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Q8C129

- LCAP_MOUSE

UniProt

Q8C129 - LCAP_MOUSE

Protein

Leucyl-cystinyl aminopeptidase

Gene

Lnpep

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 97 (01 Oct 2014)
      Sequence version 1 (01 Mar 2003)
      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: MGI
    2. metallopeptidase activity Source: UniProtKB-KW
    3. protein binding Source: MGI
    4. zinc ion binding Source: InterPro

    GO - Biological processi

    1. protein catabolic process Source: MGI

    Keywords - Molecular functioni

    Aminopeptidase, Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_199054. Translocation of GLUT4 to the plasma membrane.
    REACT_199112. Endosomal/Vacuolar pathway.
    REACT_199115. 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):
    Oxytocinase
    Short name:
    OTase
    Gene namesi
    Name:Lnpep
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 17

    Organism-specific databases

    MGIiMGI:2387123. Lnpep.

    Subcellular locationi

    Cell membrane By similarity; Single-pass type II membrane protein By similarity. Endomembrane system By similarity; Single-pass type II membrane protein By similarity
    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 By similarity.By similarity

    GO - Cellular componenti

    1. cytoplasmic vesicle membrane Source: Reactome
    2. endomembrane system Source: UniProtKB-SubCell
    3. integral component of membrane Source: UniProtKB-KW
    4. lysosomal membrane Source: Ensembl
    5. membrane Source: MGI
    6. perinuclear region of cytoplasm Source: MGI
    7. plasma membrane Source: MGI

    Keywords - Cellular componenti

    Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10251025Leucyl-cystinyl aminopeptidasePRO_0000278198Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity
    Modified residuei70 – 701Phosphotyrosine1 Publication
    Modified residuei80 – 801Phosphoserine1 Publication
    Modified residuei91 – 911Phosphoserine1 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...)1 Publication
    Glycosylationi525 – 5251N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi578 – 5781N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi664 – 6641N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi682 – 6821N-linked (GlcNAc...)1 Publication
    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

    Keywords - PTMi

    Acetylation, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiQ8C129.
    PaxDbiQ8C129.
    PRIDEiQ8C129.

    PTM databases

    PhosphoSiteiQ8C129.

    Expressioni

    Gene expression databases

    ArrayExpressiQ8C129.
    BgeeiQ8C129.
    CleanExiMM_LNPEP.
    GenevestigatoriQ8C129.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    BioGridi232146. 2 interactions.
    IntActiQ8C129. 1 interaction.
    MINTiMINT-4113930.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8C129.
    SMRiQ8C129. Positions 161-1025.
    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.
    InParanoidiQ8C129.
    KOiK01257.
    OMAiMEPFTND.
    OrthoDBiEOG754HNR.
    PhylomeDBiQ8C129.
    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]

    Sequencei

    Sequence statusi: Complete.

    Q8C129-1 [UniParc]FASTAAdd to Basket

    « Hide

    MESFTNDRLQ LPRNMIENSM FEEEPDVVDL AKEPCLHPLE PDEVEYEPRG     50
    SRLLVRGLGE HEMDEDEEDY ESSAKLLGMS FMNRSSGLRN SAAGYRQSPD 100
    GTCSLPSART LVICVFVIVV AVSVIMVIYL LPRCTFTKEG CHKTNQSAEL 150
    IQPVATNGKV FPWAQIRLPT AIIPLCYELS LHPNLTSMTF RGSVTISLQA 200
    LQDTRDIILH STGHNISRVT FMSAVSSQEK QVEILEYPYH EQIAVVAPEP 250
    LLTGHNYTLK IEYSANISNS YYGFYGITYT DKSNEKKYFA ATQFEPLAAR 300
    SAFPCFDEPA FKATFIIKIT RNEHHTALSN MPKKSSVPAE EGLIQDEFSE 350
    SVKMSTYLVA FIVGEMRNLS QDVNGTLVSV YAVPEKIGQV HHALDTTIKL 400
    LEFYQTYFEI QYPLKKLDLV AIPDFEAGAM ENWGLLTFRE ETLLYDNATS 450
    SVADRKLVTK IIAHELAHQW FGNLVTMQWW NDLWLNEGFA TFMEYFSVEK 500
    IFKELNSYED FLDARFKTMR KDSLNSSHPI SSSVQSSEQI EEMFDSLSYF 550
    KGASLLLMLK SYLSEDVFRH AVILYLHNHS YAAIQSDDLW DSFNEVTDKT 600
    LDVKKMMKTW TLQKGFPLVT VQRKGTELLL QQERFFLRMQ PESQPSDTSH 650
    LWHIPISYVT DGRNYSEYRS VSLLDKKSDV INLTEQVQWV KVNSNMTGYY 700
    IVHYAHDDWT ALINQLKRNP YVLSDKDRAN LINNIFELAG LGKVPLRMAF 750
    DLIDYLKNET HTAPITEALF QTNLIYNLLE KLGHMDLSSR LVARVHKLLQ 800
    NQIQQQTWTD EGTPSMRELR SALLEFACAH SLENCTTMAT NLFDSWMASN 850
    GTQSLPTDVM VTVFKVGART EKGWLFLFSM YSSMGSEAEK NKILEALASS 900
    EDVHKLYWLM KSSLDGDIIR TQKLSLIIRT VGRHFPGHLL AWDFVKENWN 950
    KLVHKFHLGS YTIQSIVAGS THLFSTKTHL SEVQAFFENQ SEATLKLRCV 1000
    QEALEVIQLN IQWMVRNLKT LSQWL 1025
    Length:1,025
    Mass (Da):117,304
    Last modified:March 1, 2003 - v1
    Checksum:iAD6F98196EBA683B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK029094 mRNA. Translation: BAC26293.1.
    BC120925 mRNA. Translation: AAI20926.1.
    BC120926 mRNA. Translation: AAI20927.1.
    CCDSiCCDS37457.1.
    RefSeqiNP_766415.1. NM_172827.3.
    UniGeneiMm.328807.
    Mm.393452.

    Genome annotation databases

    EnsembliENSMUST00000041047; ENSMUSP00000036998; ENSMUSG00000023845.
    GeneIDi240028.
    KEGGimmu:240028.
    UCSCiuc008apj.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK029094 mRNA. Translation: BAC26293.1 .
    BC120925 mRNA. Translation: AAI20926.1 .
    BC120926 mRNA. Translation: AAI20927.1 .
    CCDSi CCDS37457.1.
    RefSeqi NP_766415.1. NM_172827.3.
    UniGenei Mm.328807.
    Mm.393452.

    3D structure databases

    ProteinModelPortali Q8C129.
    SMRi Q8C129. Positions 161-1025.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 232146. 2 interactions.
    IntActi Q8C129. 1 interaction.
    MINTi MINT-4113930.

    Protein family/group databases

    MEROPSi M01.011.

    PTM databases

    PhosphoSitei Q8C129.

    Proteomic databases

    MaxQBi Q8C129.
    PaxDbi Q8C129.
    PRIDEi Q8C129.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000041047 ; ENSMUSP00000036998 ; ENSMUSG00000023845 .
    GeneIDi 240028.
    KEGGi mmu:240028.
    UCSCi uc008apj.1. mouse.

    Organism-specific databases

    CTDi 4012.
    MGIi MGI:2387123. Lnpep.

    Phylogenomic databases

    eggNOGi COG0308.
    GeneTreei ENSGT00740000115181.
    HOGENOMi HOG000106482.
    HOVERGENi HBG108296.
    InParanoidi Q8C129.
    KOi K01257.
    OMAi MEPFTND.
    OrthoDBi EOG754HNR.
    PhylomeDBi Q8C129.
    TreeFami TF300395.

    Enzyme and pathway databases

    Reactomei REACT_199054. Translocation of GLUT4 to the plasma membrane.
    REACT_199112. Endosomal/Vacuolar pathway.
    REACT_199115. Antigen processing: Ubiquitination & Proteasome degradation.

    Miscellaneous databases

    NextBioi 384369.
    PROi Q8C129.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8C129.
    Bgeei Q8C129.
    CleanExi MM_LNPEP.
    Genevestigatori Q8C129.

    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. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Skin.
    2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    3. "The phagosomal proteome in interferon-gamma-activated macrophages."
      Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
      Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-70; SER-80 AND SER-91, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    4. "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-447 AND ASN-682.

    Entry informationi

    Entry nameiLCAP_MOUSE
    AccessioniPrimary (citable) accession number: Q8C129
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 20, 2007
    Last sequence update: March 1, 2003
    Last modified: October 1, 2014
    This is version 97 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, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3