LAMP1_HUMAN
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 03-AUG-2022, entry version 207.
DE RecName: Full=Lysosome-associated membrane glycoprotein 1 {ECO:0000305};
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 {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 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 human
RT lysosomal membrane glycoproteins lamp-1 and lamp-2.";
RL Arch. Biochem. Biophys. 304:65-73(1993).
RN [13]
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 [14]
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 [15]
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 [16]
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 [17]
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 [18]
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 [19]
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 [20]
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 [21]
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 [22]
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 [23]
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 [24]
RP FUNCTION (MICROBIAL INFECTION), INTERACTION WITH LASSA VIRUS PROTEIN
RP GLYCOPROTEIN, 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 [25]
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 [26]
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 [27]
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).
CC -!- FUNCTION: Lysosomal membrane glycoprotein which plays an important role
CC in lysosome biogenesis, autophagy, and cholesterol homeostasis (By
CC similarity). Also plays an important role in NK-cells cytotoxicity
CC (PubMed:23632890, PubMed:2022921). Mechanistically, participates in
CC cytotoxic granule movement to the cell surface and perforin trafficking
CC to the lytic granule (PubMed:23632890). In addition, protects NK-cells
CC from degranulation-associated damage induced by their own cytotoxic
CC granule content (PubMed:23847195). Presents carbohydrate ligands to
CC selectins. Also implicated in tumor cell metastasis.
CC {ECO:0000250|UniProtKB:P11438, ECO:0000269|PubMed:2022921,
CC ECO:0000269|PubMed:23632890, ECO:0000269|PubMed:23847195}.
CC -!- FUNCTION: (Microbial infection) Acts as a receptor for Lassa virus
CC glycoprotein (PubMed:24970085). Promotes also fusion of the virus with
CC host membrane in less acidic endosomes (PubMed:29295909).
CC {ECO:0000269|PubMed:24970085, 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: (Microbial infection) Interacts with Lassa virus protein
CC glycoprotein. {ECO:0000269|PubMed:24970085}.
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 -!- SUBUNIT: Interacts with ABCB9; this interaction strongly stabilizes
CC ABCB9 and protects ABCB9 against lysosomal degradation
CC (PubMed:22641697). Interacts with FURIN (PubMed:32295904).
CC {ECO:0000269|PubMed:22641697, 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: Cell membrane {ECO:0000269|PubMed:2022921,
CC ECO:0000269|PubMed:23847195}; Single-pass type I membrane protein
CC {ECO:0000255}. Endosome membrane; Single-pass type I membrane protein
CC {ECO:0000255}. Lysosome membrane {ECO:0000269|PubMed:16176980,
CC ECO:0000269|PubMed:17897319}; Single-pass type I membrane protein
CC {ECO:0000255}. Late endosome membrane {ECO:0000269|PubMed:16176980};
CC Single-pass type I membrane protein {ECO:0000255}. Cytolytic granule
CC membrane {ECO:0000269|PubMed:2022921, ECO:0000269|PubMed:24088571};
CC Single-pass type I membrane protein {ECO:0000255}. Note=This protein
CC shuttles between lysosomes, endosomes, and the plasma membrane (By
CC similarity). Colocalizes with OSBPL1A at the late endosome
CC (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. The glycosylation of N-76 is essential for
CC Lassa virus entry into cells. {ECO:0000269|PubMed:12754519,
CC ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218,
CC ECO:0000269|PubMed:24970085, ECO:0000269|PubMed:8323299}.
CC -!- SIMILARITY: Belongs to the LAMP family. {ECO:0000255|PROSITE-
CC ProRule:PRU00740}.
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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 AlphaFoldDB; P11279; -.
DR SMR; P11279; -.
DR BioGRID; 110110; 575.
DR DIP; DIP-44670N; -.
DR ELM; P11279; -.
DR IntAct; P11279; 345.
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 GlyGen; P11279; 29 sites, 166 N-linked glycans (10 sites), 11 O-linked glycans (7 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; P11279; -.
DR PeptideAtlas; P11279; -.
DR PRIDE; P11279; -.
DR ProteomicsDB; 52734; -. [P11279-1]
DR ProteomicsDB; 5353; -.
DR TopDownProteomics; P11279-1; -. [P11279-1]
DR ABCD; P11279; 10 sequenced antibodies.
DR Antibodypedia; 2703; 1397 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 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; NSYKCSA; -.
DR OrthoDB; 993446at2759; -.
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 1077 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 211 other tissues.
DR ExpressionAtlas; P11279; baseline and differential.
DR Genevisible; P11279; HS.
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:0005887; C:integral component of plasma membrane; TAS:ProtInc.
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; ISS:UniProtKB.
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: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: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 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 Alternative splicing; Cell membrane; Direct protein sequencing;
KW Disulfide bond; Endosome; Glycoprotein; Host cell receptor for virus entry;
KW Host-virus interaction; Lysosome; Membrane; Receptor; Reference proteome;
KW Signal; Transmembrane; 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..405
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00740"
FT TOPO_DOM 406..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"
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
