LAMP2_CHICK
ID LAMP2_CHICK Reviewed; 425 AA.
AC Q90617; Q90616; Q90618;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Lysosome-associated membrane glycoprotein 2;
DE Short=LAMP-2;
DE Short=Lysosome-associated membrane protein 2;
DE Flags: Precursor;
GN Name=LAMP2;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LAMP-2A; LAMP-2B AND LAMP-2C).
RC STRAIN=White leghorn; 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).
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).
CC {ECO:0000250|UniProtKB:P13473, ECO:0000250|UniProtKB:P17046}.
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:0000255|PROSITE-
CC ProRule:PRU00740}; Single-pass type I membrane protein
CC {ECO:0000255|PROSITE-ProRule:PRU00740}. Cytoplasmic vesicle,
CC autophagosome membrane {ECO:0000250|UniProtKB:P17047}. Note=This
CC protein shuttles between lysosomes, endosomes, and the plasma membrane.
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=LAMP-2B;
CC IsoId=Q90617-1; Sequence=Displayed;
CC Name=LAMP-2A;
CC IsoId=Q90617-2; Sequence=VSP_003048;
CC Name=LAMP-2C;
CC IsoId=Q90617-3; Sequence=VSP_003047;
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; U10547; AAA99540.1; -; mRNA.
DR EMBL; U10546; AAA99539.1; -; mRNA.
DR EMBL; U10548; AAA99541.1; -; mRNA.
DR RefSeq; NP_001001749.1; NM_001001749.1. [Q90617-1]
DR AlphaFoldDB; Q90617; -.
DR SMR; Q90617; -.
DR STRING; 9031.ENSGALP00000013946; -.
DR PaxDb; Q90617; -.
DR GeneID; 414800; -.
DR KEGG; gga:414800; -.
DR CTD; 3920; -.
DR VEuPathDB; HostDB:geneid_414800; -.
DR eggNOG; KOG4818; Eukaryota.
DR HOGENOM; CLU_055379_2_0_1; -.
DR InParanoid; Q90617; -.
DR OrthoDB; 1042920at2759; -.
DR PhylomeDB; Q90617; -.
DR TreeFam; TF316339; -.
DR PRO; PR:Q90617; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0097637; C:integral component of autophagosome membrane; IBA:GO_Central.
DR GO; GO:0031902; C:late endosome membrane; IBA:GO_Central.
DR GO; GO:0005765; C:lysosomal membrane; IBA:GO_Central.
DR GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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: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: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; PS51407; LAMP_3; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Autophagy; Cell membrane; Cytoplasmic vesicle;
KW Disulfide bond; Endosome; Glycoprotein; Lysosome; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..425
FT /note="Lysosome-associated membrane glycoprotein 2"
FT /id="PRO_0000017114"
FT TOPO_DOM 28..389
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 390..414
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00740"
FT TOPO_DOM 415..425
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00740"
FT REGION 28..192
FT /note="First lumenal domain"
FT REGION 193..238
FT /note="Hinge"
FT REGION 239..390
FT /note="Second lumenal domain"
FT REGION 416..419
FT /note="Important for binding and subsequent lysosomal
FT degradation of target proteins"
FT /evidence="ECO:0000250|UniProtKB:P13473"
FT CARBOHYD 37
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 170
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 206
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 232
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 239
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 252
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 287
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 298
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 320
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 331
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 40..78
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00740"
FT DISULFID 153..189
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00740"
FT DISULFID 242..274
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00740"
FT DISULFID 345..382
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00740"
FT VAR_SEQ 380..425
FT /note="EECFADSDLNFLIPVAVGMALGFLIILVFISYIIGRRKSRTGYQSV -> QE
FT CSLDDDTILIPIVVGAALAGLIVIIVIAYIIGRRKSYAGYQTL (in isoform
FT LAMP-2C)"
FT /evidence="ECO:0000303|PubMed:7546292"
FT /id="VSP_003047"
FT VAR_SEQ 381..425
FT /note="ECFADSDLNFLIPVAVGMALGFLIILVFISYIIGRRKSRTGYQSV -> DCS
FT PEVDYFIVPIAVGAALGGLVVLVIMAYFLGHKKHHNTGYEQF (in isoform
FT LAMP-2A)"
FT /evidence="ECO:0000303|PubMed:7546292"
FT /id="VSP_003048"
FT CONFLICT 261
FT /note="I -> L (in Ref. 1; AAA99539/AAA99541)"
FT /evidence="ECO:0000305"
FT CONFLICT 277
FT /note="T -> A (in Ref. 1; AAA99539/AAA99541)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 425 AA; 46715 MW; AC16730A98FDB359 CRC64;
MAPPRCPAGL ALLLLLLGAC GFFQSYAVEV DVKDASNFTC LYAQWMMKFL IKYETNSSDY
KNASLDLTST VTHNGSICGS DTQAALLAVQ FGDGHSWSIN FTKNNETYRA EFITFTYNTN
DTAVFPDARR QGPVTIVVKD AMHPIQLNNV FVCHHTTSLE AENVTQIFWN VTMQPFVQNG
TISKKESRCY ADTPTAAPTV LPTVANVTTA STTISPAPTT APKPAENPVT GNYSLKTGNK
TCLLATVGLQ LNISQDKPLL INIDPKTTHA DGTCGNTSAT LKLNDGNRTL IDFTFIVNAS
ASVQKFYLRE VNVTLLNYQN GSVILSADNN NLSKWDASLG NSYMCRKEQT LEINENLQVH
TFNLWVQPFL VKENKFSIAE ECFADSDLNF LIPVAVGMAL GFLIILVFIS YIIGRRKSRT
GYQSV
