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Lysosome-associated membrane glycoprotein 1 (LAMP-1) (Lysosome-associated membrane protein 1) (120 kDa lysosomal membrane glycoprotein) (CD107 antigen-like family member A) (LGP-120) (Lysosomal membrane glycoprotein A) (LGP-A) (P2B) (CD antigen CD107a)

 LAMP1_MOUSE             Reviewed;         406 AA.
P11438; Q62020;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
01-AUG-1990, sequence version 2.
07-JUN-2017, entry version 153.
RecName: Full=Lysosome-associated membrane glycoprotein 1;
Short=LAMP-1;
Short=Lysosome-associated membrane protein 1;
AltName: Full=120 kDa lysosomal membrane glycoprotein;
AltName: Full=CD107 antigen-like family member A;
AltName: Full=LGP-120;
AltName: Full=Lysosomal membrane glycoprotein A;
Short=LGP-A;
AltName: Full=P2B;
AltName: CD_antigen=CD107a;
Flags: Precursor;
Name=Lamp1; Synonyms=Lamp-1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2142158;
Granger B.L., Green S.A., Gabel C.A., Howe C.L., Mellman I.,
Helenius A.;
"Characterization and cloning of lgp110, a lysosomal membrane
glycoprotein from mouse and rat cells.";
J. Biol. Chem. 265:12036-12043(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2676155;
Heffernan M., Yousefi S., Dennis J.W.;
"Molecular characterization of P2B/LAMP-1, a major protein target of a
metastasis-associated oligosaccharide structure.";
Cancer Res. 49:6077-6084(1989).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 25-406, AND PARTIAL PROTEIN SEQUENCE.
PubMed=3379044;
Chen J.W., Cha Y., Yuksel K.U., Gracy R.W., August J.T.;
"Isolation and sequencing of a cDNA clone encoding lysosomal membrane
glycoprotein mouse LAMP-1. Sequence similarity to proteins bearing
onco-differentiation antigens.";
J. Biol. Chem. 263:8754-8758(1988).
[5]
DISULFIDE BONDS.
PubMed=2332434;
Arterburn L.M., Earles B.J., August J.T.;
"The disulfide structure of mouse lysosome-associated membrane protein
1.";
J. Biol. Chem. 265:7419-7423(1990).
[6]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-252.
TISSUE=Epidermis;
PubMed=16170054; DOI=10.1074/mcp.M500203-MCP200;
Uematsu R., Furukawa J., Nakagawa H., Shinohara Y., Deguchi K.,
Monde K., Nishimura S.;
"High throughput quantitative glycomics and glycoform-focused
proteomics of murine dermis and epidermis.";
Mol. Cell. Proteomics 4:1977-1989(2005).
[7]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-97.
STRAIN=C57BL/6J; TISSUE=Plasma;
PubMed=16944957; DOI=10.1021/pr060186m;
Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J.,
Gevaert K.;
"Proteome-wide characterization of N-glycosylation events by diagonal
chromatography.";
J. Proteome Res. 5:2438-2447(2006).
[8]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-177.
TISSUE=Myoblast;
PubMed=19656770; DOI=10.1074/mcp.M900195-MCP200;
Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I.,
Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E.,
Wollscheid B.;
"The mouse C2C12 myoblast cell surface N-linked glycoproteome:
identification, glycosite occupancy, and membrane orientation.";
Mol. Cell. Proteomics 8:2555-2569(2009).
[9]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-97; ASN-101; ASN-159 AND
ASN-177.
PubMed=19349973; DOI=10.1038/nbt.1532;
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
Schiess R., Aebersold R., Watts J.D.;
"Mass-spectrometric identification and relative quantification of N-
linked cell surface glycoproteins.";
Nat. Biotechnol. 27:378-386(2009).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Presents carbohydrate ligands to selectins. Also
implicated in tumor cell metastasis.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P05300}; Single-pass type I membrane
protein {ECO:0000250|UniProtKB:P11279}. Endosome membrane
{ECO:0000250|UniProtKB:P11279}; Single-pass type I membrane
protein {ECO:0000250|UniProtKB:P11279}. Lysosome membrane
{ECO:0000250|UniProtKB:P11279}; Single-pass type I membrane
protein {ECO:0000250|UniProtKB:P11279}. Late endosome
{ECO:0000250|UniProtKB:P11279}. Note=This protein shuttles between
lysosomes, endosomes, and the plasma membrane. Colocalizes with
OSBPL1A at the late endosome. {ECO:0000250|UniProtKB:P05300,
ECO:0000250|UniProtKB:P11279}.
-!- PTM: O- and N-glycosylated; some of the N-glycans attached to
LAMP-1 are polylactosaminoglycans. {ECO:0000250}.
-!- SIMILARITY: Belongs to the LAMP family. {ECO:0000255|PROSITE-
ProRule:PRU00740}.
-----------------------------------------------------------------------
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EMBL; M32015; AAA39428.1; -; mRNA.
EMBL; M25244; AAA39869.1; -; mRNA.
EMBL; BC049097; AAH49097.1; -; mRNA.
EMBL; J03881; AAA39411.1; -; mRNA.
CCDS; CCDS22106.1; -.
PIR; A28067; A28067.
PIR; A60534; A60534.
RefSeq; NP_001304282.1; NM_001317353.1.
RefSeq; NP_034814.2; NM_010684.3.
UniGene; Mm.16716; -.
PDB; 5GV0; X-ray; 1.50 A; A=208-370.
PDBsum; 5GV0; -.
ProteinModelPortal; P11438; -.
SMR; P11438; -.
IntAct; P11438; 18.
MINT; MINT-1858576; -.
STRING; 10090.ENSMUSP00000033824; -.
iPTMnet; P11438; -.
PhosphoSitePlus; P11438; -.
UniCarbKB; P11438; -.
EPD; P11438; -.
PaxDb; P11438; -.
PeptideAtlas; P11438; -.
PRIDE; P11438; -.
Ensembl; ENSMUST00000033824; ENSMUSP00000033824; ENSMUSG00000031447.
GeneID; 16783; -.
KEGG; mmu:16783; -.
UCSC; uc009kxa.1; mouse.
CTD; 3916; -.
MGI; MGI:96745; Lamp1.
eggNOG; KOG4818; Eukaryota.
eggNOG; ENOG410XQ96; LUCA.
GeneTree; ENSGT00530000063068; -.
HOGENOM; HOG000230942; -.
HOVERGEN; HBG052303; -.
InParanoid; P11438; -.
KO; K06528; -.
OMA; NGTACIM; -.
OrthoDB; EOG091G09EV; -.
PhylomeDB; P11438; -.
TreeFam; TF316339; -.
Reactome; R-MMU-6798695; Neutrophil degranulation.
ChiTaRS; Lamp1; mouse.
PRO; PR:P11438; -.
Proteomes; UP000000589; Chromosome 8.
Bgee; ENSMUSG00000031447; -.
CleanEx; MM_LAMP1; -.
ExpressionAtlas; P11438; baseline and differential.
Genevisible; P11438; MM.
GO; GO:0097208; C:alveolar lamellar body; IEA:Ensembl.
GO; GO:0044754; C:autolysosome; IDA:MGI.
GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
GO; GO:0044194; C:cytolytic granule; IDA:MGI.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0005829; C:cytosol; IEA:GOC.
GO; GO:0030425; C:dendrite; IEA:Ensembl.
GO; GO:0005768; C:endosome; IDA:MGI.
GO; GO:0010008; C:endosome membrane; ISS:UniProtKB.
GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005770; C:late endosome; IDA:MGI.
GO; GO:0005764; C:lysosome; IDA:MGI.
GO; GO:0042470; C:melanosome; IDA:MGI.
GO; GO:0016020; C:membrane; ISO:MGI.
GO; GO:0005771; C:multivesicular body; IDA:MGI.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
GO; GO:0045335; C:phagocytic vesicle; IMP:AgBase.
GO; GO:0061474; C:phagolysosome membrane; IDA:MGI.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0042383; C:sarcolemma; IDA:MGI.
GO; GO:0008021; C:synaptic vesicle; IDA:MGI.
GO; GO:0031982; C:vesicle; IDA:MGI.
GO; GO:0019899; F:enzyme binding; ISO:MGI.
GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
GO; GO:0048102; P:autophagic cell death; IEA:Ensembl.
GO; GO:0072594; P:establishment of protein localization to organelle; ISO:MGI.
GO; GO:0090160; P:Golgi to lysosome transport; ISO:MGI.
GO; GO:0008626; P:granzyme-mediated apoptotic signaling pathway; ISO:MGI.
GO; GO:0043323; P:positive regulation of natural killer cell degranulation; ISO:MGI.
GO; GO:0045954; P:positive regulation of natural killer cell mediated cytotoxicity; ISO:MGI.
GO; GO:0050821; P:protein stabilization; IMP:UniProtKB.
GO; GO:1902513; P:regulation of organelle transport along microtubule; ISO:MGI.
GO; GO:0007283; P:spermatogenesis; TAS:MGI.
InterPro; IPR018134; LAMP_CS.
InterPro; IPR002000; Lysosome-assoc_membr_glycop.
PANTHER; PTHR11506; PTHR11506; 1.
Pfam; PF01299; Lamp; 1.
PRINTS; PR00336; LYSASSOCTDMP.
PROSITE; PS00310; LAMP_1; 2.
PROSITE; PS00311; LAMP_2; 1.
PROSITE; PS51407; LAMP_3; 1.
1: Evidence at protein level;
3D-structure; Cell membrane; Complete proteome;
Direct protein sequencing; Disulfide bond; Endosome; Glycoprotein;
Lysosome; Membrane; Reference proteome; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 24 {ECO:0000269|PubMed:3379044}.
CHAIN 25 406 Lysosome-associated membrane glycoprotein
1.
/FTId=PRO_0000017105.
TOPO_DOM 25 370 Lumenal. {ECO:0000255}.
TRANSMEM 371 394 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00740}.
TOPO_DOM 395 406 Cytoplasmic. {ECO:0000255|PROSITE-
ProRule:PRU00740}.
REGION 25 188 First lumenal domain.
REGION 189 218 Hinge.
REGION 219 370 Second lumenal domain.
CARBOHYD 31 31 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 52 52 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 58 58 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 70 70 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 78 78 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 97 97 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16944957,
ECO:0000269|PubMed:19349973}.
CARBOHYD 101 101 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
CARBOHYD 115 115 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 159 159 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
CARBOHYD 177 177 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973,
ECO:0000269|PubMed:19656770}.
CARBOHYD 214 214 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 219 219 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 232 232 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 240 240 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 252 252 N-linked (GlcNAc...) (high mannose)
asparagine.
{ECO:0000269|PubMed:16170054}.
CARBOHYD 282 282 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 296 296 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 311 311 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 35 74 {ECO:0000255|PROSITE-ProRule:PRU00740,
ECO:0000269|PubMed:2332434}.
DISULFID 149 185 {ECO:0000255|PROSITE-ProRule:PRU00740,
ECO:0000269|PubMed:2332434}.
DISULFID 222 259 {ECO:0000255|PROSITE-ProRule:PRU00740,
ECO:0000269|PubMed:2332434}.
DISULFID 327 364 {ECO:0000255|PROSITE-ProRule:PRU00740,
ECO:0000269|PubMed:2332434}.
CONFLICT 1 10 MAAPGARRPL -> MRPPRAAAV (in Ref. 2).
{ECO:0000305}.
CONFLICT 25 26 LF -> IP (in Ref. 4; AAA39411).
{ECO:0000305}.
CONFLICT 385 385 V -> I (in Ref. 2 and 4). {ECO:0000305}.
STRAND 211 217 {ECO:0000244|PDB:5GV0}.
STRAND 220 237 {ECO:0000244|PDB:5GV0}.
STRAND 242 248 {ECO:0000244|PDB:5GV0}.
STRAND 253 258 {ECO:0000244|PDB:5GV0}.
STRAND 261 270 {ECO:0000244|PDB:5GV0}.
STRAND 273 281 {ECO:0000244|PDB:5GV0}.
TURN 283 285 {ECO:0000244|PDB:5GV0}.
STRAND 287 298 {ECO:0000244|PDB:5GV0}.
STRAND 302 304 {ECO:0000244|PDB:5GV0}.
STRAND 306 311 {ECO:0000244|PDB:5GV0}.
STRAND 316 320 {ECO:0000244|PDB:5GV0}.
STRAND 323 327 {ECO:0000244|PDB:5GV0}.
STRAND 331 336 {ECO:0000244|PDB:5GV0}.
STRAND 339 351 {ECO:0000244|PDB:5GV0}.
STRAND 360 363 {ECO:0000244|PDB:5GV0}.
HELIX 365 367 {ECO:0000244|PDB:5GV0}.
SEQUENCE 406 AA; 43865 MW; C1BD373548BB9655 CRC64;
MAAPGARRPL LLLLLAGLAH GASALFEVKN NGTTCIMASF SASFLTTYET ANGSQIVNIS
LPASAEVLKN GSSCGKENVS DPSLTITFGR GYLLTLNFTK NTTRYSVQHM YFTYNLSDTE
HFPNAISKEI YTMDSTTDIK ADINKAYRCV SDIRVYMKNV TVVLRDATIQ AYLSSGNFSK
EETHCTQDGP SPTTGPPSPS PPLVPTNPTV SKYNVTGNNG TCLLASMALQ LNITYLKKDN
KTVTRAFNIS PNDTSSGSCG INLVTLKVEN KNRALELQFG MNASSSLFFL QGVRLNMTLP
DALVPTFSIS NHSLKALQAT VGNSYKCNTE EHIFVSKMLS LNVFSVQVQA FKVDSDRFGS
VEECVQDGNN MLIPIAVGGA LAGLVLIVLI AYLIGRKRSH AGYQTI


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