LAMP5_MOUSE
ID LAMP5_MOUSE Reviewed; 280 AA.
AC Q9D387; Q9CXQ4;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2002, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Lysosome-associated membrane glycoprotein 5;
DE AltName: Full=Brain and dendritic cell-associated LAMP;
DE AltName: Full=Brain-associated LAMP-like protein;
DE Short=BAD-LAMP;
DE AltName: Full=Lysosome-associated membrane protein 5;
DE Short=LAMP-5;
DE Flags: Precursor;
GN Name=Lamp5;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryonic head, and Medulla oblongata;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 114-280.
RC STRAIN=Czech II; TISSUE=Mammary fibroblast;
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).
RN [3]
RP SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-276, GLYCOSYLATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=17215451; DOI=10.1242/jcs.03316;
RA David A., Tiveron M.C., Defays A., Beclin C., Camosseto V., Gatti E.,
RA Cremer H., Pierre P.;
RT "BAD-LAMP defines a subset of early endocytic organelles in subpopulations
RT of cortical projection neurons.";
RL J. Cell Sci. 120:353-365(2007).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=27272053; DOI=10.1371/journal.pone.0157052;
RA Tiveron M.C., Beurrier C., Ceni C., Andriambao N., Combes A., Koehl M.,
RA Maurice N., Gatti E., Abrous D.N., Kerkerian-Le Goff L., Pierre P.,
RA Cremer H.;
RT "LAMP5 fine-tunes GABAergic synaptic transmission in defined circuits of
RT the mouse brain.";
RL PLoS ONE 11:E0157052-E0157052(2016).
CC -!- FUNCTION: Plays a role in short-term synaptic plasticity in a subset of
CC GABAergic neurons in the brain. {ECO:0000269|PubMed:27272053}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane
CC {ECO:0000269|PubMed:17215451}; Single-pass type I membrane protein
CC {ECO:0000305}. Cell membrane {ECO:0000269|PubMed:17215451}; Single-pass
CC type I membrane protein {ECO:0000269|PubMed:17215451}. Cell projection,
CC dendrite {ECO:0000269|PubMed:17215451}. Cytoplasmic vesicle, secretory
CC vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:27272053};
CC Single-pass type I membrane protein {ECO:0000305}. Cell projection,
CC growth cone membrane {ECO:0000269|PubMed:17215451}; Single-pass type I
CC membrane protein {ECO:0000305}. Early endosome membrane
CC {ECO:0000269|PubMed:17215451}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:17215451}. Recycling endosome
CC {ECO:0000269|PubMed:17215451}. Endoplasmic reticulum-Golgi intermediate
CC compartment membrane {ECO:0000250|UniProtKB:Q9UJQ1}; Single-pass type I
CC membrane protein {ECO:0000305}. Endosome membrane
CC {ECO:0000250|UniProtKB:Q9UJQ1}; Single-pass type I membrane protein
CC {ECO:0000305}. Note=Recycles from the vesicles of the endocytic
CC recycling compartment (ERC) to the plasma membrane (PubMed:17215451).
CC Colocalizes with UNC93B1 in large endosomal intracellular vesicles (By
CC similarity). Accumulates in the endoplasmic reticulum-Golgi
CC intermediate compartment (ERGIC) before its disappearance upon
CC activation by CpG dinucleotides (By similarity). Associates with
CC cortical membranes (By similarity). Localizes mostly in cytoplasmic
CC vesicles of neuronal cell body (PubMed:17215451). Localizes to synaptic
CC vesicles in a subset of GABAergic neurons (PubMed:27272053).
CC {ECO:0000250|UniProtKB:Q9UJQ1, ECO:0000269|PubMed:27272053}.
CC -!- TISSUE SPECIFICITY: In brain, strongly expressed in the globus
CC pallidus/ventral pallidum complex, the substantia nigra pars reticulata
CC and the entopeduncular nucleus (at protein level) (PubMed:27272053).
CC Expressed in the external plexiform layer of the olfactory bulb (at
CC protein level). May be weakly expressed in neocortex and striatum (at
CC protein level) (PubMed:27272053). Highly expressed in brain; not
CC detected in other tissues tested (PubMed:17215451). Detected in the
CC cingulate cortex, cortical plate and caudate putamen (PubMed:17215451).
CC In neocortex, specifically expressed in neurons of layers II/III and V
CC (PubMed:17215451). {ECO:0000269|PubMed:17215451,
CC ECO:0000269|PubMed:27272053}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryo at 14 dpc.
CC {ECO:0000269|PubMed:17215451}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:17215451}.
CC -!- DISRUPTION PHENOTYPE: Gross morphology and brain structure are normal.
CC Behavioral assays of locomotory activity, exploratory behavior and
CC motor coordination are also normal. However, some subtle behavioral
CC defects are observed: anxiety levels are decreased and animals also
CC show mild defects in odor discrimination. Electrophysiological assays
CC of striatopallidal synapses indicate defects in short-term synaptic
CC plasticity. {ECO:0000269|PubMed:27272053}.
CC -!- SIMILARITY: Belongs to the LAMP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH04791.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AK018222; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAB29169.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK014127; BAB29169.1; ALT_INIT; mRNA.
DR EMBL; AK018222; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC004791; AAH04791.1; ALT_INIT; mRNA.
DR CCDS; CCDS16789.1; -.
DR RefSeq; NP_083806.2; NM_029530.2.
DR RefSeq; XP_006500427.1; XM_006500364.3.
DR RefSeq; XP_017174807.1; XM_017319318.1.
DR AlphaFoldDB; Q9D387; -.
DR SMR; Q9D387; -.
DR STRING; 10090.ENSMUSP00000061180; -.
DR GlyConnect; 2496; 6 N-Linked glycans (1 site).
DR GlyGen; Q9D387; 4 sites, 6 N-linked glycans (1 site).
DR PhosphoSitePlus; Q9D387; -.
DR MaxQB; Q9D387; -.
DR PaxDb; Q9D387; -.
DR PeptideAtlas; Q9D387; -.
DR PRIDE; Q9D387; -.
DR ProteomicsDB; 263701; -.
DR ABCD; Q9D387; 4 sequenced antibodies.
DR Antibodypedia; 24121; 94 antibodies from 17 providers.
DR DNASU; 76161; -.
DR Ensembl; ENSMUST00000057503; ENSMUSP00000061180; ENSMUSG00000027270.
DR GeneID; 76161; -.
DR KEGG; mmu:76161; -.
DR UCSC; uc008mog.1; mouse.
DR CTD; 24141; -.
DR MGI; MGI:1923411; Lamp5.
DR VEuPathDB; HostDB:ENSMUSG00000027270; -.
DR eggNOG; KOG4818; Eukaryota.
DR GeneTree; ENSGT00950000182899; -.
DR HOGENOM; CLU_090529_0_0_1; -.
DR InParanoid; Q9D387; -.
DR OMA; WKNNAYI; -.
DR OrthoDB; 1377400at2759; -.
DR PhylomeDB; Q9D387; -.
DR TreeFam; TF330776; -.
DR BioGRID-ORCS; 76161; 0 hits in 75 CRISPR screens.
DR ChiTaRS; Lamp5; mouse.
DR PRO; PR:Q9D387; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9D387; protein.
DR Bgee; ENSMUSG00000027270; Expressed in medial vestibular nucleus and 115 other tissues.
DR ExpressionAtlas; Q9D387; baseline and differential.
DR Genevisible; Q9D387; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IDA:UniProtKB.
DR GO; GO:0032590; C:dendrite membrane; IDA:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; IDA:UniProtKB.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; ISS:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; ISS:UniProtKB.
DR GO; GO:0032584; C:growth cone membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005770; C:late endosome; IDA:MGI.
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; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0055038; C:recycling endosome membrane; IDA:UniProtKB.
DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
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 PROSITE; PS00310; LAMP_1; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell projection; Cytoplasmic vesicle; Endosome;
KW Glycoprotein; Membrane; Reference proteome; Signal; Synapse; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..280
FT /note="Lysosome-associated membrane glycoprotein 5"
FT /id="PRO_0000021032"
FT TOPO_DOM 30..235
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 236..256
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 257..280
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 35
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 127
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 276
FT /note="Y->A: Cell surface localization."
FT /evidence="ECO:0000269|PubMed:17215451"
FT CONFLICT 221
FT /note="E -> V (in Ref. 1; AK018222)"
FT /evidence="ECO:0000305"
FT CONFLICT 230
FT /note="Q -> P (in Ref. 1; AK018222)"
FT /evidence="ECO:0000305"
FT CONFLICT 238
FT /note="P -> A (in Ref. 1; AK018222)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 280 AA; 31721 MW; FA11D7BF9FD5CCEF CRC64;
MDLRVRTLLG GDRLRILLMF FHVMVQTVAE QEVENLSGLS TNPEKDIFVV RENGTTCLMA
EFAAKFIVPY DVWASNYVDL ITEQAEISLT RGAEVKGHCG HNESELEVFW VDHAYTLRML
FVKESHNTSK GPEATWNLNK VHFVYDSSEK THFKAPVKVN KYIASSHHLS ALVTPAGMSY
ECQAQQTISL ASSDPQKTVT MILSAVHIQP FDIISDFVFS EEHKCPVDEQ EQLEETLPLI
LGLILGLVIV ITLVIYHIHH KMTANQVQIP RDRSQYKHMG
