ID   LAMP1_CRIGR             Reviewed;         407 AA.
AC   P49129;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   27-MAR-2024, entry version 94.
DE   RecName: Full=Lysosome-associated membrane glycoprotein 1;
DE            Short=LAMP-1;
DE            Short=Lysosome-associated membrane protein 1;
DE   AltName: Full=CD107 antigen-like family member A;
DE   AltName: Full=Lysosomal membrane glycoprotein A;
DE            Short=LGP-A;
DE   AltName: CD_antigen=CD107a;
DE   Flags: Precursor;
GN   Name=LAMP1; Synonyms=LGPA;
OS   Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Cricetulus.
OX   NCBI_TaxID=10029;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8867788;
RA   Uthayakumar S., Granger B.L.;
RT   "Cell surface accumulation of overexpressed hamster lysosomal membrane
RT   glycoproteins.";
RL   Cell. Mol. Biol. Res. 41:405-420(1995).
CC   -!- FUNCTION: Lysosomal membrane glycoprotein which plays an important role
CC       in lysosome biogenesis, lysosomal pH regulation, autophagy and
CC       cholesterol homeostasis. Acts as an important regulator of lysosomal
CC       lumen pH regulation by acting as a direct inhibitor of the proton
CC       channel TMEM175, facilitating lysosomal acidification for optimal
CC       hydrolase activity. Also plays an important role in NK-cells
CC       cytotoxicity. Mechanistically, participates in cytotoxic granule
CC       movement to the cell surface and perforin trafficking to the lytic
CC       granule. In addition, protects NK-cells from degranulation-associated
CC       damage induced by their own cytotoxic granule content. Presents
CC       carbohydrate ligands to selectins. {ECO:0000250|UniProtKB:P11279}.
CC   -!- SUBUNIT: Interacts with ABCB9; this interaction strongly stabilizes
CC       ABCB9 and protects ABCB9 against lysosomal degradation. Interacts with
CC       FURIN. Interacts with TMEM175; inhibiting the proton channel activity
CC       of TMEM175. {ECO:0000250|UniProtKB:P11279}.
CC   -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:P11279};
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}. Late endosome membrane {ECO:0000250|UniProtKB:P11279};
CC       Single-pass type I membrane protein {ECO:0000255}. Cell membrane
CC       {ECO:0000250|UniProtKB:P11279}; Single-pass type I membrane protein
CC       {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|UniProtKB:P11279}.
CC   -!- SIMILARITY: Belongs to the LAMP family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00740}.
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DR   EMBL; L18986; AAC37682.1; -; mRNA.
DR   RefSeq; NP_001233759.1; NM_001246830.1.
DR   AlphaFoldDB; P49129; -.
DR   SMR; P49129; -.
DR   IntAct; P49129; 1.
DR   MINT; P49129; -.
DR   GlyCosmos; P49129; 21 sites, No reported glycans.
DR   PaxDb; 10029-NP_001233759-1; -.
DR   Ensembl; ENSCGRT00001007016.1; ENSCGRP00001004655.1; ENSCGRG00001005956.1.
DR   GeneID; 100689406; -.
DR   KEGG; cge:100689406; -.
DR   CTD; 3916; -.
DR   eggNOG; KOG4818; Eukaryota.
DR   GeneTree; ENSGT00950000182899; -.
DR   OrthoDB; 5404772at2759; -.
DR   Proteomes; UP000694386; Unplaced.
DR   Proteomes; UP001108280; Chromosome 1.
DR   GO; GO:0101004; C:cytolytic granule membrane; ISS:UniProtKB.
DR   GO; GO:0010008; C:endosome membrane; ISS:UniProtKB.
DR   GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005765; C:lysosomal membrane; ISS:UniProtKB.
DR   GO; GO:0005764; C:lysosome; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0008200; F:ion channel inhibitor activity; ISS:UniProtKB.
DR   GO; GO:0007042; P:lysosomal lumen acidification; ISS:UniProtKB.
DR   GO; GO:0050821; P:protein stabilization; ISS:CAFA.
DR   CDD; cd12087; TM_EGFR-like; 1.
DR   Gene3D; 2.40.160.110; -; 2.
DR   InterPro; IPR048528; Lamp2-like_luminal.
DR   InterPro; IPR048524; Lamp2-like_TM.
DR   InterPro; IPR018134; LAMP_CS.
DR   InterPro; IPR002000; Lysosome-assoc_membr_glycop.
DR   PANTHER; PTHR11506; LYSOSOME-ASSOCIATED MEMBRANE GLYCOPROTEIN; 1.
DR   PANTHER; PTHR11506:SF27; LYSOSOME-ASSOCIATED MEMBRANE GLYCOPROTEIN 1; 1.
DR   Pfam; PF01299; Lamp; 2.
DR   Pfam; PF21222; Lamp2_2nd; 1.
DR   PRINTS; PR00336; LYSASSOCTDMP.
DR   PROSITE; PS00310; LAMP_1; 2.
DR   PROSITE; PS00311; LAMP_2; 1.
DR   PROSITE; PS51407; LAMP_3; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Disulfide bond; Endosome; Glycoprotein; Lysosome; Membrane;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000250|UniProtKB:P14562"
FT   CHAIN           22..407
FT                   /note="Lysosome-associated membrane glycoprotein 1"
FT                   /id="PRO_0000017108"
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          183..206
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   CARBOHYD        32
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        40
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        57
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        72
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        98
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        253
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        304
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"
SQ   SEQUENCE   407 AA;  43787 MW;  651002040F86BB3D CRC64;
     MAAPGAPRSL LLLLLAGLAH GASALFVVKD SNGTACIMAN FSASFFTIYE TGHGSKNSTF
     ELPSSAEVLN SNSSCGRENV SEPILTIAFG SGYLLTLNFT RNATRYSVQD MYFAYNLSDT
     QHFLNASNKG IHSVDSSTDI KADINKTYRC LSAIQVHMGN VTVTLSDATI QAYLLNSNFS
     KEETRCTQDG PSPTTVPPSP SPPLVPTNPT VIKYNVTGEN GTCLLASMAL QMNITYMKKD
     NMTVTRALNI SPNDTASGSC SPHVVTLTVE SKNSILDLKF GMNGSSSLFF LQEVRLNMTL
     PDANVSSLMA SNQSLRALQA TVGNSYKCNT EEHIFVTKEF SLNVFSVQVQ AFKVESDRFG
     SVEECMQDGN NMLIPIAVGG ALAGLVLIVL IAYLIGRKRS HAGYQTI
//