LAMP2_MOUSE
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 03-AUG-2022, entry version 176.
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, Pancreas,
RC 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).
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:10972293). Functions by binding
CC target proteins, such as GAPDH and MLLT11, and targeting them for
CC lysosomal degradation (By similarity). 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). Plays a role in lysosomal protein
CC degradation in response to starvation (PubMed:27628032). Required for
CC efficient MHCII-mediated presentation of exogenous antigens via its
CC function in lysosomal protein degradation; antigenic peptides generated
CC by proteases in the endosomal/lysosomal compartment are captured by
CC nascent MHCII subunits. Is not required for efficient MHCII-mediated
CC presentation of endogenous antigens (By similarity).
CC {ECO:0000250|UniProtKB:P13473, ECO:0000250|UniProtKB:P17046,
CC ECO:0000269|PubMed:10972293, ECO:0000269|PubMed:12221139,
CC ECO:0000269|PubMed:27628032}.
CC -!- SUBUNIT: Monomer. Forms large homooligomers. Interacts (via its
CC cytoplasmic region) with HSPA8. Interacts with HSP90 in the lysosome
CC lumen; this enhances LAMP2 stability (By similarity). Interacts with
CC MLLT11 (By similarity). Interacts with ABCB9 (PubMed:22641697).
CC Interacts with FURIN (By similarity). {ECO:0000250|UniProtKB:P13473,
CC ECO:0000250|UniProtKB:P17046, ECO:0000269|PubMed:22641697}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P13473};
CC Single-pass type I membrane protein {ECO:0000255|PROSITE-
CC ProRule:PRU00740}. Endosome membrane {ECO:0000250|UniProtKB:P13473};
CC Single-pass type I membrane protein {ECO:0000255|PROSITE-
CC ProRule:PRU00740}. Cytoplasmic vesicle, autophagosome membrane
CC {ECO:0000269|PubMed:12221139}. Lysosome membrane
CC {ECO:0000269|PubMed:11082038, ECO:0000269|PubMed:2142158}; Single-pass
CC type I membrane protein {ECO:0000255|PROSITE-ProRule:PRU00740}.
CC Note=This protein shuttles between lysosomes, endosomes, and the plasma
CC membrane.
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; 34.
DR IntAct; P17047; 7.
DR MINT; P17047; -.
DR STRING; 10090.ENSMUSP00000052283; -.
DR ChEMBL; CHEMBL4630812; -.
DR GlyConnect; 2495; 10 N-Linked glycans (6 sites).
DR GlyGen; P17047; 17 sites, 10 N-linked glycans (6 sites).
DR iPTMnet; P17047; -.
DR PhosphoSitePlus; P17047; -.
DR SwissPalm; P17047; -.
DR EPD; P17047; -.
DR jPOST; P17047; -.
DR MaxQB; P17047; -.
DR PaxDb; P17047; -.
DR PeptideAtlas; P17047; -.
DR PRIDE; P17047; -.
DR ProteomicsDB; 263697; -. [P17047-1]
DR ProteomicsDB; 263698; -. [P17047-2]
DR ProteomicsDB; 263699; -. [P17047-3]
DR ABCD; P17047; 13 sequenced antibodies.
DR Antibodypedia; 3938; 1317 antibodies from 52 providers.
DR DNASU; 16784; -.
DR Ensembl; ENSMUST00000016678; ENSMUSP00000016678; ENSMUSG00000016534. [P17047-1]
DR Ensembl; ENSMUST00000061755; ENSMUSP00000052283; ENSMUSG00000016534. [P17047-3]
DR Ensembl; ENSMUST00000074913; ENSMUSP00000074448; ENSMUSG00000016534. [P17047-2]
DR GeneID; 16784; -.
DR KEGG; mmu:16784; -.
DR UCSC; uc009szw.2; mouse. [P17047-1]
DR UCSC; uc009szx.2; mouse. [P17047-3]
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; NMATGYE; -.
DR TreeFam; TF316339; -.
DR Reactome; R-MMU-114608; Platelet degranulation.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 16784; 0 hits in 72 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 257 other tissues.
DR ExpressionAtlas; P17047; baseline and differential.
DR Genevisible; P17047; MM.
DR GO; GO:0044754; C:autolysosome; ISO:MGI.
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:0097637; C:integral component of autophagosome membrane; IDA:UniProtKB.
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:0045121; C:membrane raft; 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:0019904; F:protein domain specific binding; IPI:UniProtKB.
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:0072594; P:establishment of protein localization to organelle; IBA:GO_Central.
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:0031333; P:negative regulation of protein-containing complex assembly; 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 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; 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:0000255"
FT CARBOHYD 45
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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:0000255"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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 DISULFID 149..185
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00740"
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 LAMP-
FT 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
