LAMP5_PONAB
ID LAMP5_PONAB Reviewed; 261 AA.
AC Q5R5V2; H2P108;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2017, sequence version 2.
DT 03-AUG-2022, entry version 62.
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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wilson R.K., Mardis E.;
RT "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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: Cytoplasmic vesicle membrane
CC {ECO:0000250|UniProtKB:Q9D387}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:Q9D387}. Cell membrane
CC {ECO:0000250|UniProtKB:Q9D387}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:Q9D387}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:Q9D387}. Cytoplasmic vesicle, secretory vesicle,
CC synaptic vesicle membrane {ECO:0000250|UniProtKB:Q9D387}; Single-pass
CC type I membrane protein {ECO:0000250|UniProtKB:Q9D387}. Cell
CC projection, growth cone membrane {ECO:0000250|UniProtKB:Q9D387};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q9D387}.
CC Early endosome membrane {ECO:0000250|UniProtKB:Q9D387}; Single-pass
CC type I membrane protein {ECO:0000250|UniProtKB:Q9D387}. Recycling
CC endosome {ECO:0000250|UniProtKB:Q9D387}. Endoplasmic reticulum-Golgi
CC intermediate compartment membrane {ECO:0000250|UniProtKB:Q9UJQ1};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q9D387}.
CC Endosome membrane {ECO:0000250|UniProtKB:Q9UJQ1}; Single-pass type I
CC membrane protein {ECO:0000250|UniProtKB:Q9D387}. Note=Recycles from the
CC vesicles of the endocytic recycling compartment (ERC) to the plasma
CC membrane (By similarity). Colocalizes with UNC93B1 in large endosomal
CC intracellular vesicles (By similarity). Accumulates in the endoplasmic
CC reticulum-Golgi intermediate compartment (ERGIC) before its
CC disappearance upon activation by CpG dinucleotides (By similarity).
CC Associates with cortical membranes (By similarity). Localizes mostly in
CC cytoplasmic vesicles of neuronal cell body. Localizes to synaptic
CC vesicles in a subset of GABAergic neurons (By similarity).
CC {ECO:0000250|UniProtKB:Q9D387, ECO:0000250|UniProtKB:Q9UJQ1}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5R5V2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5R5V2-2; Sequence=VSP_059121;
CC -!- PTM: Glycosylated. {ECO:0000250|UniProtKB:Q9D387}.
CC -!- SIMILARITY: Belongs to the LAMP family. {ECO:0000305}.
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DR EMBL; CR860751; CAH92864.1; -; mRNA.
DR EMBL; ABGA01004038; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ABGA01004039; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001126676.1; NM_001133204.1.
DR AlphaFoldDB; Q5R5V2; -.
DR SMR; Q5R5V2; -.
DR STRING; 9601.ENSPPYP00000011964; -.
DR GeneID; 100173676; -.
DR KEGG; pon:100173676; -.
DR CTD; 24141; -.
DR eggNOG; KOG4818; Eukaryota.
DR InParanoid; Q5R5V2; -.
DR OMA; WKNNAYI; -.
DR OrthoDB; 1377400at2759; -.
DR TreeFam; TF330776; -.
DR Proteomes; UP000001595; Chromosome 20.
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; ISS:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; ISS: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:0005770; C:late endosome; IEA:Ensembl.
DR GO; GO:0005764; C:lysosome; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0055038; C:recycling endosome membrane; ISS:UniProtKB.
DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR InterPro; IPR002000; Lysosome-assoc_membr_glycop.
DR PANTHER; PTHR11506; PTHR11506; 1.
DR Pfam; PF01299; Lamp; 1.
DR PROSITE; PS00310; LAMP_1; 1.
PE 2: Evidence at transcript 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..261
FT /note="Lysosome-associated membrane glycoprotein 5"
FT /id="PRO_0000042643"
FT TOPO_DOM 30..234
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 235..255
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 256..261
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT CARBOHYD 35
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT VAR_SEQ 221..261
FT /note="EHKCAVDEREQLEETLPLILGLILGLVIVVTLAIYHVHPQK -> GN (in
FT isoform 2)"
FT /id="VSP_059121"
FT CONFLICT 95
FT /note="V -> VK (in Ref. 2; ABGA01004038/ABGA01004039)"
FT /evidence="ECO:0000305"
FT CONFLICT 197
FT /note="T -> I (in Ref. 2; ABGA01004038/ABGA01004039)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 261 AA; 29190 MW; E4E1B6E99648AB6A CRC64;
MDLQGRAVPS VDRLRVLLML FHTMAQIMAE QEVENLSGLS TNPEKDIFVV RENGTTCLMA
EFAAKFIVPY DVWASNYVDL ITEQADIALT RGAEVGRCGH SESELQVFWV DRAYALKMLF
VKESHNMSKG PEETWRLSKV QFVYDSSEKT HFKDAVSAGK HTANSHHLSA LVTPAGKSYE
CQAQQTISLA SSDPQKTVTM ILSAVHIQPF DIISDFVFSE EHKCAVDERE QLEETLPLIL
GLILGLVIVV TLAIYHVHPQ K
