Full text data of LAMP1
LAMP1
[Confidence: high (a blood group or CD marker)]
Lysosome-associated membrane glycoprotein 1; LAMP-1; Lysosome-associated membrane protein 1 (CD107 antigen-like family member A; CD107a; Flags: Precursor)
Lysosome-associated membrane glycoprotein 1; LAMP-1; Lysosome-associated membrane protein 1 (CD107 antigen-like family member A; CD107a; Flags: Precursor)
UniProt
P11279
ID LAMP1_HUMAN Reviewed; 417 AA.
AC P11279; Q8WU33; Q96I40; Q9BRD2; Q9NP13;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-SEP-2008, sequence version 3.
DT 22-JAN-2014, entry version 136.
DE RecName: Full=Lysosome-associated membrane glycoprotein 1;
DE Short=LAMP-1;
DE Short=Lysosome-associated membrane protein 1;
DE AltName: Full=CD107 antigen-like family member A;
DE AltName: CD_antigen=CD107a;
DE Flags: Precursor;
GN Name=LAMP1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 29-51; 117-131 AND
RP 164-198.
RX PubMed=3198605;
RA Fukuda M., Viitala J., Matteson J., Carlsson S.R.;
RT "Cloning of cDNAs encoding human lysosomal membrane glycoproteins, h-
RT lamp-1 and h-lamp-2. Comparison of their deduced amino acid
RT sequences.";
RL J. Biol. Chem. 263:18920-18928(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E.,
RA Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.,
RA Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R.,
RA Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S.,
RA Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M.,
RA Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J.,
RA Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E.,
RA Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L.,
RA Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J.,
RA Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S.,
RA Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J.,
RA Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M.,
RA King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A.,
RA Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S.,
RA Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I.,
RA Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S.,
RA Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A.,
RA Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L.,
RA Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M.,
RA Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Pancreas, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 29-59.
RX PubMed=2912382; DOI=10.1016/0003-9861(89)90597-3;
RA Mane S.M., Marzella L., Bainton D.F., Holt V.K., Cha Y.,
RA Hildreth J.E.K., August J.T.;
RT "Purification and characterization of human lysosomal membrane
RT glycoproteins.";
RL Arch. Biochem. Biophys. 268:360-378(1989).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 33-417, AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=3131762; DOI=10.1073/pnas.85.11.3743;
RA Viitala J., Carlsson S.R., Siebert P.D., Fukuda M.;
RT "Molecular cloning of cDNAs encoding lamp A, a human lysosomal
RT membrane glycoprotein with apparent Mr approximately equal to
RT 120,000.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:3743-3747(1988).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 62-417.
RC TISSUE=Placenta;
RX PubMed=8517882;
RA Sawada R., Jardine K.A., Fukuda M.;
RT "The genes of major lysosomal membrane glycoproteins, lamp-1 and lamp-
RT 2. 5'-flanking sequence of lamp-2 gene and comparison of exon
RT organization in two genes.";
RL J. Biol. Chem. 268:9014-9022(1993).
RN [8]
RP DISULFIDE BONDS.
RX PubMed=2584229;
RA Carlsson S.R., Fukuda M.;
RT "Structure of human lysosomal membrane glycoprotein 1. Assignment of
RT disulfide bonds and visualization of its domain arrangement.";
RL J. Biol. Chem. 264:20526-20531(1989).
RN [9]
RP POLYLACTOSAMINOGLYCANS.
RX PubMed=2243102;
RA Carlsson S.R., Fukuda M.;
RT "The polylactosaminoglycans of human lysosomal membrane glycoproteins
RT lamp-1 and lamp-2. Localization on the peptide backbones.";
RL J. Biol. Chem. 265:20488-20495(1990).
RN [10]
RP GLYCOSYLATION OF HINGE REGION, AND PROTEIN SEQUENCE OF 191-215.
RX PubMed=8323299; DOI=10.1006/abbi.1993.1322;
RA Carlsson S.R., Lycksell P.-O., Fukuda M.;
RT "Assignment of O-glycan attachment sites to the hinge-like regions of
RT human lysosomal membrane glycoproteins lamp-1 and lamp-2.";
RL Arch. Biochem. Biophys. 304:65-73(1993).
RN [11]
RP GLYCOSYLATION AT ASN-62 AND ASN-103.
RX PubMed=12754519; DOI=10.1038/nbt827;
RA Zhang H., Li X.-J., Martin D.B., Aebersold R.;
RT "Identification and quantification of N-linked glycoproteins using
RT hydrazide chemistry, stable isotope labeling and mass spectrometry.";
RL Nat. Biotechnol. 21:660-666(2003).
RN [12]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-103 AND ASN-249, AND MASS
RP SPECTROMETRY.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
RA Moore R.J., Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [13]
RP SUBCELLULAR LOCATION.
RX PubMed=16176980; DOI=10.1091/mbc.E05-03-0189;
RA Johansson M., Lehto M., Tanhuanpaeae K., Cover T.L., Olkkonen V.M.;
RT "The oxysterol-binding protein homologue ORP1L interacts with Rab7 and
RT alters functional properties of late endocytic compartments.";
RL Mol. Biol. Cell 16:5480-5492(2005).
RN [14]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RC TISSUE=Placenta;
RX PubMed=17897319; DOI=10.1111/j.1600-0854.2007.00643.x;
RA Schroeder B., Wrocklage C., Pan C., Jaeger R., Koesters B.,
RA Schaefer H., Elsaesser H.-P., Mann M., Hasilik A.;
RT "Integral and associated lysosomal membrane proteins.";
RL Traffic 8:1676-1686(2007).
RN [15]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-62; ASN-76; ASN-84;
RP ASN-103; ASN-121; ASN-130; ASN-249 AND ASN-293, AND MASS SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of
RT multiple enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Presents carbohydrate ligands to selectins. Also
CC implicated in tumor cell metastasis.
CC -!- INTERACTION:
CC Q5VZM2:RRAGB; NbExp=2; IntAct=EBI-2805407, EBI-993049;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein. Endosome membrane; Single-pass type I membrane protein.
CC Lysosome membrane; Single-pass type I membrane protein. Late
CC endosome. Note=This protein shuttles between lysosomes, endosomes,
CC and the plasma membrane. Colocalizes with OSBPL1A at the late
CC endosome.
CC -!- PTM: O- and N-glycosylated; some of the 18 N-linked glycans are
CC polylactosaminoglycans.
CC -!- SIMILARITY: Belongs to the LAMP family.
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DR EMBL; J04182; AAA60382.1; -; mRNA.
DR EMBL; AL136221; CAI13797.1; -; Genomic_DNA.
DR EMBL; CH471085; EAX09202.1; -; Genomic_DNA.
DR EMBL; BC006345; AAH06345.2; -; mRNA.
DR EMBL; BC007845; AAH07845.2; -; mRNA.
DR EMBL; BC021288; AAH21288.1; -; mRNA.
DR EMBL; BC093044; AAH93044.1; -; mRNA.
DR EMBL; J03263; AAA59524.1; -; mRNA.
DR EMBL; AH003113; AAF66141.1; -; Genomic_DNA.
DR PIR; A31959; A31959.
DR RefSeq; NP_005552.3; NM_005561.3.
DR UniGene; Hs.494419; -.
DR ProteinModelPortal; P11279; -.
DR IntAct; P11279; 16.
DR MINT; MINT-3007678; -.
DR STRING; 9606.ENSP00000333298; -.
DR TCDB; 9.A.16.1.1; the lysosomal protein import (lpi) family.
DR PhosphoSite; P11279; -.
DR UniCarbKB; P11279; -.
DR DMDM; 206729915; -.
DR PaxDb; P11279; -.
DR PRIDE; P11279; -.
DR DNASU; 3916; -.
DR Ensembl; ENST00000332556; ENSP00000333298; ENSG00000185896.
DR GeneID; 3916; -.
DR KEGG; hsa:3916; -.
DR UCSC; uc001vtm.1; human.
DR CTD; 3916; -.
DR GeneCards; GC13P113951; -.
DR H-InvDB; HIX0030831; -.
DR HGNC; HGNC:6499; LAMP1.
DR HPA; CAB004260; -.
DR HPA; HPA014750; -.
DR MIM; 153330; gene.
DR neXtProt; NX_P11279; -.
DR PharmGKB; PA30283; -.
DR eggNOG; NOG301998; -.
DR HOGENOM; HOG000230942; -.
DR HOVERGEN; HBG052303; -.
DR InParanoid; P11279; -.
DR KO; K06528; -.
DR OMA; GTACIMA; -.
DR OrthoDB; EOG7ZD1VH; -.
DR ChiTaRS; Lamp1; human.
DR GeneWiki; LAMP1; -.
DR GenomeRNAi; 3916; -.
DR NextBio; 15385; -.
DR PRO; PR:P11279; -.
DR ArrayExpress; P11279; -.
DR Bgee; P11279; -.
DR CleanEx; HS_LAMP1; -.
DR Genevestigator; P11279; -.
DR GO; GO:0097208; C:alveolar lamellar body; IEA:Ensembl.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR GO; GO:0005887; C:integral to plasma membrane; TAS:ProtInc.
DR GO; GO:0005770; C:late endosome; IDA:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; IDA:UniProtKB.
DR GO; GO:0042470; C:melanosome; IEA:Ensembl.
DR GO; GO:0005771; C:multivesicular body; IEA:Ensembl.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0042383; C:sarcolemma; IEA:Ensembl.
DR GO; GO:0048102; P:autophagic cell death; IEA:Ensembl.
DR GO; GO:0006914; P:autophagy; IEA:Ensembl.
DR InterPro; IPR018134; LAMP_CS.
DR InterPro; IPR002000; Lysosome-assoc_membr_glycop.
DR PANTHER; PTHR11506; PTHR11506; 1.
DR Pfam; PF01299; Lamp; 1.
DR PRINTS; PR00336; LYSASSOCTDMP.
DR PROSITE; PS00310; LAMP_1; 2.
DR PROSITE; PS00311; LAMP_2; 1.
DR PROSITE; PS51407; LAMP_3; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Complete proteome; Direct protein sequencing;
KW Disulfide bond; Endosome; Glycoprotein; Lysosome; Membrane;
KW Polymorphism; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1 28
FT CHAIN 29 417 Lysosome-associated membrane glycoprotein
FT 1.
FT /FTId=PRO_0000017104.
FT TOPO_DOM 29 382 Lumenal (Potential).
FT TRANSMEM 383 405 Helical; (Potential).
FT TOPO_DOM 406 417 Cytoplasmic (Potential).
FT REGION 29 194 First lumenal domain.
FT REGION 195 227 Hinge.
FT REGION 228 382 Second lumenal domain.
FT CARBOHYD 37 37 N-linked (GlcNAc...).
FT CARBOHYD 45 45 N-linked (GlcNAc...).
FT CARBOHYD 62 62 N-linked (GlcNAc...)
FT (polylactosaminoglycan).
FT CARBOHYD 76 76 N-linked (GlcNAc...).
FT CARBOHYD 84 84 N-linked (GlcNAc...).
FT CARBOHYD 103 103 N-linked (GlcNAc...).
FT CARBOHYD 107 107 N-linked (GlcNAc...).
FT CARBOHYD 121 121 N-linked (GlcNAc...)
FT (polylactosaminoglycan).
FT CARBOHYD 130 130 N-linked (GlcNAc...)
FT (polylactosaminoglycan).
FT CARBOHYD 165 165 N-linked (GlcNAc...).
FT CARBOHYD 181 181 N-linked (GlcNAc...).
FT CARBOHYD 197 197 O-linked (GalNAc...); partial.
FT CARBOHYD 199 199 O-linked (GalNAc...).
FT CARBOHYD 200 200 O-linked (GalNAc...).
FT CARBOHYD 207 207 O-linked (GalNAc...).
FT CARBOHYD 209 209 O-linked (GalNAc...).
FT CARBOHYD 211 211 O-linked (GalNAc...).
FT CARBOHYD 223 223 N-linked (GlcNAc...)
FT (polylactosaminoglycan).
FT CARBOHYD 228 228 N-linked (GlcNAc...)
FT (polylactosaminoglycan).
FT CARBOHYD 241 241 N-linked (GlcNAc...).
FT CARBOHYD 249 249 N-linked (GlcNAc...).
FT CARBOHYD 261 261 N-linked (GlcNAc...).
FT CARBOHYD 293 293 N-linked (GlcNAc...).
FT CARBOHYD 322 322 N-linked (GlcNAc...).
FT DISULFID 41 80
FT DISULFID 155 191
FT DISULFID 231 269
FT DISULFID 338 375
FT VARIANT 309 309 I -> T (in dbSNP:rs9577230).
FT /FTId=VAR_046450.
FT CONFLICT 2 2 A -> M (in Ref. 1; AAA60382).
FT CONFLICT 5 5 G -> R (in Ref. 1; AAA60382).
FT CONFLICT 16 26 LLLLLGLMHCA -> PVAAARPHALS (in Ref. 1;
FT AAA60382).
FT CONFLICT 33 40 VKNGNGTA -> MARGGRVR (in Ref. 6;
FT AAA59524).
FT CONFLICT 262 262 K -> T (in Ref. 7; AAF66141).
FT CONFLICT 377 377 Missing (in Ref. 7; AAF66141).
FT CONFLICT 382 382 M -> T (in Ref. 1; AAA60382, 6; AAA59524
FT and 7; AAF66141).
SQ SEQUENCE 417 AA; 44882 MW; 3E0A285744DD6588 CRC64;
MAAPGSARRP LLLLLLLLLL GLMHCASAAM FMVKNGNGTA CIMANFSAAF SVNYDTKSGP
KNMTFDLPSD ATVVLNRSSC GKENTSDPSL VIAFGRGHTL TLNFTRNATR YSVQLMSFVY
NLSDTHLFPN ASSKEIKTVE SITDIRADID KKYRCVSGTQ VHMNNVTVTL HDATIQAYLS
NSSFSRGETR CEQDRPSPTT APPAPPSPSP SPVPKSPSVD KYNVSGTNGT CLLASMGLQL
NLTYERKDNT TVTRLLNINP NKTSASGSCG AHLVTLELHS EGTTVLLFQF GMNASSSRFF
LQGIQLNTIL PDARDPAFKA ANGSLRALQA TVGNSYKCNA EEHVRVTKAF SVNIFKVWVQ
AFKVEGGQFG SVEECLLDEN SMLIPIAVGG ALAGLVLIVL IAYLVGRKRS HAGYQTI
//
ID LAMP1_HUMAN Reviewed; 417 AA.
AC P11279; Q8WU33; Q96I40; Q9BRD2; Q9NP13;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-SEP-2008, sequence version 3.
DT 22-JAN-2014, entry version 136.
DE RecName: Full=Lysosome-associated membrane glycoprotein 1;
DE Short=LAMP-1;
DE Short=Lysosome-associated membrane protein 1;
DE AltName: Full=CD107 antigen-like family member A;
DE AltName: CD_antigen=CD107a;
DE Flags: Precursor;
GN Name=LAMP1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 29-51; 117-131 AND
RP 164-198.
RX PubMed=3198605;
RA Fukuda M., Viitala J., Matteson J., Carlsson S.R.;
RT "Cloning of cDNAs encoding human lysosomal membrane glycoproteins, h-
RT lamp-1 and h-lamp-2. Comparison of their deduced amino acid
RT sequences.";
RL J. Biol. Chem. 263:18920-18928(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E.,
RA Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.,
RA Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R.,
RA Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S.,
RA Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M.,
RA Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J.,
RA Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E.,
RA Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L.,
RA Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J.,
RA Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S.,
RA Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J.,
RA Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M.,
RA King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A.,
RA Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S.,
RA Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I.,
RA Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S.,
RA Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A.,
RA Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L.,
RA Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M.,
RA Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Pancreas, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 29-59.
RX PubMed=2912382; DOI=10.1016/0003-9861(89)90597-3;
RA Mane S.M., Marzella L., Bainton D.F., Holt V.K., Cha Y.,
RA Hildreth J.E.K., August J.T.;
RT "Purification and characterization of human lysosomal membrane
RT glycoproteins.";
RL Arch. Biochem. Biophys. 268:360-378(1989).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 33-417, AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=3131762; DOI=10.1073/pnas.85.11.3743;
RA Viitala J., Carlsson S.R., Siebert P.D., Fukuda M.;
RT "Molecular cloning of cDNAs encoding lamp A, a human lysosomal
RT membrane glycoprotein with apparent Mr approximately equal to
RT 120,000.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:3743-3747(1988).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 62-417.
RC TISSUE=Placenta;
RX PubMed=8517882;
RA Sawada R., Jardine K.A., Fukuda M.;
RT "The genes of major lysosomal membrane glycoproteins, lamp-1 and lamp-
RT 2. 5'-flanking sequence of lamp-2 gene and comparison of exon
RT organization in two genes.";
RL J. Biol. Chem. 268:9014-9022(1993).
RN [8]
RP DISULFIDE BONDS.
RX PubMed=2584229;
RA Carlsson S.R., Fukuda M.;
RT "Structure of human lysosomal membrane glycoprotein 1. Assignment of
RT disulfide bonds and visualization of its domain arrangement.";
RL J. Biol. Chem. 264:20526-20531(1989).
RN [9]
RP POLYLACTOSAMINOGLYCANS.
RX PubMed=2243102;
RA Carlsson S.R., Fukuda M.;
RT "The polylactosaminoglycans of human lysosomal membrane glycoproteins
RT lamp-1 and lamp-2. Localization on the peptide backbones.";
RL J. Biol. Chem. 265:20488-20495(1990).
RN [10]
RP GLYCOSYLATION OF HINGE REGION, AND PROTEIN SEQUENCE OF 191-215.
RX PubMed=8323299; DOI=10.1006/abbi.1993.1322;
RA Carlsson S.R., Lycksell P.-O., Fukuda M.;
RT "Assignment of O-glycan attachment sites to the hinge-like regions of
RT human lysosomal membrane glycoproteins lamp-1 and lamp-2.";
RL Arch. Biochem. Biophys. 304:65-73(1993).
RN [11]
RP GLYCOSYLATION AT ASN-62 AND ASN-103.
RX PubMed=12754519; DOI=10.1038/nbt827;
RA Zhang H., Li X.-J., Martin D.B., Aebersold R.;
RT "Identification and quantification of N-linked glycoproteins using
RT hydrazide chemistry, stable isotope labeling and mass spectrometry.";
RL Nat. Biotechnol. 21:660-666(2003).
RN [12]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-103 AND ASN-249, AND MASS
RP SPECTROMETRY.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
RA Moore R.J., Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [13]
RP SUBCELLULAR LOCATION.
RX PubMed=16176980; DOI=10.1091/mbc.E05-03-0189;
RA Johansson M., Lehto M., Tanhuanpaeae K., Cover T.L., Olkkonen V.M.;
RT "The oxysterol-binding protein homologue ORP1L interacts with Rab7 and
RT alters functional properties of late endocytic compartments.";
RL Mol. Biol. Cell 16:5480-5492(2005).
RN [14]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RC TISSUE=Placenta;
RX PubMed=17897319; DOI=10.1111/j.1600-0854.2007.00643.x;
RA Schroeder B., Wrocklage C., Pan C., Jaeger R., Koesters B.,
RA Schaefer H., Elsaesser H.-P., Mann M., Hasilik A.;
RT "Integral and associated lysosomal membrane proteins.";
RL Traffic 8:1676-1686(2007).
RN [15]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-62; ASN-76; ASN-84;
RP ASN-103; ASN-121; ASN-130; ASN-249 AND ASN-293, AND MASS SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of
RT multiple enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Presents carbohydrate ligands to selectins. Also
CC implicated in tumor cell metastasis.
CC -!- INTERACTION:
CC Q5VZM2:RRAGB; NbExp=2; IntAct=EBI-2805407, EBI-993049;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein. Endosome membrane; Single-pass type I membrane protein.
CC Lysosome membrane; Single-pass type I membrane protein. Late
CC endosome. Note=This protein shuttles between lysosomes, endosomes,
CC and the plasma membrane. Colocalizes with OSBPL1A at the late
CC endosome.
CC -!- PTM: O- and N-glycosylated; some of the 18 N-linked glycans are
CC polylactosaminoglycans.
CC -!- SIMILARITY: Belongs to the LAMP family.
CC -----------------------------------------------------------------------
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CC Distributed under the Creative Commons Attribution-NoDerivs License
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DR EMBL; J04182; AAA60382.1; -; mRNA.
DR EMBL; AL136221; CAI13797.1; -; Genomic_DNA.
DR EMBL; CH471085; EAX09202.1; -; Genomic_DNA.
DR EMBL; BC006345; AAH06345.2; -; mRNA.
DR EMBL; BC007845; AAH07845.2; -; mRNA.
DR EMBL; BC021288; AAH21288.1; -; mRNA.
DR EMBL; BC093044; AAH93044.1; -; mRNA.
DR EMBL; J03263; AAA59524.1; -; mRNA.
DR EMBL; AH003113; AAF66141.1; -; Genomic_DNA.
DR PIR; A31959; A31959.
DR RefSeq; NP_005552.3; NM_005561.3.
DR UniGene; Hs.494419; -.
DR ProteinModelPortal; P11279; -.
DR IntAct; P11279; 16.
DR MINT; MINT-3007678; -.
DR STRING; 9606.ENSP00000333298; -.
DR TCDB; 9.A.16.1.1; the lysosomal protein import (lpi) family.
DR PhosphoSite; P11279; -.
DR UniCarbKB; P11279; -.
DR DMDM; 206729915; -.
DR PaxDb; P11279; -.
DR PRIDE; P11279; -.
DR DNASU; 3916; -.
DR Ensembl; ENST00000332556; ENSP00000333298; ENSG00000185896.
DR GeneID; 3916; -.
DR KEGG; hsa:3916; -.
DR UCSC; uc001vtm.1; human.
DR CTD; 3916; -.
DR GeneCards; GC13P113951; -.
DR H-InvDB; HIX0030831; -.
DR HGNC; HGNC:6499; LAMP1.
DR HPA; CAB004260; -.
DR HPA; HPA014750; -.
DR MIM; 153330; gene.
DR neXtProt; NX_P11279; -.
DR PharmGKB; PA30283; -.
DR eggNOG; NOG301998; -.
DR HOGENOM; HOG000230942; -.
DR HOVERGEN; HBG052303; -.
DR InParanoid; P11279; -.
DR KO; K06528; -.
DR OMA; GTACIMA; -.
DR OrthoDB; EOG7ZD1VH; -.
DR ChiTaRS; Lamp1; human.
DR GeneWiki; LAMP1; -.
DR GenomeRNAi; 3916; -.
DR NextBio; 15385; -.
DR PRO; PR:P11279; -.
DR ArrayExpress; P11279; -.
DR Bgee; P11279; -.
DR CleanEx; HS_LAMP1; -.
DR Genevestigator; P11279; -.
DR GO; GO:0097208; C:alveolar lamellar body; IEA:Ensembl.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR GO; GO:0005887; C:integral to plasma membrane; TAS:ProtInc.
DR GO; GO:0005770; C:late endosome; IDA:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; IDA:UniProtKB.
DR GO; GO:0042470; C:melanosome; IEA:Ensembl.
DR GO; GO:0005771; C:multivesicular body; IEA:Ensembl.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0042383; C:sarcolemma; IEA:Ensembl.
DR GO; GO:0048102; P:autophagic cell death; IEA:Ensembl.
DR GO; GO:0006914; P:autophagy; IEA:Ensembl.
DR InterPro; IPR018134; LAMP_CS.
DR InterPro; IPR002000; Lysosome-assoc_membr_glycop.
DR PANTHER; PTHR11506; PTHR11506; 1.
DR Pfam; PF01299; Lamp; 1.
DR PRINTS; PR00336; LYSASSOCTDMP.
DR PROSITE; PS00310; LAMP_1; 2.
DR PROSITE; PS00311; LAMP_2; 1.
DR PROSITE; PS51407; LAMP_3; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Complete proteome; Direct protein sequencing;
KW Disulfide bond; Endosome; Glycoprotein; Lysosome; Membrane;
KW Polymorphism; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1 28
FT CHAIN 29 417 Lysosome-associated membrane glycoprotein
FT 1.
FT /FTId=PRO_0000017104.
FT TOPO_DOM 29 382 Lumenal (Potential).
FT TRANSMEM 383 405 Helical; (Potential).
FT TOPO_DOM 406 417 Cytoplasmic (Potential).
FT REGION 29 194 First lumenal domain.
FT REGION 195 227 Hinge.
FT REGION 228 382 Second lumenal domain.
FT CARBOHYD 37 37 N-linked (GlcNAc...).
FT CARBOHYD 45 45 N-linked (GlcNAc...).
FT CARBOHYD 62 62 N-linked (GlcNAc...)
FT (polylactosaminoglycan).
FT CARBOHYD 76 76 N-linked (GlcNAc...).
FT CARBOHYD 84 84 N-linked (GlcNAc...).
FT CARBOHYD 103 103 N-linked (GlcNAc...).
FT CARBOHYD 107 107 N-linked (GlcNAc...).
FT CARBOHYD 121 121 N-linked (GlcNAc...)
FT (polylactosaminoglycan).
FT CARBOHYD 130 130 N-linked (GlcNAc...)
FT (polylactosaminoglycan).
FT CARBOHYD 165 165 N-linked (GlcNAc...).
FT CARBOHYD 181 181 N-linked (GlcNAc...).
FT CARBOHYD 197 197 O-linked (GalNAc...); partial.
FT CARBOHYD 199 199 O-linked (GalNAc...).
FT CARBOHYD 200 200 O-linked (GalNAc...).
FT CARBOHYD 207 207 O-linked (GalNAc...).
FT CARBOHYD 209 209 O-linked (GalNAc...).
FT CARBOHYD 211 211 O-linked (GalNAc...).
FT CARBOHYD 223 223 N-linked (GlcNAc...)
FT (polylactosaminoglycan).
FT CARBOHYD 228 228 N-linked (GlcNAc...)
FT (polylactosaminoglycan).
FT CARBOHYD 241 241 N-linked (GlcNAc...).
FT CARBOHYD 249 249 N-linked (GlcNAc...).
FT CARBOHYD 261 261 N-linked (GlcNAc...).
FT CARBOHYD 293 293 N-linked (GlcNAc...).
FT CARBOHYD 322 322 N-linked (GlcNAc...).
FT DISULFID 41 80
FT DISULFID 155 191
FT DISULFID 231 269
FT DISULFID 338 375
FT VARIANT 309 309 I -> T (in dbSNP:rs9577230).
FT /FTId=VAR_046450.
FT CONFLICT 2 2 A -> M (in Ref. 1; AAA60382).
FT CONFLICT 5 5 G -> R (in Ref. 1; AAA60382).
FT CONFLICT 16 26 LLLLLGLMHCA -> PVAAARPHALS (in Ref. 1;
FT AAA60382).
FT CONFLICT 33 40 VKNGNGTA -> MARGGRVR (in Ref. 6;
FT AAA59524).
FT CONFLICT 262 262 K -> T (in Ref. 7; AAF66141).
FT CONFLICT 377 377 Missing (in Ref. 7; AAF66141).
FT CONFLICT 382 382 M -> T (in Ref. 1; AAA60382, 6; AAA59524
FT and 7; AAF66141).
SQ SEQUENCE 417 AA; 44882 MW; 3E0A285744DD6588 CRC64;
MAAPGSARRP LLLLLLLLLL GLMHCASAAM FMVKNGNGTA CIMANFSAAF SVNYDTKSGP
KNMTFDLPSD ATVVLNRSSC GKENTSDPSL VIAFGRGHTL TLNFTRNATR YSVQLMSFVY
NLSDTHLFPN ASSKEIKTVE SITDIRADID KKYRCVSGTQ VHMNNVTVTL HDATIQAYLS
NSSFSRGETR CEQDRPSPTT APPAPPSPSP SPVPKSPSVD KYNVSGTNGT CLLASMGLQL
NLTYERKDNT TVTRLLNINP NKTSASGSCG AHLVTLELHS EGTTVLLFQF GMNASSSRFF
LQGIQLNTIL PDARDPAFKA ANGSLRALQA TVGNSYKCNA EEHVRVTKAF SVNIFKVWVQ
AFKVEGGQFG SVEECLLDEN SMLIPIAVGG ALAGLVLIVL IAYLVGRKRS HAGYQTI
//
MIM
153330
*RECORD*
*FIELD* NO
153330
*FIELD* TI
*153330 LYSOSOME-ASSOCIATED MEMBRANE PROTEIN 1; LAMP1
;;LYSOSOME-ASSOCIATED MEMBRANE PROTEIN A; LAMPA;;
read moreLYSOSOMAL MEMBRANE GLYCOPROTEIN, 120-KD; LGP120;;
CD107A
*FIELD* TX
CLONING
The 120-kD lysosomal membrane glycoprotein is an acidic, heavily
glycosylated membrane protein enriched in the lysosomal membrane. By
using an oligonucleotide probe corresponding to the amino terminus of
rat lgp120, Howe et al. (1988) isolated and characterized cDNA clones
containing the entire coding region. The deduced amino acid sequence
demonstrated that the rat LGP120 contains a putative signal peptide, 18
sites for N-linked glycosylation, a single membrane-spanning segment,
and a short (11 amino acid) cytosolic tail. LGP120 showed similarity to
2 other lysosomal membrane proteins and showed a high degree of
conservation in domain organization and primary structure with the
proteins in other species.
Viitala et al. (1988) reported the complete amino acid sequence for the
human lysosome-associated membrane glycoprotein with M(r) about 120,000.
The amino acid sequence, which was deduced from analysis of the cDNA,
contains 385 amino acid residues.
Mattei et al. (1990) noted that, although LAMP1 contains a functional
hinge region, it has a disulfide arrangement different from that
observed in members of the immunoglobulin superfamily and thus may
represent a novel family of membrane glycoproteins. The amino acid
sequence of LAMP1 is more homologous to corresponding molecules from
other species than it is to LAMP2 (309060). Furthermore, LAMP1 and LAMP2
are immunologically distinguishable from each other. Mattei et al.
(1990) proposed that LAMP1 and LAMP2 diverged relatively early in
evolution, but that LAMP1 (and possibly LAMP2) structures have been
strongly conserved.
GENE FUNCTION
Yogalingam et al. (2008) stated that LAMP1 is involved in lysosomal
exocytosis, movement of lysosomes along microtubules, and fusion of
phagosomes with lysosomes. They found that hematopoietic cells from
neuraminidase-1 (NEU1; 608272) -/- mice, a model of human sialidosis
(256550), showed increased plasma membrane expression of a
hypersialylated form of Lamp1 compared with wildtype mice. Yogalingam et
al. (2008) confirmed that Lamp1, but not other lysosomal membrane
proteins, was an endogenous Neu1 substrate. Accumulation of Lamp1 on the
plasma membrane of Neu1 -/- macrophages was associated with enhanced
exocytosis of lysosomal hydrolases. Overexpression of wildtype Lamp1 did
not fully recapitulate the effects of accumulated hypersialylated Lamp1
on lysosomal exocytosis. Reduced Lamp1 expression in both Neu1 -/- and
wildtype mouse macrophages via small interfering RNA reduced lysosomal
exocytosis, particularly in Neu1 -/- cells. Yogalingam et al. (2008)
found that fibroblasts from 2 patients with early-onset (type II)
sialidosis due to mutations that eliminated NEU1 activity showed
increased plasma membrane LAMP1 compared with normal fibroblasts. In
contrast, fibroblasts from a patient with late-onset (type I) sialidosis
with residual NEU1 activity exhibited a more normal LAMP1 distribution.
The culture medium of type II sialidosis fibroblasts also showed
elevated alpha-mannosidase activity (see 609458), suggesting increased
lysosomal exocytosis.
MAPPING
By means of in situ hybridization, Mattei et al. (1990) assigned the
LAMP1 gene to chromosome 13q34. A related gene, which may be a
pseudogene, mapped to chromosome 12p13.3. Hybridization of LAMP1 cDNA to
chromosome 12p13.3 was observed even when probes representing different
portions of the LAMP1 cDNA were used.
Using Southern hybridization in hamster/human hybrid cell panels,
Schleutker et al. (1991) confirmed the assignment of the LAMP1 gene to
chromosome 13. Furthermore, Schleutker et al. (1991) demonstrated
absence of genetic linkage of either LAMP1 or LAMP2 with Salla disease
(604369), a condition in which defective function of a lysosomal
membrane transporter protein is the probable cause of accumulation of
sialic acid in lysosomes.
Bermingham et al. (1996) demonstrated that the Lamp1 gene is located on
mouse chromosome 8. They could find no evidence that it is the site of
the mutation in mnd (motorneuron degeneration) mice.
*FIELD* RF
1. Bermingham, N. A.; Martin, J. E.; Fisher, E. M. C.: The mouse
lysosomal membrane protein 1 gene as a candidate for the motorneuron
degeneration (mnd) locus. Genomics 32: 266-271, 1996.
2. Howe, C. L.; Granger, B. L.; Hull, M.; Green, S. A.; Gabel, C.
A.; Helenius, A.; Mellman, I.: Derived protein sequence, oligosaccharides,
and membrane insertion of the 120-kDa lysosomal membrane glycoprotein
(lgp120): identification of a highly conserved family of lysosomal
membrane glycoproteins. Proc. Nat. Acad. Sci. 85: 7577-7581, 1988.
3. Mattei, M.-G.; Matterson, J.; Chen, J. W.; Williams, M. A.; Fukuda,
M.: Two human lysosomal membrane glycoproteins, h-lamp-1 and h-lamp-2,
are encoded by genes localized to chromosome 13q34 and chromosome
Xq24-25, respectively. J. Biol. Chem. 265: 7548-7551, 1990.
4. Schleutker, J.; Haataja, L.; Renlund, M.; Puhakka, L.; Viitala,
J.; Peltonen, L.; Aula, P.: Confirmation of the chromosomal localization
of human lamp genes and their exclusion as candidate genes for Salla
disease. Hum. Genet. 88: 95-97, 1991.
5. Viitala, J.; Carlsson, S. R.; Siebert, P. D.; Fukuda, M.: Molecular
cloning of cDNAs encoding lamp A, a human lysosomal membrane glycoprotein
with apparent M(r) about 120,000. Proc. Nat. Acad. Sci. 85: 3743-3747,
1988.
6. Yogalingam, G.; Bonten, E. J.; van de Vlekkert, D.; Hu, H.; Moshiach,
S.; Connell, S. A.; d'Azzo, A.: Neuraminidase 1 is a negative regulator
of lysosomal exocytosis. Dev. Cell 15: 74-86, 2008.
*FIELD* CN
Patricia A. Hartz - updated: 9/5/2008
*FIELD* CD
Victor A. McKusick: 6/28/1988
*FIELD* ED
mgross: 01/19/2012
mgross: 9/10/2008
terry: 9/5/2008
mgross: 12/27/1999
carol: 8/19/1998
mark: 3/25/1996
terry: 3/14/1996
carol: 2/7/1995
carol: 3/26/1992
supermim: 3/16/1992
carol: 2/29/1992
carol: 1/3/1992
carol: 7/2/1991
*RECORD*
*FIELD* NO
153330
*FIELD* TI
*153330 LYSOSOME-ASSOCIATED MEMBRANE PROTEIN 1; LAMP1
;;LYSOSOME-ASSOCIATED MEMBRANE PROTEIN A; LAMPA;;
read moreLYSOSOMAL MEMBRANE GLYCOPROTEIN, 120-KD; LGP120;;
CD107A
*FIELD* TX
CLONING
The 120-kD lysosomal membrane glycoprotein is an acidic, heavily
glycosylated membrane protein enriched in the lysosomal membrane. By
using an oligonucleotide probe corresponding to the amino terminus of
rat lgp120, Howe et al. (1988) isolated and characterized cDNA clones
containing the entire coding region. The deduced amino acid sequence
demonstrated that the rat LGP120 contains a putative signal peptide, 18
sites for N-linked glycosylation, a single membrane-spanning segment,
and a short (11 amino acid) cytosolic tail. LGP120 showed similarity to
2 other lysosomal membrane proteins and showed a high degree of
conservation in domain organization and primary structure with the
proteins in other species.
Viitala et al. (1988) reported the complete amino acid sequence for the
human lysosome-associated membrane glycoprotein with M(r) about 120,000.
The amino acid sequence, which was deduced from analysis of the cDNA,
contains 385 amino acid residues.
Mattei et al. (1990) noted that, although LAMP1 contains a functional
hinge region, it has a disulfide arrangement different from that
observed in members of the immunoglobulin superfamily and thus may
represent a novel family of membrane glycoproteins. The amino acid
sequence of LAMP1 is more homologous to corresponding molecules from
other species than it is to LAMP2 (309060). Furthermore, LAMP1 and LAMP2
are immunologically distinguishable from each other. Mattei et al.
(1990) proposed that LAMP1 and LAMP2 diverged relatively early in
evolution, but that LAMP1 (and possibly LAMP2) structures have been
strongly conserved.
GENE FUNCTION
Yogalingam et al. (2008) stated that LAMP1 is involved in lysosomal
exocytosis, movement of lysosomes along microtubules, and fusion of
phagosomes with lysosomes. They found that hematopoietic cells from
neuraminidase-1 (NEU1; 608272) -/- mice, a model of human sialidosis
(256550), showed increased plasma membrane expression of a
hypersialylated form of Lamp1 compared with wildtype mice. Yogalingam et
al. (2008) confirmed that Lamp1, but not other lysosomal membrane
proteins, was an endogenous Neu1 substrate. Accumulation of Lamp1 on the
plasma membrane of Neu1 -/- macrophages was associated with enhanced
exocytosis of lysosomal hydrolases. Overexpression of wildtype Lamp1 did
not fully recapitulate the effects of accumulated hypersialylated Lamp1
on lysosomal exocytosis. Reduced Lamp1 expression in both Neu1 -/- and
wildtype mouse macrophages via small interfering RNA reduced lysosomal
exocytosis, particularly in Neu1 -/- cells. Yogalingam et al. (2008)
found that fibroblasts from 2 patients with early-onset (type II)
sialidosis due to mutations that eliminated NEU1 activity showed
increased plasma membrane LAMP1 compared with normal fibroblasts. In
contrast, fibroblasts from a patient with late-onset (type I) sialidosis
with residual NEU1 activity exhibited a more normal LAMP1 distribution.
The culture medium of type II sialidosis fibroblasts also showed
elevated alpha-mannosidase activity (see 609458), suggesting increased
lysosomal exocytosis.
MAPPING
By means of in situ hybridization, Mattei et al. (1990) assigned the
LAMP1 gene to chromosome 13q34. A related gene, which may be a
pseudogene, mapped to chromosome 12p13.3. Hybridization of LAMP1 cDNA to
chromosome 12p13.3 was observed even when probes representing different
portions of the LAMP1 cDNA were used.
Using Southern hybridization in hamster/human hybrid cell panels,
Schleutker et al. (1991) confirmed the assignment of the LAMP1 gene to
chromosome 13. Furthermore, Schleutker et al. (1991) demonstrated
absence of genetic linkage of either LAMP1 or LAMP2 with Salla disease
(604369), a condition in which defective function of a lysosomal
membrane transporter protein is the probable cause of accumulation of
sialic acid in lysosomes.
Bermingham et al. (1996) demonstrated that the Lamp1 gene is located on
mouse chromosome 8. They could find no evidence that it is the site of
the mutation in mnd (motorneuron degeneration) mice.
*FIELD* RF
1. Bermingham, N. A.; Martin, J. E.; Fisher, E. M. C.: The mouse
lysosomal membrane protein 1 gene as a candidate for the motorneuron
degeneration (mnd) locus. Genomics 32: 266-271, 1996.
2. Howe, C. L.; Granger, B. L.; Hull, M.; Green, S. A.; Gabel, C.
A.; Helenius, A.; Mellman, I.: Derived protein sequence, oligosaccharides,
and membrane insertion of the 120-kDa lysosomal membrane glycoprotein
(lgp120): identification of a highly conserved family of lysosomal
membrane glycoproteins. Proc. Nat. Acad. Sci. 85: 7577-7581, 1988.
3. Mattei, M.-G.; Matterson, J.; Chen, J. W.; Williams, M. A.; Fukuda,
M.: Two human lysosomal membrane glycoproteins, h-lamp-1 and h-lamp-2,
are encoded by genes localized to chromosome 13q34 and chromosome
Xq24-25, respectively. J. Biol. Chem. 265: 7548-7551, 1990.
4. Schleutker, J.; Haataja, L.; Renlund, M.; Puhakka, L.; Viitala,
J.; Peltonen, L.; Aula, P.: Confirmation of the chromosomal localization
of human lamp genes and their exclusion as candidate genes for Salla
disease. Hum. Genet. 88: 95-97, 1991.
5. Viitala, J.; Carlsson, S. R.; Siebert, P. D.; Fukuda, M.: Molecular
cloning of cDNAs encoding lamp A, a human lysosomal membrane glycoprotein
with apparent M(r) about 120,000. Proc. Nat. Acad. Sci. 85: 3743-3747,
1988.
6. Yogalingam, G.; Bonten, E. J.; van de Vlekkert, D.; Hu, H.; Moshiach,
S.; Connell, S. A.; d'Azzo, A.: Neuraminidase 1 is a negative regulator
of lysosomal exocytosis. Dev. Cell 15: 74-86, 2008.
*FIELD* CN
Patricia A. Hartz - updated: 9/5/2008
*FIELD* CD
Victor A. McKusick: 6/28/1988
*FIELD* ED
mgross: 01/19/2012
mgross: 9/10/2008
terry: 9/5/2008
mgross: 12/27/1999
carol: 8/19/1998
mark: 3/25/1996
terry: 3/14/1996
carol: 2/7/1995
carol: 3/26/1992
supermim: 3/16/1992
carol: 2/29/1992
carol: 1/3/1992
carol: 7/2/1991