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P11438 (LAMP1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Lamp1
Synonyms:Lamp-1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length406 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subcellular location

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.

Post-translational modification

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

Sequence similarities

Belongs to the LAMP family.

Ontologies

Keywords
   Cellular componentCell membrane
Endosome
Lysosome
Membrane
   DomainSignal
Transmembrane
Transmembrane helix
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processautophagic cell death

Inferred from electronic annotation. Source: Ensembl

autophagy

Inferred from electronic annotation. Source: Ensembl

protein stabilization

Inferred from mutant phenotype PubMed 22641697. Source: UniProt

spermatogenesis

Traceable author statement PubMed 18689890. Source: MGI

   Cellular_componentalveolar lamellar body

Inferred from electronic annotation. Source: Ensembl

cell surface

Inferred from direct assay PubMed 16674683. Source: BHF-UCL

cytolytic granule

Inferred from direct assay PubMed 19915045. Source: MGI

cytoplasm

Inferred from sequence orthology PubMed 21266579. Source: MGI

dendrite

Inferred from electronic annotation. Source: Ensembl

endosome

Inferred from direct assay PubMed 10787428. Source: MGI

endosome membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

external side of plasma membrane

Inferred from direct assay PubMed 16973387. Source: MGI

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

late endosome

Inferred from direct assay PubMed 12446704PubMed 14668490PubMed 15294975PubMed 16415873PubMed 17620357PubMed 18477453. Source: MGI

lysosome

Inferred from direct assay PubMed 10787428PubMed 11486041PubMed 11854359PubMed 12925704PubMed 14643301PubMed 15006695PubMed 15294975PubMed 15588329PubMed 16415873PubMed 16542649PubMed 18477453PubMed 23926254PubMed 24029230PubMed 24035762. Source: MGI

melanosome

Inferred from direct assay PubMed 11266470. Source: MGI

multivesicular body

Inferred from direct assay PubMed 11854359. Source: MGI

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

phagolysosome membrane

Inferred from direct assay PubMed 23395172. Source: MGI

sarcolemma

Inferred from direct assay PubMed 14506282. Source: MGI

vesicle

Inferred from direct assay PubMed 10787428. Source: MGI

   Molecular_functionprotein binding

Inferred from physical interaction PubMed 16674683. Source: BHF-UCL

protein domain specific binding

Inferred from physical interaction PubMed 22641697. Source: UniProt

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424
Chain25 – 406382Lysosome-associated membrane glycoprotein 1
PRO_0000017105

Regions

Topological domain25 – 370346Lumenal Potential
Transmembrane371 – 39424Helical; Potential
Topological domain395 – 40612Cytoplasmic Potential
Region25 – 188164First lumenal domain
Region189 – 21830Hinge
Region219 – 370152Second lumenal domain

Amino acid modifications

Glycosylation311N-linked (GlcNAc...) Potential
Glycosylation521N-linked (GlcNAc...) Potential
Glycosylation581N-linked (GlcNAc...) Potential
Glycosylation701N-linked (GlcNAc...) Potential
Glycosylation781N-linked (GlcNAc...) Potential
Glycosylation971N-linked (GlcNAc...) Ref.7 Ref.9
Glycosylation1011N-linked (GlcNAc...) Ref.9
Glycosylation1151N-linked (GlcNAc...) Potential
Glycosylation1591N-linked (GlcNAc...) Ref.9
Glycosylation1771N-linked (GlcNAc...) Ref.8 Ref.9
Glycosylation2141N-linked (GlcNAc...) Potential
Glycosylation2191N-linked (GlcNAc...) Potential
Glycosylation2321N-linked (GlcNAc...) Potential
Glycosylation2401N-linked (GlcNAc...) Potential
Glycosylation2521N-linked (GlcNAc...) (high mannose) Ref.6
Glycosylation2821N-linked (GlcNAc...) Potential
Glycosylation2961N-linked (GlcNAc...) Potential
Glycosylation3111N-linked (GlcNAc...) Potential
Disulfide bond35 ↔ 74 Ref.5
Disulfide bond149 ↔ 185 Ref.5
Disulfide bond222 ↔ 259 Ref.5
Disulfide bond327 ↔ 364 Ref.5

Experimental info

Sequence conflict1 – 1010MAAPGARRPL → MRPPRAAAV Ref.2
Sequence conflict25 – 262LF → IP in AAA39411. Ref.4
Sequence conflict3851V → I Ref.2
Sequence conflict3851V → I Ref.4

Sequences

Sequence LengthMass (Da)Tools
P11438 [UniParc].

Last modified August 1, 1990. Version 2.
Checksum: C1BD373548BB9655

FASTA40643,865
        10         20         30         40         50         60 
MAAPGARRPL LLLLLAGLAH GASALFEVKN NGTTCIMASF SASFLTTYET ANGSQIVNIS 

        70         80         90        100        110        120 
LPASAEVLKN GSSCGKENVS DPSLTITFGR GYLLTLNFTK NTTRYSVQHM YFTYNLSDTE 

       130        140        150        160        170        180 
HFPNAISKEI YTMDSTTDIK ADINKAYRCV SDIRVYMKNV TVVLRDATIQ AYLSSGNFSK 

       190        200        210        220        230        240 
EETHCTQDGP SPTTGPPSPS PPLVPTNPTV SKYNVTGNNG TCLLASMALQ LNITYLKKDN 

       250        260        270        280        290        300 
KTVTRAFNIS PNDTSSGSCG INLVTLKVEN KNRALELQFG MNASSSLFFL QGVRLNMTLP 

       310        320        330        340        350        360 
DALVPTFSIS NHSLKALQAT VGNSYKCNTE EHIFVSKMLS LNVFSVQVQA FKVDSDRFGS 

       370        380        390        400 
VEECVQDGNN MLIPIAVGGA LAGLVLIVLI AYLIGRKRSH AGYQTI 

« Hide

References

« Hide 'large scale' references
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M32015 mRNA. Translation: AAA39428.1.
M25244 mRNA. Translation: AAA39869.1.
BC049097 mRNA. Translation: AAH49097.1.
J03881 mRNA. Translation: AAA39411.1.
CCDSCCDS22106.1.
PIRA28067.
A60534.
RefSeqNP_034814.2. NM_010684.2.
UniGeneMm.16716.

3D structure databases

ProteinModelPortalP11438.
SMRP11438. Positions 207-366.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP11438. 10 interactions.
MINTMINT-1858576.

PTM databases

PhosphoSiteP11438.

Proteomic databases

MaxQBP11438.
PaxDbP11438.
PRIDEP11438.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000033824; ENSMUSP00000033824; ENSMUSG00000031447.
GeneID16783.
KEGGmmu:16783.
UCSCuc009kxa.1. mouse.

Organism-specific databases

CTD3916.
MGIMGI:96745. Lamp1.

Phylogenomic databases

eggNOGNOG301998.
HOGENOMHOG000230942.
HOVERGENHBG052303.
KOK06528.
OMAENNMLIP.
OrthoDBEOG7ZD1VH.
PhylomeDBP11438.
TreeFamTF316339.

Gene expression databases

ArrayExpressP11438.
BgeeP11438.
CleanExMM_LAMP1.
GenevestigatorP11438.

Family and domain databases

InterProIPR018134. LAMP_CS.
IPR002000. Lysosome-assoc_membr_glycop.
[Graphical view]
PANTHERPTHR11506. PTHR11506. 1 hit.
PfamPF01299. Lamp. 1 hit.
[Graphical view]
PRINTSPR00336. LYSASSOCTDMP.
PROSITEPS00310. LAMP_1. 2 hits.
PS00311. LAMP_2. 1 hit.
PS51407. LAMP_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSLamp1. mouse.
NextBio290640.
PROP11438.
SOURCESearch...

Entry information

Entry nameLAMP1_MOUSE
AccessionPrimary (citable) accession number: P11438
Secondary accession number(s): Q62020
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: August 1, 1990
Last modified: July 9, 2014
This is version 128 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot