LAMP1_RAT
ID LAMP1_RAT Reviewed; 407 AA.
AC P14562; P97620;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Lysosome-associated membrane glycoprotein 1;
DE Short=LAMP-1;
DE Short=Lysosome-associated membrane protein 1;
DE AltName: Full=120 kDa lysosomal membrane glycoprotein;
DE Short=LGP-120;
DE AltName: Full=CD107 antigen-like family member A;
DE AltName: CD_antigen=CD107a;
DE Flags: Precursor;
GN Name=Lamp1; Synonyms=Lamp-1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3174652; DOI=10.1073/pnas.85.20.7577;
RA Howe C.L., Granger B.L., Hull M., Green S.A., Gabel C.A., Helenius A.,
RA Mellman I.;
RT "Derived protein sequence, oligosaccharides, and membrane insertion of the
RT 120-kDa lysosomal membrane glycoprotein (lgp120): identification of a
RT highly conserved family of lysosomal membrane glycoproteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:7577-7581(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 22-407.
RX PubMed=2920835; DOI=10.1016/0014-5793(89)80561-7;
RA Himeno M., Noguchi Y., Sasaki H., Tanaka Y., Furuno K., Kono A., Sakaki Y.,
RA Kato K.;
RT "Isolation and sequencing of a cDNA clone encoding 107 kDa
RT sialoglycoprotein in rat liver lysosomal membranes.";
RL FEBS Lett. 244:351-356(1989).
RN [3]
RP PROTEIN SEQUENCE OF 130-141; 147-155; 247-268 AND 317-353, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U., Lubec S.;
RL Submitted (SEP-2007) to UniProtKB.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 283-357.
RC STRAIN=Wistar Kyoto; TISSUE=Aortic smooth muscle;
RA Adams L.A., Werny I., Schwartz S.M.;
RL Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Lysosomal membrane glycoprotein which plays an important role
CC in lysosome biogenesis, autophagy, and cholesterol homeostasis (By
CC similarity). Also plays an important role in NK-cells cytotoxicity.
CC Mechanistically, participates in cytotoxic granule movement to the cell
CC surface and perforin trafficking to the lytic granule. In addition,
CC protects NK-cells from degranulation-associated damage induced by their
CC own cytotoxic granule content. Presents carbohydrate ligands to
CC selectins. Also implicated in tumor cell metastasis (By similarity).
CC {ECO:0000250|UniProtKB:P11279, ECO:0000250|UniProtKB:P11438}.
CC -!- SUBUNIT: Interacts with ABCB9; this interaction strongly stabilizes
CC ABCB9 and protects ABCB9 against lysosomal degradation. Interacts with
CC FURIN. {ECO:0000250|UniProtKB:P11279}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P05300};
CC Single-pass type I membrane protein {ECO:0000255}. Endosome membrane
CC {ECO:0000250|UniProtKB:P11279}; Single-pass type I membrane protein
CC {ECO:0000255}. Lysosome membrane {ECO:0000250|UniProtKB:P11279};
CC Single-pass type I membrane protein {ECO:0000255}. Late endosome
CC membrane {ECO:0000250|UniProtKB:P11279}; Single-pass type I membrane
CC protein {ECO:0000255}. Cytolytic granule membrane
CC {ECO:0000250|UniProtKB:P11279}; Single-pass type I membrane protein
CC {ECO:0000255}. Note=This protein shuttles between lysosomes, endosomes,
CC and the plasma membrane (By similarity). Colocalizes with OSBPL1A at
CC the late endosome (By similarity). {ECO:0000250|UniProtKB:P05300,
CC ECO:0000250|UniProtKB:P11279}.
CC -!- PTM: O- and N-glycosylated; some of the N-glycans attached to LAMP-1
CC are polylactosaminoglycans. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the LAMP family. {ECO:0000255|PROSITE-
CC ProRule:PRU00740}.
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DR EMBL; M34959; AAA41525.1; -; mRNA.
DR EMBL; X14765; CAA32873.1; -; mRNA.
DR EMBL; U75406; AAB19108.1; -; mRNA.
DR PIR; A30200; A30200.
DR RefSeq; NP_036989.1; NM_012857.2.
DR RefSeq; XP_017455483.1; XM_017599994.1.
DR AlphaFoldDB; P14562; -.
DR SMR; P14562; -.
DR BioGRID; 247367; 1.
DR IntAct; P14562; 4.
DR MINT; P14562; -.
DR STRING; 10116.ENSRNOP00000026580; -.
DR GlyGen; P14562; 18 sites.
DR PhosphoSitePlus; P14562; -.
DR jPOST; P14562; -.
DR PaxDb; P14562; -.
DR PRIDE; P14562; -.
DR GeneID; 25328; -.
DR KEGG; rno:25328; -.
DR UCSC; RGD:2989; rat.
DR CTD; 3916; -.
DR RGD; 2989; Lamp1.
DR VEuPathDB; HostDB:ENSRNOG00000019629; -.
DR eggNOG; KOG4818; Eukaryota.
DR HOGENOM; CLU_055379_2_0_1; -.
DR InParanoid; P14562; -.
DR OMA; NSYKCSA; -.
DR OrthoDB; 1042920at2759; -.
DR PhylomeDB; P14562; -.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR PRO; PR:P14562; -.
DR Proteomes; UP000002494; Chromosome 16.
DR Bgee; ENSRNOG00000019629; Expressed in adult mammalian kidney and 19 other tissues.
DR ExpressionAtlas; P14562; baseline and differential.
DR Genevisible; P14562; RN.
DR GO; GO:0097208; C:alveolar lamellar body; IDA:RGD.
DR GO; GO:0044754; C:autolysosome; ISO:RGD.
DR GO; GO:0000421; C:autophagosome membrane; ISO:RGD.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0044194; C:cytolytic granule; ISO:RGD.
DR GO; GO:0101004; C:cytolytic granule membrane; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0030425; C:dendrite; IDA:BHF-UCL.
DR GO; GO:0005768; C:endosome; ISO:RGD.
DR GO; GO:0010008; C:endosome membrane; ISS:UniProtKB.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
DR GO; GO:0030285; C:integral component of synaptic vesicle membrane; IDA:SynGO.
DR GO; GO:0005770; C:late endosome; ISO:RGD.
DR GO; GO:0031902; C:late endosome membrane; IBA:GO_Central.
DR GO; GO:0005765; C:lysosomal membrane; ISS:UniProtKB.
DR GO; GO:0005764; C:lysosome; IDA:UniProtKB.
DR GO; GO:0042470; C:melanosome; ISO:RGD.
DR GO; GO:0005771; C:multivesicular body; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:BHF-UCL.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0045335; C:phagocytic vesicle; ISO:RGD.
DR GO; GO:0061474; C:phagolysosome membrane; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0042383; C:sarcolemma; ISO:RGD.
DR GO; GO:0008021; C:synaptic vesicle; ISO:RGD.
DR GO; GO:0005773; C:vacuole; IDA:RGD.
DR GO; GO:0031982; C:vesicle; ISO:RGD.
DR GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR GO; GO:0019904; F:protein domain specific binding; ISO:RGD.
DR GO; GO:0048102; P:autophagic cell death; IDA:RGD.
DR GO; GO:0072594; P:establishment of protein localization to organelle; ISO:RGD.
DR GO; GO:0090160; P:Golgi to lysosome transport; ISO:RGD.
DR GO; GO:0140507; P:granzyme-mediated programmed cell death signaling pathway; ISO:RGD.
DR GO; GO:0043323; P:positive regulation of natural killer cell degranulation; ISO:RGD.
DR GO; GO:0045954; P:positive regulation of natural killer cell mediated cytotoxicity; ISO:RGD.
DR GO; GO:0050821; P:protein stabilization; ISS:CAFA.
DR GO; GO:1902513; P:regulation of organelle transport along microtubule; ISO:RGD.
DR InterPro; IPR018134; LAMP_CS.
DR InterPro; IPR002000; Lysosome-assoc_membr_glycop.
DR PANTHER; PTHR11506; PTHR11506; 1.
DR Pfam; PF01299; Lamp; 1.
DR PRINTS; PR00336; LYSASSOCTDMP.
DR PROSITE; PS00310; LAMP_1; 2.
DR PROSITE; PS00311; LAMP_2; 1.
DR PROSITE; PS51407; LAMP_3; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Direct protein sequencing; Disulfide bond; Endosome;
KW Glycoprotein; Lysosome; Membrane; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:2920835"
FT CHAIN 22..407
FT /note="Lysosome-associated membrane glycoprotein 1"
FT /id="PRO_0000017106"
FT TOPO_DOM 22..371
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 372..395
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00740"
FT TOPO_DOM 396..407
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00740"
FT REGION 22..189
FT /note="First lumenal domain"
FT REGION 180..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 190..219
FT /note="Hinge"
FT REGION 220..371
FT /note="Second lumenal domain"
FT COMPBIAS 191..207
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 32
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 59
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 79
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 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 160
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 178
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 215
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 220
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 233
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 241
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 271
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 283
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 297
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 312
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 36..75
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00740"
FT DISULFID 150..186
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00740"
FT DISULFID 223..260
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00740"
FT DISULFID 328..365
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00740"
FT CONFLICT 293..294
FT /note="GV -> EF (in Ref. 4; AAB19108)"
FT /evidence="ECO:0000305"
FT CONFLICT 329
FT /note="N -> T (in Ref. 4; AAB19108)"
FT /evidence="ECO:0000305"
FT CONFLICT 356..357
FT /note="SD -> VT (in Ref. 4)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 407 AA; 43969 MW; 25947490749A7C88 CRC64;
MAAPGARRPL LLLLLAGLAH SAPALFEVKD NNGTACIMAS FSASFLTTYD AGHVSKVSNM
TLPASAEVLK NSSSCGEKNA SEPTLAITFG EGYLLKLTFT KNTTRYSVQH MYFTYNLSDT
QFFPNASSKG PDTVDSTTDI KADINKTYRC VSDIRVYMKN VTIVLWDATI QAYLPSSNFS
KEETRCPQDQ PSPTTGPPSP SPPLVPTNPS VSKYNVTGDN GTCLLASMAL QLNITYMKKD
NTTVTRAFNI NPSDKYSGTC GAQLVTLKVG NKSRVLELQF GMNATSSLFF LQGVQLNMTL
PDAIEPTFST SNYSLKALQA SVGNSYKCNS EEHIFVSKAL ALNVFSVQVQ AFRVESDRFG
SVEECVQDGN NMLIPIAVGG ALAGLVLIVL IAYLIGRKRS HAGYQTI
