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P97629

- LCAP_RAT

UniProt

P97629 - LCAP_RAT

Protein

Leucyl-cystinyl aminopeptidase

Gene

Lnpep

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 1 (01 May 1997)
      Previous versions | rss
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    Functioni

    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.By similarity

    Catalytic activityi

    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.

    Cofactori

    Binds 1 zinc ion per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei295 – 2951SubstrateBy similarity
    Metal bindingi464 – 4641Zinc; catalyticPROSITE-ProRule annotation
    Active sitei465 – 4651Proton acceptorPROSITE-ProRule annotation
    Metal bindingi468 – 4681Zinc; catalyticPROSITE-ProRule annotation
    Metal bindingi487 – 4871Zinc; catalyticPROSITE-ProRule annotation
    Sitei549 – 5491Transition state stabilizerBy similarity

    GO - Molecular functioni

    1. aminopeptidase activity Source: RGD
    2. angiotensin receptor activity Source: RGD
    3. metallopeptidase activity Source: UniProtKB-KW
    4. peptide hormone binding Source: RGD
    5. zinc ion binding Source: InterPro

    GO - Biological processi

    1. angiotensin-activated signaling pathway Source: GOC
    2. neuropeptide catabolic process Source: RGD
    3. peptide catabolic process Source: RGD
    4. positive regulation of blood pressure Source: RGD
    5. regulation of long-term neuronal synaptic plasticity Source: RGD
    6. response to hormone Source: RGD

    Keywords - Molecular functioni

    Aminopeptidase, Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_199176. Translocation of GLUT4 to the plasma membrane.
    REACT_199254. Antigen processing: Ubiquitination & Proteasome degradation.

    Protein family/group databases

    MEROPSiM01.011.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Leucyl-cystinyl aminopeptidase (EC:3.4.11.3)
    Short name:
    Cystinyl aminopeptidase
    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 namesi
    Name:Lnpep
    Synonyms:Irap, Otase
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 1

    Organism-specific databases

    RGDi621752. Lnpep.

    Subcellular locationi

    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.

    GO - Cellular componenti

    1. cell surface Source: RGD
    2. cytoplasm Source: RGD
    3. insulin-responsive compartment Source: RGD
    4. integral component of membrane Source: UniProtKB-KW
    5. intracellular membrane-bounded organelle Source: RGD
    6. intracellular organelle Source: RGD
    7. neuronal cell body Source: RGD
    8. perinuclear region of cytoplasm Source: RGD
    9. plasma membrane Source: RGD
    10. vesicle Source: RGD

    Keywords - Cellular componenti

    Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10251025Leucyl-cystinyl aminopeptidasePRO_0000095115Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity
    Modified residuei70 – 701PhosphotyrosineBy similarity
    Modified residuei80 – 801Phosphoserine; by PKC/PRKCZ; in vitro1 Publication
    Modified residuei91 – 911Phosphoserine; by PKC/PRKCZ; in vitro1 Publication
    Glycosylationi145 – 1451N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi184 – 1841N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi215 – 2151N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi256 – 2561N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi266 – 2661N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi368 – 3681N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi374 – 3741N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi447 – 4471N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi525 – 5251N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi578 – 5781N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi664 – 6641N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi682 – 6821N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi695 – 6951N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi758 – 7581N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi834 – 8341N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi850 – 8501N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi989 – 9891N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    N-glycosylated.

    Keywords - PTMi

    Acetylation, Glycoprotein, Phosphoprotein

    Proteomic databases

    PaxDbiP97629.
    PRIDEiP97629.

    PTM databases

    PhosphoSiteiP97629.

    Expressioni

    Tissue specificityi

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

    Gene expression databases

    GenevestigatoriP97629.

    Interactioni

    Subunit structurei

    Homodimer. Binds tankyrases 1 and 2 By similarity.By similarity

    Protein-protein interaction databases

    IntActiP97629. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliP97629.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 109109CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini132 – 1025894ExtracellularSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei110 – 13122Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni96 – 1016Tankyrase bindingBy similarity
    Regioni428 – 4325Substrate bindingBy similarity

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi53 – 542Dileucine internalization motifSequence Analysis
    Motifi76 – 772Dileucine internalization motifSequence Analysis

    Sequence similaritiesi

    Belongs to the peptidase M1 family.Curated

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0308.
    GeneTreeiENSGT00740000115181.
    HOGENOMiHOG000106482.
    HOVERGENiHBG108296.
    InParanoidiP97629.
    KOiK01257.
    OMAiMEPFTND.
    OrthoDBiEOG754HNR.
    PhylomeDBiP97629.

    Family and domain databases

    InterProiIPR024571. ERAP1-like_C_dom.
    IPR001930. Peptidase_M1.
    IPR014782. Peptidase_M1_N.
    [Graphical view]
    PANTHERiPTHR11533. PTHR11533. 1 hit.
    PfamiPF11838. ERAP1_C. 1 hit.
    PF01433. Peptidase_M1. 1 hit.
    [Graphical view]
    PRINTSiPR00756. ALADIPTASE.
    PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P97629-1 [UniParc]FASTAAdd to Basket

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    METFTNDRLQ LPRNMIENSM FEEEPDVVDL AKEPCLHPLE PDEVEYEPRG     50
    SRLLVRGLGE HEMDEDEEDY ESSAKLLGMS FMNRSSGLRN SATGYRQSPD 100
    GTCSVPSART LVICVFVIVV AVSVIMVIYL LPRCTFTKEG CHKTNQSAEL 150
    IQPIATNGKV FPWAQIRLPT AIIPQRYELS LHPNLTSMTF RGSVTISLQA 200
    LQDTRDIILH STGHNISSVT FMSAVSSQEK QVEILEYPYH EQIAVVAPES 250
    LLTGHNYTLK IEYSANISNS YYGFYGITYT DKSNEKKNFA ATQFEPLAAR 300
    SAFPCFDEPA FKATFIIKIT RDEHHTALSN MPKKSSVPTE EGLIQDEFSE 350
    SVKMSTYLVA FIVGEMRNLS QDVNGTLVSV YAVPEKIDQV YHALDTTVKL 400
    LEFYQNYFEI QYPLKKLDLV AIPDFEAGAM ENWGLLTFRE ETLLYDNATS 450
    SVADRKLVTK IIAHELAHQW FGNLVTMQWW NDLWLNEGFA TFMEYFSVEK 500
    IFKELNSYED FLDARFKTMR KDSLNSSHPI SSSVQSSEQI EEMFDSLSYF 550
    KGASLLLMLK SYLSEDVFQH AIILYLHNHS YAAIQSDDLW DSFNEVTGKT 600
    LDVKKMMKTW TLQKGFPLVT VQRKGTELLL QQERFFPSMQ PEIQDSDTSH 650
    LWHIPISYVT DGRNYSEYRS VSLLDKKSDV INLTEQVQWV KVNTNMTGYY 700
    IVHYAHDGWA ALINQLKRNP YVLSDKDRAN LINNIFELAG LGKVPLQMAF 750
    DLIDYLRNET HTAPITEALF QTDLIYNLLE KLGHMDLSSR LVTRVHKLLQ 800
    NQIQQQTWTD EGTPSMRELR SALLEFACAH SLENCTTMAT KLFDGWMASN 850
    GTQSLPTDVM TTVFKVGART EKGWLFLFSM YSSMGSEAEK DKILEALASS 900
    ADAHKLYWLM KSSLDGDIIR TQKLSLIIRT VGRQFPGHLL AWDFVKENWN 950
    KLVHKFHLGS YTIQSIVAGS THLFSTKTHL SEVQEFFENQ SEATLQLRCV 1000
    QEAFEVIELN IQWMARNLKT LTLWL 1025
    Length:1,025
    Mass (Da):117,201
    Last modified:May 1, 1997 - v1
    Checksum:i8AD3BA3A446FB5EF
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti909 – 9168LMKSSLDG → YGTTQRAW in AAB38021. (PubMed:7559527)Curated
    Sequence conflicti916 – 1025110Missing in AAB38021. (PubMed:7559527)CuratedAdd
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U76997 mRNA. Translation: AAB19066.1.
    U32990 mRNA. Translation: AAB38021.1.
    PIRiI55441.
    RefSeqiNP_001106874.1. NM_001113403.1.
    NP_598258.1. NM_133574.1.
    XP_003748754.1. XM_003748706.2.
    UniGeneiRn.10614.

    Genome annotation databases

    EnsembliENSRNOT00000017718; ENSRNOP00000017718; ENSRNOG00000047387.
    GeneIDi100912445.
    171105.
    KEGGirno:100912445.
    rno:171105.
    UCSCiRGD:621752. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U76997 mRNA. Translation: AAB19066.1 .
    U32990 mRNA. Translation: AAB38021.1 .
    PIRi I55441.
    RefSeqi NP_001106874.1. NM_001113403.1.
    NP_598258.1. NM_133574.1.
    XP_003748754.1. XM_003748706.2.
    UniGenei Rn.10614.

    3D structure databases

    ProteinModelPortali P97629.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P97629. 1 interaction.

    Chemistry

    BindingDBi P97629.
    ChEMBLi CHEMBL3712.

    Protein family/group databases

    MEROPSi M01.011.

    PTM databases

    PhosphoSitei P97629.

    Proteomic databases

    PaxDbi P97629.
    PRIDEi P97629.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000017718 ; ENSRNOP00000017718 ; ENSRNOG00000047387 .
    GeneIDi 100912445.
    171105.
    KEGGi rno:100912445.
    rno:171105.
    UCSCi RGD:621752. rat.

    Organism-specific databases

    CTDi 4012.
    RGDi 621752. Lnpep.

    Phylogenomic databases

    eggNOGi COG0308.
    GeneTreei ENSGT00740000115181.
    HOGENOMi HOG000106482.
    HOVERGENi HBG108296.
    InParanoidi P97629.
    KOi K01257.
    OMAi MEPFTND.
    OrthoDBi EOG754HNR.
    PhylomeDBi P97629.

    Enzyme and pathway databases

    Reactomei REACT_199176. Translocation of GLUT4 to the plasma membrane.
    REACT_199254. Antigen processing: Ubiquitination & Proteasome degradation.

    Miscellaneous databases

    NextBioi 621794.
    PROi P97629.

    Gene expression databases

    Genevestigatori P97629.

    Family and domain databases

    InterProi IPR024571. ERAP1-like_C_dom.
    IPR001930. Peptidase_M1.
    IPR014782. Peptidase_M1_N.
    [Graphical view ]
    PANTHERi PTHR11533. PTHR11533. 1 hit.
    Pfami PF11838. ERAP1_C. 1 hit.
    PF01433. Peptidase_M1. 1 hit.
    [Graphical view ]
    PRINTSi PR00756. ALADIPTASE.
    PROSITEi PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.

    Entry informationi

    Entry nameiLCAP_RAT
    AccessioniPrimary (citable) accession number: P97629
    Secondary accession number(s): Q11009
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 27, 2002
    Last sequence update: May 1, 1997
    Last modified: October 1, 2014
    This is version 121 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Peptidase families
      Classification of peptidase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3