LAMP1_CRIGR
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 03-AUG-2022, entry version 89.
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, 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; 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 STRING; 10029.NP_001233759.1; -.
DR Ensembl; ENSCGRT00001007016; ENSCGRP00001004655; ENSCGRG00001005956.
DR GeneID; 100689406; -.
DR KEGG; cge:100689406; -.
DR CTD; 3916; -.
DR eggNOG; KOG4818; Eukaryota.
DR GeneTree; ENSGT00950000182899; -.
DR OrthoDB; 1042920at2759; -.
DR GO; GO:0101004; C:cytolytic granule membrane; ISS:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0050821; P:protein stabilization; ISS:CAFA.
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 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
