LAMP3_MACMU
ID LAMP3_MACMU Reviewed; 416 AA.
AC Q8MJJ2;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Lysosome-associated membrane glycoprotein 3;
DE Short=LAMP-3;
DE Short=Lysosomal-associated membrane protein 3;
DE AltName: Full=DC-lysosome-associated membrane glycoprotein;
DE Short=DC LAMP;
DE AltName: CD_antigen=CD208;
DE Flags: Precursor;
GN Name=LAMP3;
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lung;
RX PubMed=12213725; DOI=10.1016/s0002-9440(10)64257-5;
RA Fuller C.L., Choi Y.K., Fallert B.A., Capuano S. III, Rajakumar P.,
RA Murphey-Corb M., Reinhart T.A.;
RT "Restricted SIV replication in rhesus macaque lung tissues during the acute
RT phase of infection.";
RL Am. J. Pathol. 161:969-978(2002).
CC -!- FUNCTION: Lysosomal membrane glycoprotein which plays a role in the
CC unfolded protein response (UPR) that contributes to protein degradation
CC and cell survival during proteasomal dysfunction. Plays a role in the
CC process of fusion of the lysosome with the autophagosome, thereby
CC modulating the autophagic process. Promotes hepatocellular lipogenesis
CC through activation of the PI3K/Akt pathway. May also play a role in
CC dendritic cell function and in adaptive immunity.
CC {ECO:0000250|UniProtKB:Q9UQV4}.
CC -!- SUBUNIT: Monomer. Interacts with FURIN. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000250|UniProtKB:Q9UQV4}.
CC Lysosome membrane {ECO:0000250|UniProtKB:Q9UQV4}; Single-pass type I
CC membrane protein {ECO:0000255}. Cytoplasmic vesicle membrane
CC {ECO:0000250|UniProtKB:Q9UQV4}; Single-pass type I membrane protein
CC {ECO:0000255}. Early endosome membrane {ECO:0000250|UniProtKB:Q9UQV4};
CC Single-pass type I membrane protein {ECO:0000255}. Note=During
CC dendritic cell maturation, detected on cytoplasmic vesicles (the MHC II
CC compartment) that contain MHC II proteins, LAMP1, LAMP2 and LAMP3.
CC Detected on lysosomes in mature dendritic cells.
CC {ECO:0000250|UniProtKB:Q9UQV4}.
CC -!- SIMILARITY: Belongs to the LAMP family. {ECO:0000255|PROSITE-
CC ProRule:PRU00740}.
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DR EMBL; AF416334; AAM90730.1; -; mRNA.
DR RefSeq; NP_001028044.1; NM_001032872.1.
DR AlphaFoldDB; Q8MJJ2; -.
DR SMR; Q8MJJ2; -.
DR STRING; 9544.ENSMMUP00000013842; -.
DR Ensembl; ENSMMUT00000083884; ENSMMUP00000074108; ENSMMUG00000010555.
DR GeneID; 574213; -.
DR KEGG; mcc:574213; -.
DR CTD; 27074; -.
DR VEuPathDB; HostDB:ENSMMUG00000010555; -.
DR VGNC; VGNC:74045; LAMP3.
DR eggNOG; KOG4818; Eukaryota.
DR GeneTree; ENSGT00940000164015; -.
DR InParanoid; Q8MJJ2; -.
DR Proteomes; UP000006718; Chromosome 2.
DR Bgee; ENSMMUG00000010555; Expressed in lung and 5 other tissues.
DR ExpressionAtlas; Q8MJJ2; baseline.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031902; C:late endosome membrane; IBA:GO_Central.
DR GO; GO:0005765; C:lysosomal membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0072594; P:establishment of protein localization to organelle; IBA:GO_Central.
DR InterPro; IPR002000; Lysosome-assoc_membr_glycop.
DR PANTHER; PTHR11506; PTHR11506; 1.
DR Pfam; PF01299; Lamp; 1.
DR PRINTS; PR00336; LYSASSOCTDMP.
DR PROSITE; PS51407; LAMP_3; 1.
PE 2: Evidence at transcript level;
KW Adaptive immunity; Cytoplasmic vesicle; Disulfide bond; Endosome;
KW Glycoprotein; Immunity; Lysosome; Membrane; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..416
FT /note="Lysosome-associated membrane glycoprotein 3"
FT /id="PRO_0000223696"
FT TOPO_DOM 28..381
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 382..402
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00740"
FT TOPO_DOM 403..416
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00740"
FT REGION 135..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 200
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 291
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 237..274
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00740"
FT DISULFID 339..376
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00740"
SQ SEQUENCE 416 AA; 44163 MW; E5EABD7B23ABFDDB CRC64;
MPRQLSAAAV LFASLAVILH DGSQMRAKAF PKTRDYSQPT AAATGQDIAK PVQQPANQAP
HQTLAARLMD GHITFQTAAT IKTPTTTPVT TKNTPTTSPI IYTLVTTQAT SNNSHTAPPL
TKVTVGPSLA PYSLPPTITP PAHTTGTSSS TVNHTTGNAT QPSNQTTLPA TLSIAPHKST
TGQKPVQPTH APGTTAAAHN TTRTAAPAST VPGSTLAPQP SSIKTGIYQV LNGSRLCIKA
EMGIQLIVQD KESVFSPRRY FNLDPNATQA SGNCGTRNSN LLLNFQGGFV NLTFTKDEGS
YYISEVGACL TVSDPETIYQ GMKHAVVMFQ TVVGHSFKCV SEQSLQLSAH LQLKTTNVQL
QAFDFEDDHF GNVDECSSDY TIVLPVIGAI VVGLCLVGMG VYKIRLRCQS SGYQRI
