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P11438

- LAMP1_MOUSE

UniProt

P11438 - LAMP1_MOUSE

Protein

Lysosome-associated membrane glycoprotein 1

Gene

Lamp1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 2 (01 Aug 1990)
      Previous versions | rss
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    Functioni

    Presents carbohydrate ligands to selectins. Also implicated in tumor cell metastasis.

    GO - Molecular functioni

    1. protein binding Source: BHF-UCL
    2. protein domain specific binding Source: UniProt

    GO - Biological processi

    1. autophagic cell death Source: Ensembl
    2. autophagy Source: Ensembl
    3. protein stabilization Source: UniProt
    4. spermatogenesis Source: MGI

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lysosome-associated membrane glycoprotein 1
    Short name:
    LAMP-1
    Short name:
    Lysosome-associated membrane protein 1
    Alternative name(s):
    120 kDa lysosomal membrane glycoprotein
    CD107 antigen-like family member A
    LGP-120
    Lysosomal membrane glycoprotein A
    Short name:
    LGP-A
    P2B
    CD_antigen: CD107a
    Gene namesi
    Name:Lamp1
    Synonyms:Lamp-1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 8

    Organism-specific databases

    MGIiMGI:96745. Lamp1.

    Subcellular locationi

    Cell membrane; Single-pass type I membrane protein. Endosome membrane; Single-pass type I membrane protein. Lysosome membrane; Single-pass type I membrane protein. Late endosome By similarity
    Note: This protein shuttles between lysosomes, endosomes, and the plasma membrane. Colocalizes with OSBPL1A at the late endosome By similarity.By similarity

    GO - Cellular componenti

    1. alveolar lamellar body Source: Ensembl
    2. cell surface Source: BHF-UCL
    3. cytolytic granule Source: MGI
    4. cytoplasm Source: MGI
    5. dendrite Source: Ensembl
    6. endosome Source: MGI
    7. endosome membrane Source: UniProtKB-SubCell
    8. external side of plasma membrane Source: MGI
    9. integral component of membrane Source: UniProtKB-KW
    10. late endosome Source: MGI
    11. lysosome Source: MGI
    12. melanosome Source: MGI
    13. multivesicular body Source: MGI
    14. neuronal cell body Source: Ensembl
    15. phagolysosome membrane Source: MGI
    16. sarcolemma Source: MGI
    17. vesicle Source: MGI

    Keywords - Cellular componenti

    Cell membrane, Endosome, Lysosome, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2424Add
    BLAST
    Chaini25 – 406382Lysosome-associated membrane glycoprotein 1PRO_0000017105Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi31 – 311N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi35 ↔ 741 PublicationPROSITE-ProRule annotation
    Glycosylationi52 – 521N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi58 – 581N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi70 – 701N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi78 – 781N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi97 – 971N-linked (GlcNAc...)2 Publications
    Glycosylationi101 – 1011N-linked (GlcNAc...)1 Publication
    Glycosylationi115 – 1151N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi149 ↔ 1851 PublicationPROSITE-ProRule annotation
    Glycosylationi159 – 1591N-linked (GlcNAc...)1 Publication
    Glycosylationi177 – 1771N-linked (GlcNAc...)2 Publications
    Glycosylationi214 – 2141N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi219 – 2191N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi222 ↔ 2591 PublicationPROSITE-ProRule annotation
    Glycosylationi232 – 2321N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi240 – 2401N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi252 – 2521N-linked (GlcNAc...) (high mannose)1 Publication
    Glycosylationi282 – 2821N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi296 – 2961N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi311 – 3111N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi327 ↔ 3641 PublicationPROSITE-ProRule annotation

    Post-translational modificationi

    O- and N-glycosylated; some of the N-glycans attached to LAMP-1 are polylactosaminoglycans.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiP11438.
    PaxDbiP11438.
    PRIDEiP11438.

    PTM databases

    PhosphoSiteiP11438.

    Expressioni

    Gene expression databases

    ArrayExpressiP11438.
    BgeeiP11438.
    CleanExiMM_LAMP1.
    GenevestigatoriP11438.

    Interactioni

    Protein-protein interaction databases

    IntActiP11438. 16 interactions.
    MINTiMINT-1858576.

    Structurei

    3D structure databases

    ProteinModelPortaliP11438.
    SMRiP11438. Positions 207-366.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini25 – 370346LumenalSequence AnalysisAdd
    BLAST
    Topological domaini395 – 40612CytoplasmicPROSITE-ProRule annotationAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei371 – 39424HelicalPROSITE-ProRule annotationAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni25 – 188164First lumenal domainAdd
    BLAST
    Regioni189 – 21830HingeAdd
    BLAST
    Regioni219 – 370152Second lumenal domainAdd
    BLAST

    Sequence similaritiesi

    Belongs to the LAMP family.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG301998.
    HOGENOMiHOG000230942.
    HOVERGENiHBG052303.
    KOiK06528.
    OMAiENNMLIP.
    OrthoDBiEOG7ZD1VH.
    PhylomeDBiP11438.
    TreeFamiTF316339.

    Family and domain databases

    InterProiIPR018134. LAMP_CS.
    IPR002000. Lysosome-assoc_membr_glycop.
    [Graphical view]
    PANTHERiPTHR11506. PTHR11506. 1 hit.
    PfamiPF01299. Lamp. 1 hit.
    [Graphical view]
    PRINTSiPR00336. LYSASSOCTDMP.
    PROSITEiPS00310. LAMP_1. 2 hits.
    PS00311. LAMP_2. 1 hit.
    PS51407. LAMP_3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P11438-1 [UniParc]FASTAAdd to Basket

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    MAAPGARRPL LLLLLAGLAH GASALFEVKN NGTTCIMASF SASFLTTYET    50
    ANGSQIVNIS LPASAEVLKN GSSCGKENVS DPSLTITFGR GYLLTLNFTK 100
    NTTRYSVQHM YFTYNLSDTE HFPNAISKEI YTMDSTTDIK ADINKAYRCV 150
    SDIRVYMKNV TVVLRDATIQ AYLSSGNFSK EETHCTQDGP SPTTGPPSPS 200
    PPLVPTNPTV SKYNVTGNNG TCLLASMALQ LNITYLKKDN KTVTRAFNIS 250
    PNDTSSGSCG INLVTLKVEN KNRALELQFG MNASSSLFFL QGVRLNMTLP 300
    DALVPTFSIS NHSLKALQAT VGNSYKCNTE EHIFVSKMLS LNVFSVQVQA 350
    FKVDSDRFGS VEECVQDGNN MLIPIAVGGA LAGLVLIVLI AYLIGRKRSH 400
    AGYQTI 406
    Length:406
    Mass (Da):43,865
    Last modified:August 1, 1990 - v2
    Checksum:iC1BD373548BB9655
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1 – 1010MAAPGARRPL → MRPPRAAAV(PubMed:2676155)Curated
    Sequence conflicti25 – 262LF → IP in AAA39411. (PubMed:3379044)Curated
    Sequence conflicti385 – 3851V → I(PubMed:2676155)Curated
    Sequence conflicti385 – 3851V → I(PubMed:3379044)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M32015 mRNA. Translation: AAA39428.1.
    M25244 mRNA. Translation: AAA39869.1.
    BC049097 mRNA. Translation: AAH49097.1.
    J03881 mRNA. Translation: AAA39411.1.
    CCDSiCCDS22106.1.
    PIRiA28067.
    A60534.
    RefSeqiNP_034814.2. NM_010684.2.
    UniGeneiMm.16716.

    Genome annotation databases

    EnsembliENSMUST00000033824; ENSMUSP00000033824; ENSMUSG00000031447.
    GeneIDi16783.
    KEGGimmu:16783.
    UCSCiuc009kxa.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M32015 mRNA. Translation: AAA39428.1 .
    M25244 mRNA. Translation: AAA39869.1 .
    BC049097 mRNA. Translation: AAH49097.1 .
    J03881 mRNA. Translation: AAA39411.1 .
    CCDSi CCDS22106.1.
    PIRi A28067.
    A60534.
    RefSeqi NP_034814.2. NM_010684.2.
    UniGenei Mm.16716.

    3D structure databases

    ProteinModelPortali P11438.
    SMRi P11438. Positions 207-366.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P11438. 16 interactions.
    MINTi MINT-1858576.

    PTM databases

    PhosphoSitei P11438.

    Proteomic databases

    MaxQBi P11438.
    PaxDbi P11438.
    PRIDEi P11438.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000033824 ; ENSMUSP00000033824 ; ENSMUSG00000031447 .
    GeneIDi 16783.
    KEGGi mmu:16783.
    UCSCi uc009kxa.1. mouse.

    Organism-specific databases

    CTDi 3916.
    MGIi MGI:96745. Lamp1.

    Phylogenomic databases

    eggNOGi NOG301998.
    HOGENOMi HOG000230942.
    HOVERGENi HBG052303.
    KOi K06528.
    OMAi ENNMLIP.
    OrthoDBi EOG7ZD1VH.
    PhylomeDBi P11438.
    TreeFami TF316339.

    Miscellaneous databases

    ChiTaRSi Lamp1. mouse.
    NextBioi 290640.
    PROi P11438.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P11438.
    Bgeei P11438.
    CleanExi MM_LAMP1.
    Genevestigatori P11438.

    Family and domain databases

    InterProi IPR018134. LAMP_CS.
    IPR002000. Lysosome-assoc_membr_glycop.
    [Graphical view ]
    PANTHERi PTHR11506. PTHR11506. 1 hit.
    Pfami PF01299. Lamp. 1 hit.
    [Graphical view ]
    PRINTSi PR00336. LYSASSOCTDMP.
    PROSITEi PS00310. LAMP_1. 2 hits.
    PS00311. LAMP_2. 1 hit.
    PS51407. LAMP_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization and cloning of lgp110, a lysosomal membrane glycoprotein from mouse and rat cells."
      Granger B.L., Green S.A., Gabel C.A., Howe C.L., Mellman I., Helenius A.
      J. Biol. Chem. 265:12036-12043(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Molecular characterization of P2B/LAMP-1, a major protein target of a metastasis-associated oligosaccharide structure."
      Heffernan M., Yousefi S., Dennis J.W.
      Cancer Res. 49:6077-6084(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "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].
      Strain: C57BL/6.
      Tissue: Brain.
    4. "Isolation and sequencing of a cDNA clone encoding lysosomal membrane glycoprotein mouse LAMP-1. Sequence similarity to proteins bearing onco-differentiation antigens."
      Chen J.W., Cha Y., Yuksel K.U., Gracy R.W., August J.T.
      J. Biol. Chem. 263:8754-8758(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 25-406, PARTIAL PROTEIN SEQUENCE.
    5. "The disulfide structure of mouse lysosome-associated membrane protein 1."
      Arterburn L.M., Earles B.J., August J.T.
      J. Biol. Chem. 265:7419-7423(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISULFIDE BONDS.
    6. "High throughput quantitative glycomics and glycoform-focused proteomics of murine dermis and epidermis."
      Uematsu R., Furukawa J., Nakagawa H., Shinohara Y., Deguchi K., Monde K., Nishimura S.
      Mol. Cell. Proteomics 4:1977-1989(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-252.
      Tissue: Epidermis.
    7. "Proteome-wide characterization of N-glycosylation events by diagonal chromatography."
      Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.
      J. Proteome Res. 5:2438-2447(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-97.
      Strain: C57BL/6.
      Tissue: Plasma.
    8. "The mouse C2C12 myoblast cell surface N-linked glycoproteome: identification, glycosite occupancy, and membrane orientation."
      Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.
      Mol. Cell. Proteomics 8:2555-2569(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-177.
      Tissue: Myoblast.
    9. "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-97; ASN-101; ASN-159 AND ASN-177.

    Entry informationi

    Entry nameiLAMP1_MOUSE
    AccessioniPrimary (citable) accession number: P11438
    Secondary accession number(s): Q62020
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: August 1, 1990
    Last modified: October 1, 2014
    This is version 129 of the entry and version 2 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. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3