LAMP3_RAT
ID LAMP3_RAT Reviewed; 408 AA.
AC Q5XI99;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Lysosome-associated membrane glycoprotein 3;
DE Short=LAMP-3;
DE Short=Lysosomal-associated membrane protein 3;
DE AltName: CD_antigen=CD208;
DE Flags: Precursor;
GN Name=Lamp3;
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 [LARGE SCALE MRNA].
RC TISSUE=Lung;
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).
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; BC083787; AAH83787.1; -; mRNA.
DR RefSeq; NP_001012015.1; NM_001012015.1.
DR RefSeq; XP_017453457.1; XM_017597968.1.
DR AlphaFoldDB; Q5XI99; -.
DR SMR; Q5XI99; -.
DR STRING; 10116.ENSRNOP00000038456; -.
DR GlyGen; Q5XI99; 3 sites.
DR PaxDb; Q5XI99; -.
DR PRIDE; Q5XI99; -.
DR Ensembl; ENSRNOT00000034498; ENSRNOP00000038456; ENSRNOG00000022792.
DR GeneID; 303801; -.
DR KEGG; rno:303801; -.
DR CTD; 27074; -.
DR RGD; 1307928; Lamp3.
DR eggNOG; KOG4818; Eukaryota.
DR GeneTree; ENSGT00950000182899; -.
DR HOGENOM; CLU_057804_0_0_1; -.
DR InParanoid; Q5XI99; -.
DR OMA; ECFSDRN; -.
DR OrthoDB; 829830at2759; -.
DR PhylomeDB; Q5XI99; -.
DR TreeFam; TF316339; -.
DR PRO; PR:Q5XI99; -.
DR Proteomes; UP000002494; Chromosome 11.
DR Bgee; ENSRNOG00000022792; Expressed in lung and 7 other tissues.
DR Genevisible; Q5XI99; RN.
DR GO; GO:0097233; C:alveolar lamellar body membrane; IDA:ParkinsonsUK-UCL.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005769; C:early endosome; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0005764; C:lysosome; ISO:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0031982; C:vesicle; ISO:RGD.
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 GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:RGD.
DR GO; GO:1901799; P:negative regulation of proteasomal protein catabolic process; ISO:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:0010506; P:regulation of autophagy; ISO:RGD.
DR GO; GO:1903900; P:regulation of viral life cycle; ISO:RGD.
DR GO; GO:0035455; P:response to interferon-alpha; ISO:RGD.
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..20
FT /evidence="ECO:0000255"
FT CHAIN 21..408
FT /note="Lysosome-associated membrane glycoprotein 3"
FT /id="PRO_0000223698"
FT TOPO_DOM 21..373
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 374..394
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00740"
FT TOPO_DOM 395..408
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00740"
FT CARBOHYD 55
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 225
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 284
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 230..267
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00740"
FT DISULFID 331..368
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00740"
SQ SEQUENCE 408 AA; 44388 MW; 45FBA0878F0EABE8 CRC64;
MPGQTSAVAV LLCLAVILHG YQIREKEFPE ARGYLQYTAT TTEQITAKPP LPLTNQTSHA
TLASRSKDDY IQTAAETSTF EDTAHITMKT AIPVTTKSLL PISSTSYTFV RTNNSHMTAS
STEDTIGSGS ITHLPFPTTR ASLAAVNHIT GRSTQLGGQT TLPKALFTPS HESTTTQRPT
LSTIVSELTP TGKDRSTTSS VPLVPRPTFV TWSSPAKIGT YEVLNGSRLC IKAEMGIALI
VQEKGLDSAT QRHFNIDPSL THASGKCGSQ NSNLFLNFQG GSVNVTFTKE ENLYYVSEVG
AYLTISNTEK TYQGKSTMMM FETVVGHSFK CVSEQSIQLS AQLQMKTMNI HLQAFDFEGD
SFGIVDECLS DYTVVLPVVG IIVVVLCVVG LGIYKIRQRR QSSAYQRI
