LAMP3_MOUSE
ID LAMP3_MOUSE Reviewed; 411 AA.
AC Q7TST5; Q8C1F6;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 112.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Lung;
RA Salaun B.P.A., de Saint-Vis B.M., Clair-Moninot V.A., Pin J.J.,
RA Dubois-Barthelemy C., Kissenpfennig A., Peronne C., Mattei M.-G.,
RA Davoust J., Kleijmeer M.J., Lebecque S.J.E.;
RT "Murine CD208/DC-LAMP is associated with the surfactant secretory
RT organelles in type II pneumocytes.";
RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Lung;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
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; AJ510130; CAD52824.1; -; mRNA.
DR EMBL; AK028039; BAC25713.1; -; mRNA.
DR CCDS; CCDS37285.1; -.
DR RefSeq; NP_796330.2; NM_177356.3.
DR AlphaFoldDB; Q7TST5; -.
DR SMR; Q7TST5; -.
DR STRING; 10090.ENSMUSP00000080556; -.
DR GlyGen; Q7TST5; 1 site.
DR iPTMnet; Q7TST5; -.
DR PhosphoSitePlus; Q7TST5; -.
DR MaxQB; Q7TST5; -.
DR PaxDb; Q7TST5; -.
DR PeptideAtlas; Q7TST5; -.
DR PRIDE; Q7TST5; -.
DR ProteomicsDB; 263700; -.
DR DNASU; 239739; -.
DR Ensembl; ENSMUST00000081880; ENSMUSP00000080556; ENSMUSG00000041247.
DR GeneID; 239739; -.
DR KEGG; mmu:239739; -.
DR UCSC; uc007ypb.1; mouse.
DR CTD; 27074; -.
DR MGI; MGI:2441659; Lamp3.
DR VEuPathDB; HostDB:ENSMUSG00000041247; -.
DR eggNOG; KOG4818; Eukaryota.
DR GeneTree; ENSGT00950000182899; -.
DR HOGENOM; CLU_057804_0_0_1; -.
DR InParanoid; Q7TST5; -.
DR OMA; ECFSDRN; -.
DR OrthoDB; 829830at2759; -.
DR PhylomeDB; Q7TST5; -.
DR TreeFam; TF316339; -.
DR BioGRID-ORCS; 239739; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Lamp3; mouse.
DR PRO; PR:Q7TST5; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q7TST5; protein.
DR Bgee; ENSMUSG00000041247; Expressed in lung and 6 other tissues.
DR Genevisible; Q7TST5; MM.
DR GO; GO:0097233; C:alveolar lamellar body membrane; IDA:MGI.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005769; C:early endosome; ISO:MGI.
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:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0031902; C:late endosome membrane; IBA:GO_Central.
DR GO; GO:0005765; C:lysosomal membrane; IDA:MGI.
DR GO; GO:0005764; C:lysosome; IDA:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0031982; C:vesicle; ISO:MGI.
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:MGI.
DR GO; GO:1901799; P:negative regulation of proteasomal protein catabolic process; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:0010506; P:regulation of autophagy; ISO:MGI.
DR GO; GO:1903900; P:regulation of viral life cycle; ISO:MGI.
DR GO; GO:0035455; P:response to interferon-alpha; ISO:MGI.
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..21
FT /evidence="ECO:0000255"
FT CHAIN 22..411
FT /note="Lysosome-associated membrane glycoprotein 3"
FT /id="PRO_0000223697"
FT TOPO_DOM 22..376
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 377..397
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00740"
FT TOPO_DOM 398..411
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00740"
FT REGION 172..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 227
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 232..269
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00740"
FT DISULFID 334..371
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00740"
FT CONFLICT 75
FT /note="A -> G (in Ref. 2; BAC25713)"
FT /evidence="ECO:0000305"
FT CONFLICT 109
FT /note="T -> S (in Ref. 2; BAC25713)"
FT /evidence="ECO:0000305"
FT CONFLICT 195..196
FT /note="KD -> TG (in Ref. 2; BAC25713)"
FT /evidence="ECO:0000305"
FT CONFLICT 248
FT /note="L -> W (in Ref. 2; BAC25713)"
FT /evidence="ECO:0000305"
FT CONFLICT 257
FT /note="N -> H (in Ref. 2; BAC25713)"
FT /evidence="ECO:0000305"
FT CONFLICT 268
FT /note="K -> N (in Ref. 2; BAC25713)"
FT /evidence="ECO:0000305"
FT CONFLICT 272
FT /note="Q -> H (in Ref. 2; BAC25713)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 411 AA; 45129 MW; FC7D6F16485A02ED CRC64;
MPGQISAVAV LFLSLTVILH GYQIREKEFP KARGYLQYTA TSAEQITTKP LLQLINQRSH
ITLASRFKDD YIQMAAETSA IENTAHITMK TVTPVTTKSL PPISSASYTF VRSNNAHMTA
SSTDDTIGSG SIAHLPVPTT RASLAIVNYI TGRATQLGGQ TTLPKTFFTA SHKSTTNQRP
TLSTNVLGTS TPTHKDRSTT SPVPLVPRPT LVTWSSPAKI GTYEVLNGSR LCIKAEMGLA
LIVQEKDLDS ATQRYFNIDP SLTHASGKCD SQKSNLFLNF QGGSVNITFT KEENLYYISE
VGAYLTISNT EKTYQGKKNT LMMFETVVGH SFKCVSEQSI QLSAQLQMKT MNIHLQAFDF
EGDSFGNVNE CLSDYTVVLP MVAIIVVVIC VVGLSVYKIR QRHQSSAYQR I
