LAMP2_CRIGR
ID LAMP2_CRIGR Reviewed; 410 AA.
AC P49130;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 25-MAY-2022, entry version 88.
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 B;
DE Short=LGP-B;
DE AltName: CD_antigen=CD107b;
DE Flags: Precursor;
GN Name=LAMP2; Synonyms=LGPB;
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RX PubMed=8867788;
RA Uthayakumar S., Granger B.L.;
RT "Cell surface accumulation of overexpressed hamster lysosomal membrane
RT glycoproteins.";
RL Cell. Mol. Biol. Res. 41:405-420(1995).
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. Functions by binding target proteins, such
CC as GAPDH and MLLT11, and targeting them for lysosomal degradation (By
CC similarity). Plays a role in lysosomal protein degradation in response
CC to starvation (By similarity). Required for the fusion of
CC autophagosomes with lysosomes during autophagy. Cells that lack LAMP2
CC express normal levels of VAMP8, but fail to accumulate STX17 on
CC autophagosomes, which is the most likely explanation for the lack of
CC fusion between autophagosomes and lysosomes. Required for normal
CC degradation of the contents of autophagosomes. 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. Is not required for efficient MHCII-mediated
CC presentation of endogenous antigens (By similarity).
CC {ECO:0000250|UniProtKB:P13473, ECO:0000250|UniProtKB:P17046}.
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 (By similarity). Interacts
CC with FURIN (By similarity). {ECO:0000250|UniProtKB:P13473,
CC ECO:0000250|UniProtKB:P17046}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8867788};
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:0000255|PROSITE-
CC ProRule:PRU00740, ECO:0000269|PubMed:8867788}; Single-pass type I
CC membrane protein {ECO:0000255|PROSITE-ProRule:PRU00740}. Cytoplasmic
CC vesicle, autophagosome membrane {ECO:0000250|UniProtKB:P17047}.
CC Note=This protein shuttles between lysosomes, endosomes, and the plasma
CC membrane. {ECO:0000250}.
CC -!- PTM: Extensively N-glycosylated. Contains a minor proportion of O-
CC linked glycans. {ECO:0000250|UniProtKB:P17046}.
CC -!- SIMILARITY: Belongs to the LAMP family. {ECO:0000255|PROSITE-
CC ProRule:PRU00740}.
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DR EMBL; L19357; AAC37683.1; -; mRNA.
DR RefSeq; NP_001233678.1; NM_001246749.1.
DR AlphaFoldDB; P49130; -.
DR SMR; P49130; -.
DR STRING; 10029.NP_001233678.1; -.
DR GeneID; 100689316; -.
DR KEGG; cge:100689316; -.
DR CTD; 3920; -.
DR eggNOG; KOG4818; Eukaryota.
DR OrthoDB; 1042920at2759; -.
DR GO; GO:0000421; C:autophagosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; ISS:UniProtKB.
DR GO; GO:1905146; P:lysosomal protein catabolic process; ISS:UniProtKB.
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; ISS:UniProtKB.
DR InterPro; IPR018134; LAMP_CS.
DR InterPro; IPR002000; Lysosome-assoc_membr_glycop.
DR PANTHER; PTHR11506; PTHR11506; 1.
DR Pfam; PF01299; Lamp; 1.
DR PRINTS; PR00336; LYSASSOCTDMP.
DR PROSITE; PS00310; LAMP_1; 1.
DR PROSITE; PS00311; LAMP_2; 1.
DR PROSITE; PS51407; LAMP_3; 1.
PE 2: Evidence at transcript level;
KW Autophagy; Cell membrane; Cytoplasmic vesicle; Disulfide bond; Endosome;
KW Glycoprotein; Lysosome; Membrane; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..410
FT /note="Lysosome-associated membrane glycoprotein 2"
FT /id="PRO_0000017113"
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 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:0000250|UniProtKB:P13473"
FT CARBOHYD 48
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 58
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 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 123
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 222
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 229
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 242
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 260
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 307
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 356
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 40..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"
SQ SEQUENCE 410 AA; 45028 MW; ADA8EBF04285C406 CRC64;
MMCFRLSPVS GSGLVLSCLL LGAVQSYAFE LNLPDSKATC LFAKWKMNFT ISYETTTNKT
LKTVTISEPH NVTYNGSSCG DDQGVAKIAV QFGSTVSWNV TFTKEESHYV IGSIWLVYNT
SDNTTFPGAI PKGSATVISS QSIEIPLDDI FRCNSLLTFK TGNVVQNYWD IHLQAFVQNG
TVSKEEFVCE EDKSVTTVRP IIHTTVPPPT TTPTPLPPKV GNYSVSNGNA TCLLATMGLQ
LNVTEEKVPF IFNINPSTTN FTGSCHPQTA QLRLNNSQIK YLDFIFAVKS ESHFYLKEVN
VSMYMANGSV FSVANNNLSF WDAPLGSSYM CNKEQVVSVS RTFQINTFNL KVQPFNVTKG
KYATAQDCSA DEDNFLVPIA VGAALAGVLA LVLLAYFIGL KRHHTGYEQF
