Protein kinase C-zeta phosphorylates insulin-responsive aminopeptidase in vitro at Ser-80 and Ser-91."
Ryu J., Hah J.S., Park J.S.S., Lee W., Rampal A.L., Jung C.Y.
Arch. Biochem. Biophys. 403:71-82(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-80 AND SER-91, IDENTIFICATION BY MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U76997 mRNA. Translation: AAB19066.1.
U32990 mRNA. Translation: AAB38021.1.
PIRI55441.
RefSeqNP_001106874.1. NM_001113403.1.
NP_598258.1. NM_133574.1.
XP_003748754.1. XM_003748706.2.
UniGeneRn.10614.

3D structure databases

ProteinModelPortalP97629.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP97629. 1 interaction.

Chemistry

BindingDBP97629.
ChEMBLCHEMBL3712.

Protein family/group databases

MEROPSM01.011.

PTM databases

PhosphoSiteP97629.

Proteomic databases

PaxDbP97629.
PRIDEP97629.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000017718; ENSRNOP00000017718; ENSRNOG00000047387.
GeneID100912445.
171105.
KEGGrno:100912445.
rno:171105.
UCSCRGD:621752. rat.

Organism-specific databases

CTD4012.
RGD621752. Lnpep.

Phylogenomic databases

eggNOGCOG0308.
GeneTreeENSGT00740000115181.
HOGENOMHOG000106482.
HOVERGENHBG108296.
InParanoidP97629.
KOK01257.
OMAMEPFTND.
OrthoDBEOG754HNR.
PhylomeDBP97629.

Gene expression databases

GenevestigatorP97629.

Family and domain databases

InterProIPR024571. ERAP1-like_C_dom.
IPR001930. Peptidase_M1.
IPR014782. Peptidase_M1_N.
[Graphical view]
PANTHERPTHR11533. PTHR11533. 1 hit.
PfamPF11838. ERAP1_C. 1 hit.
PF01433. Peptidase_M1. 1 hit.
[Graphical view]
PRINTSPR00756. ALADIPTASE.
PROSITEPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio621794.
PROP97629.

Entry information

Entry nameLCAP_RAT
AccessionPrimary (citable) accession number: P97629
Secondary accession number(s): Q11009
Entry history
Integrated into UniProtKB/Swiss-Prot: March 27, 2002
Last sequence update: May 1, 1997
Last modified: May 14, 2014
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries