Lysosome-associated membrane glycoprotein 1 precursor

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P11438 (LAMP1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 117. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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 names

Name:	Lamp1
Synonyms:	Lamp-1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	406 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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. Co-localizes 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 component	Cell membrane Endosome Lysosome Membrane
Domain	Signal Transmembrane Transmembrane helix
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	autophagic cell death Inferred from electronic annotation. Source: Compara autophagy Inferred from electronic annotation. Source: Compara spermatogenesis Traceable author statement PubMed 18689890. Source: MGI
Cellular_component	alveolar lamellar body Inferred from electronic annotation. Source: Compara dendrite Inferred from electronic annotation. Source: Compara endosome membrane Inferred from electronic annotation. Source: UniProtKB-SubCell external side of plasma membrane Inferred from direct assay PubMed 16973387. Source: MGI integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW lysosomal membrane Inferred from electronic annotation. Source: UniProtKB-SubCell lysosome Inferred from direct assay PubMed 10787428 PubMed 11486041 PubMed 11854359 PubMed 12925704 PubMed 14643301 PubMed 15006695 PubMed 15294975 PubMed 15588329 PubMed 16415873 PubMed 16542649 PubMed 18477453. 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: Compara sarcolemma Inferred from direct assay PubMed 14506282. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 24

Chain

25 – 406

382

Lysosome-associated membrane glycoprotein 1

PRO_0000017105

Regions

Topological domain

25 – 370

346

Lumenal Potential

Transmembrane

371 – 394

Helical; Potential

Topological domain

395 – 406

Cytoplasmic Potential

Region

25 – 188

164

First lumenal domain

Region

189 – 218

Hinge

Region

219 – 370

152

Second lumenal domain

Amino acid modifications

Glycosylation

N-linked (GlcNAc...) Potential

Glycosylation

N-linked (GlcNAc...) Potential

Glycosylation

N-linked (GlcNAc...) Potential

Glycosylation

N-linked (GlcNAc...) Potential

Glycosylation

N-linked (GlcNAc...) Potential

Glycosylation

N-linked (GlcNAc...) Ref.7 Ref.9

Glycosylation

101

N-linked (GlcNAc...) Ref.9

Glycosylation

115

N-linked (GlcNAc...) Potential

Glycosylation

159

N-linked (GlcNAc...) Ref.9

Glycosylation

177

N-linked (GlcNAc...) Ref.8 Ref.9

Glycosylation

214

N-linked (GlcNAc...) Potential

Glycosylation

219

N-linked (GlcNAc...) Potential

Glycosylation

232

N-linked (GlcNAc...) Potential

Glycosylation

240

N-linked (GlcNAc...) Potential

Glycosylation

252

N-linked (GlcNAc...) (high mannose) Ref.6

Glycosylation

282

N-linked (GlcNAc...) Potential

Glycosylation

296

N-linked (GlcNAc...) Potential

Glycosylation

311

N-linked (GlcNAc...) Potential

Disulfide bond

Disulfide bond

Disulfide bond

Disulfide bond

Experimental info

Sequence conflict

1 – 10

MAAPGARRPL → MRPPRAAAV Ref.2

Sequence conflict

25 – 26

LF → IP in AAA39411. Ref.4

Sequence conflict

385

V → I Ref.2

Sequence conflict

385

V → I Ref.4

Sequences

Sequence

Length

Mass (Da)

Tools

P11438 [UniParc].

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

FASTA

406

43,865

        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' referencesShow '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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
+	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.
IPI	IPI00469218.
PIR	A28067. A60534.
RefSeq	NP_034814.2. NM_010684.2.
UniGene	Mm.16716. Mm.463967.
3D structure databases
ProteinModelPortal	P11438.
SMR	P11438. Positions 207-366.
ModBase	Search...
Protein-protein interaction databases
IntAct	P11438. 2 interactions.
MINT	MINT-1858576.
PTM databases
PhosphoSite	P11438.
Proteomic databases
PaxDb	P11438.
PRIDE	P11438.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000033824; ENSMUSP00000033824; ENSMUSG00000031447.
GeneID	16783.
KEGG	mmu:16783.
Organism-specific databases
CTD	3916.
MGI	MGI:96745. Lamp1.
Phylogenomic databases
eggNOG	NOG301998.
HOGENOM	HOG000230942.
HOVERGEN	HBG052303.
KO	K06528.
OMA	ENNMLIP.
OrthoDB	EOG4MPHQD.
Gene expression databases
ArrayExpress	P11438.
Bgee	P11438.
CleanEx	MM_LAMP1.
Genevestigator	P11438.
GermOnline	ENSMUSG00000031447. Mus musculus.
Family and domain databases
InterPro	IPR018134. LAMP_CS. IPR002000. Lysosome-assoc_membr_glycop. [Graphical view]
PANTHER	PTHR11506. PTHR11506. 1 hit.
Pfam	PF01299. Lamp. 1 hit. [Graphical view]
PRINTS	PR00336. LYSASSOCTDMP.
PROSITE	PS00310. LAMP_1. 2 hits. PS00311. LAMP_2. 1 hit. PS51407. LAMP_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	Lamp1. mouse.
NextBio	290640.
SOURCE	Search...

Entry information

Entry name

LAMP1_MOUSE

Accession

Primary (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:	April 3, 2013
This is version 117 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents