Reviewed, UniProtKB/Swiss-Prot P13473 (LAMP2_HUMAN)

Names and origin

Protein names

Recommended name:
    Lysosome-associated membrane glycoprotein 2
      Short name=LAMP-2
Alternative name(s):
    CD107 antigen-like family member B
    CD_antigen=CD107b

Gene names

Name:

LAMP2

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	410 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	Implicated in tumor cell metastasis. May function in protection of the lysosomal membrane from autodigestion, maintenance of the acidic environment of the lysosome, adhesion when expressed on the cell surface (plasma membrane), and inter- and intracellular signal transduction.
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. Note: This protein shuttles between lysosomes, endosomes, and the plasma membrane.
Tissue specificity	Isoform LAMP-2A is highly expressed in placenta, lung and liver, less in kidney and pancreas, low in brain and skeletal muscle. Isoform LAMP-2B is highly expressed in skeletal muscle, less in brain, placenta, lung, kidney and pancreas, very low in liver.
Post-translational modification	O- and N-glycosylated; some of the 16 N-linked glycans are polylactosaminoglycans. Ref.10 Ref.11 Ref.12
Involvement in disease	Defects in LAMP2 are the cause of Danon disease (DAND) [MIM:300257]; also known as glycogen storage disease type 2B (GSD2B). DAND is a lysosomal glycogen storage disease characterized by the clinical triad of cardiomyopathy, vacuolar myopathy and mental retardation. It is often associated with an accumulation of glycogen in muscle and lysosomes. Ref.15 Ref.16
Sequence similarities	Belongs to the LAMP family.

Ontologies

Keywords
Cellular component	Cell membrane Endosome Lysosome Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation Glycogen storage disease
Domain	Signal Transmembrane
PTM	Disulfide bond Glycoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	glycogen metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	endosome membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW late endosome Inferred from direct assay. Source: MGI lysosomal membrane Inferred from direct assay. Source: MGI membrane fraction Inferred from direct assay. Source: MGI plasma membrane Inferred from Experiment. Source: Reactome platelet dense granule membrane Inferred from direct assay. Source: MGI
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform LAMP-2A (identifier: P13473-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform LAMP-2B (identifier: P13473-2)

The sequence of this isoform differs from the canonical sequence as follows:
     367-410: DCSADDDNFL...KHHHAGYEQF → ECSLDDDTIL...RKSYAGYQTL

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 28	28	Ref.1 Ref.7 Ref.8
	Chain	29 – 410	382	Lysosome-associated membrane glycoprotein 2		PRO_0000017110
Regions
	Topological domain	29 – 375	347	Lumenal Potential
	Transmembrane	376 – 399	24	Potential
	Topological domain	400 – 410	11	Cytoplasmic Potential
	Region	29 – 192	164	First lumenal domain
	Region	193 – 228	36	Hinge
	Region	229 – 375	147	Second lumenal domain
Amino acid modifications
	Glycosylation	32	1	N-linked (GlcNAc...) (polylactosaminoglycan) Ref.12 Ref.9
	Glycosylation	38	1	N-linked (GlcNAc...) (polylactosaminoglycan) Ref.12 Ref.9
	Glycosylation	49	1	N-linked (GlcNAc...) Ref.11 Ref.12
	Glycosylation	58	1	N-linked (GlcNAc...)
	Glycosylation	75	1	N-linked (GlcNAc...)
	Glycosylation	101	1	N-linked (GlcNAc...) Ref.11 Ref.12
	Glycosylation	123	1	N-linked (GlcNAc...) Ref.12
	Glycosylation	179	1	N-linked (GlcNAc...)
	Glycosylation	195	1	O-linked (GalNAc...) Ref.10
	Glycosylation	196	1	O-linked (GalNAc...) Ref.10
	Glycosylation	200	1	O-linked (GalNAc...) Ref.10
	Glycosylation	203	1	O-linked (GalNAc...) Ref.10
	Glycosylation	204	1	O-linked (GalNAc...) Ref.10
	Glycosylation	207	1	O-linked (GalNAc...); partial Ref.10
	Glycosylation	209	1	O-linked (GalNAc...); partial Ref.10
	Glycosylation	210	1	O-linked (GalNAc...) Ref.10
	Glycosylation	211	1	O-linked (GalNAc...) Ref.10
	Glycosylation	213	1	O-linked (GalNAc...); partial
	Glycosylation	229	1	N-linked (GlcNAc...)
	Glycosylation	242	1	N-linked (GlcNAc...)
	Glycosylation	257	1	N-linked (GlcNAc...) Ref.12
	Glycosylation	275	1	N-linked (GlcNAc...)
	Glycosylation	300	1	N-linked (GlcNAc...)
	Glycosylation	307	1	N-linked (GlcNAc...) (polylactosaminoglycan) Ref.9
	Glycosylation	317	1	N-linked (GlcNAc...)
	Glycosylation	356	1	N-linked (GlcNAc...)
	Disulfide bond	41 ↔ 79		By similarity
	Disulfide bond	153 ↔ 189		By similarity
	Disulfide bond	232 ↔ 265		By similarity
	Disulfide bond	331 ↔ 368		By similarity
Natural variations
	Alternative sequence	367 – 410	44	DCSAD…GYEQF → ECSLDDDTILIPIIVGAGLS GLIIVIVIAYVIGRRKSYAG YQTL in isoform LAMP-2B.		VSP_003044
	Natural variant	256	1	P → H: dbSNP rs1043878.		VAR_011992
	Natural variant	321	1	W → R in DAND. Ref.15 Ref.16		VAR_026230
Experimental info
	Sequence conflict	68	1	D → V in AAB41647. Ref.4
	Sequence conflict	111	1	I → N Ref.1
	Sequence conflict	111	1	I → N Ref.4
	Sequence conflict	143	1	I → Y in AAB41647. Ref.4
	Sequence conflict	220	1	A → P Ref.1
	Sequence conflict	220	1	A → P Ref.4
	Sequence conflict	234	1	L → R Ref.1
	Sequence conflict	234	1	L → R Ref.4
	Sequence conflict	322 – 326	5	DAPLG → MPP in AAA60383. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform LAMP-2A [UniParc]. Last modified October 1, 1996. Version 2. Checksum: 9E08E3B62D58F454	FASTA	410	44,961
	10 20 30 40 50 60 MVCFRLFPVP GSGLVLVCLV LGAVRSYALE LNLTDSENAT CLYAKWQMNF TVRYETTNKT 70 80 90 100 110 120 YKTVTISDHG TVTYNGSICG DDQNGPKIAV QFGPGFSWIA NFTKAASTYS IDSVSFSYNT 130 140 150 160 170 180 GDNTTFPDAE DKGILTVDEL LAIRIPLNDL FRCNSLSTLE KNDVVQHYWD VLVQAFVQNG 190 200 210 220 230 240 TVSTNEFLCD KDKTSTVAPT IHTTVPSPTT TPTPKEKPEA GTYSVNNGND TCLLATMGLQ 250 260 270 280 290 300 LNITQDKVAS VININPNTTH STGSCRSHTA LLRLNSSTIK YLDFVFAVKN ENRFYLKEVN 310 320 330 340 350 360 ISMYLVNGSV FSIANNNLSY WDAPLGSSYM CNKEQTVSVS GAFQINTFDL RVQPFNVTQG 370 380 390 400 410 KYSTAQDCSA DDDNFLVPIA VGAALAGVLI LVLLAYFIGL KHHHAGYEQF
	Isoform LAMP-2B. Checksum: 70B523369D40DEFA	FASTA	410	44,956
	10 20 30 40 50 60 MVCFRLFPVP GSGLVLVCLV LGAVRSYALE LNLTDSENAT CLYAKWQMNF TVRYETTNKT 70 80 90 100 110 120 YKTVTISDHG TVTYNGSICG DDQNGPKIAV QFGPGFSWIA NFTKAASTYS IDSVSFSYNT 130 140 150 160 170 180 GDNTTFPDAE DKGILTVDEL LAIRIPLNDL FRCNSLSTLE KNDVVQHYWD VLVQAFVQNG 190 200 210 220 230 240 TVSTNEFLCD KDKTSTVAPT IHTTVPSPTT TPTPKEKPEA GTYSVNNGND TCLLATMGLQ 250 260 270 280 290 300 LNITQDKVAS VININPNTTH STGSCRSHTA LLRLNSSTIK YLDFVFAVKN ENRFYLKEVN 310 320 330 340 350 360 ISMYLVNGSV FSIANNNLSY WDAPLGSSYM CNKEQTVSVS GAFQINTFDL RVQPFNVTQG 370 380 390 400 410 KYSTAQECSL DDDTILIPII VGAGLSGLII VIVIAYVIGR RKSYAGYQTL

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: 3198605] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LAMP-2A), PROTEIN SEQUENCE OF 29-64; 216-223 AND 238-256.
[2]	"Complete cDNA sequence of human lysosome-associated membrane protein-2." Konecki D.S., Foetisch K., Schlotter M., Lichter-Konecki U. Biochem. Biophys. Res. Commun. 205:1-5(1994) [PubMed: 7999007] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LAMP-2A). Tissue: Liver.
[3]	"An alternatively spliced form of the human lysosome-associated membrane protein-2 gene is expressed in a tissue-specific manner." Konecki D.S., Foetisch K., Zimmer K.P., Schlotter M., Lichter-Konecki U. Biochem. Biophys. Res. Commun. 215:757-767(1995) [PubMed: 7488019] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LAMP-2B).
[4]	"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: 8517882] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM LAMP-2A). Tissue: Placenta.
[5]	"The DNA sequence of the human X chromosome." Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R. Nature 434:325-337(2005) [PubMed: 15772651] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LAMP-2B). Tissue: Lymph.
[7]	"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: 2912382] [Abstract] Cited for: PROTEIN SEQUENCE OF 29-66.
[8]	"Signal peptide prediction based on analysis of experimentally verified cleavage sites." Zhang Z., Henzel W.J. Protein Sci. 13:2819-2824(2004) [PubMed: 15340161] [Abstract] Cited for: PROTEIN SEQUENCE OF 29-43.
[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: 2243102] [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: 8323299] [Abstract] Cited for: GLYCOSYLATION OF HINGE REGION, PROTEIN SEQUENCE OF 187-215.
[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: 12754519] [Abstract] Cited for: GLYCOSYLATION AT ASN-49 AND ASN-101.
[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: 16335952] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-32; ASN-38; ASN-49; ASN-101; ASN-123 AND ASN-257, MASS SPECTROMETRY. Tissue: Plasma.
[13]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[14]	"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: 19159218] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-101; ASN-123; ASN-257 AND ASN-356, MASS SPECTROMETRY. Tissue: Liver.
[15]	"Glycogen storage diseases presenting as hypertrophic cardiomyopathy." Arad M., Maron B.J., Gorham J.M., Johnson W.H. Jr., Saul J.P., Perez-Atayde A.R., Spirito P., Wright G.B., Kanter R.J., Seidman C.E., Seidman J.G. N. Engl. J. Med. 352:362-372(2005) [PubMed: 15673802] [Abstract] Cited for: VARIANT DAND ARG-321.
[16]	"Asymptomatic hyperCKemia in a case of Danon disease due to a missense mutation in Lamp-2 gene." Musumeci O., Rodolico C., Nishino I., Di Guardo G., Migliorato A., Aguennouz M., Mazzeo A., Messina C., Vita G., Toscano A. Neuromuscul. Disord. 15:409-411(2005) [PubMed: 15907287] [Abstract] Cited for: VARIANT DAND ARG-321.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases
EMBLGenBankDDBJ	J04183 mRNA. Translation: AAA60383.1. X77196 mRNA. Translation: CAA54416.1. U36336 mRNA. Translation: AAA91149.1. S79873 mRNA. Translation: AAB35426.1. L09717 , L09709, L09710, L09711, L09712, L09713, L09714, L09715, L09716 Genomic DNA. Translation: AAB41647.1. AC002476 Genomic DNA. Translation: AAB67314.1. AC002476 Genomic DNA. Translation: AAB67313.1. BC002965 mRNA. Translation: AAH02965.1.
IPI	IPI00009030. IPI00739827.
PIR	B31959. JC2414. JC4317.
RefSeq	NP_002285.1. NP_054701.1.
UniGene	Hs.496684
3D structure databases
ModBase	Search...
Protein family/group databases
TCDB	9.A.16.1.1. lysosomal protein import (LPI) family.
PTM databases
GlycoSuiteDB	P13473.
Proteomic databases
PRIDE	P13473.
Genome annotation databases
Ensembl	ENSG00000005893. Homo sapiens. [Contig view]
GeneID	3920.
Organism-specific databases
GeneCards	GC0XM119346.
H-InvDB	HIX0017024.
HGNC	HGNC:6501. LAMP2.
HPA	CAB005272.
MIM	300257. phenotype. 309060. gene.
Orphanet	34587. Glycogen storage disease due to LAMP-2 deficiency.
PharmGKB	PA30285.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	P13473.
OMA	P13473. DNFLVPI.
Enzyme and pathway databases
Reactome	REACT_604. Hemostasis.
Gene expression databases
ArrayExpress	P13473.
Bgee	P13473.
CleanEx	HS_LAMP2.
GermOnline	ENSG00000005893. Homo sapiens.
Family and domain databases
InterPro	IPR002000. Lamp. IPR018133. LAMP/LAMP-like_membrane. IPR018134. LAMP_CS. [Graphical view]
PANTHER	PTHR11506. Lamp. 1 hit.
Pfam	PF01299. Lamp. 1 hit. [Graphical view]
PRINTS	PR00336. LYSASSOCTDMP.
PROSITE	PS00310. LAMP_1. 1 hit. PS00311. LAMP_2. 1 hit. PS51407. LAMP_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	15399.
PMAP-CutDB	P13473.
SOURCE	Search...

Entry information

Entry name

LAMP2_HUMAN

Accession

Primary (citable) accession number: P13473
Secondary accession number(s): Q16641, Q96J30, Q99534

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	October 1, 1996
Last modified:	June 16, 2009
This is version 109 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)