ID LAMP1_HUMAN Reviewed; 417 AA. AC P11279; B4DWL3; Q8WU33; Q96I40; Q9BRD2; Q9NP13; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 23-SEP-2008, sequence version 3. DT 27-MAR-2024, entry version 216. DE RecName: Full=Lysosome-associated membrane glycoprotein 1 {ECO:0000303|PubMed:3198605}; DE Short=LAMP-1 {ECO:0000303|PubMed:3198605, ECO:0000303|PubMed:37390818}; DE Short=Lysosome-associated membrane protein 1 {ECO:0000305}; DE AltName: Full=CD107 antigen-like family member A {ECO:0000303|PubMed:23632890}; DE AltName: CD_antigen=CD107a {ECO:0000303|PubMed:23632890}; DE Flags: Precursor; GN Name=LAMP1 {ECO:0000303|PubMed:23632890, ECO:0000312|HGNC:HGNC:6499}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PROTEIN SEQUENCE OF 29-51; RP 117-131 AND 164-198. RX PubMed=3198605; DOI=10.1016/s0021-9258(18)37370-8; RA Fukuda M., Viitala J., Matteson J., Carlsson S.R.; RT "Cloning of cDNAs encoding human lysosomal membrane glycoproteins, h-lamp-1 RT and h-lamp-2. Comparison of their deduced amino acid sequences."; RL J. Biol. Chem. 263:18920-18928(1988). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Mammary gland; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] 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., Griffiths-Jones S., RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L., RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., RA Bray-Allen S., 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., Clegg S.C., RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., RA Frankish A.G., Frankland J., French L., Garner P., Garnett J., RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., RA Martin S., 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., Pelan S., RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., RA Rogers J., Ross M.T.; RT "The DNA sequence and analysis of human chromosome 13."; RL Nature 428:522-528(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). 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 project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] 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., Hildreth J.E.K., RA August J.T.; RT "Purification and characterization of human lysosomal membrane RT glycoproteins."; RL Arch. Biochem. Biophys. 268:360-378(1989). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 33-417 (ISOFORM 1), AND PARTIAL PROTEIN RP 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 membrane RT glycoprotein with apparent Mr approximately equal to 120,000."; RL Proc. Natl. Acad. Sci. U.S.A. 85:3743-3747(1988). RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 62-417. RC TISSUE=Placenta; RX PubMed=8517882; DOI=10.1016/s0021-9258(18)52972-0; RA Sawada R., Jardine K.A., Fukuda M.; RT "The genes of major lysosomal membrane glycoproteins, lamp-1 and lamp-2. RT 5'-flanking sequence of lamp-2 gene and comparison of exon organization in RT two genes."; RL J. Biol. Chem. 268:9014-9022(1993). RN [9] RP DISULFIDE BONDS. RX PubMed=2584229; DOI=10.1016/s0021-9258(19)47094-4; 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 [10] RP POLYLACTOSAMINOGLYCANS. RX PubMed=2243102; DOI=10.1016/s0021-9258(17)30530-6; RA Carlsson S.R., Fukuda M.; RT "The polylactosaminoglycans of human lysosomal membrane glycoproteins lamp- RT 1 and lamp-2. Localization on the peptide backbones."; RL J. Biol. Chem. 265:20488-20495(1990). RN [11] RP SUBCELLULAR LOCATION, AND FUNCTION. RX PubMed=2022921; DOI=10.1084/jem.173.5.1099; RA Peters P.J., Borst J., Oorschot V., Fukuda M., Kraehenbuehl O., Tschopp J., RA Slot J.W., Geuze H.J.; RT "Cytotoxic T lymphocyte granules are secretory lysosomes, containing both RT perforin and granzymes."; RL J. Exp. Med. 173:1099-1109(1991). RN [12] RP GLYCOSYLATION AT ASN-37; ASN-45; ASN-107; ASN-165; ASN-181; SER-197; RP THR-199; THR-200; SER-207; SER-209; SER-211; ASN-223; ASN-228; ASN-241; RP ASN-261 AND ASN-322, 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 human RT lysosomal membrane glycoproteins lamp-1 and lamp-2."; RL Arch. Biochem. Biophys. 304:65-73(1993). RN [13] RP FUNCTION. RX PubMed=7685349; DOI=10.1016/s0021-9258(18)31441-8; RA Sawada R., Lowe J.B., Fukuda M.; RT "E-selectin-dependent adhesion efficiency of colonic carcinoma cells is RT increased by genetic manipulation of their cell surface lysosomal membrane RT glycoprotein-1 expression levels."; RL J. Biol. Chem. 268:12675-12681(1993). RN [14] 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 [15] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-103 AND ASN-249. 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., Moore R.J., RA 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 [16] 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 [17] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. 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., Schaefer H., RA Elsaesser H.-P., Mann M., Hasilik A.; RT "Integral and associated lysosomal membrane proteins."; RL Traffic 8:1676-1686(2007). RN [18] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-62; ASN-76; ASN-84; ASN-103; RP ASN-121; ASN-130; ASN-249 AND ASN-293. 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 multiple RT enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [19] 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., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [20] RP INTERACTION WITH ABCB9. RX PubMed=22641697; DOI=10.1242/jcs.087346; RA Demirel O., Jan I., Wolters D., Blanz J., Saftig P., Tampe R., Abele R.; RT "The lysosomal polypeptide transporter TAPL is stabilized by interaction RT with LAMP-1 and LAMP-2."; RL J. Cell Sci. 125:4230-4240(2012). RN [21] RP SUBCELLULAR LOCATION. RX PubMed=24088571; DOI=10.1091/mbc.e13-05-0259; RA Tuli A., Thiery J., James A.M., Michelet X., Sharma M., Garg S., RA Sanborn K.B., Orange J.S., Lieberman J., Brenner M.B.; RT "Arf-like GTPase Arl8b regulates lytic granule polarization and natural RT killer cell-mediated cytotoxicity."; RL Mol. Biol. Cell 24:3721-3735(2013). RN [22] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=23847195; DOI=10.1182/blood-2012-07-441832; RA Cohnen A., Chiang S.C., Stojanovic A., Schmidt H., Claus M., Saftig P., RA Janssen O., Cerwenka A., Bryceson Y.T., Watzl C.; RT "Surface CD107a/LAMP-1 protects natural killer cells from degranulation- RT associated damage."; RL Blood 122:1411-1418(2013). RN [23] RP FUNCTION. RX PubMed=23632890; DOI=10.1182/blood-2012-08-453738; RA Krzewski K., Gil-Krzewska A., Nguyen V., Peruzzi G., Coligan J.E.; RT "LAMP1/CD107a is required for efficient perforin delivery to lytic granules RT and NK-cell cytotoxicity."; RL Blood 121:4672-4683(2013). RN [24] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [25] RP FUNCTION (MICROBIAL INFECTION), INTERACTION WITH LASSA VIRUS PROTEIN RP GLYCOPROTEIN (MICROBIAL INFECTION), AND MUTAGENESIS OF ASN-76. RX PubMed=24970085; DOI=10.1126/science.1252480; RA Jae L.T., Raaben M., Herbert A.S., Kuehne A.I., Wirchnianski A.S., RA Soh T.K., Stubbs S.H., Janssen H., Damme M., Saftig P., Whelan S.P., RA Dye J.M., Brummelkamp T.R.; RT "Virus entry. Lassa virus entry requires a trigger-induced receptor RT switch."; RL Science 344:1506-1510(2014). RN [26] RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH LASSA VIRUS PROTEIN RP GLYCOPROTEIN (MICROBIAL INFECTION). RX PubMed=25972533; DOI=10.1128/jvi.00651-15; RA Cohen-Dvashi H., Cohen N., Israeli H., Diskin R.; RT "Molecular Mechanism for LAMP1 Recognition by Lassa Virus."; RL J. Virol. 89:7584-7592(2015). RN [27] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [28] RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH LASSA VIRUS PROTEIN RP GLYCOPROTEIN (MICROBIAL INFECTION). RX PubMed=27605678; DOI=10.1128/jvi.01624-16; RA Cohen-Dvashi H., Israeli H., Shani O., Katz A., Diskin R.; RT "Role of LAMP1 Binding and pH Sensing by the Spike Complex of Lassa RT Virus."; RL J. Virol. 90:10329-10338(2016). RN [29] RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH LASSA VIRUS PROTEIN RP GLYCOPROTEIN (MICROBIAL INFECTION). RX PubMed=28448640; DOI=10.1371/journal.ppat.1006337; RA Israeli H., Cohen-Dvashi H., Shulman A., Shimon A., Diskin R.; RT "Mapping of the Lassa virus LAMP1 binding site reveals unique determinants RT not shared by other old world arenaviruses."; RL PLoS Pathog. 13:e1006337-e1006337(2017). RN [30] RP FUNCTION (MICROBIAL INFECTION). RX PubMed=29295909; DOI=10.1128/mbio.01818-17; RA Hulseberg C.E., Feneant L., Szymanska K.M., White J.M.; RT "Lamp1 Increases the Efficiency of Lassa Virus Infection by Promoting RT Fusion in Less Acidic Endosomal Compartments."; RL MBio 9:0-0(2018). RN [31] RP FUNCTION (MICROBIAL INFECTION), INTERACTION WITH FURIN, AND INTERACTION RP WITH MUMPS VIRURS PROTEIN F (MICROBIAL INFECTION). RX PubMed=32295904; DOI=10.1128/jvi.00050-20; RA Ueo A., Kubota M., Shirogane Y., Ohno S., Hashiguchi T., Yanagi Y.; RT "Lysosome-Associated Membrane Proteins Support the Furin-Mediated RT Processing of the Mumps Virus Fusion Protein."; RL J. Virol. 94:0-0(2020). RN [32] {ECO:0007744|PDB:8FY5} RP STRUCTURE BY ELECTRON MICROSCOPY (3.4 ANGSTROMS) IN COMPLEX WITH TMEM175, RP FUNCTION, AND INTERACTION WITH TMEM175. RX PubMed=37390818; DOI=10.1016/j.molcel.2023.06.004; RA Zhang J., Zeng W., Han Y., Lee W.R., Liou J., Jiang Y.; RT "Lysosomal LAMP proteins regulate lysosomal pH by direct inhibition of the RT TMEM175 channel."; RL Mol. Cell 83:2524-2539(2023). CC -!- FUNCTION: Lysosomal membrane glycoprotein which plays an important role CC in lysosome biogenesis, lysosomal pH regulation, autophagy and CC cholesterol homeostasis (PubMed:37390818). Acts as an important CC regulator of lysosomal lumen pH regulation by acting as a direct CC inhibitor of the proton channel TMEM175, facilitating lysosomal CC acidification for optimal hydrolase activity (PubMed:37390818). Also CC plays an important role in NK-cells cytotoxicity (PubMed:2022921, CC PubMed:23632890). Mechanistically, participates in cytotoxic granule CC movement to the cell surface and perforin trafficking to the lytic CC granule (PubMed:23632890). In addition, protects NK-cells from CC degranulation-associated damage induced by their own cytotoxic granule CC content (PubMed:23847195). Presents carbohydrate ligands to selectins CC (PubMed:7685349). {ECO:0000269|PubMed:2022921, CC ECO:0000269|PubMed:23632890, ECO:0000269|PubMed:23847195, CC ECO:0000269|PubMed:37390818, ECO:0000269|PubMed:7685349}. CC -!- FUNCTION: (Microbial infection) Acts as a receptor for Lassa virus CC glycoprotein (PubMed:24970085, PubMed:25972533, PubMed:27605678, CC PubMed:28448640). Promotes also fusion of the virus with host membrane CC in less acidic endosomes (PubMed:29295909). CC {ECO:0000269|PubMed:24970085, ECO:0000269|PubMed:25972533, CC ECO:0000269|PubMed:27605678, ECO:0000269|PubMed:28448640, CC ECO:0000269|PubMed:29295909}. CC -!- FUNCTION: (Microbial infection) Supports the FURIN-mediated cleavage of CC mumps virus fusion protein F by interacting with both FURIN and the CC unprocessed form but not the processed form of the viral protein F. CC {ECO:0000269|PubMed:32295904}. CC -!- SUBUNIT: Interacts with ABCB9; this interaction strongly stabilizes CC ABCB9 and protects ABCB9 against lysosomal degradation CC (PubMed:22641697). Interacts with FURIN (PubMed:32295904). Interacts CC with TMEM175; inhibiting the proton channel activity of TMEM175 CC (PubMed:37390818). {ECO:0000269|PubMed:22641697, CC ECO:0000269|PubMed:32295904, ECO:0000269|PubMed:37390818}. CC -!- SUBUNIT: (Microbial infection) Interacts with Lassa virus protein CC glycoprotein. {ECO:0000269|PubMed:24970085, CC ECO:0000269|PubMed:25972533, ECO:0000269|PubMed:27605678, CC ECO:0000269|PubMed:28448640}. CC -!- SUBUNIT: (Microbial infection) Interacts with mumps virus protein F; CC this interaction promotes protein F cleavage by FURIN. CC {ECO:0000269|PubMed:32295904}. CC -!- INTERACTION: CC P11279; Q5VZM2: RRAGB; NbExp=2; IntAct=EBI-2805407, EBI-993049; CC P11279; Q6P1K1: SLC48A1; NbExp=3; IntAct=EBI-2805407, EBI-1222191; CC P11279; Q6UX27-3: VSTM1; NbExp=3; IntAct=EBI-2805407, EBI-12190699; CC P11279; P08669: GPC; Xeno; NbExp=4; IntAct=EBI-2805407, EBI-8411266; CC -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:16176980, CC ECO:0000269|PubMed:17897319}; Single-pass type I membrane protein CC {ECO:0000255}. Endosome membrane {ECO:0000269|PubMed:16176980}; Single- CC pass type I membrane protein {ECO:0000255}. Late endosome membrane CC {ECO:0000269|PubMed:16176980}; Single-pass type I membrane protein CC {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:2022921, CC ECO:0000269|PubMed:23847195}; Single-pass type I membrane protein CC {ECO:0000255}. Cytolytic granule membrane {ECO:0000269|PubMed:2022921, CC ECO:0000269|PubMed:24088571}; Single-pass type I membrane protein CC {ECO:0000255}. Note=This protein shuttles between lysosomes, endosomes, CC and the plasma membrane (By similarity). Colocalizes with OSBPL1A at CC the late endosome (PubMed:16176980). {ECO:0000250|UniProtKB:P05300, CC ECO:0000269|PubMed:16176980, ECO:0000269|PubMed:17897319}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P11279-1; Sequence=Displayed; CC Name=2; CC IsoId=P11279-2; Sequence=VSP_056032; CC -!- PTM: O- and N-glycosylated; some of the 18 N-linked glycans are CC polylactosaminoglycans. {ECO:0000269|PubMed:12754519, CC ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, CC ECO:0000269|PubMed:8323299}. CC -!- PTM: (Microbial infection) The glycosylation of Asn-76 is essential for CC Lassa virus entry into cells. {ECO:0000269|PubMed:24970085}. CC -!- SIMILARITY: Belongs to the LAMP family. {ECO:0000255|PROSITE- CC ProRule:PRU00740}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; J04182; AAA60382.1; -; mRNA. DR EMBL; AK301584; BAG63075.1; -; mRNA. DR EMBL; AL136221; -; NOT_ANNOTATED_CDS; 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 CCDS; CCDS41909.1; -. [P11279-1] DR PIR; A31959; A31959. DR RefSeq; NP_005552.3; NM_005561.3. [P11279-1] DR PDB; 8ATH; X-ray; 2.37 A; A/B=29-195. DR PDB; 8FY5; EM; 3.40 A; C/D=1-417. DR PDB; 8FYF; EM; 3.40 A; C/D=1-417. DR PDBsum; 8ATH; -. DR PDBsum; 8FY5; -. DR PDBsum; 8FYF; -. DR AlphaFoldDB; P11279; -. DR EMDB; EMD-29553; -. DR EMDB; EMD-29572; -. DR EMDB; EMD-3293; -. DR SMR; P11279; -. DR BioGRID; 110110; 646. DR DIP; DIP-44670N; -. DR ELM; P11279; -. DR IntAct; P11279; 350. DR MINT; P11279; -. DR STRING; 9606.ENSP00000333298; -. DR TCDB; 9.A.16.1.1; the lysosomal protein import (lpi) family. DR GlyConnect; 355; 114 N-Linked glycans (10 sites), 3 O-Linked glycans. DR GlyCosmos; P11279; 26 sites, 173 glycans. DR GlyGen; P11279; 36 sites, 168 N-linked glycans (10 sites), 11 O-linked glycans (16 sites). DR iPTMnet; P11279; -. DR PhosphoSitePlus; P11279; -. DR SwissPalm; P11279; -. DR BioMuta; LAMP1; -. DR DMDM; 206729915; -. DR EPD; P11279; -. DR jPOST; P11279; -. DR MassIVE; P11279; -. DR MaxQB; P11279; -. DR PaxDb; 9606-ENSP00000333298; -. DR PeptideAtlas; P11279; -. DR ProteomicsDB; 52734; -. [P11279-1] DR ProteomicsDB; 5353; -. DR Pumba; P11279; -. DR TopDownProteomics; P11279-1; -. [P11279-1] DR ABCD; P11279; 10 sequenced antibodies. DR Antibodypedia; 2703; 1584 antibodies from 51 providers. DR DNASU; 3916; -. DR Ensembl; ENST00000332556.5; ENSP00000333298.4; ENSG00000185896.11. [P11279-1] DR GeneID; 3916; -. DR KEGG; hsa:3916; -. DR MANE-Select; ENST00000332556.5; ENSP00000333298.4; NM_005561.4; NP_005552.3. DR UCSC; uc001vtm.2; human. [P11279-1] DR AGR; HGNC:6499; -. DR CTD; 3916; -. DR DisGeNET; 3916; -. DR GeneCards; LAMP1; -. DR HGNC; HGNC:6499; LAMP1. DR HPA; ENSG00000185896; Low tissue specificity. DR MIM; 153330; gene. DR neXtProt; NX_P11279; -. DR OpenTargets; ENSG00000185896; -. DR PharmGKB; PA30283; -. DR VEuPathDB; HostDB:ENSG00000185896; -. DR eggNOG; KOG4818; Eukaryota. DR GeneTree; ENSGT00950000182899; -. DR HOGENOM; CLU_055379_2_0_1; -. DR InParanoid; P11279; -. DR OMA; CQMDQNQ; -. DR OrthoDB; 5404772at2759; -. DR PhylomeDB; P11279; -. DR TreeFam; TF316339; -. DR PathwayCommons; P11279; -. DR Reactome; R-HSA-6798695; Neutrophil degranulation. DR SignaLink; P11279; -. DR BioGRID-ORCS; 3916; 12 hits in 1157 CRISPR screens. DR ChiTaRS; LAMP1; human. DR GeneWiki; LAMP1; -. DR GenomeRNAi; 3916; -. DR Pharos; P11279; Tbio. DR PRO; PR:P11279; -. DR Proteomes; UP000005640; Chromosome 13. DR RNAct; P11279; Protein. DR Bgee; ENSG00000185896; Expressed in endothelial cell and 213 other cell types or tissues. DR ExpressionAtlas; P11279; baseline and differential. DR GO; GO:0044754; C:autolysosome; IEA:Ensembl. DR GO; GO:0000421; C:autophagosome membrane; IEA:Ensembl. DR GO; GO:0035577; C:azurophil granule membrane; TAS:Reactome. DR GO; GO:0101004; C:cytolytic granule membrane; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0005829; C:cytosol; IEA:GOC. DR GO; GO:0010008; C:endosome membrane; ISS:UniProtKB. DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0101003; C:ficolin-1-rich granule membrane; TAS:Reactome. DR GO; GO:0005770; C:late endosome; IDA:UniProtKB. DR GO; GO:0031902; C:late endosome membrane; IBA:GO_Central. DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProt. DR GO; GO:0005764; C:lysosome; IDA:UniProtKB. DR GO; GO:0042470; C:melanosome; IEA:Ensembl. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005771; C:multivesicular body; IEA:Ensembl. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IMP:AgBase. DR GO; GO:0061474; C:phagolysosome membrane; IEA:Ensembl. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0042383; C:sarcolemma; IEA:Ensembl. DR GO; GO:0008021; C:synaptic vesicle; IEA:Ensembl. DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB. DR GO; GO:0008200; F:ion channel inhibitor activity; IDA:UniProtKB. DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl. DR GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW. DR GO; GO:0072594; P:establishment of protein localization to organelle; IMP:UniProtKB. DR GO; GO:0090160; P:Golgi to lysosome transport; IMP:UniProtKB. DR GO; GO:0140507; P:granzyme-mediated programmed cell death signaling pathway; IMP:GO_Central. DR GO; GO:0007042; P:lysosomal lumen acidification; IDA:UniProtKB. DR GO; GO:0043323; P:positive regulation of natural killer cell degranulation; IMP:UniProtKB. DR GO; GO:0045954; P:positive regulation of natural killer cell mediated cytotoxicity; IMP:UniProtKB. DR GO; GO:0050821; P:protein stabilization; ISS:CAFA. DR GO; GO:1902513; P:regulation of organelle transport along microtubule; IMP:UniProtKB. DR CDD; cd12087; TM_EGFR-like; 1. DR Gene3D; 2.40.160.110; -; 2. DR InterPro; IPR048528; Lamp2-like_luminal. DR InterPro; IPR048524; Lamp2-like_TM. DR InterPro; IPR018134; LAMP_CS. DR InterPro; IPR002000; Lysosome-assoc_membr_glycop. DR PANTHER; PTHR11506; LYSOSOME-ASSOCIATED MEMBRANE GLYCOPROTEIN; 1. DR PANTHER; PTHR11506:SF27; LYSOSOME-ASSOCIATED MEMBRANE GLYCOPROTEIN 1; 1. DR Pfam; PF01299; Lamp; 2. DR Pfam; PF21222; Lamp2_2nd; 1. DR PRINTS; PR00336; LYSASSOCTDMP. DR PROSITE; PS00310; LAMP_1; 2. DR PROSITE; PS00311; LAMP_2; 1. DR PROSITE; PS51407; LAMP_3; 1. DR Genevisible; P11279; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell membrane; KW Direct protein sequencing; Disulfide bond; Endosome; Glycoprotein; KW Host cell receptor for virus entry; Host-virus interaction; Lysosome; KW Membrane; Receptor; Reference proteome; Signal; Transmembrane; KW Transmembrane helix. FT SIGNAL 1..28 FT /evidence="ECO:0000269|PubMed:2912382, FT ECO:0000269|PubMed:3198605" FT CHAIN 29..417 FT /note="Lysosome-associated membrane glycoprotein 1" FT /id="PRO_0000017104" FT TOPO_DOM 29..382 FT /note="Lumenal" FT /evidence="ECO:0000255" FT TRANSMEM 383..410 FT /note="Helical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00740, FT ECO:0000305|PubMed:37390818, ECO:0007744|PDB:8FY5, FT ECO:0007744|PDB:8FYF" FT TOPO_DOM 411..417 FT /note="Cytoplasmic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00740" FT REGION 29..194 FT /note="First lumenal domain" FT REGION 184..221 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 195..227 FT /note="Hinge" FT REGION 228..382 FT /note="Second lumenal domain" FT COMPBIAS 198..215 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CARBOHYD 37 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:8323299" FT CARBOHYD 45 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:8323299" FT CARBOHYD 62 FT /note="N-linked (GlcNAc...) (polylactosaminoglycan) FT asparagine" FT /evidence="ECO:0000269|PubMed:12754519, FT ECO:0000269|PubMed:19159218" FT CARBOHYD 76 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218, FT ECO:0000269|PubMed:2243102" FT CARBOHYD 84 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT CARBOHYD 103 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:12754519, FT ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218" FT CARBOHYD 107 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:8323299" FT CARBOHYD 121 FT /note="N-linked (GlcNAc...) (polylactosaminoglycan) FT asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT CARBOHYD 130 FT /note="N-linked (GlcNAc...) (polylactosaminoglycan) FT asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT CARBOHYD 165 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:2243102, FT ECO:0000269|PubMed:8323299" FT CARBOHYD 181 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:2243102, FT ECO:0000269|PubMed:8323299" FT CARBOHYD 197 FT /note="O-linked (GalNAc...) serine; partial" FT /evidence="ECO:0000269|PubMed:8323299" FT CARBOHYD 199 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:8323299" FT CARBOHYD 200 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:8323299" FT CARBOHYD 207 FT /note="O-linked (GalNAc...) serine" FT /evidence="ECO:0000269|PubMed:8323299" FT CARBOHYD 209 FT /note="O-linked (GalNAc...) serine" FT /evidence="ECO:0000269|PubMed:8323299" FT CARBOHYD 211 FT /note="O-linked (GalNAc...) serine" FT /evidence="ECO:0000269|PubMed:8323299" FT CARBOHYD 223 FT /note="N-linked (GlcNAc...) (polylactosaminoglycan) FT asparagine" FT /evidence="ECO:0000269|PubMed:8323299" FT CARBOHYD 228 FT /note="N-linked (GlcNAc...) (polylactosaminoglycan) FT asparagine" FT /evidence="ECO:0000269|PubMed:8323299" FT CARBOHYD 241 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:8323299" FT CARBOHYD 249 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:16335952, FT ECO:0000269|PubMed:19159218" FT CARBOHYD 261 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:2243102, FT ECO:0000269|PubMed:8323299" FT CARBOHYD 293 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT CARBOHYD 322 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:8323299" FT DISULFID 41..80 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00740, FT ECO:0000269|PubMed:2584229" FT DISULFID 155..191 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00740, FT ECO:0000269|PubMed:2584229" FT DISULFID 231..269 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00740, FT ECO:0000269|PubMed:2584229" FT DISULFID 338..375 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00740, FT ECO:0000269|PubMed:2584229" FT VAR_SEQ 135..187 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_056032" FT VARIANT 309 FT /note="I -> T (in dbSNP:rs9577230)" FT /id="VAR_046450" FT MUTAGEN 76 FT /note="N->S: Complete loss of interaction with Lassa virus FT protein GPC." FT /evidence="ECO:0000269|PubMed:24970085" FT CONFLICT 2 FT /note="A -> M (in Ref. 1; AAA60382)" FT /evidence="ECO:0000305" FT CONFLICT 5 FT /note="G -> R (in Ref. 1; AAA60382)" FT /evidence="ECO:0000305" FT CONFLICT 16..26 FT /note="LLLLLGLMHCA -> PVAAARPHALS (in Ref. 1; AAA60382)" FT /evidence="ECO:0000305" FT CONFLICT 33..40 FT /note="VKNGNGTA -> MARGGRVR (in Ref. 7; AAA59524)" FT /evidence="ECO:0000305" FT CONFLICT 262 FT /note="K -> T (in Ref. 8; AAF66141)" FT /evidence="ECO:0000305" FT CONFLICT 377 FT /note="Missing (in Ref. 8; AAF66141)" FT /evidence="ECO:0000305" FT CONFLICT 382 FT /note="M -> T (in Ref. 1; AAA60382, 7; AAA59524 and 8; FT AAF66141)" FT /evidence="ECO:0000305" FT HELIX 384..409 FT /evidence="ECO:0007829|PDB:8FYF" 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 //