LAMP2_HUMAN
ID LAMP2_HUMAN Reviewed; 410 AA.
AC P13473; A8K4X5; D3DTF0; Q16641; Q6Q3G8; Q96J30; Q99534; Q9UD93;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 223.
DE RecName: Full=Lysosome-associated membrane glycoprotein 2;
DE Short=LAMP-2;
DE Short=Lysosome-associated membrane protein 2;
DE AltName: Full=CD107 antigen-like family member B;
DE AltName: Full=LGP-96 {ECO:0000303|PubMed:8662539};
DE AltName: CD_antigen=CD107b;
DE Flags: Precursor;
GN Name=LAMP2;
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 LAMP-2A), AND PROTEIN SEQUENCE OF
RP 29-64; 216-223 AND 238-256.
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 [GENOMIC DNA] (ISOFORM LAMP-2A).
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LAMP-2B).
RC TISSUE=Fibroblast;
RX PubMed=8407947; DOI=10.1016/s0021-9258(19)36899-1;
RA Fritz G., Dosch J., Thielmann H.W., Kaina B.;
RT "Molecular and cellular characterization of Mex-/methylation-resistant
RT phenotype. Gene and cDNA cloning, serum dependence, and tumor suppression
RT of transfectant strains.";
RL J. Biol. Chem. 268:21102-21112(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LAMP-2A).
RC TISSUE=Liver;
RX PubMed=7999007; DOI=10.1006/bbrc.1994.2620;
RA Konecki D.S., Foetisch K., Schlotter M., Lichter-Konecki U.;
RT "Complete cDNA sequence of human lysosome-associated membrane protein-2.";
RL Biochem. Biophys. Res. Commun. 205:1-5(1994).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LAMP-2B), AND TISSUE SPECIFICITY.
RX PubMed=7488019; DOI=10.1006/bbrc.1995.2528;
RA Konecki D.S., Foetisch K., Zimmer K.P., Schlotter M., Lichter-Konecki U.;
RT "An alternatively spliced form of the human lysosome-associated membrane
RT protein-2 gene is expressed in a tissue-specific manner.";
RL Biochem. Biophys. Res. Commun. 215:757-767(1995).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LAMP-2C).
RA Zhou D., Blum J.S.;
RT "Lamp-2 isoforms play different roles in lysosomal biogenesis.";
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LAMP-2A).
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [9]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LAMP-2B).
RC TISSUE=Lymph;
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 [11]
RP PROTEIN SEQUENCE OF 29-66, GLYCOSYLATION, AND SUBCELLULAR LOCATION.
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 [12]
RP PROTEIN SEQUENCE OF 29-43.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally verified
RT cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
RN [13]
RP POLYLACTOSAMINOGLYCANS, AND GLYCOSYLATION.
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 [14]
RP GLYCOSYLATION OF HINGE REGION, AND PROTEIN SEQUENCE OF 187-215.
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 [15]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=8662539; DOI=10.1126/science.273.5274.501;
RA Cuervo A.M., Dice J.F.;
RT "A receptor for the selective uptake and degradation of proteins by
RT lysosomes.";
RL Science 273:501-503(1996).
RN [16]
RP FUNCTION (ISOFORM LAMP-2A), SUBCELLULAR LOCATION, TOPOLOGY, AND MUTAGENESIS
RP OF 401-LYS--HIS-404.
RX PubMed=11082038; DOI=10.1242/jcs.113.24.4441;
RA Cuervo A.M., Dice J.F.;
RT "Unique properties of lamp2a compared to other lamp2 isoforms.";
RL J. Cell Sci. 113:4441-4450(2000).
RN [17]
RP GLYCOSYLATION AT ASN-49 AND ASN-101.
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 [18]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-32; ASN-38; ASN-49; ASN-101;
RP ASN-123 AND ASN-257.
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 [19]
RP NOMENCLATURE.
RX PubMed=16190986; DOI=10.1111/j.1600-0854.2005.00337.x;
RA Eskelinen E.L., Cuervo A.M., Taylor M.R., Nishino I., Blum J.S., Dice J.F.,
RA Sandoval I.V., Lippincott-Schwartz J., August J.T., Saftig P.;
RT "Unifying nomenclature for the isoforms of the lysosomal membrane protein
RT LAMP-2.";
RL Traffic 6:1058-1061(2005).
RN [20]
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 [21]
RP FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=18644871; DOI=10.1128/mcb.02070-07;
RA Bandyopadhyay U., Kaushik S., Varticovski L., Cuervo A.M.;
RT "The chaperone-mediated autophagy receptor organizes in dynamic protein
RT complexes at the lysosomal membrane.";
RL Mol. Cell. Biol. 28:5747-5763(2008).
RN [22]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-101; ASN-123; ASN-257 AND
RP ASN-356.
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 [23]
RP FUNCTION.
RX PubMed=20518820; DOI=10.1111/j.1365-2567.2010.03309.x;
RA Crotzer V.L., Glosson N., Zhou D., Nishino I., Blum J.S.;
RT "LAMP-2-deficient human B cells exhibit altered MHC class II presentation
RT of exogenous antigens.";
RL Immunology 131:318-330(2010).
RN [24]
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 [25]
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 [26]
RP INTERACTION WITH MLLT11, AND FUNCTION.
RX PubMed=24880125; DOI=10.1016/j.yexcr.2014.05.013;
RA Li P., Ji M., Lu F., Zhang J., Li H., Cui T., Li Wang X., Tang D., Ji C.;
RT "Degradation of AF1Q by chaperone-mediated autophagy.";
RL Exp. Cell Res. 327:48-56(2014).
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.
RX PubMed=27628032; DOI=10.1242/bio.018648;
RA Hubert V., Peschel A., Langer B., Groeger M., Rees A., Kain R.;
RT "LAMP-2 is required for incorporating syntaxin-17 into autophagosomes and
RT for their fusion with lysosomes.";
RL Biol. Open 5:1516-1529(2016).
RN [29]
RP FUNCTION (ISOFORM LAMP-2C), TISSUE SPECIFICITY, AND INDUCTION BY B CELL
RP STIMULATION.
RX PubMed=26856698; DOI=10.4049/jimmunol.1501476;
RA Perez L., McLetchie S., Gardiner G.J., Deffit S.N., Zhou D., Blum J.S.;
RT "LAMP-2C inhibits MHC class II presentation of cytoplasmic antigens by
RT disrupting chaperone-mediated autophagy.";
RL J. Immunol. 196:2457-2465(2016).
RN [30]
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 [31]
RP STRUCTURE BY NMR OF 369-410, INTERACTION WITH HSPA8, AND SUBUNIT.
RX PubMed=25342746; DOI=10.1074/jbc.m114.609446;
RA Rout A.K., Strub M.P., Piszczek G., Tjandra N.;
RT "Structure of transmembrane domain of lysosome-associated membrane protein
RT type 2a (LAMP-2A) reveals key features for substrate specificity in
RT chaperone-mediated autophagy.";
RL J. Biol. Chem. 289:35111-35123(2014).
RN [32]
RP VARIANT DAND ARG-321.
RX PubMed=15673802; DOI=10.1056/nejmoa033349;
RA Arad M., Maron B.J., Gorham J.M., Johnson W.H. Jr., Saul J.P.,
RA Perez-Atayde A.R., Spirito P., Wright G.B., Kanter R.J., Seidman C.E.,
RA Seidman J.G.;
RT "Glycogen storage diseases presenting as hypertrophic cardiomyopathy.";
RL N. Engl. J. Med. 352:362-372(2005).
RN [33]
RP VARIANT DAND ARG-321.
RX PubMed=15907287; DOI=10.1016/j.nmd.2005.02.008;
RA Musumeci O., Rodolico C., Nishino I., Di Guardo G., Migliorato A.,
RA Aguennouz M., Mazzeo A., Messina C., Vita G., Toscano A.;
RT "Asymptomatic hyperCKemia in a case of Danon disease due to a missense
RT mutation in Lamp-2 gene.";
RL Neuromuscul. Disord. 15:409-411(2005).
CC -!- FUNCTION: Plays an important role in chaperone-mediated autophagy, a
CC process that mediates lysosomal degradation of proteins in response to
CC various stresses and as part of the normal turnover of proteins with a
CC long biological half-live (PubMed:8662539, PubMed:11082038,
CC PubMed:18644871, PubMed:24880125, PubMed:27628032). Functions by
CC binding target proteins, such as GAPDH and MLLT11, and targeting them
CC for lysosomal degradation (PubMed:8662539, PubMed:11082038,
CC PubMed:18644871, PubMed:24880125). Plays a role in lysosomal protein
CC degradation in response to starvation (By similarity). Required for the
CC fusion of autophagosomes with lysosomes during autophagy
CC (PubMed:27628032). Cells that lack LAMP2 express normal levels of
CC VAMP8, but fail to accumulate STX17 on autophagosomes, which is the
CC most likely explanation for the lack of fusion between autophagosomes
CC and lysosomes (PubMed:27628032). Required for normal degradation of the
CC contents of autophagosomes (PubMed:27628032). Required for efficient
CC MHCII-mediated presentation of exogenous antigens via its function in
CC lysosomal protein degradation; antigenic peptides generated by
CC proteases in the endosomal/lysosomal compartment are captured by
CC nascent MHCII subunits (PubMed:20518820). Is not required for efficient
CC MHCII-mediated presentation of endogenous antigens (PubMed:20518820).
CC {ECO:0000250|UniProtKB:P17046, ECO:0000269|PubMed:11082038,
CC ECO:0000269|PubMed:18644871, ECO:0000269|PubMed:20518820,
CC ECO:0000269|PubMed:24880125, ECO:0000269|PubMed:27628032,
CC ECO:0000269|PubMed:8662539}.
CC -!- FUNCTION: [Isoform LAMP-2C]: Modulates chaperone-mediated autophagy.
CC Decreases presentation of endogenous antigens by MHCII. Does not play a
CC role in the presentation of exogenous and membrane-derived antigens by
CC MHCII. {ECO:0000269|PubMed:26856698}.
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: Monomer (PubMed:18644871, PubMed:25342746). Homodimer
CC (PubMed:25342746). Homotrimer (PubMed:25342746). Forms large
CC homooligomers (PubMed:18644871). Interacts (via its cytoplasmic region)
CC with HSPA8 (PubMed:25342746). Interacts with HSP90 in the lysosome
CC lumen; this enhances LAMP2 stability (By similarity). Interacts with
CC MLLT11 (PubMed:24880125). Interacts with ABCB9 (PubMed:22641697).
CC Interacts with FURIN (PubMed:32295904). {ECO:0000250|UniProtKB:P17046,
CC ECO:0000269|PubMed:18644871, ECO:0000269|PubMed:22641697,
CC ECO:0000269|PubMed:24880125, ECO:0000269|PubMed:25342746,
CC ECO:0000269|PubMed:32295904}.
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 P13473-2; P45844-6: ABCG1; NbExp=3; IntAct=EBI-21591415, EBI-25873349;
CC P13473-2; Q7Z5M8-2: ABHD12B; NbExp=3; IntAct=EBI-21591415, EBI-21854797;
CC P13473-2; Q9Y614: ACTL7B; NbExp=3; IntAct=EBI-21591415, EBI-25835070;
CC P13473-2; Q6DHV7-2: ADAL; NbExp=3; IntAct=EBI-21591415, EBI-18899653;
CC P13473-2; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-21591415, EBI-10173507;
CC P13473-2; Q96MA6: AK8; NbExp=3; IntAct=EBI-21591415, EBI-8466265;
CC P13473-2; Q5T2L2: AKR1C8P; NbExp=3; IntAct=EBI-21591415, EBI-22006248;
CC P13473-2; Q96Q83-2: ALKBH3; NbExp=3; IntAct=EBI-21591415, EBI-9089544;
CC P13473-2; Q9Y303-2: AMDHD2; NbExp=3; IntAct=EBI-21591415, EBI-12323557;
CC P13473-2; Q9NU02: ANKEF1; NbExp=3; IntAct=EBI-21591415, EBI-8464238;
CC P13473-2; Q6LES2: ANXA4; NbExp=3; IntAct=EBI-21591415, EBI-10250835;
CC P13473-2; P02647: APOA1; NbExp=3; IntAct=EBI-21591415, EBI-701692;
CC P13473-2; P02749: APOH; NbExp=3; IntAct=EBI-21591415, EBI-2114682;
CC P13473-2; P53365: ARFIP2; NbExp=3; IntAct=EBI-21591415, EBI-638194;
CC P13473-2; Q66PJ3-4: ARL6IP4; NbExp=3; IntAct=EBI-21591415, EBI-5280499;
CC P13473-2; Q6XD76: ASCL4; NbExp=3; IntAct=EBI-21591415, EBI-10254793;
CC P13473-2; P18848: ATF4; NbExp=3; IntAct=EBI-21591415, EBI-492498;
CC P13473-2; Q9H0Y0: ATG10; NbExp=3; IntAct=EBI-21591415, EBI-1048913;
CC P13473-2; C1IDX9: ATG12; NbExp=3; IntAct=EBI-21591415, EBI-25836940;
CC P13473-2; O75964: ATP5MG; NbExp=3; IntAct=EBI-21591415, EBI-1044001;
CC P13473-2; Q14032: BAAT; NbExp=3; IntAct=EBI-21591415, EBI-8994378;
CC P13473-2; P54687-4: BCAT1; NbExp=3; IntAct=EBI-21591415, EBI-25834445;
CC P13473-2; P06276: BCHE; NbExp=3; IntAct=EBI-21591415, EBI-7936069;
CC P13473-2; Q9NSI6-4: BRWD1; NbExp=3; IntAct=EBI-21591415, EBI-10693038;
CC P13473-2; Q8WZ55: BSND; NbExp=3; IntAct=EBI-21591415, EBI-7996695;
CC P13473-2; Q96Q07-2: BTBD9; NbExp=3; IntAct=EBI-21591415, EBI-22006737;
CC P13473-2; Q9H0W9-3: C11orf54; NbExp=3; IntAct=EBI-21591415, EBI-12108466;
CC P13473-2; Q9NQ89: C12orf4; NbExp=3; IntAct=EBI-21591415, EBI-11090973;
CC P13473-2; Q13901: C1D; NbExp=3; IntAct=EBI-21591415, EBI-3844053;
CC P13473-2; Q3SXR2: C3orf36; NbExp=3; IntAct=EBI-21591415, EBI-18036948;
CC P13473-2; Q8N1A6: C4orf33; NbExp=3; IntAct=EBI-21591415, EBI-10264911;
CC P13473-2; P17655: CAPN2; NbExp=3; IntAct=EBI-21591415, EBI-1028956;
CC P13473-2; P20807-4: CAPN3; NbExp=3; IntAct=EBI-21591415, EBI-11532021;
CC P13473-2; P55212: CASP6; NbExp=3; IntAct=EBI-21591415, EBI-718729;
CC P13473-2; Q5JTY5: CBWD3; NbExp=3; IntAct=EBI-21591415, EBI-723434;
CC P13473-2; O00257-3: CBX4; NbExp=3; IntAct=EBI-21591415, EBI-4392727;
CC P13473-2; P24863: CCNC; NbExp=3; IntAct=EBI-21591415, EBI-395261;
CC P13473-2; Q9UK58-5: CCNL1; NbExp=3; IntAct=EBI-21591415, EBI-25873837;
CC P13473-2; Q9NNX6-10: CD209; NbExp=3; IntAct=EBI-21591415, EBI-12300031;
CC P13473-2; P01730: CD4; NbExp=3; IntAct=EBI-21591415, EBI-353826;
CC P13473-2; Q9UJX2: CDC23; NbExp=3; IntAct=EBI-21591415, EBI-396137;
CC P13473-2; P42773: CDKN2C; NbExp=3; IntAct=EBI-21591415, EBI-711290;
CC P13473-2; O95674: CDS2; NbExp=3; IntAct=EBI-21591415, EBI-3913685;
CC P13473-2; O15182: CETN3; NbExp=3; IntAct=EBI-21591415, EBI-712959;
CC P13473-2; Q8WUX9: CHMP7; NbExp=3; IntAct=EBI-21591415, EBI-749253;
CC P13473-2; Q9Y3D0: CIAO2B; NbExp=3; IntAct=EBI-21591415, EBI-744045;
CC P13473-2; Q8N365: CIART; NbExp=3; IntAct=EBI-21591415, EBI-10265133;
CC P13473-2; Q9UHD4: CIDEB; NbExp=3; IntAct=EBI-21591415, EBI-7062247;
CC P13473-2; Q99966: CITED1; NbExp=3; IntAct=EBI-21591415, EBI-2624951;
CC P13473-2; P09496-2: CLTA; NbExp=3; IntAct=EBI-21591415, EBI-4401010;
CC P13473-2; Q6PJW8-3: CNST; NbExp=3; IntAct=EBI-21591415, EBI-25836090;
CC P13473-2; Q96BR5: COA7; NbExp=3; IntAct=EBI-21591415, EBI-6269632;
CC P13473-2; P02458-1: COL2A1; NbExp=3; IntAct=EBI-21591415, EBI-12375799;
CC P13473-2; Q8NI60: COQ8A; NbExp=3; IntAct=EBI-21591415, EBI-745535;
CC P13473-2; Q9UGL9: CRCT1; NbExp=3; IntAct=EBI-21591415, EBI-713677;
CC P13473-2; P26998: CRYBB3; NbExp=3; IntAct=EBI-21591415, EBI-1965681;
CC P13473-2; P35222: CTNNB1; NbExp=3; IntAct=EBI-21591415, EBI-491549;
CC P13473-2; Q53TN4: CYBRD1; NbExp=3; IntAct=EBI-21591415, EBI-8637742;
CC P13473-2; P10632: CYP2C8; NbExp=3; IntAct=EBI-21591415, EBI-2951522;
CC P13473-2; P61962: DCAF7; NbExp=3; IntAct=EBI-21591415, EBI-359808;
CC P13473-2; Q96LJ7: DHRS1; NbExp=3; IntAct=EBI-21591415, EBI-746300;
CC P13473-2; O60479: DLX3; NbExp=3; IntAct=EBI-21591415, EBI-3908248;
CC P13473-2; Q96EY1-3: DNAJA3; NbExp=3; IntAct=EBI-21591415, EBI-11526226;
CC P13473-2; Q96KC8: DNAJC1; NbExp=3; IntAct=EBI-21591415, EBI-296550;
CC P13473-2; Q92782-2: DPF1; NbExp=3; IntAct=EBI-21591415, EBI-23669343;
CC P13473-2; Q9BPU6: DPYSL5; NbExp=3; IntAct=EBI-21591415, EBI-724653;
CC P13473-2; Q658K8: EEF1DP3; NbExp=3; IntAct=EBI-21591415, EBI-10248874;
CC P13473-2; O00303: EIF3F; NbExp=3; IntAct=EBI-21591415, EBI-711990;
CC P13473-2; Q13347: EIF3I; NbExp=3; IntAct=EBI-21591415, EBI-354047;
CC P13473-2; O00472: ELL2; NbExp=3; IntAct=EBI-21591415, EBI-395274;
CC P13473-2; O00423: EML1; NbExp=3; IntAct=EBI-21591415, EBI-751327;
CC P13473-2; O95278-6: EPM2A; NbExp=3; IntAct=EBI-21591415, EBI-25836908;
CC P13473-2; Q6NXG1-3: ESRP1; NbExp=3; IntAct=EBI-21591415, EBI-21567429;
CC P13473-2; P00748: F12; NbExp=3; IntAct=EBI-21591415, EBI-6378830;
CC P13473-2; Q49AJ0-4: FAM135B; NbExp=3; IntAct=EBI-21591415, EBI-25835236;
CC P13473-2; Q96KS9: FAM167A; NbExp=3; IntAct=EBI-21591415, EBI-10290462;
CC P13473-2; Q8N128-2: FAM177A1; NbExp=3; IntAct=EBI-21591415, EBI-12201693;
CC P13473-2; Q8IZU1: FAM9A; NbExp=3; IntAct=EBI-21591415, EBI-8468186;
CC P13473-2; Q9NYY8: FASTKD2; NbExp=3; IntAct=EBI-21591415, EBI-1055752;
CC P13473-2; P02671-2: FGA; NbExp=3; IntAct=EBI-21591415, EBI-9640259;
CC P13473-2; Q6ZNL6: FGD5; NbExp=3; IntAct=EBI-21591415, EBI-7962481;
CC P13473-2; Q9NSA1: FGF21; NbExp=3; IntAct=EBI-21591415, EBI-3909329;
CC P13473-2; P49771-3: FLT3LG; NbExp=3; IntAct=EBI-21591415, EBI-25872794;
CC P13473-2; Q3SYB3: FOXD4L6; NbExp=3; IntAct=EBI-21591415, EBI-6425864;
CC P13473-2; Q6P7E6: FUT6; NbExp=3; IntAct=EBI-21591415, EBI-25872807;
CC P13473-2; P06241: FYN; NbExp=3; IntAct=EBI-21591415, EBI-515315;
CC P13473-2; Q06547-3: GABPB1; NbExp=3; IntAct=EBI-21591415, EBI-9088619;
CC P13473-2; Q9H3K2: GHITM; NbExp=3; IntAct=EBI-21591415, EBI-2868909;
CC P13473-2; Q8WWP7: GIMAP1; NbExp=3; IntAct=EBI-21591415, EBI-11991950;
CC P13473-2; Q49A26-4: GLYR1; NbExp=3; IntAct=EBI-21591415, EBI-12143817;
CC P13473-2; Q9HAV0: GNB4; NbExp=3; IntAct=EBI-21591415, EBI-358539;
CC P13473-2; P32780: GTF2H1; NbExp=3; IntAct=EBI-21591415, EBI-715539;
CC P13473-2; O75409: H2AP; NbExp=3; IntAct=EBI-21591415, EBI-6447217;
CC P13473-2; Q6NXT2: H3-5; NbExp=3; IntAct=EBI-21591415, EBI-2868501;
CC P13473-2; P68431: H3C12; NbExp=3; IntAct=EBI-21591415, EBI-79722;
CC P13473-2; Q9BT25: HAUS8; NbExp=3; IntAct=EBI-21591415, EBI-2558143;
CC P13473-2; Q9NRZ9-6: HELLS; NbExp=3; IntAct=EBI-21591415, EBI-12003732;
CC P13473-2; Q96EW2-2: HSPBAP1; NbExp=3; IntAct=EBI-21591415, EBI-25835621;
CC P13473-2; Q8N6M8-2: IQCF1; NbExp=3; IntAct=EBI-21591415, EBI-21771049;
CC P13473-2; Q92613: JADE3; NbExp=3; IntAct=EBI-21591415, EBI-10278909;
CC P13473-2; P0C870: JMJD7; NbExp=3; IntAct=EBI-21591415, EBI-9090173;
CC P13473-2; Q9UK76: JPT1; NbExp=3; IntAct=EBI-21591415, EBI-720411;
CC P13473-2; Q8N5Z5: KCTD17; NbExp=3; IntAct=EBI-21591415, EBI-743960;
CC P13473-2; Q8TBB5-2: KLHDC4; NbExp=3; IntAct=EBI-21591415, EBI-21838933;
CC P13473-2; Q9UH77: KLHL3; NbExp=3; IntAct=EBI-21591415, EBI-8524663;
CC P13473-2; Q8N4N3-2: KLHL36; NbExp=3; IntAct=EBI-21591415, EBI-10973851;
CC P13473-2; Q8N1A0: KRT222; NbExp=3; IntAct=EBI-21591415, EBI-8473062;
CC P13473-2; Q6DKI2: LGALS9C; NbExp=3; IntAct=EBI-21591415, EBI-9088829;
CC P13473-2; Q9H2C1: LHX5; NbExp=3; IntAct=EBI-21591415, EBI-25835523;
CC P13473-2; Q8N0U6: LINC00518; NbExp=3; IntAct=EBI-21591415, EBI-10264791;
CC P13473-2; Q9Y234: LIPT1; NbExp=3; IntAct=EBI-21591415, EBI-727376;
CC P13473-2; Q99732: LITAF; NbExp=3; IntAct=EBI-21591415, EBI-725647;
CC P13473-2; Q1L5Z9: LONRF2; NbExp=3; IntAct=EBI-21591415, EBI-2510853;
CC P13473-2; Q96JB6: LOXL4; NbExp=3; IntAct=EBI-21591415, EBI-749562;
CC P13473-2; Q8IYG6: LRRC56; NbExp=3; IntAct=EBI-21591415, EBI-14752528;
CC P13473-2; Q5VYH9: LY9; NbExp=3; IntAct=EBI-21591415, EBI-25872860;
CC P13473-2; P0DP58-2: LYNX1; NbExp=3; IntAct=EBI-21591415, EBI-21916939;
CC P13473-2; P43361: MAGEA8; NbExp=3; IntAct=EBI-21591415, EBI-10182930;
CC P13473-2; Q96M61: MAGEB18; NbExp=3; IntAct=EBI-21591415, EBI-741835;
CC P13473-2; Q969L2: MAL2; NbExp=3; IntAct=EBI-21591415, EBI-944295;
CC P13473-2; P27338: MAOB; NbExp=3; IntAct=EBI-21591415, EBI-3911344;
CC P13473-2; Q8NI22: MCFD2; NbExp=3; IntAct=EBI-21591415, EBI-2689785;
CC P13473-2; A6NJ78-4: METTL15; NbExp=3; IntAct=EBI-21591415, EBI-10174029;
CC P13473-2; A0A0A0MR05: MLST8; NbExp=3; IntAct=EBI-21591415, EBI-25835557;
CC P13473-2; P34949-2: MPI; NbExp=3; IntAct=EBI-21591415, EBI-21823432;
CC P13473-2; Q9BV20: MRI1; NbExp=3; IntAct=EBI-21591415, EBI-747381;
CC P13473-2; Q6IN84-2: MRM1; NbExp=3; IntAct=EBI-21591415, EBI-25835707;
CC P13473-2; Q8N387: MUC15; NbExp=3; IntAct=EBI-21591415, EBI-17937277;
CC P13473-2; A2RUH7: MYBPHL; NbExp=3; IntAct=EBI-21591415, EBI-9088235;
CC P13473-2; P01106: MYC; NbExp=3; IntAct=EBI-21591415, EBI-447544;
CC P13473-2; Q9H7X0: NAA60; NbExp=3; IntAct=EBI-21591415, EBI-12260336;
CC P13473-2; Q15742-2: NAB2; NbExp=3; IntAct=EBI-21591415, EBI-25834665;
CC P13473-2; Q9UJ70-2: NAGK; NbExp=3; IntAct=EBI-21591415, EBI-11526455;
CC P13473-2; Q69YL0: NCBP2AS2; NbExp=3; IntAct=EBI-21591415, EBI-10986258;
CC P13473-2; P25208: NFYB; NbExp=3; IntAct=EBI-21591415, EBI-389728;
CC P13473-2; Q8NDH3-5: NPEPL1; NbExp=3; IntAct=EBI-21591415, EBI-12329915;
CC P13473-2; O15130-2: NPFF; NbExp=3; IntAct=EBI-21591415, EBI-25840002;
CC P13473-2; P36639-4: NUDT1; NbExp=3; IntAct=EBI-21591415, EBI-25834643;
CC P13473-2; Q8NFH4: NUP37; NbExp=3; IntAct=EBI-21591415, EBI-2563158;
CC P13473-2; Q8NFH3: NUP43; NbExp=3; IntAct=EBI-21591415, EBI-1059321;
CC P13473-2; Q7Z3B4: NUP54; NbExp=3; IntAct=EBI-21591415, EBI-741048;
CC P13473-2; Q6N063-2: OGFOD2; NbExp=3; IntAct=EBI-21591415, EBI-22006224;
CC P13473-2; Q6GQQ9-2: OTUD7B; NbExp=3; IntAct=EBI-21591415, EBI-25830200;
CC P13473-2; Q99447: PCYT2; NbExp=3; IntAct=EBI-21591415, EBI-750317;
CC P13473-2; P27815-4: PDE4A; NbExp=3; IntAct=EBI-21591415, EBI-12080840;
CC P13473-2; A5PLL7: PEDS1; NbExp=3; IntAct=EBI-21591415, EBI-11337896;
CC P13473-2; Q9BUL5: PHF23; NbExp=3; IntAct=EBI-21591415, EBI-722852;
CC P13473-2; Q00169: PITPNA; NbExp=3; IntAct=EBI-21591415, EBI-1042490;
CC P13473-2; P48739: PITPNB; NbExp=3; IntAct=EBI-21591415, EBI-1047143;
CC P13473-2; Q58EX7-2: PLEKHG4; NbExp=3; IntAct=EBI-21591415, EBI-21503705;
CC P13473-2; O60664: PLIN3; NbExp=3; IntAct=EBI-21591415, EBI-725795;
CC P13473-2; Q14181: POLA2; NbExp=3; IntAct=EBI-21591415, EBI-712752;
CC P13473-2; P0DPB6: POLR1D; NbExp=3; IntAct=EBI-21591415, EBI-359498;
CC P13473-2; P36954: POLR2I; NbExp=3; IntAct=EBI-21591415, EBI-395202;
CC P13473-2; Q07869: PPARA; NbExp=3; IntAct=EBI-21591415, EBI-78615;
CC P13473-2; O60927: PPP1R11; NbExp=3; IntAct=EBI-21591415, EBI-1048104;
CC P13473-2; Q6ZMI0-5: PPP1R21; NbExp=3; IntAct=EBI-21591415, EBI-25835994;
CC P13473-2; Q8NCQ7-2: PROCA1; NbExp=3; IntAct=EBI-21591415, EBI-25836043;
CC P13473-2; P23942: PRPH2; NbExp=3; IntAct=EBI-21591415, EBI-25836834;
CC P13473-2; P41222: PTGDS; NbExp=3; IntAct=EBI-21591415, EBI-948821;
CC P13473-2; P29074: PTPN4; NbExp=3; IntAct=EBI-21591415, EBI-710431;
CC P13473-2; Q8WUD1-2: RAB2B; NbExp=3; IntAct=EBI-21591415, EBI-25835884;
CC P13473-2; Q5R372-9: RABGAP1L; NbExp=3; IntAct=EBI-21591415, EBI-10699389;
CC P13473-2; Q9HD47-3: RANGRF; NbExp=3; IntAct=EBI-21591415, EBI-9089733;
CC P13473-2; Q09028: RBBP4; NbExp=3; IntAct=EBI-21591415, EBI-620823;
CC P13473-2; Q14498: RBM39; NbExp=3; IntAct=EBI-21591415, EBI-395290;
CC P13473-2; Q96HR9-2: REEP6; NbExp=3; IntAct=EBI-21591415, EBI-14065960;
CC P13473-2; Q04206: RELA; NbExp=3; IntAct=EBI-21591415, EBI-73886;
CC P13473-2; P47804-3: RGR; NbExp=3; IntAct=EBI-21591415, EBI-25834767;
CC P13473-2; Q15382: RHEB; NbExp=4; IntAct=EBI-21591415, EBI-1055287;
CC P13473-2; Q9NPQ8-4: RIC8A; NbExp=3; IntAct=EBI-21591415, EBI-9091816;
CC P13473-2; Q06587: RING1; NbExp=3; IntAct=EBI-21591415, EBI-752313;
CC P13473-2; Q8N5U6: RNF10; NbExp=3; IntAct=EBI-21591415, EBI-714023;
CC P13473-2; Q96IZ7: RSRC1; NbExp=3; IntAct=EBI-21591415, EBI-712189;
CC P13473-2; Q66K80: RUSC1-AS1; NbExp=3; IntAct=EBI-21591415, EBI-10248967;
CC P13473-2; O15126: SCAMP1; NbExp=3; IntAct=EBI-21591415, EBI-954338;
CC P13473-2; P22307-3: SCP2; NbExp=3; IntAct=EBI-21591415, EBI-25834804;
CC P13473-2; Q9BRK5: SDF4; NbExp=3; IntAct=EBI-21591415, EBI-1389808;
CC P13473-2; Q9NTN9-3: SEMA4G; NbExp=3; IntAct=EBI-21591415, EBI-9089805;
CC P13473-2; P01011: SERPINA3; NbExp=3; IntAct=EBI-21591415, EBI-296557;
CC P13473-2; A0A1P0AYU5: SFXN3; NbExp=3; IntAct=EBI-21591415, EBI-14193895;
CC P13473-2; Q9NR46: SH3GLB2; NbExp=3; IntAct=EBI-21591415, EBI-749607;
CC P13473-2; Q9BZQ2: SHCBP1L; NbExp=3; IntAct=EBI-21591415, EBI-10818532;
CC P13473-2; O60902-3: SHOX2; NbExp=3; IntAct=EBI-21591415, EBI-9092164;
CC P13473-2; O43772: SLC25A20; NbExp=3; IntAct=EBI-21591415, EBI-727085;
CC P13473-2; Q8IYM2: SLFN12; NbExp=3; IntAct=EBI-21591415, EBI-2822550;
CC P13473-2; Q86US8: SMG6; NbExp=3; IntAct=EBI-21591415, EBI-3232100;
CC P13473-2; Q96EX1: SMIM12; NbExp=3; IntAct=EBI-21591415, EBI-2874543;
CC P13473-2; P37840: SNCA; NbExp=3; IntAct=EBI-21591415, EBI-985879;
CC P13473-2; Q96H20: SNF8; NbExp=3; IntAct=EBI-21591415, EBI-747719;
CC P13473-2; Q8N0X7: SPART; NbExp=3; IntAct=EBI-21591415, EBI-2643803;
CC P13473-2; Q496A3: SPATS1; NbExp=3; IntAct=EBI-21591415, EBI-3923692;
CC P13473-2; Q9NYA1-2: SPHK1; NbExp=3; IntAct=EBI-21591415, EBI-12512419;
CC P13473-2; Q9BPZ2: SPIN2B; NbExp=3; IntAct=EBI-21591415, EBI-21726245;
CC P13473-2; Q9C004: SPRY4; NbExp=3; IntAct=EBI-21591415, EBI-354861;
CC P13473-2; Q96BD6: SPSB1; NbExp=3; IntAct=EBI-21591415, EBI-2659201;
CC P13473-2; Q9BXA5: SUCNR1; NbExp=3; IntAct=EBI-21591415, EBI-17962797;
CC P13473-2; Q92797-2: SYMPK; NbExp=3; IntAct=EBI-21591415, EBI-21560407;
CC P13473-2; O60506-4: SYNCRIP; NbExp=3; IntAct=EBI-21591415, EBI-11123832;
CC P13473-2; P08247: SYP; NbExp=3; IntAct=EBI-21591415, EBI-9071725;
CC P13473-2; Q17RD7: SYT16; NbExp=3; IntAct=EBI-21591415, EBI-10238936;
CC P13473-2; O95947: TBX6; NbExp=3; IntAct=EBI-21591415, EBI-2824328;
CC P13473-2; O15273: TCAP; NbExp=3; IntAct=EBI-21591415, EBI-954089;
CC P13473-2; Q86WV5: TEN1; NbExp=3; IntAct=EBI-21591415, EBI-2562799;
CC P13473-2; P54274-2: TERF1; NbExp=3; IntAct=EBI-21591415, EBI-711018;
CC P13473-2; P22735: TGM1; NbExp=3; IntAct=EBI-21591415, EBI-2562368;
CC P13473-2; O43548: TGM5; NbExp=3; IntAct=EBI-21591415, EBI-12027348;
CC P13473-2; Q9P2T0: THEG; NbExp=3; IntAct=EBI-21591415, EBI-751020;
CC P13473-2; Q9NQ88: TIGAR; NbExp=3; IntAct=EBI-21591415, EBI-3920747;
CC P13473-2; O14925: TIMM23; NbExp=3; IntAct=EBI-21591415, EBI-1047996;
CC P13473-2; Q12893: TMEM115; NbExp=3; IntAct=EBI-21591415, EBI-8633987;
CC P13473-2; Q8WVE6-2: TMEM171; NbExp=3; IntAct=EBI-21591415, EBI-25874374;
CC P13473-2; Q3YBM2: TMEM176B; NbExp=3; IntAct=EBI-21591415, EBI-2821479;
CC P13473-2; Q53NU3: tmp_locus_54; NbExp=3; IntAct=EBI-21591415, EBI-10242677;
CC P13473-2; Q9NS69: TOMM22; NbExp=3; IntAct=EBI-21591415, EBI-1047508;
CC P13473-2; P04637: TP53; NbExp=3; IntAct=EBI-21591415, EBI-366083;
CC P13473-2; Q12888: TP53BP1; NbExp=3; IntAct=EBI-21591415, EBI-396540;
CC P13473-2; O00463: TRAF5; NbExp=3; IntAct=EBI-21591415, EBI-523498;
CC P13473-2; P36406: TRIM23; NbExp=3; IntAct=EBI-21591415, EBI-740098;
CC P13473-2; Q9C035-3: TRIM5; NbExp=3; IntAct=EBI-21591415, EBI-12840050;
CC P13473-2; Q86WT6-2: TRIM69; NbExp=3; IntAct=EBI-21591415, EBI-11525489;
CC P13473-2; Q9H313-4: TTYH1; NbExp=3; IntAct=EBI-21591415, EBI-17671298;
CC P13473-2; Q9BQE3: TUBA1C; NbExp=3; IntAct=EBI-21591415, EBI-1103245;
CC P13473-2; P49459: UBE2A; NbExp=3; IntAct=EBI-21591415, EBI-2339348;
CC P13473-2; P62253: UBE2G1; NbExp=3; IntAct=EBI-21591415, EBI-2340619;
CC P13473-2; P09936: UCHL1; NbExp=3; IntAct=EBI-21591415, EBI-714860;
CC P13473-2; Q9P1Q0-4: VPS54; NbExp=3; IntAct=EBI-21591415, EBI-25835297;
CC P13473-2; Q9NX94: WBP1L; NbExp=3; IntAct=EBI-21591415, EBI-10316321;
CC P13473-2; Q6ICG8: WBP2NL; NbExp=3; IntAct=EBI-21591415, EBI-17769315;
CC P13473-2; Q8NA23-2: WDR31; NbExp=3; IntAct=EBI-21591415, EBI-25835937;
CC P13473-2; Q9BQA1: WDR77; NbExp=3; IntAct=EBI-21591415, EBI-1237307;
CC P13473-2; O00755: WNT7A; NbExp=3; IntAct=EBI-21591415, EBI-727198;
CC P13473-2; O95070: YIF1A; NbExp=3; IntAct=EBI-21591415, EBI-2799703;
CC P13473-2; Q8IWT0-2: ZBTB8OS; NbExp=3; IntAct=EBI-21591415, EBI-12956041;
CC P13473-2; Q53FD0-2: ZC2HC1C; NbExp=3; IntAct=EBI-21591415, EBI-14104088;
CC P13473-2; Q05CR2: ZNF248; NbExp=3; IntAct=EBI-21591415, EBI-25835471;
CC P13473-2; Q96JL9-2: ZNF333; NbExp=3; IntAct=EBI-21591415, EBI-25835852;
CC P13473-2; Q96LX8: ZNF597; NbExp=3; IntAct=EBI-21591415, EBI-9091553;
CC P13473-2; Q3KNS6-3: ZNF829; NbExp=3; IntAct=EBI-21591415, EBI-18036029;
CC P13473-2; A0A384MDV8; NbExp=3; IntAct=EBI-21591415, EBI-25834468;
CC P13473-2; B7Z3E8; NbExp=3; IntAct=EBI-21591415, EBI-25831617;
CC P13473-2; Q86V28; NbExp=3; IntAct=EBI-21591415, EBI-10259496;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17897319,
CC ECO:0000269|PubMed:2912382}; Single-pass type I membrane protein
CC {ECO:0000255|PROSITE-ProRule:PRU00740, ECO:0000269|PubMed:17897319}.
CC Endosome membrane {ECO:0000269|PubMed:17897319}; Single-pass type I
CC membrane protein {ECO:0000255|PROSITE-ProRule:PRU00740,
CC ECO:0000269|PubMed:17897319}. Lysosome membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00740, ECO:0000269|PubMed:11082038,
CC ECO:0000269|PubMed:17897319, ECO:0000269|PubMed:18644871,
CC ECO:0000269|PubMed:2912382}; Single-pass type I membrane protein
CC {ECO:0000255|PROSITE-ProRule:PRU00740, ECO:0000269|PubMed:17897319}.
CC Cytoplasmic vesicle, autophagosome membrane
CC {ECO:0000250|UniProtKB:P17047}. Note=This protein shuttles between
CC lysosomes, endosomes, and the plasma membrane.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=LAMP-2A;
CC IsoId=P13473-1; Sequence=Displayed;
CC Name=LAMP-2B;
CC IsoId=P13473-2; Sequence=VSP_003044;
CC Name=LAMP-2C;
CC IsoId=P13473-3; Sequence=VSP_042519;
CC -!- TISSUE SPECIFICITY: Isoform LAMP-2A is highly expressed in placenta,
CC lung and liver, less in kidney and pancreas, low in brain and skeletal
CC muscle (PubMed:7488019, PubMed:26856698). Isoform LAMP-2B is detected
CC in spleen, thymus, prostate, testis, small intestine, colon, skeletal
CC muscle, brain, placenta, lung, kidney, ovary and pancreas and liver
CC (PubMed:7488019, PubMed:26856698). Isoform LAMP-2C is detected in small
CC intestine, colon, heart, brain, skeletal muscle, and at lower levels in
CC kidney and placenta (PubMed:26856698). {ECO:0000269|PubMed:26856698,
CC ECO:0000269|PubMed:7488019}.
CC -!- INDUCTION: In peripheral blood B cells isoform LAMP-2A, LAMP-2B and
CC LAMP-2C are up-regulated in response to treatments that stimulate
CC immune responses via the Toll-like receptors TLR7 or TLR9.
CC {ECO:0000269|PubMed:26856698}.
CC -!- PTM: O- and N-glycosylated; some of the 16 N-linked glycans are
CC polylactosaminoglycans. {ECO:0000269|PubMed:12754519,
CC ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218,
CC ECO:0000269|PubMed:2243102, ECO:0000269|PubMed:2912382,
CC ECO:0000269|PubMed:8323299}.
CC -!- DISEASE: Danon disease (DAND) [MIM:300257]: DAND is a lysosomal
CC glycogen storage disease characterized by the clinical triad of
CC cardiomyopathy, vacuolar myopathy and intellectual disability. It is
CC often associated with an accumulation of glycogen in muscle and
CC lysosomes. {ECO:0000269|PubMed:15673802, ECO:0000269|PubMed:15907287}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the LAMP family. {ECO:0000255|PROSITE-
CC ProRule:PRU00740}.
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DR EMBL; J04183; AAA60383.1; -; mRNA.
DR EMBL; L09717; AAB41647.1; -; Genomic_DNA.
DR EMBL; L09709; AAB41647.1; JOINED; Genomic_DNA.
DR EMBL; L09710; AAB41647.1; JOINED; Genomic_DNA.
DR EMBL; L09711; AAB41647.1; JOINED; Genomic_DNA.
DR EMBL; L09712; AAB41647.1; JOINED; Genomic_DNA.
DR EMBL; L09713; AAB41647.1; JOINED; Genomic_DNA.
DR EMBL; L09714; AAB41647.1; JOINED; Genomic_DNA.
DR EMBL; L09715; AAB41647.1; JOINED; Genomic_DNA.
DR EMBL; L09716; AAB41647.1; JOINED; Genomic_DNA.
DR EMBL; X77196; CAA54416.1; -; mRNA.
DR EMBL; S79873; AAB35426.1; -; mRNA.
DR EMBL; U36336; AAA91149.1; -; mRNA.
DR EMBL; AY561849; AAS67876.1; -; mRNA.
DR EMBL; AK291090; BAF83779.1; -; mRNA.
DR EMBL; AC002476; AAB67313.1; -; Genomic_DNA.
DR EMBL; AC002476; AAB67314.1; -; Genomic_DNA.
DR EMBL; CH471107; EAX11881.1; -; Genomic_DNA.
DR EMBL; CH471107; EAX11882.1; -; Genomic_DNA.
DR EMBL; CH471107; EAX11883.1; -; Genomic_DNA.
DR EMBL; CH471107; EAX11884.1; -; Genomic_DNA.
DR EMBL; BC002965; AAH02965.1; -; mRNA.
DR CCDS; CCDS14599.1; -. [P13473-1]
DR CCDS; CCDS14600.1; -. [P13473-2]
DR CCDS; CCDS48159.1; -. [P13473-3]
DR PIR; JC2414; B31959.
DR PIR; JC4317; JC4317.
DR RefSeq; NP_001116078.1; NM_001122606.1. [P13473-3]
DR RefSeq; NP_002285.1; NM_002294.2. [P13473-1]
DR RefSeq; NP_054701.1; NM_013995.2. [P13473-2]
DR PDB; 2MOF; NMR; -; A=369-410.
DR PDB; 2MOM; NMR; -; A/B/C=369-410.
DR PDBsum; 2MOF; -.
DR PDBsum; 2MOM; -.
DR AlphaFoldDB; P13473; -.
DR BMRB; P13473; -.
DR SMR; P13473; -.
DR BioGRID; 110114; 609.
DR IntAct; P13473; 304.
DR MINT; P13473; -.
DR STRING; 9606.ENSP00000408411; -.
DR TCDB; 9.A.16.1.2; the lysosomal protein import (lpi) family.
DR GlyConnect; 356; 115 N-Linked glycans (12 sites), 3 O-Linked glycans.
DR GlyGen; P13473; 27 sites, 145 N-linked glycans (12 sites), 6 O-linked glycans (10 sites).
DR iPTMnet; P13473; -.
DR PhosphoSitePlus; P13473; -.
DR SwissPalm; P13473; -.
DR BioMuta; LAMP2; -.
DR DMDM; 1708854; -.
DR CPTAC; CPTAC-1494; -.
DR CPTAC; CPTAC-689; -.
DR EPD; P13473; -.
DR jPOST; P13473; -.
DR MassIVE; P13473; -.
DR MaxQB; P13473; -.
DR PeptideAtlas; P13473; -.
DR PRIDE; P13473; -.
DR ProteomicsDB; 52910; -. [P13473-1]
DR ProteomicsDB; 52911; -. [P13473-2]
DR ProteomicsDB; 52912; -. [P13473-3]
DR Antibodypedia; 3938; 1317 antibodies from 52 providers.
DR DNASU; 3920; -.
DR Ensembl; ENST00000200639.9; ENSP00000200639.4; ENSG00000005893.16. [P13473-1]
DR Ensembl; ENST00000371335.4; ENSP00000360386.4; ENSG00000005893.16. [P13473-2]
DR Ensembl; ENST00000434600.6; ENSP00000408411.2; ENSG00000005893.16. [P13473-3]
DR GeneID; 3920; -.
DR KEGG; hsa:3920; -.
DR MANE-Select; ENST00000200639.9; ENSP00000200639.4; NM_002294.3; NP_002285.1.
DR UCSC; uc004ess.5; human. [P13473-1]
DR CTD; 3920; -.
DR DisGeNET; 3920; -.
DR GeneCards; LAMP2; -.
DR GeneReviews; LAMP2; -.
DR HGNC; HGNC:6501; LAMP2.
DR HPA; ENSG00000005893; Low tissue specificity.
DR MalaCards; LAMP2; -.
DR MIM; 300257; phenotype.
DR MIM; 309060; gene.
DR neXtProt; NX_P13473; -.
DR OpenTargets; ENSG00000005893; -.
DR Orphanet; 34587; Glycogen storage disease due to LAMP-2 deficiency.
DR PharmGKB; PA30285; -.
DR VEuPathDB; HostDB:ENSG00000005893; -.
DR eggNOG; KOG4818; Eukaryota.
DR GeneTree; ENSGT00950000182899; -.
DR HOGENOM; CLU_055379_2_0_1; -.
DR InParanoid; P13473; -.
DR OMA; NMATGYE; -.
DR OrthoDB; 1042920at2759; -.
DR PhylomeDB; P13473; -.
DR TreeFam; TF316339; -.
DR PathwayCommons; P13473; -.
DR Reactome; R-HSA-114608; Platelet degranulation.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-9613829; Chaperone Mediated Autophagy.
DR SignaLink; P13473; -.
DR SIGNOR; P13473; -.
DR BioGRID-ORCS; 3920; 10 hits in 707 CRISPR screens.
DR ChiTaRS; LAMP2; human.
DR GeneWiki; LAMP2; -.
DR GenomeRNAi; 3920; -.
DR Pharos; P13473; Tbio.
DR PRO; PR:P13473; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P13473; protein.
DR Bgee; ENSG00000005893; Expressed in corpus callosum and 206 other tissues.
DR ExpressionAtlas; P13473; baseline and differential.
DR Genevisible; P13473; HS.
DR GO; GO:0044754; C:autolysosome; IDA:MGI.
DR GO; GO:0035577; C:azurophil granule membrane; TAS:Reactome.
DR GO; GO:0061742; C:chaperone-mediated autophagy translocation complex; IMP:ParkinsonsUK-UCL.
DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0101003; C:ficolin-1-rich granule membrane; TAS:Reactome.
DR GO; GO:0097637; C:integral component of autophagosome membrane; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005770; C:late endosome; IDA:MGI.
DR GO; GO:0031902; C:late endosome membrane; IDA:MGI.
DR GO; GO:0043202; C:lysosomal lumen; TAS:ParkinsonsUK-UCL.
DR GO; GO:0005765; C:lysosomal membrane; IDA:MGI.
DR GO; GO:0005764; C:lysosome; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IMP:ParkinsonsUK-UCL.
DR GO; GO:0030670; C:phagocytic vesicle membrane; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0031088; C:platelet dense granule membrane; IDA:MGI.
DR GO; GO:0005802; C:trans-Golgi network; IMP:ParkinsonsUK-UCL.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0097352; P:autophagosome maturation; ISS:UniProtKB.
DR GO; GO:0009267; P:cellular response to starvation; ISS:UniProtKB.
DR GO; GO:0061684; P:chaperone-mediated autophagy; IMP:ParkinsonsUK-UCL.
DR GO; GO:0072594; P:establishment of protein localization to organelle; IBA:GO_Central.
DR GO; GO:1905146; P:lysosomal protein catabolic process; IMP:UniProtKB.
DR GO; GO:0046716; P:muscle cell cellular homeostasis; IEA:Ensembl.
DR GO; GO:0031333; P:negative regulation of protein-containing complex assembly; IDA:ParkinsonsUK-UCL.
DR GO; GO:0017038; P:protein import; TAS:ParkinsonsUK-UCL.
DR GO; GO:0050821; P:protein stabilization; ISS:CAFA.
DR GO; GO:0006605; P:protein targeting; ISS:UniProtKB.
DR GO; GO:0061740; P:protein targeting to lysosome involved in chaperone-mediated autophagy; IMP:UniProtKB.
DR GO; GO:0031647; P:regulation of protein stability; IMP:ParkinsonsUK-UCL.
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; 1.
DR PROSITE; PS00311; LAMP_2; 1.
DR PROSITE; PS51407; LAMP_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Autophagy; Cell membrane;
KW Cytoplasmic vesicle; Direct protein sequencing; Disease variant;
KW Disulfide bond; Endosome; Glycogen storage disease; Glycoprotein; Lysosome;
KW Membrane; Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..28
FT /evidence="ECO:0000269|PubMed:15340161,
FT ECO:0000269|PubMed:2912382, ECO:0000269|PubMed:3198605"
FT CHAIN 29..410
FT /note="Lysosome-associated membrane glycoprotein 2"
FT /id="PRO_0000017110"
FT TOPO_DOM 29..375
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 376..399
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00740"
FT TOPO_DOM 400..410
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00740"
FT REGION 29..192
FT /note="First lumenal domain"
FT REGION 193..228
FT /note="Hinge"
FT REGION 199..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 229..375
FT /note="Second lumenal domain"
FT REGION 401..404
FT /note="Important for binding and subsequent lysosomal
FT degradation of target proteins"
FT /evidence="ECO:0000269|PubMed:11082038"
FT CARBOHYD 32
FT /note="N-linked (GlcNAc...) (polylactosaminoglycan)
FT asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) (polylactosaminoglycan)
FT asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 49
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754519,
FT ECO:0000269|PubMed:16335952"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:8323299"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:8323299"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754519,
FT ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218"
FT CARBOHYD 123
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19159218"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:8323299"
FT CARBOHYD 195
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000269|PubMed:8323299"
FT CARBOHYD 196
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 203
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:8323299"
FT CARBOHYD 204
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:8323299"
FT CARBOHYD 207
FT /note="O-linked (GalNAc...) serine; partial"
FT /evidence="ECO:0000269|PubMed:8323299"
FT CARBOHYD 209
FT /note="O-linked (GalNAc...) threonine; partial"
FT /evidence="ECO:0000269|PubMed:8323299"
FT CARBOHYD 210
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:8323299"
FT CARBOHYD 211
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:8323299"
FT CARBOHYD 213
FT /note="O-linked (GalNAc...) threonine; partial"
FT /evidence="ECO:0000269|PubMed:8323299"
FT CARBOHYD 229
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:8323299"
FT CARBOHYD 242
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:8323299"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19159218"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:8323299"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:8323299"
FT CARBOHYD 307
FT /note="N-linked (GlcNAc...) (polylactosaminoglycan)
FT asparagine"
FT /evidence="ECO:0000269|PubMed:8323299"
FT CARBOHYD 317
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:8323299"
FT CARBOHYD 356
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT DISULFID 41..79
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00740"
FT DISULFID 153..189
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00740"
FT DISULFID 232..265
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00740"
FT DISULFID 331..368
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00740"
FT VAR_SEQ 366..410
FT /note="QDCSADDDNFLVPIAVGAALAGVLILVLLAYFIGLKHHHAGYEQF -> EEC
FT SADSDLNFLIPVAVGVALGFLIIVVFISYMIGRRKSRTGYQSV (in isoform
FT LAMP-2C)"
FT /evidence="ECO:0000303|Ref.6"
FT /id="VSP_042519"
FT VAR_SEQ 367..410
FT /note="DCSADDDNFLVPIAVGAALAGVLILVLLAYFIGLKHHHAGYEQF -> ECSL
FT DDDTILIPIIVGAGLSGLIIVIVIAYVIGRRKSYAGYQTL (in isoform LAMP-
FT 2B)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:7488019, ECO:0000303|PubMed:8407947"
FT /id="VSP_003044"
FT VARIANT 256
FT /note="P -> H (in dbSNP:rs1043878)"
FT /id="VAR_011992"
FT VARIANT 321
FT /note="W -> R (in DAND; dbSNP:rs104894859)"
FT /evidence="ECO:0000269|PubMed:15673802,
FT ECO:0000269|PubMed:15907287"
FT /id="VAR_026230"
FT MUTAGEN 401..404
FT /note="KHHH->AAAA: Impairs binding and subsequent lysosomal
FT degradation of target proteins, such as GAPDH."
FT /evidence="ECO:0000269|PubMed:11082038"
FT CONFLICT 8..13
FT /note="PVPGSG -> RFRSGLR (in Ref. 3; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 53
FT /note="R -> G (in Ref. 3; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 68
FT /note="D -> V (in Ref. 2; AAB41647)"
FT /evidence="ECO:0000305"
FT CONFLICT 111
FT /note="I -> N (in Ref. 2; AAB41647)"
FT /evidence="ECO:0000305"
FT CONFLICT 143
FT /note="I -> Y (in Ref. 2; AAB41647)"
FT /evidence="ECO:0000305"
FT CONFLICT 220
FT /note="A -> P (in Ref. 2; AAB41647)"
FT /evidence="ECO:0000305"
FT CONFLICT 234
FT /note="L -> R (in Ref. 2; AAB41647)"
FT /evidence="ECO:0000305"
FT CONFLICT 263..269
FT /note="GSCRSHT -> AAAVSH (in Ref. 3; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 322..326
FT /note="DAPLG -> MPP (in Ref. 1; AAA60383)"
FT /evidence="ECO:0000305"
FT STRAND 374..377
FT /evidence="ECO:0007829|PDB:2MOF"
FT HELIX 380..400
FT /evidence="ECO:0007829|PDB:2MOF"
SQ SEQUENCE 410 AA; 44961 MW; 9E08E3B62D58F454 CRC64;
MVCFRLFPVP GSGLVLVCLV LGAVRSYALE LNLTDSENAT CLYAKWQMNF TVRYETTNKT
YKTVTISDHG TVTYNGSICG DDQNGPKIAV QFGPGFSWIA NFTKAASTYS IDSVSFSYNT
GDNTTFPDAE DKGILTVDEL LAIRIPLNDL FRCNSLSTLE KNDVVQHYWD VLVQAFVQNG
TVSTNEFLCD KDKTSTVAPT IHTTVPSPTT TPTPKEKPEA GTYSVNNGND TCLLATMGLQ
LNITQDKVAS VININPNTTH STGSCRSHTA LLRLNSSTIK YLDFVFAVKN ENRFYLKEVN
ISMYLVNGSV FSIANNNLSY WDAPLGSSYM CNKEQTVSVS GAFQINTFDL RVQPFNVTQG
KYSTAQDCSA DDDNFLVPIA VGAALAGVLI LVLLAYFIGL KHHHAGYEQF
