LAMP5_HUMAN
ID LAMP5_HUMAN Reviewed; 280 AA.
AC Q9UJQ1; B4DHZ7; B7Z9Z9;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 147.
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; Synonyms=C20orf103;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Stavrides G.S., Huckle E.J., Deloukas P.;
RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Caudate nucleus, and Thalamus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
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 [5]
RP SUBCELLULAR LOCATION, INDUCTION, MUTAGENESIS OF TYR-276, AND TISSUE
RP SPECIFICITY.
RX PubMed=21642595; DOI=10.1182/blood-2010-11-319699;
RA Defays A., David A., de Gassart A., De Angelis Rigotti F., Wenger T.,
RA Camossetto V., Brousset P., Petrella T., Dalod M., Gatti E., Pierre P.;
RT "BAD-LAMP is a novel biomarker of nonactivated human plasmacytoid dendritic
RT cells.";
RL Blood 118:609-617(2011).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Plays a role in short-term synaptic plasticity in a subset of
CC GABAergic neurons in the brain. {ECO:0000250|UniProtKB:Q9D387}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21642595};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:21642595}.
CC Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane
CC {ECO:0000250|UniProtKB:Q9D387}; Single-pass type I membrane protein
CC {ECO:0000305}. Endoplasmic reticulum-Golgi intermediate compartment
CC membrane {ECO:0000269|PubMed:21642595}; Single-pass type I membrane
CC protein {ECO:0000269|PubMed:21642595}. Endosome membrane
CC {ECO:0000269|PubMed:21642595}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:21642595}. Cytoplasmic vesicle membrane
CC {ECO:0000250|UniProtKB:Q9D387}; Single-pass type I membrane protein
CC {ECO:0000305}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:Q9D387}. Cell projection, growth cone membrane
CC {ECO:0000250|UniProtKB:Q9D387}; Single-pass type I membrane protein
CC {ECO:0000305}. Early endosome membrane {ECO:0000250|UniProtKB:Q9D387};
CC Single-pass type I membrane protein {ECO:0000305}. Recycling endosome
CC {ECO:0000250|UniProtKB:Q9D387}. Note=Recycles from the vesicles of the
CC endocytic recycling compartment (ERC) to the plasma membrane (By
CC similarity). Colocalizes with UNC93B1 in large endosomal intracellular
CC vesicles (PubMed:21642595). Accumulates in the endoplasmic reticulum-
CC Golgi intermediate compartment (ERGIC) before its disappearance upon
CC activation by CpG dinucleotides (PubMed:21642595). Associates with
CC cortical membranes (PubMed:21642595). Localizes mostly in cytoplasmic
CC vesicles of neuronal cell body (By similarity). Localizes to synaptic
CC vesicles in a subset of GABAergic neurons (By similarity).
CC {ECO:0000250|UniProtKB:Q9D387, ECO:0000269|PubMed:21642595}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UJQ1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UJQ1-2; Sequence=VSP_037186;
CC -!- TISSUE SPECIFICITY: Expressed in plasmocytoid dendritic cells.
CC Expressed in suprabasal skin keratinocytes and squamous cells (at
CC protein level). Expressed in the brain and weakly in spleen and skin.
CC Expressed in plasmocytoid dendritic cells.
CC {ECO:0000269|PubMed:21642595}.
CC -!- INDUCTION: Up-regulated upon CpG dinucleotides activation. Down-
CC regulated upon activation by Toll-like receptor (TLR) ligands.
CC {ECO:0000269|PubMed:21642595}.
CC -!- PTM: Glycosylated. {ECO:0000250|UniProtKB:Q9D387}.
CC -!- MISCELLANEOUS: Appears to be a novel specific biomarker for blastic
CC plasmocytoid dendritic cells neoplasia. {ECO:0000305|PubMed:21642595}.
CC -!- SIMILARITY: Belongs to the LAMP family. {ECO:0000305}.
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DR EMBL; AL121740; CAB57330.1; -; mRNA.
DR EMBL; AK295336; BAG58309.1; -; mRNA.
DR EMBL; AK316114; BAH14485.1; -; mRNA.
DR EMBL; AL031652; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC050727; AAH50727.1; -; mRNA.
DR CCDS; CCDS13106.1; -. [Q9UJQ1-1]
DR CCDS; CCDS56177.1; -. [Q9UJQ1-2]
DR RefSeq; NP_001186826.1; NM_001199897.1. [Q9UJQ1-2]
DR RefSeq; NP_036393.1; NM_012261.3. [Q9UJQ1-1]
DR AlphaFoldDB; Q9UJQ1; -.
DR SMR; Q9UJQ1; -.
DR BioGRID; 117292; 11.
DR IntAct; Q9UJQ1; 1.
DR MINT; Q9UJQ1; -.
DR STRING; 9606.ENSP00000246070; -.
DR GlyGen; Q9UJQ1; 3 sites.
DR iPTMnet; Q9UJQ1; -.
DR PhosphoSitePlus; Q9UJQ1; -.
DR BioMuta; LAMP5; -.
DR DMDM; 26392602; -.
DR EPD; Q9UJQ1; -.
DR MassIVE; Q9UJQ1; -.
DR PaxDb; Q9UJQ1; -.
DR PeptideAtlas; Q9UJQ1; -.
DR PRIDE; Q9UJQ1; -.
DR ProteomicsDB; 84637; -. [Q9UJQ1-1]
DR ProteomicsDB; 84638; -. [Q9UJQ1-2]
DR Antibodypedia; 24121; 94 antibodies from 17 providers.
DR DNASU; 24141; -.
DR Ensembl; ENST00000246070.3; ENSP00000246070.2; ENSG00000125869.10. [Q9UJQ1-1]
DR Ensembl; ENST00000427562.6; ENSP00000406360.1; ENSG00000125869.10. [Q9UJQ1-2]
DR GeneID; 24141; -.
DR KEGG; hsa:24141; -.
DR MANE-Select; ENST00000246070.3; ENSP00000246070.2; NM_012261.4; NP_036393.1.
DR UCSC; uc002wni.3; human. [Q9UJQ1-1]
DR CTD; 24141; -.
DR DisGeNET; 24141; -.
DR GeneCards; LAMP5; -.
DR HGNC; HGNC:16097; LAMP5.
DR HPA; ENSG00000125869; Tissue enhanced (brain, retina).
DR MIM; 614641; gene.
DR neXtProt; NX_Q9UJQ1; -.
DR OpenTargets; ENSG00000125869; -.
DR PharmGKB; PA25643; -.
DR VEuPathDB; HostDB:ENSG00000125869; -.
DR eggNOG; KOG4818; Eukaryota.
DR GeneTree; ENSGT00950000182899; -.
DR HOGENOM; CLU_090529_0_0_1; -.
DR InParanoid; Q9UJQ1; -.
DR OMA; WKNNAYI; -.
DR OrthoDB; 1377400at2759; -.
DR PhylomeDB; Q9UJQ1; -.
DR TreeFam; TF330776; -.
DR PathwayCommons; Q9UJQ1; -.
DR SignaLink; Q9UJQ1; -.
DR BioGRID-ORCS; 24141; 8 hits in 1061 CRISPR screens.
DR ChiTaRS; LAMP5; human.
DR GenomeRNAi; 24141; -.
DR Pharos; Q9UJQ1; Tbio.
DR PRO; PR:Q9UJQ1; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q9UJQ1; protein.
DR Bgee; ENSG00000125869; Expressed in nucleus accumbens and 129 other tissues.
DR Genevisible; Q9UJQ1; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; ISS:UniProtKB.
DR GO; GO:0032590; C:dendrite membrane; ISS:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; ISS:UniProtKB.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IDA:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; IDA:UniProtKB.
DR GO; GO:0032584; C:growth cone membrane; ISS:UniProtKB.
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; IDA:UniProtKB.
DR GO; GO:0055038; C:recycling endosome membrane; ISS: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 Alternative splicing; Cell membrane; Cell projection; Cytoplasmic vesicle;
KW Endosome; Glycoprotein; Membrane; Reference proteome; Signal; Synapse;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..280
FT /note="Lysosome-associated membrane glycoprotein 5"
FT /id="PRO_0000021031"
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 127
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 80..123
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_037186"
FT VARIANT 12
FT /note="D -> G (in dbSNP:rs2232259)"
FT /id="VAR_014401"
FT VARIANT 81
FT /note="I -> V (in dbSNP:rs2232263)"
FT /id="VAR_014402"
FT VARIANT 103
FT /note="Q -> E (in dbSNP:rs2232264)"
FT /id="VAR_014403"
FT VARIANT 158
FT /note="S -> G (in dbSNP:rs2232266)"
FT /id="VAR_014404"
FT MUTAGEN 276
FT /note="Y->A: Cell surface localization."
FT /evidence="ECO:0000269|PubMed:21642595"
FT CONFLICT 251
FT /note="V -> A (in Ref. 2; BAG58309)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 280 AA; 31472 MW; 7D811D7C04EE70B8 CRC64;
MDLQGRGVPS IDRLRVLLML FHTMAQIMAE QEVENLSGLS TNPEKDIFVV RENGTTCLMA
EFAAKFIVPY DVWASNYVDL ITEQADIALT RGAEVKGRCG HSQSELQVFW VDRAYALKML
FVKESHNMSK GPEATWRLSK VQFVYDSSEK THFKDAVSAG KHTANSHHLS ALVTPAGKSY
ECQAQQTISL ASSDPQKTVT MILSAVHIQP FDIISDFVFS EEHKCPVDER EQLEETLPLI
LGLILGLVIM VTLAIYHVHH KMTANQVQIP RDRSQYKHMG
