LAMP2_RAT
ID LAMP2_RAT Reviewed; 411 AA.
AC P17046; F1LLX8; Q6P6W1;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2017, sequence version 3.
DT 03-AUG-2022, entry version 146.
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-110 {ECO:0000303|PubMed:2142158};
DE AltName: Full=LGP-96 {ECO:0000303|PubMed:2590192};
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 27-45, AND SUBCELLULAR
RP LOCATION.
RX PubMed=2590192; DOI=10.1016/0006-291x(89)91784-1;
RA Noguchi Y., Himeno M., Sasaki H., Tanaka Y., Kono A., Sakaki Y., Kato K.;
RT "Isolation and sequencing of a cDNA clone encoding 96 kDa sialoglycoprotein
RT in rat liver lysosomal membranes.";
RL Biochem. Biophys. Res. Commun. 164:1113-1120(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate {ECO:0000312|EMBL:AAH61990.1};
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 19-411.
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 [5]
RP PROTEIN SEQUENCE OF 27-36, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP GLYCOSYLATION.
RC TISSUE=Liver;
RX PubMed=1794981; DOI=10.1093/oxfordjournals.jbchem.a123690;
RA Akasaki K., Yamaguchi Y., Furuno K., Tsuji H.;
RT "Purification, some properties, and tissue distribution of a major
RT lysosome-associated membrane glycoprotein (r-lamp-2) of rat liver.";
RL J. Biochem. 110:922-927(1991).
RN [6]
RP PROTEIN SEQUENCE OF 121-148; 282-290 AND 404-411, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U., Lubec S.;
RL Submitted (SEP-2007) to UniProtKB.
RN [7]
RP PROTEIN SEQUENCE OF 27-36, 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 [8]
RP FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, AND SUBUNIT.
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 FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, INTERACTION WITH HSPA8 AND HSP90,
RP AND GLYCOSYLATION.
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).
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). Binds
CC target proteins, such as GAPDH, and targets them for lysosomal
CC degradation (PubMed:8662539, PubMed:11082038, PubMed:18644871). Plays a
CC role in lysosomal protein degradation in response to starvation
CC (PubMed:11082038). Required for the fusion of autophagosomes with
CC lysosomes during autophagy. Cells that lack LAMP2 express normal levels
CC of 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. Required for normal degradation of the contents of
CC autophagosomes. Required for efficient MHCII-mediated presentation of
CC exogenous antigens via its function in lysosomal protein degradation;
CC antigenic peptides generated by proteases in the endosomal/lysosomal
CC compartment are captured by nascent MHCII subunits. Is not required for
CC efficient MHCII-mediated presentation of endogenous antigens (By
CC similarity). {ECO:0000250|UniProtKB:P13473,
CC ECO:0000269|PubMed:11082038, ECO:0000269|PubMed:8662539}.
CC -!- SUBUNIT: Monomer (PubMed:18644871). Forms large homooligomers
CC (PubMed:11082038, PubMed:18644871). Interacts (via its cytoplasmic
CC region) with HSPA8 (PubMed:18644871). Interacts with HSP90 in the
CC lysosome lumen; this enhances LAMP2 stability (PubMed:18644871).
CC Interacts with MLLT11 (By similarity). Interacts with ABCB9 (By
CC similarity). Interacts with FURIN (By similarity).
CC {ECO:0000250|UniProtKB:P13473, ECO:0000269|PubMed:11082038,
CC ECO:0000269|PubMed:18644871}.
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}. Lysosome membrane {ECO:0000269|PubMed:11082038,
CC ECO:0000269|PubMed:1794981, ECO:0000269|PubMed:18644871,
CC ECO:0000269|PubMed:2590192, ECO:0000269|PubMed:8662539}; Single-pass
CC type I membrane protein {ECO:0000269|PubMed:11082038}. Cytoplasmic
CC vesicle, autophagosome membrane {ECO:0000250|UniProtKB:P17047}.
CC Note=This protein shuttles between lysosomes, endosomes, and the plasma
CC membrane.
CC -!- TISSUE SPECIFICITY: Detected in liver, kidney, spleen and macrophages
CC (at protein level). {ECO:0000269|PubMed:1794981}.
CC -!- PTM: Extensively N-glycosylated (PubMed:1794981, PubMed:18644871).
CC Contains a minor proportion of O-linked glycans (PubMed:1794981).
CC Contains sialylated glycans (PubMed:1794981).
CC {ECO:0000269|PubMed:1794981, ECO:0000269|PubMed:18644871}.
CC -!- SIMILARITY: Belongs to the LAMP family. {ECO:0000255|PROSITE-
CC ProRule:PRU00740}.
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DR EMBL; D90211; BAA14236.1; -; mRNA.
DR EMBL; AABR07041263; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC061990; AAH61990.1; -; mRNA.
DR EMBL; M32016; AAA41526.1; -; mRNA.
DR PIR; A33664; A33664.
DR RefSeq; NP_058764.2; NM_017068.2.
DR AlphaFoldDB; P17046; -.
DR SMR; P17046; -.
DR IntAct; P17046; 6.
DR MINT; P17046; -.
DR STRING; 10116.ENSRNOP00000000177; -.
DR GlyGen; P17046; 16 sites, 7 N-linked glycans (3 sites).
DR jPOST; P17046; -.
DR PaxDb; P17046; -.
DR PRIDE; P17046; -.
DR Ensembl; ENSRNOT00000000177; ENSRNOP00000000177; ENSRNOG00000000164.
DR GeneID; 24944; -.
DR KEGG; rno:24944; -.
DR UCSC; RGD:2990; rat.
DR CTD; 3920; -.
DR RGD; 2990; Lamp2.
DR eggNOG; KOG4818; Eukaryota.
DR GeneTree; ENSGT00950000182899; -.
DR InParanoid; P17046; -.
DR OMA; NMATGYE; -.
DR OrthoDB; 1042920at2759; -.
DR PhylomeDB; P17046; -.
DR TreeFam; TF316339; -.
DR Reactome; R-RNO-114608; Platelet degranulation.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR PRO; PR:P17046; -.
DR Proteomes; UP000002494; Chromosome X.
DR Bgee; ENSRNOG00000000164; Expressed in liver and 20 other tissues.
DR Genevisible; Q6P6W1; RN.
DR GO; GO:0044754; C:autolysosome; ISO:RGD.
DR GO; GO:0061742; C:chaperone-mediated autophagy translocation complex; ISS:ParkinsonsUK-UCL.
DR GO; GO:0005768; C:endosome; IDA:RGD.
DR GO; GO:0070062; C:extracellular exosome; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; ISO:RGD.
DR GO; GO:0097637; C:integral component of autophagosome membrane; ISO:RGD.
DR GO; GO:0005770; C:late endosome; ISO:RGD.
DR GO; GO:0031902; C:late endosome membrane; ISO:RGD.
DR GO; GO:1990836; C:lysosomal matrix; IDA:MGI.
DR GO; GO:0005765; C:lysosomal membrane; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005764; C:lysosome; IDA:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0030670; C:phagocytic vesicle membrane; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0031088; C:platelet dense granule membrane; ISO:RGD.
DR GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR GO; GO:0019904; F:protein domain specific binding; ISO:RGD.
DR GO; GO:0097352; P:autophagosome maturation; ISS:UniProtKB.
DR GO; GO:0006914; P:autophagy; ISO:RGD.
DR GO; GO:0009267; P:cellular response to starvation; ISS:UniProtKB.
DR GO; GO:0061684; P:chaperone-mediated autophagy; IDA: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; ISS:UniProtKB.
DR GO; GO:0046716; P:muscle cell cellular homeostasis; ISO:RGD.
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:MGI.
DR GO; GO:0031647; P:regulation of protein stability; ISO:RGD.
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 Autophagy; Cell membrane; Cytoplasmic vesicle; Direct protein sequencing;
KW Disulfide bond; Endosome; Glycoprotein; Lysosome; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000269|PubMed:1794981,
FT ECO:0000269|PubMed:2590192, ECO:0000269|PubMed:8662539"
FT CHAIN 27..411
FT /note="Lysosome-associated membrane glycoprotein 2"
FT /id="PRO_0000017112"
FT TOPO_DOM 27..376
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 377..400
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00740"
FT TOPO_DOM 401..411
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00740,
FT ECO:0000305|PubMed:1794981"
FT REGION 27..188
FT /note="First lumenal domain"
FT REGION 189..229
FT /note="Hinge"
FT REGION 230..376
FT /note="Second lumenal domain"
FT REGION 402..405
FT /note="Important for binding and subsequent lysosomal
FT degradation of target proteins"
FT /evidence="ECO:0000250|UniProtKB:P13473"
FT CARBOHYD 30
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 46
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 71
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 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 117
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 223
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 230
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 243
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 261
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 276
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 308
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 318
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 357
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 38..75
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00740"
FT DISULFID 149..185
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00740"
FT DISULFID 233..266
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00740"
FT DISULFID 332..369
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00740"
FT CONFLICT 4..8
FT /note="LSPVT -> PLSGY (in Ref. 1; BAA14236)"
FT CONFLICT 259
FT /note="I -> T (in Ref. 1; BAA14236, 4; AAA41526 and 3;
FT AAH61990)"
SQ SEQUENCE 411 AA; 45156 MW; 001CFBA548AD3869 CRC64;
MRLLSPVTGS KLVLLFLFLG AVRSDALKLN LTDSKGTCLY AEWEMNFTIT YEALKVNETV
TITVPDKVTY NGSSCGDDKN GAKIMIQYGS TLSWAVNFTK EASQYFINNI TLSYNTNDTK
TFPGAVPKGI LTVIIPVGSQ LPLGVIFKCS SVLTFNLSPV VQHYWGIHLQ AFVQNGTVSK
HEQVCKEDKT ATTVAPIIHT TVPSPTTTLT PTSIPVPTPT VGNYTISNGN ATCLLATMGL
QLNITEEKVP FIFNINPAIT NFTGSCQPQT AQLRLNNSQI KYLDFIFAVK NEKRFYLKEV
NVNMYLANGS AFHVSNNNLS FWDAPLGSSY MCNKEQVVSV SRTFQINTFN LKVQPFNVTK
GEYSTAQDCS ADEDNFLVPI AVGAALGGVL ILVLLAYFIG LKRHHTGYEQ F
