ID   LAMP2_MOUSE             Reviewed;         415 AA.
AC   P17047; A2A430; Q3TXG5; Q8BSG8;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   31-MAY-2011, sequence version 2.
DT   27-MAR-2024, entry version 185.
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=Lysosomal membrane glycoprotein type B;
DE            Short=LGP-B;
DE   AltName: CD_antigen=CD107b;
DE   Flags: Precursor;
GN   Name=Lamp2; Synonyms=Lamp-2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LAMP-2A).
RX   PubMed=2318880; DOI=10.1016/s0021-9258(19)34076-1;
RA   Cha Y., Holland S.M., August J.T.;
RT   "The cDNA sequence of mouse LAMP-2. Evidence for two classes of lysosomal
RT   membrane glycoproteins.";
RL   J. Biol. Chem. 265:5008-5013(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS LAMP-2A AND LAMP-2B).
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LAMP-2B).
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   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 58-128 AND 186-415,
RP   GLYCOSYLATION, AND SUBCELLULAR LOCATION.
RX   PubMed=2142158; DOI=10.1016/s0021-9258(19)38504-7;
RA   Granger B.L., Green S.A., Gabel C.A., Howe C.L., Mellman I., Helenius A.;
RT   "Characterization and cloning of lgp110, a lysosomal membrane glycoprotein
RT   from mouse and rat cells.";
RL   J. Biol. Chem. 265:12036-12043(1990).
RN   [7]
RP   ALTERNATIVE SPLICING.
RC   TISSUE=Brain;
RX   PubMed=7546292; DOI=10.1089/dna.1995.14.863;
RA   Gough N.R., Hatem C.L., Fambrough D.M.;
RT   "The family of LAMP-2 proteins arises by alternative splicing from a single
RT   gene: characterization of the avian LAMP-2 gene and identification of
RT   mammalian homologs of LAMP-2b and LAMP-2c.";
RL   DNA Cell Biol. 14:863-867(1995).
RN   [8]
RP   SUBCELLULAR LOCATION.
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   [9]
RP   DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=10972293; DOI=10.1038/35022595;
RA   Tanaka Y., Guhde G., Suter A., Eskelinen E.L., Hartmann D.,
RA   Luellmann-Rauch R., Janssen P.M., Blanz J., von Figura K., Saftig P.;
RT   "Accumulation of autophagic vacuoles and cardiomyopathy in LAMP-2-deficient
RT   mice.";
RL   Nature 406:902-906(2000).
RN   [10]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=12221139; DOI=10.1091/mbc.e02-02-0114;
RA   Eskelinen E.L., Illert A.L., Tanaka Y., Schwarzmann G., Blanz J.,
RA   Von Figura K., Saftig P.;
RT   "Role of LAMP-2 in lysosome biogenesis and autophagy.";
RL   Mol. Biol. Cell 13:3355-3368(2002).
RN   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [12]
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   [13]
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   [14] {ECO:0007744|PDB:5GV3}
RP   X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 26-189, DISULFIDE BONDS, AND
RP   GLYCOSYLATION AT ASN-29; ASN-45; ASN-57; ASN-97 AND ASN-115.
RX   PubMed=27663661; DOI=10.1016/j.bbrc.2016.09.093;
RA   Terasawa K., Tomabechi Y., Ikeda M., Ehara H., Kukimoto-Niino M.,
RA   Wakiyama M., Podyma-Inoue K.A., Rajapakshe A.R., Watabe T., Shirouzu M.,
RA   Hara-Yokoyama M.;
RT   "Lysosome-associated membrane proteins-1 and -2 (LAMP-1 and LAMP-2)
RT   assemble via distinct modes.";
RL   Biochem. Biophys. Res. Commun. 479:489-495(2016).
CC   -!- FUNCTION: Lysosomal membrane glycoprotein which plays an important role
CC       in lysosome biogenesis, lysosomal pH regulation and autophagy
CC       (PubMed:10972293). Acts as an important regulator of lysosomal lumen pH
CC       regulation by acting as a direct inhibitor of the proton channel
CC       TMEM175, facilitating lysosomal acidification for optimal hydrolase
CC       activity (By similarity). Plays an important role in chaperone-mediated
CC       autophagy, a process that mediates lysosomal degradation of proteins in
CC       response to various stresses and as part of the normal turnover of
CC       proteins with a long biological half-live (By similarity). Functions by
CC       binding target proteins, such as GAPDH, NLRP3 and MLLT11, and targeting
CC       them for lysosomal degradation (By similarity). In the chaperone-
CC       mediated autophagy, acts downstream of chaperones, such as HSPA8/HSC70,
CC       which recognize and bind substrate proteins and mediate their
CC       recruitment to lysosomes, where target proteins bind LAMP2 (By
CC       similarity). Plays a role in lysosomal protein degradation in response
CC       to starvation (PubMed:27628032). Required for the fusion of
CC       autophagosomes with lysosomes during autophagy (PubMed:27628032). Cells
CC       that lack LAMP2 express normal levels of VAMP8, but fail to accumulate
CC       STX17 on autophagosomes, which is the most likely explanation for the
CC       lack of fusion between autophagosomes and lysosomes (PubMed:27628032).
CC       Required for normal degradation of the contents of autophagosomes
CC       (PubMed:10972293, PubMed:12221139). Required for efficient MHC class
CC       II-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 MHC II subunits (By similarity). Is not required for efficient
CC       MHC class II-mediated presentation of endogenous antigens (By
CC       similarity). {ECO:0000250|UniProtKB:P13473,
CC       ECO:0000269|PubMed:10972293, ECO:0000269|PubMed:12221139,
CC       ECO:0000269|PubMed:27628032}.
CC   -!- SUBUNIT: Monomer. Forms large homooligomers (By similarity). Interacts
CC       (via its cytoplasmic region) with HSPA8; HSPA8 mediates recruitment of
CC       proteins with a KFERQ motif to the surface of the lysosome for
CC       chaperone-mediated autophagy (By similarity). Interacts with HSP90 in
CC       the lysosome lumen; this enhances LAMP2 stability (By similarity).
CC       Interacts with MLLT11 (By similarity). Interacts with ABCB9
CC       (PubMed:22641697). Interacts with FURIN (By similarity). Interacts with
CC       CT55; this interaction may be important for LAMP2 protein stability (By
CC       similarity). Interacts with TMEM175; inhibiting the proton channel
CC       activity of TMEM175 (By similarity). {ECO:0000250|UniProtKB:P13473,
CC       ECO:0000250|UniProtKB:P17046, ECO:0000269|PubMed:22641697}.
CC   -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:11082038,
CC       ECO:0000269|PubMed:2142158}; Single-pass type I membrane protein
CC       {ECO:0000255|PROSITE-ProRule:PRU00740}. Endosome membrane
CC       {ECO:0000250|UniProtKB:P13473}; Single-pass type I membrane protein
CC       {ECO:0000255|PROSITE-ProRule:PRU00740}. Cytoplasmic vesicle,
CC       autophagosome membrane {ECO:0000269|PubMed:12221139}. Cell membrane
CC       {ECO:0000250|UniProtKB:P13473}; Single-pass type I membrane protein
CC       {ECO:0000255|PROSITE-ProRule:PRU00740}. Note=This protein shuttles
CC       between lysosomes, endosomes, and the plasma membrane.
CC       {ECO:0000250|UniProtKB:P13473}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=LAMP-2A;
CC         IsoId=P17047-1; Sequence=Displayed;
CC       Name=LAMP-2B;
CC         IsoId=P17047-2; Sequence=VSP_003045;
CC       Name=LAMP-2C;
CC         IsoId=P17047-3; Sequence=VSP_003046;
CC   -!- TISSUE SPECIFICITY: Detected in liver and kidney (at protein level).
CC       Detected in liver and kidney. {ECO:0000269|PubMed:10972293}.
CC   -!- PTM: Extensively N-glycosylated. Contains a minor proportion of O-
CC       linked glycans. {ECO:0000269|PubMed:2142158}.
CC   -!- DISRUPTION PHENOTYPE: About half of the mutant mice die between 20 and
CC       40 days after birth. Survivors are smaller, weigh 10 to 15 % less than
CC       their littermates, but show normal lifespan. Both mice that die early
CC       and long-time survivors display an accumulation of autophagic vacuoles
CC       in liver, pancreas, cardiac and skeletal muscle. Mutant mice display an
CC       increased ratio of heart weight to body weight and severely impaired
CC       contractile function of the heart muscle. Hepatocytes from mutant mice
CC       show a decreased rate of degradation of long-lived proteins.
CC       {ECO:0000269|PubMed:10972293}.
CC   -!- SIMILARITY: Belongs to the LAMP family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00740}.
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DR   EMBL; J05287; AAA39412.1; -; mRNA.
DR   EMBL; AK159272; BAE34951.1; -; mRNA.
DR   EMBL; AK032974; BAC28106.1; -; mRNA.
DR   EMBL; AK163933; BAE37543.1; -; mRNA.
DR   EMBL; AL513356; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH466570; EDL29016.1; -; Genomic_DNA.
DR   EMBL; CH466570; EDL29018.1; -; Genomic_DNA.
DR   EMBL; BC138718; AAI38719.1; -; mRNA.
DR   EMBL; BC138723; AAI38724.1; -; mRNA.
DR   EMBL; M32017; AAA39429.1; -; mRNA.
DR   EMBL; M32018; AAA39430.1; -; Genomic_DNA.
DR   CCDS; CCDS30092.1; -. [P17047-1]
DR   CCDS; CCDS30093.1; -. [P17047-3]
DR   CCDS; CCDS72369.1; -. [P17047-2]
DR   PIR; A35560; A35560.
DR   RefSeq; NP_001017959.1; NM_001017959.2. [P17047-1]
DR   RefSeq; NP_034815.2; NM_010685.4. [P17047-3]
DR   PDB; 5GV3; X-ray; 2.10 A; A/B=26-189.
DR   PDBsum; 5GV3; -.
DR   AlphaFoldDB; P17047; -.
DR   SMR; P17047; -.
DR   BioGRID; 201106; 35.
DR   IntAct; P17047; 7.
DR   MINT; P17047; -.
DR   STRING; 10090.ENSMUSP00000074448; -.
DR   ChEMBL; CHEMBL4630812; -.
DR   GlyConnect; 2495; 10 N-Linked glycans (6 sites).
DR   GlyCosmos; P17047; 17 sites, 10 glycans.
DR   GlyGen; P17047; 18 sites, 10 N-linked glycans (6 sites), 1 O-linked glycan (1 site).
DR   iPTMnet; P17047; -.
DR   PhosphoSitePlus; P17047; -.
DR   SwissPalm; P17047; -.
DR   EPD; P17047; -.
DR   jPOST; P17047; -.
DR   MaxQB; P17047; -.
DR   PaxDb; 10090-ENSMUSP00000052283; -.
DR   PeptideAtlas; P17047; -.
DR   ProteomicsDB; 263697; -. [P17047-1]
DR   ProteomicsDB; 263698; -. [P17047-2]
DR   ProteomicsDB; 263699; -. [P17047-3]
DR   Pumba; P17047; -.
DR   ABCD; P17047; 13 sequenced antibodies.
DR   Antibodypedia; 3938; 1439 antibodies from 52 providers.
DR   DNASU; 16784; -.
DR   Ensembl; ENSMUST00000016678.14; ENSMUSP00000016678.8; ENSMUSG00000016534.16. [P17047-1]
DR   Ensembl; ENSMUST00000061755.9; ENSMUSP00000052283.9; ENSMUSG00000016534.16. [P17047-3]
DR   Ensembl; ENSMUST00000074913.12; ENSMUSP00000074448.6; ENSMUSG00000016534.16. [P17047-2]
DR   GeneID; 16784; -.
DR   KEGG; mmu:16784; -.
DR   UCSC; uc009szw.2; mouse. [P17047-1]
DR   UCSC; uc009szx.2; mouse. [P17047-3]
DR   AGR; MGI:96748; -.
DR   CTD; 3920; -.
DR   MGI; MGI:96748; Lamp2.
DR   VEuPathDB; HostDB:ENSMUSG00000016534; -.
DR   eggNOG; KOG4818; Eukaryota.
DR   GeneTree; ENSGT00950000182899; -.
DR   HOGENOM; CLU_055379_2_0_1; -.
DR   InParanoid; P17047; -.
DR   OMA; CHPQTAQ; -.
DR   OrthoDB; 5317371at2759; -.
DR   TreeFam; TF316339; -.
DR   Reactome; R-MMU-114608; Platelet degranulation.
DR   Reactome; R-MMU-6798695; Neutrophil degranulation.
DR   BioGRID-ORCS; 16784; 0 hits in 77 CRISPR screens.
DR   ChiTaRS; Lamp2; mouse.
DR   PRO; PR:P17047; -.
DR   Proteomes; UP000000589; Chromosome X.
DR   RNAct; P17047; Protein.
DR   Bgee; ENSMUSG00000016534; Expressed in ciliary body and 261 other cell types or tissues.
DR   ExpressionAtlas; P17047; baseline and differential.
DR   GO; GO:0044754; C:autolysosome; ISO:MGI.
DR   GO; GO:0000421; C:autophagosome membrane; IDA:UniProtKB.
DR   GO; GO:0061742; C:chaperone-mediated autophagy translocation complex; ISS:ParkinsonsUK-UCL.
DR   GO; GO:0005768; C:endosome; ISO:MGI.
DR   GO; GO:0070062; C:extracellular exosome; ISO:MGI.
DR   GO; GO:0005615; C:extracellular space; ISO:MGI.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR   GO; GO:0005770; C:late endosome; IDA:MGI.
DR   GO; GO:0031902; C:late endosome membrane; IDA:MGI.
DR   GO; GO:1990836; C:lysosomal matrix; ISO:MGI.
DR   GO; GO:0005765; C:lysosomal membrane; IDA:BHF-UCL.
DR   GO; GO:0005764; C:lysosome; IDA:MGI.
DR   GO; GO:0016020; C:membrane; ISO:MGI.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR   GO; GO:0030670; C:phagocytic vesicle membrane; IMP:MGI.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0031088; C:platelet dense granule membrane; ISO:MGI.
DR   GO; GO:0005802; C:trans-Golgi network; ISO:MGI.
DR   GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR   GO; GO:0008200; F:ion channel inhibitor activity; ISS:UniProtKB.
DR   GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
DR   GO; GO:0035591; F:signaling adaptor activity; ISO:MGI.
DR   GO; GO:0097352; P:autophagosome maturation; IMP:UniProtKB.
DR   GO; GO:0006914; P:autophagy; IMP:UniProtKB.
DR   GO; GO:0009267; P:cellular response to starvation; IMP:UniProtKB.
DR   GO; GO:0061684; P:chaperone-mediated autophagy; IMP:UniProtKB.
DR   GO; GO:0007042; P:lysosomal lumen acidification; ISS:UniProtKB.
DR   GO; GO:1905146; P:lysosomal protein catabolic process; ISS:UniProtKB.
DR   GO; GO:0046716; P:muscle cell cellular homeostasis; IMP:MGI.
DR   GO; GO:1900226; P:negative regulation of NLRP3 inflammasome complex assembly; ISO:MGI.
DR   GO; GO:0031333; P:negative regulation of protein-containing complex assembly; ISO:MGI.
DR   GO; GO:0030163; P:protein catabolic process; ISO:MGI.
DR   GO; GO:0050821; P:protein stabilization; IMP:UniProtKB.
DR   GO; GO:0006605; P:protein targeting; IMP: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; ISO:MGI.
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:SF28; FI04419P; 1.
DR   PANTHER; PTHR11506; LYSOSOME-ASSOCIATED MEMBRANE GLYCOPROTEIN; 1.
DR   Pfam; PF01299; Lamp; 2.
DR   Pfam; PF21222; Lamp2_2nd; 1.
DR   PRINTS; PR00336; LYSASSOCTDMP.
DR   PROSITE; PS00310; LAMP_1; 1.
DR   PROSITE; PS00311; LAMP_2; 1.
DR   PROSITE; PS51407; LAMP_3; 1.
DR   Genevisible; P17047; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Autophagy; Cell membrane;
KW   Cytoplasmic vesicle; Disulfide bond; Endosome; Glycoprotein; Lysosome;
KW   Membrane; Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..25
FT   CHAIN           26..415
FT                   /note="Lysosome-associated membrane glycoprotein 2"
FT                   /id="PRO_0000017111"
FT   TOPO_DOM        26..379
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        380..404
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00740"
FT   TOPO_DOM        405..415
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00740"
FT   REGION          26..188
FT                   /note="First lumenal domain"
FT   REGION          189..233
FT                   /note="Hinge"
FT   REGION          202..227
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          234..379
FT                   /note="Second lumenal domain"
FT   REGION          406..409
FT                   /note="Important for binding and subsequent lysosomal
FT                   degradation of target proteins"
FT                   /evidence="ECO:0000250|UniProtKB:P13473"
FT   CARBOHYD        29
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:27663661,
FT                   ECO:0007744|PDB:5GV3"
FT   CARBOHYD        45
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:27663661,
FT                   ECO:0007744|PDB:5GV3"
FT   CARBOHYD        54
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        57
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:27663661,
FT                   ECO:0007744|PDB:5GV3"
FT   CARBOHYD        97
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:27663661,
FT                   ECO:0007744|PDB:5GV3"
FT   CARBOHYD        115
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:27663661,
FT                   ECO:0007744|PDB:5GV3"
FT   CARBOHYD        175
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        227
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        234
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        247
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        265
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        280
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        312
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        317
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        322
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        361
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        37..75
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00740,
FT                   ECO:0000269|PubMed:27663661, ECO:0007744|PDB:5GV3"
FT   DISULFID        149..185
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00740,
FT                   ECO:0000269|PubMed:27663661, ECO:0007744|PDB:5GV3"
FT   DISULFID        237..270
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00740"
FT   DISULFID        336..373
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00740"
FT   VAR_SEQ         371..415
FT                   /note="QDCSADEDNFLVPIAVGAALGGVLILVLLAYFIGLKRHHTGYEQF -> EEC
FT                   AADSDLNFLIPVAVGVALGFLIIAVFISYMIGRRKSRTGYQSV (in isoform
FT                   LAMP-2B)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:16141072"
FT                   /id="VSP_003045"
FT   VAR_SEQ         372..415
FT                   /note="DCSADEDNFLVPIAVGAALGGVLILVLLAYFIGLKRHHTGYEQF -> ECSL
FT                   DDDTILIPIIVGAGLSGLIIVIVIAYLIGRRKTYAGYQTL (in isoform
FT                   LAMP-2C)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_003046"
FT   CONFLICT        272
FT                   /note="P -> H (in Ref. 2; BAE34951)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        289
FT                   /note="F -> L (in Ref. 1; AAA39412)"
FT                   /evidence="ECO:0000305"
FT   STRAND          26..32
FT                   /evidence="ECO:0007829|PDB:5GV3"
FT   STRAND          35..52
FT                   /evidence="ECO:0007829|PDB:5GV3"
FT   TURN            53..55
FT                   /evidence="ECO:0007829|PDB:5GV3"
FT   STRAND          56..63
FT                   /evidence="ECO:0007829|PDB:5GV3"
FT   STRAND          83..88
FT                   /evidence="ECO:0007829|PDB:5GV3"
FT   TURN            89..91
FT                   /evidence="ECO:0007829|PDB:5GV3"
FT   STRAND          92..100
FT                   /evidence="ECO:0007829|PDB:5GV3"
FT   STRAND          102..115
FT                   /evidence="ECO:0007829|PDB:5GV3"
FT   TURN            119..121
FT                   /evidence="ECO:0007829|PDB:5GV3"
FT   STRAND          125..127
FT                   /evidence="ECO:0007829|PDB:5GV3"
FT   STRAND          129..134
FT                   /evidence="ECO:0007829|PDB:5GV3"
FT   STRAND          139..141
FT                   /evidence="ECO:0007829|PDB:5GV3"
FT   STRAND          145..149
FT                   /evidence="ECO:0007829|PDB:5GV3"
FT   STRAND          153..157
FT                   /evidence="ECO:0007829|PDB:5GV3"
FT   STRAND          160..172
FT                   /evidence="ECO:0007829|PDB:5GV3"
FT   STRAND          182..184
FT                   /evidence="ECO:0007829|PDB:5GV3"
FT   HELIX           186..188
FT                   /evidence="ECO:0007829|PDB:5GV3"
SQ   SEQUENCE   415 AA;  45681 MW;  053A874B4DF67C88 CRC64;
     MCLSPVKGAK LILIFLFLGA VQSNALIVNL TDSKGTCLYA EWEMNFTITY ETTNQTNKTI
     TIAVPDKATH DGSSCGDDRN SAKIMIQFGF AVSWAVNFTK EASHYSIHDI VLSYNTSDST
     VFPGAVAKGV HTVKNPENFK VPLDVIFKCN SVLTYNLTPV VQKYWGIHLQ AFVQNGTVSK
     NEQVCEEDQT PTTVAPIIHT TAPSTTTTLT PTSTPTPTPT PTPTVGNYSI RNGNTTCLLA
     TMGLQLNITE EKVPFIFNIN PATTNFTGSC QPQSAQLRLN NSQIKYLDFI FAVKNEKRFY
     LKEVNVYMYL ANGSAFNISN KNLSFWDAPL GSSYMCNKEQ VLSVSRAFQI NTFNLKVQPF
     NVTKGQYSTA QDCSADEDNF LVPIAVGAAL GGVLILVLLA YFIGLKRHHT GYEQF
//