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   27-MAR-2024, entry version 120.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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   GlyCosmos; Q7TST5; 1 site, No reported glycans.
DR   GlyGen; Q7TST5; 1 site.
DR   iPTMnet; Q7TST5; -.
DR   PhosphoSitePlus; Q7TST5; -.
DR   MaxQB; Q7TST5; -.
DR   PaxDb; 10090-ENSMUSP00000080556; -.
DR   PeptideAtlas; Q7TST5; -.
DR   ProteomicsDB; 263700; -.
DR   DNASU; 239739; -.
DR   Ensembl; ENSMUST00000081880.7; ENSMUSP00000080556.6; ENSMUSG00000041247.9.
DR   GeneID; 239739; -.
DR   KEGG; mmu:239739; -.
DR   UCSC; uc007ypb.1; mouse.
DR   AGR; MGI:2441659; -.
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; QLLFVNM; -.
DR   OrthoDB; 5323545at2759; -.
DR   PhylomeDB; Q7TST5; -.
DR   TreeFam; TF316339; -.
DR   BioGRID-ORCS; 239739; 2 hits in 79 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 cell types or tissues.
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: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: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   Gene3D; 2.40.160.110; -; 1.
DR   InterPro; IPR048528; Lamp2-like_luminal.
DR   InterPro; IPR002000; Lysosome-assoc_membr_glycop.
DR   PANTHER; PTHR11506; LYSOSOME-ASSOCIATED MEMBRANE GLYCOPROTEIN; 1.
DR   PANTHER; PTHR11506:SF30; LYSOSOME-ASSOCIATED MEMBRANE GLYCOPROTEIN 3; 1.
DR   Pfam; PF01299; Lamp; 1.
DR   PRINTS; PR00336; LYSASSOCTDMP.
DR   PROSITE; PS51407; LAMP_3; 1.
DR   Genevisible; Q7TST5; MM.
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
//