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Q9UIQ6

- LCAP_HUMAN

UniProt

Q9UIQ6 - LCAP_HUMAN

Protein

Leucyl-cystinyl aminopeptidase

Gene

LNPEP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 144 (01 Oct 2014)
      Sequence version 3 (17 Apr 2007)
      Previous versions | rss
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    Functioni

    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.3 Publications

    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.2 Publications

    Cofactori

    Binds 1 zinc ion per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei154 – 1552Cleavage; to produce pregnancy serum form
    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: HGNC
    2. metallopeptidase activity Source: ProtInc
    3. zinc ion binding Source: ProtInc

    GO - Biological processi

    1. antigen processing and presentation of exogenous peptide antigen via MHC class I Source: Reactome
    2. antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-independent Source: Reactome
    3. antigen processing and presentation of peptide antigen via MHC class I Source: Reactome
    4. cell-cell signaling Source: ProtInc
    5. female pregnancy Source: ProtInc
    6. membrane organization Source: Reactome
    7. protein catabolic process Source: Ensembl
    8. protein polyubiquitination Source: Reactome
    9. proteolysis Source: ProtInc

    Keywords - Molecular functioni

    Aminopeptidase, Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_111168. Endosomal/Vacuolar pathway.
    REACT_147867. Translocation of GLUT4 to the plasma membrane.
    REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    SABIO-RKQ9UIQ6.

    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):
    Insulin-regulated membrane aminopeptidase
    Insulin-responsive aminopeptidase
    Short name:
    IRAP
    Oxytocinase
    Short name:
    OTase
    Placental leucine aminopeptidase
    Short name:
    P-LAP
    Cleaved into the following chain:
    Gene namesi
    Name:LNPEP
    Synonyms:OTASE
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:6656. LNPEP.

    Subcellular locationi

    Cell membrane 1 Publication; Single-pass type II membrane protein 1 Publication
    Note: In brain only the membrane-bound form is found. The protein resides in intracellular vesicles together with GLUT4 and can then translocate to the cell surface in response to insulin and/or oxytocin. Localization may be determined by dileucine internalization motifs, and/or by interaction with tankyrases.
    Chain Leucyl-cystinyl aminopeptidase, pregnancy serum form : Secreted
    Note: During pregnancy serum levels are low in the first trimester, rise progressively during the second and third trimester and decrease rapidly after parturition.

    GO - Cellular componenti

    1. cytoplasmic vesicle membrane Source: Reactome
    2. cytosol Source: Reactome
    3. early endosome lumen Source: Reactome
    4. extracellular region Source: UniProtKB-SubCell
    5. integral component of plasma membrane Source: ProtInc
    6. intracellular Source: HGNC
    7. lysosomal membrane Source: UniProtKB
    8. membrane Source: UniProtKB
    9. perinuclear region of cytoplasm Source: Ensembl
    10. plasma membrane Source: ProtInc

    Keywords - Cellular componenti

    Cell membrane, Membrane, Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA30418.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10251025Leucyl-cystinyl aminopeptidasePRO_0000095114Add
    BLAST
    Chaini155 – 1025871Leucyl-cystinyl aminopeptidase, pregnancy serum formPRO_0000292264Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei70 – 701PhosphotyrosineBy similarity
    Modified residuei80 – 801PhosphoserineBy similarity
    Modified residuei91 – 911PhosphoserineBy similarity
    Glycosylationi145 – 1451N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi184 – 1841N-linked (GlcNAc...)1 Publication
    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
    Glycosylationi448 – 4481N-linked (GlcNAc...)1 Publication
    Glycosylationi525 – 5251N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi578 – 5781N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi598 – 5981N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi664 – 6641N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi682 – 6821N-linked (GlcNAc...)1 Publication
    Glycosylationi760 – 7601N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi834 – 8341N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi850 – 8501N-linked (GlcNAc...)1 Publication
    Glycosylationi989 – 9891N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    The pregnancy serum form is derived from the membrane-bound form by proteolytic processing.
    N-glycosylated.1 Publication

    Keywords - PTMi

    Acetylation, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiQ9UIQ6.
    PaxDbiQ9UIQ6.
    PeptideAtlasiQ9UIQ6.
    PRIDEiQ9UIQ6.

    PTM databases

    PhosphoSiteiQ9UIQ6.

    Miscellaneous databases

    PMAP-CutDBQ9UIQ6.

    Expressioni

    Tissue specificityi

    Highly expressed in placenta, heart, kidney and small intestine. Detected at lower levels in neuronal cells in the brain, in skeletal muscle, spleen, liver, testes and colon.3 Publications

    Gene expression databases

    BgeeiQ9UIQ6.
    CleanExiHS_LNPEP.
    GenevestigatoriQ9UIQ6.

    Organism-specific databases

    HPAiHPA043642.

    Interactioni

    Subunit structurei

    Homodimer. Binds tankyrases 1 and 2.

    Protein-protein interaction databases

    BioGridi110196. 7 interactions.
    IntActiQ9UIQ6. 4 interactions.
    STRINGi9606.ENSP00000231368.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9UIQ6.
    SMRiQ9UIQ6. Positions 161-1025.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 110110CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini132 – 1025894ExtracellularSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei111 – 13121Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni96 – 1016Tankyrase binding
    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.
    HOVERGENiHBG108296.
    InParanoidiQ9UIQ6.
    KOiK01257.
    OMAiMEPFTND.
    OrthoDBiEOG754HNR.
    PhylomeDBiQ9UIQ6.
    TreeFamiTF300395.

    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]

    Sequences (3)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Note: Experimental confirmation may be lacking for some isoforms.

    Isoform 1 (identifier: Q9UIQ6-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MEPFTNDRLQ LPRNMIENSM FEEEPDVVDL AKEPCLHPLE PDEVEYEPRG     50
    SRLLVRGLGE HEMEEDEEDY ESSAKLLGMS FMNRSSGLRN SATGYRQSPD 100
    GACSVPSART MVVCAFVIVV AVSVIMVIYL LPRCTFTKEG CHKKNQSIGL 150
    IQPFATNGKL FPWAQIRLPT AVVPLRYELS LHPNLTSMTF RGSVTISVQA 200
    LQVTWNIILH STGHNISRVT FMSAVSSQEK QAEILEYAYH GQIAIVAPEA 250
    LLAGHNYTLK IEYSANISSS YYGFYGFSYT DESNEKKYFA ATQFEPLAAR 300
    SAFPCFDEPA FKATFIIKII RDEQYTALSN MPKKSSVVLD DGLVQDEFSE 350
    SVKMSTYLVA FIVGEMKNLS QDVNGTLVSI YAVPEKIGQV HYALETTVKL 400
    LEFFQNYFEI QYPLKKLDLV AIPDFEAGAM ENWGLLTFRE ETLLYDSNTS 450
    SMADRKLVTK IIAHELAHQW FGNLVTMKWW NDLWLNEGFA TFMEYFSLEK 500
    IFKELSSYED FLDARFKTMK KDSLNSSHPI SSSVQSSEQI EEMFDSLSYF 550
    KGSSLLLMLK TYLSEDVFQH AVVLYLHNHS YASIQSDDLW DSFNEVTNQT 600
    LDVKRMMKTW TLQKGFPLVT VQKKGKELFI QQERFFLNMK PEIQPSDTSY 650
    LWHIPLSYVT EGRNYSKYQS VSLLDKKSGV INLTEEVLWV KVNINMNGYY 700
    IVHYADDDWE ALIHQLKINP YVLSDKDRAN LINNIFELAG LGKVPLKRAF 750
    DLINYLGNEN HTAPITEALF QTDLIYNLLE KLGYMDLASR LVTRVFKLLQ 800
    NQIQQQTWTD EGTPSMRELR SALLEFACTH NLGNCSTTAM KLFDDWMASN 850
    GTQSLPTDVM TTVFKVGAKT DKGWSFLLGK YISIGSEAEK NKILEALASS 900
    EDVRKLYWLM KSSLNGDNFR TQKLSFIIRT VGRHFPGHLL AWDFVKENWN 950
    KLVQKFPLGS YTIQNIVAGS TYLFSTKTHL SEVQAFFENQ SEATFRLRCV 1000
    QEALEVIQLN IQWMEKNLKS LTWWL 1025
    Length:1,025
    Mass (Da):117,349
    Last modified:April 17, 2007 - v3
    Checksum:iF84C0EA9D48DC2C0
    GO
    Isoform 2 (identifier: Q9UIQ6-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-14: Missing.

    Show »
    Length:1,011
    Mass (Da):115,636
    Checksum:iFBB54EFECFBA8FD9
    GO
    Isoform 3 (identifier: Q9UIQ6-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-19: Missing.

    Show »
    Length:1,006
    Mass (Da):115,062
    Checksum:iF57E71F1AA3C28E3
    GO

    Sequence cautioni

    The sequence BAD92120.1 differs from that shown. Reason: Frameshift at position 405.
    The sequence BAA09436.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti66 – 661D → V in CAB61646. (PubMed:10759854)Curated
    Sequence conflicti66 – 661D → V in CAB94753. (PubMed:10759854)Curated
    Sequence conflicti301 – 3011S → L AA sequence (PubMed:8119729)Curated
    Sequence conflicti386 – 3861K → N in AAB66672. (PubMed:9177475)Curated
    Sequence conflicti386 – 3861K → N in AAB66673. (PubMed:9177475)Curated
    Sequence conflicti386 – 3861K → N in CAB61646. (PubMed:10759854)Curated
    Sequence conflicti386 – 3861K → N in CAB94753. (PubMed:10759854)Curated
    Sequence conflicti892 – 8921K → Q in BAA09436. (PubMed:8550619)Curated
    Sequence conflicti944 – 9441F → L in BAA09436. (PubMed:8550619)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti86 – 861S → P.
    Corresponds to variant rs3797799 [ dbSNP | Ensembl ].
    VAR_031616
    Natural varianti594 – 5941N → I.
    Corresponds to variant rs12520455 [ dbSNP | Ensembl ].
    VAR_051567
    Natural varianti763 – 7631A → T.
    Corresponds to variant rs2303138 [ dbSNP | Ensembl ].
    VAR_012812
    Natural varianti913 – 9131S → T.
    Corresponds to variant rs17087233 [ dbSNP | Ensembl ].
    VAR_051568
    Natural varianti963 – 9631I → V.
    Corresponds to variant rs11746232 [ dbSNP | Ensembl ].
    VAR_031617

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 1919Missing in isoform 3. 1 PublicationVSP_005449Add
    BLAST
    Alternative sequencei1 – 1414Missing in isoform 2. 2 PublicationsVSP_005448Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D50810 mRNA. Translation: BAA09436.1. Different initiation.
    U62768 mRNA. Translation: AAB66672.1.
    U62769 mRNA. Translation: AAB66673.1.
    AJ131023
    , AJ131025, AJ131026, AJ131027, AJ131028, AJ131029, AJ131030, AJ131031, AJ131032, AJ131033, AJ131034, AJ131035, AJ131036, AJ131037, AJ131038, AJ131039 Genomic DNA. Translation: CAB61646.1.
    AJ131025
    , AJ131026, AJ131027, AJ131028, AJ131029, AJ131030, AJ131031, AJ131032, AJ131033, AJ131034, AJ131035, AJ131036, AJ131037, AJ131038, AJ131039 Genomic DNA. Translation: CAB94753.1.
    AB208883 mRNA. Translation: BAD92120.1. Frameshift.
    CCDSiCCDS4087.1. [Q9UIQ6-1]
    CCDS43346.1. [Q9UIQ6-2]
    PIRiA59383.
    A59384.
    RefSeqiNP_005566.2. NM_005575.2. [Q9UIQ6-1]
    NP_787116.2. NM_175920.3. [Q9UIQ6-2]
    UniGeneiHs.527199.
    Hs.656905.

    Genome annotation databases

    EnsembliENST00000231368; ENSP00000231368; ENSG00000113441. [Q9UIQ6-1]
    ENST00000395770; ENSP00000379117; ENSG00000113441. [Q9UIQ6-2]
    GeneIDi4012.
    KEGGihsa:4012.
    UCSCiuc003kmv.1. human. [Q9UIQ6-1]

    Polymorphism databases

    DMDMi145559489.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D50810 mRNA. Translation: BAA09436.1 . Different initiation.
    U62768 mRNA. Translation: AAB66672.1 .
    U62769 mRNA. Translation: AAB66673.1 .
    AJ131023
    , AJ131025 , AJ131026 , AJ131027 , AJ131028 , AJ131029 , AJ131030 , AJ131031 , AJ131032 , AJ131033 , AJ131034 , AJ131035 , AJ131036 , AJ131037 , AJ131038 , AJ131039 Genomic DNA. Translation: CAB61646.1 .
    AJ131025
    , AJ131026 , AJ131027 , AJ131028 , AJ131029 , AJ131030 , AJ131031 , AJ131032 , AJ131033 , AJ131034 , AJ131035 , AJ131036 , AJ131037 , AJ131038 , AJ131039 Genomic DNA. Translation: CAB94753.1 .
    AB208883 mRNA. Translation: BAD92120.1 . Frameshift.
    CCDSi CCDS4087.1. [Q9UIQ6-1 ]
    CCDS43346.1. [Q9UIQ6-2 ]
    PIRi A59383.
    A59384.
    RefSeqi NP_005566.2. NM_005575.2. [Q9UIQ6-1 ]
    NP_787116.2. NM_175920.3. [Q9UIQ6-2 ]
    UniGenei Hs.527199.
    Hs.656905.

    3D structure databases

    ProteinModelPortali Q9UIQ6.
    SMRi Q9UIQ6. Positions 161-1025.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110196. 7 interactions.
    IntActi Q9UIQ6. 4 interactions.
    STRINGi 9606.ENSP00000231368.

    Chemistry

    BindingDBi Q9UIQ6.
    ChEMBLi CHEMBL2693.

    Protein family/group databases

    MEROPSi M01.011.

    PTM databases

    PhosphoSitei Q9UIQ6.

    Polymorphism databases

    DMDMi 145559489.

    Proteomic databases

    MaxQBi Q9UIQ6.
    PaxDbi Q9UIQ6.
    PeptideAtlasi Q9UIQ6.
    PRIDEi Q9UIQ6.

    Protocols and materials databases

    DNASUi 4012.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000231368 ; ENSP00000231368 ; ENSG00000113441 . [Q9UIQ6-1 ]
    ENST00000395770 ; ENSP00000379117 ; ENSG00000113441 . [Q9UIQ6-2 ]
    GeneIDi 4012.
    KEGGi hsa:4012.
    UCSCi uc003kmv.1. human. [Q9UIQ6-1 ]

    Organism-specific databases

    CTDi 4012.
    GeneCardsi GC05P096272.
    H-InvDB HIX0005054.
    HGNCi HGNC:6656. LNPEP.
    HPAi HPA043642.
    MIMi 151300. gene.
    neXtProti NX_Q9UIQ6.
    PharmGKBi PA30418.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0308.
    HOVERGENi HBG108296.
    InParanoidi Q9UIQ6.
    KOi K01257.
    OMAi MEPFTND.
    OrthoDBi EOG754HNR.
    PhylomeDBi Q9UIQ6.
    TreeFami TF300395.

    Enzyme and pathway databases

    Reactomei REACT_111168. Endosomal/Vacuolar pathway.
    REACT_147867. Translocation of GLUT4 to the plasma membrane.
    REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    SABIO-RK Q9UIQ6.

    Miscellaneous databases

    GeneWikii Cystinyl_aminopeptidase.
    GenomeRNAii 4012.
    NextBioi 15736.
    PMAP-CutDB Q9UIQ6.
    PROi Q9UIQ6.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9UIQ6.
    CleanExi HS_LNPEP.
    Genevestigatori Q9UIQ6.

    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. "Human placental leucine aminopeptidase/oxytocinase. A new member of type II membrane-spanning zinc metallopeptidase family."
      Rogi T., Tsujimoto M., Nakazato H., Mizutani S., Tomoda Y.
      J. Biol. Chem. 271:56-61(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 160-168; 319-332; 615-624; 635-647; 798-814 AND 870-880, TISSUE SPECIFICITY.
      Tissue: Placenta.
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY.
      Tissue: Placenta.
    3. "Structure of the human oxytocinase/insulin-regulated aminopeptidase gene and localization to chromosome 5q21."
      Rasmussen T.E., Pedraza-Diaz S., Hardre R., Laustsen P.G., Carrion A.G., Kristensen T.
      Eur. J. Biochem. 267:2297-2306(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 3).
    4. "Expression of placental leucine aminopeptidase/oxytocinase in neuronal cells and its action on neuronal peptides."
      Matsumoto H., Nagasaka T., Hattori A., Rogi T., Tsuruoka N., Mizutani S., Tsujimoto M.
      Eur. J. Biochem. 268:3259-3266(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    5. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 206-1025.
      Tissue: Brain.
    6. "Pool sequencing of natural HLA-DR, DQ, and DP ligands reveals detailed peptide motifs, constraints of processing, and general rules."
      Falk K., Roetzschke O., Stevanovic S., Jung G., Rammensee H.G.
      Immunogenetics 39:230-242(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 285-301 AND 710-724.
    7. "Identification of human placental leucine aminopeptidase as oxytocinase."
      Tsujimoto M., Mizutani S., Adachi H., Kimura M., Nakazato H., Tomoda Y.
      Arch. Biochem. Biophys. 292:388-392(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY.
    8. "Evidence that the angiotensin IV (AT(4)) receptor is the enzyme insulin-regulated aminopeptidase."
      Albiston A.L., McDowall S.G., Matsacos D., Sim P., Clune E., Mustafa T., Lee J., Mendelsohn F.A., Simpson R.J., Connolly L.M., Chai S.Y.
      J. Biol. Chem. 276:48623-48626(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
      Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
      Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-184; ASN-448; ASN-682 AND ASN-850.
      Tissue: Leukemic T-cell.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiLCAP_HUMAN
    AccessioniPrimary (citable) accession number: Q9UIQ6
    Secondary accession number(s): O00769
    , Q15145, Q59H76, Q9TNQ2, Q9TNQ3, Q9UIQ7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 27, 2002
    Last sequence update: April 17, 2007
    Last modified: October 1, 2014
    This is version 144 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 5
      Human chromosome 5: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. Peptidase families
      Classification of peptidase families and list of entries
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3