P11279 (LAMP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

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):
CD107 antigen-like family member A
CD_antigen=CD107a

Gene names

Name:

LAMP1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	417 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. Note: This protein shuttles between lysosomes, endosomes, and the plasma membrane. Co-localizes with OSBPL1A at the late endosome. Ref.13 Ref.14
Post-translational modification	O- and N-glycosylated; some of the 18 N-linked glycans are polylactosaminoglycans. Ref.10 Ref.11
Sequence similarities	Belongs to the LAMP family.

Ontologies

Keywords
Cellular component	Cell membrane Endosome Lysosome Membrane
Coding sequence diversity	Polymorphism
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
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 electronic annotation. Source: Compara integral to plasma membrane Traceable author statement PubMed 3174652. Source: ProtInc late endosome Inferred from direct assay PubMed 15052268PubMed 15792797. Source: UniProtKB lysosomal membrane Inferred from electronic annotation. Source: UniProtKB-SubCell lysosome Inferred from direct assay PubMed 15052268PubMed 15613468. Source: UniProtKB melanosome Inferred from electronic annotation. Source: Compara multivesicular body Inferred from electronic annotation. Source: Compara neuronal cell body Inferred from electronic annotation. Source: Compara sarcolemma Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 28	28	Ref.1 Ref.5
	Chain	29 – 417	389	Lysosome-associated membrane glycoprotein 1		PRO_0000017104
Regions
	Topological domain	29 – 382	354	Lumenal Potential
	Transmembrane	383 – 405	23	Helical; Potential
	Topological domain	406 – 417	12	Cytoplasmic Potential
	Region	29 – 194	166	First lumenal domain
	Region	195 – 227	33	Hinge
	Region	228 – 382	155	Second lumenal domain
Amino acid modifications
	Glycosylation	37	1	N-linked (GlcNAc...)
	Glycosylation	45	1	N-linked (GlcNAc...)
	Glycosylation	62	1	N-linked (GlcNAc...) (polylactosaminoglycan) Ref.9 Ref.11 Ref.15
	Glycosylation	76	1	N-linked (GlcNAc...) Ref.9 Ref.15
	Glycosylation	84	1	N-linked (GlcNAc...) Ref.15
	Glycosylation	103	1	N-linked (GlcNAc...) Ref.11 Ref.12 Ref.15
	Glycosylation	107	1	N-linked (GlcNAc...)
	Glycosylation	121	1	N-linked (GlcNAc...) (polylactosaminoglycan) Ref.9 Ref.15
	Glycosylation	130	1	N-linked (GlcNAc...) (polylactosaminoglycan) Ref.9 Ref.15
	Glycosylation	165	1	N-linked (GlcNAc...) Ref.9
	Glycosylation	181	1	N-linked (GlcNAc...) Ref.9
	Glycosylation	197	1	O-linked (GalNAc...); partial Ref.10
	Glycosylation	199	1	O-linked (GalNAc...) Ref.10
	Glycosylation	200	1	O-linked (GalNAc...) Ref.10
	Glycosylation	207	1	O-linked (GalNAc...) Ref.10
	Glycosylation	209	1	O-linked (GalNAc...) Ref.10
	Glycosylation	211	1	O-linked (GalNAc...) Ref.10
	Glycosylation	223	1	N-linked (GlcNAc...) (polylactosaminoglycan) Ref.9
	Glycosylation	228	1	N-linked (GlcNAc...) (polylactosaminoglycan) Ref.9
	Glycosylation	241	1	N-linked (GlcNAc...)
	Glycosylation	249	1	N-linked (GlcNAc...) Ref.12 Ref.15
	Glycosylation	261	1	N-linked (GlcNAc...) Ref.9
	Glycosylation	293	1	N-linked (GlcNAc...) Ref.15
	Glycosylation	322	1	N-linked (GlcNAc...)
	Disulfide bond	41 ↔ 80		Ref.8
	Disulfide bond	155 ↔ 191		Ref.8
	Disulfide bond	231 ↔ 269		Ref.8
	Disulfide bond	338 ↔ 375		Ref.8
Natural variations
	Natural variant	309	1	I → T. Corresponds to variant rs9577230 [ dbSNP | Ensembl ].		VAR_046450
Experimental info
	Sequence conflict	2	1	A → M in AAA60382. Ref.1
	Sequence conflict	5	1	G → R in AAA60382. Ref.1
	Sequence conflict	16 – 26	11	LLLLLGLMHCA → PVAAARPHALS in AAA60382. Ref.1
	Sequence conflict	33 – 40	8	VKNGNGTA → MARGGRVR in AAA59524. Ref.6
	Sequence conflict	262	1	K → T in AAF66141. Ref.7
	Sequence conflict	377	1	Missing in AAF66141. Ref.7
	Sequence conflict	382	1	M → T in AAA60382. Ref.1
	Sequence conflict	382	1	M → T in AAA59524. Ref.6
	Sequence conflict	382	1	M → T in AAF66141. Ref.7

Sequences

	Sequence		Length	Mass (Da)
	P11279 [UniParc]. Last modified September 23, 2008. Version 3. Checksum: 3E0A285744DD6588	FASTA	417	44,882
	10 20 30 40 50 60 MAAPGSARRP LLLLLLLLLL GLMHCASAAM FMVKNGNGTA CIMANFSAAF SVNYDTKSGP 70 80 90 100 110 120 KNMTFDLPSD ATVVLNRSSC GKENTSDPSL VIAFGRGHTL TLNFTRNATR YSVQLMSFVY 130 140 150 160 170 180 NLSDTHLFPN ASSKEIKTVE SITDIRADID KKYRCVSGTQ VHMNNVTVTL HDATIQAYLS 190 200 210 220 230 240 NSSFSRGETR CEQDRPSPTT APPAPPSPSP SPVPKSPSVD KYNVSGTNGT CLLASMGLQL 250 260 270 280 290 300 NLTYERKDNT TVTRLLNINP NKTSASGSCG AHLVTLELHS EGTTVLLFQF GMNASSSRFF 310 320 330 340 350 360 LQGIQLNTIL PDARDPAFKA ANGSLRALQA TVGNSYKCNA EEHVRVTKAF SVNIFKVWVQ 370 380 390 400 410 AFKVEGGQFG SVEECLLDEN SMLIPIAVGG ALAGLVLIVL IAYLVGRKRS HAGYQTI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of cDNAs encoding human lysosomal membrane glycoproteins, h-lamp-1 and h-lamp-2. Comparison of their deduced amino acid sequences." Fukuda M., Viitala J., Matteson J., Carlsson S.R. J. Biol. Chem. 263:18920-18928(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 29-51; 117-131 AND 164-198.
[2]	"The DNA sequence and analysis of human chromosome 13." Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T. Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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]. Tissue: Brain, Pancreas and Testis.
[5]	"Purification and characterization of human lysosomal membrane glycoproteins." Mane S.M., Marzella L., Bainton D.F., Holt V.K., Cha Y., Hildreth J.E.K., August J.T. Arch. Biochem. Biophys. 268:360-378(1989) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 29-59.
[6]	"Molecular cloning of cDNAs encoding lamp A, a human lysosomal membrane glycoprotein with apparent Mr approximately equal to 120,000." Viitala J., Carlsson S.R., Siebert P.D., Fukuda M. Proc. Natl. Acad. Sci. U.S.A. 85:3743-3747(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 33-417, PARTIAL PROTEIN SEQUENCE.
[7]	"The genes of major lysosomal membrane glycoproteins, lamp-1 and lamp-2. 5'-flanking sequence of lamp-2 gene and comparison of exon organization in two genes." Sawada R., Jardine K.A., Fukuda M. J. Biol. Chem. 268:9014-9022(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 62-417. Tissue: Placenta.
[8]	"Structure of human lysosomal membrane glycoprotein 1. Assignment of disulfide bonds and visualization of its domain arrangement." Carlsson S.R., Fukuda M. J. Biol. Chem. 264:20526-20531(1989) [PubMed] [Europe PMC] [Abstract] Cited for: DISULFIDE BONDS.
[9]	"The polylactosaminoglycans of human lysosomal membrane glycoproteins lamp-1 and lamp-2. Localization on the peptide backbones." Carlsson S.R., Fukuda M. J. Biol. Chem. 265:20488-20495(1990) [PubMed] [Europe PMC] [Abstract] Cited for: POLYLACTOSAMINOGLYCANS.
[10]	"Assignment of O-glycan attachment sites to the hinge-like regions of human lysosomal membrane glycoproteins lamp-1 and lamp-2." Carlsson S.R., Lycksell P.-O., Fukuda M. Arch. Biochem. Biophys. 304:65-73(1993) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION OF HINGE REGION, PROTEIN SEQUENCE OF 191-215.
[11]	"Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry." Zhang H., Li X.-J., Martin D.B., Aebersold R. Nat. Biotechnol. 21:660-666(2003) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION AT ASN-62 AND ASN-103.
[12]	"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry." Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D. J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-103 AND ASN-249, MASS SPECTROMETRY. Tissue: Plasma.
[13]	"The oxysterol-binding protein homologue ORP1L interacts with Rab7 and alters functional properties of late endocytic compartments." Johansson M., Lehto M., Tanhuanpaeae K., Cover T.L., Olkkonen V.M. Mol. Biol. Cell 16:5480-5492(2005) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[14]	"Integral and associated lysosomal membrane proteins." Schroeder B., Wrocklage C., Pan C., Jaeger R., Koesters B., Schaefer H., Elsaesser H.-P., Mann M., Hasilik A. Traffic 8:1676-1686(2007) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. Tissue: Placenta.
[15]	"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry." Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H. J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-62; ASN-76; ASN-84; ASN-103; ASN-121; ASN-130; ASN-249 AND ASN-293, MASS SPECTROMETRY. Tissue: Liver.
[16]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	J04182 mRNA. Translation: AAA60382.1. AL136221 Genomic DNA. Translation: CAI13797.1. CH471085 Genomic DNA. Translation: EAX09202.1. BC006345 mRNA. Translation: AAH06345.2. BC007845 mRNA. Translation: AAH07845.2. BC021288 mRNA. Translation: AAH21288.1. BC093044 mRNA. Translation: AAH93044.1. J03263 mRNA. Translation: AAA59524.1. AH003113 Genomic DNA. Translation: AAF66141.1.
IPI	IPI00884105.
PIR	A31959.
RefSeq	NP_005552.3. NM_005561.3.
UniGene	Hs.494419.
3D structure databases
ProteinModelPortal	P11279.
SMR	P11279. Positions 216-377.
ModBase	Search...
Protein-protein interaction databases
IntAct	P11279. 9 interactions.
MINT	MINT-3007678.
STRING	9606.ENSP00000333298.
PTM databases
GlycoSuiteDB	P11279.
PhosphoSite	P11279.
Polymorphism databases
DMDM	206729915.
Proteomic databases
PaxDb	P11279.
PRIDE	P11279.
Protocols and materials databases
DNASU	3916.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000332556; ENSP00000333298; ENSG00000185896.
GeneID	3916.
KEGG	hsa:3916.
UCSC	uc001vtm.1. human.
Organism-specific databases
CTD	3916.
GeneCards	GC13P113951.
H-InvDB	HIX0030831.
HGNC	HGNC:6499. LAMP1.
HPA	CAB004260. HPA014750.
MIM	153330. gene.
neXtProt	NX_P11279.
PharmGKB	PA30283.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG301998.
HOGENOM	HOG000230942.
HOVERGEN	HBG052303.
InParanoid	P11279.
KO	K06528.
OMA	ENNMLIP.
OrthoDB	EOG4MPHQD.
Gene expression databases
ArrayExpress	P11279.
Bgee	P11279.
CleanEx	HS_LAMP1.
Genevestigator	P11279.
GermOnline	ENSG00000185896. Homo sapiens.
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. human.
GenomeRNAi	3916.
NextBio	15385.
SOURCE	Search...

Entry information

Entry name

LAMP1_HUMAN

Accession

Primary (citable) accession number: P11279
Secondary accession number(s): Q8WU33 , Q96I40, Q9BRD2, Q9NP13

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	September 23, 2008
Last modified:	April 3, 2013
This is version 130 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.