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P11438

- LAMP1_MOUSE

UniProt

P11438 - LAMP1_MOUSE

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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

Functioni

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

GO - Molecular functioni

  1. protein domain specific binding Source: UniProt

GO - Biological processi

  1. autophagic cell death Source: Ensembl
  2. autophagy Source: Ensembl
  3. establishment of protein localization to organelle Source: Ensembl
  4. Golgi to lysosome transport Source: Ensembl
  5. granzyme-mediated apoptotic signaling pathway Source: Ensembl
  6. positive regulation of natural killer cell degranulation Source: Ensembl
  7. positive regulation of natural killer cell mediated cytotoxicity Source: Ensembl
  8. protein stabilization Source: UniProt
  9. regulation of organelle transport along microtubule Source: Ensembl
  10. spermatogenesis Source: MGI
Complete GO annotation...

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. external side of plasma membrane Source: MGI
  8. extracellular vesicular exosome Source: Ensembl
  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
Complete GO annotation...

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

BgeeiP11438.
CleanExiMM_LAMP1.
ExpressionAtlasiP11438. baseline and differential.
GenevestigatoriP11438.

Interactioni

Protein-protein interaction databases

IntActiP11438. 17 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.
InParanoidiP11438.
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

« Hide

        10         20         30         40         50
MAAPGARRPL LLLLLAGLAH GASALFEVKN NGTTCIMASF SASFLTTYET
60 70 80 90 100
ANGSQIVNIS LPASAEVLKN GSSCGKENVS DPSLTITFGR GYLLTLNFTK
110 120 130 140 150
NTTRYSVQHM YFTYNLSDTE HFPNAISKEI YTMDSTTDIK ADINKAYRCV
160 170 180 190 200
SDIRVYMKNV TVVLRDATIQ AYLSSGNFSK EETHCTQDGP SPTTGPPSPS
210 220 230 240 250
PPLVPTNPTV SKYNVTGNNG TCLLASMALQ LNITYLKKDN KTVTRAFNIS
260 270 280 290 300
PNDTSSGSCG INLVTLKVEN KNRALELQFG MNASSSLFFL QGVRLNMTLP
310 320 330 340 350
DALVPTFSIS NHSLKALQAT VGNSYKCNTE EHIFVSKMLS LNVFSVQVQA
360 370 380 390 400
FKVDSDRFGS VEECVQDGNN MLIPIAVGGA LAGLVLIVLI AYLIGRKRSH

AGYQTI
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. 17 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.
InParanoidi P11438.
KOi K06528.
OMAi ENNMLIP.
OrthoDBi EOG7ZD1VH.
PhylomeDBi P11438.
TreeFami TF316339.

Miscellaneous databases

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

Gene expression databases

Bgeei P11438.
CleanExi MM_LAMP1.
ExpressionAtlasi P11438. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 130 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