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Lysosome-associated membrane glycoprotein 1 (LAMP-1) (Lysosome-associated membrane protein 1) (CD107 antigen-like family member A) (Lysosomal membrane glycoprotein A) (LGP-A) (CD antigen CD107a)

 LAMP1_CRIGR             Reviewed;         407 AA.
P49129;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 1.
25-OCT-2017, entry version 74.
RecName: Full=Lysosome-associated membrane glycoprotein 1;
Short=LAMP-1;
Short=Lysosome-associated membrane protein 1;
AltName: Full=CD107 antigen-like family member A;
AltName: Full=Lysosomal membrane glycoprotein A;
Short=LGP-A;
AltName: CD_antigen=CD107a;
Flags: Precursor;
Name=LAMP1; Synonyms=LGPA;
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Cricetidae; Cricetinae; Cricetulus.
NCBI_TaxID=10029;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8867788;
Uthayakumar S., Granger B.L.;
"Cell surface accumulation of overexpressed hamster lysosomal membrane
glycoproteins.";
Cell. Mol. Biol. Res. 41:405-420(1995).
-!- FUNCTION: Presents carbohydrate ligands to selectins. Also
implicated in tumor cell metastasis (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P05300}; Single-pass type I membrane
protein {ECO:0000250|UniProtKB:P11279}. Endosome membrane
{ECO:0000250|UniProtKB:P11279}; Single-pass type I membrane
protein {ECO:0000250|UniProtKB:P11279}. Lysosome membrane
{ECO:0000250|UniProtKB:P11279}; Single-pass type I membrane
protein {ECO:0000250|UniProtKB:P11279}. Late endosome
{ECO:0000250|UniProtKB:P11279}. Note=This protein shuttles between
lysosomes, endosomes, and the plasma membrane. Colocalizes with
OSBPL1A at the late endosome. {ECO:0000250|UniProtKB:P05300,
ECO:0000250|UniProtKB:P11279}.
-!- PTM: O- and N-glycosylated; some of the N-glycans attached to
LAMP-1 are polylactosaminoglycans. {ECO:0000250}.
-!- SIMILARITY: Belongs to the LAMP family. {ECO:0000255|PROSITE-
ProRule:PRU00740}.
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EMBL; L18986; AAC37682.1; -; mRNA.
RefSeq; NP_001233759.1; NM_001246830.1.
SMR; P49129; -.
PRIDE; P49129; -.
Ensembl; ENSCGRT00001007016; ENSCGRP00001004655; ENSCGRG00001005956.
GeneID; 100689406; -.
KEGG; cge:100689406; -.
CTD; 3916; -.
HOVERGEN; HBG052303; -.
KO; K06528; -.
GO; GO:0010008; C:endosome membrane; ISS:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005770; C:late endosome; IEA:UniProtKB-SubCell.
GO; GO:0005765; C:lysosomal membrane; ISS:UniProtKB.
GO; GO:0005764; C:lysosome; IDA:MGI.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
InterPro; IPR018134; LAMP_CS.
InterPro; IPR002000; Lysosome-assoc_membr_glycop.
PANTHER; PTHR11506; PTHR11506; 1.
Pfam; PF01299; Lamp; 1.
PRINTS; PR00336; LYSASSOCTDMP.
PROSITE; PS00310; LAMP_1; 2.
PROSITE; PS00311; LAMP_2; 1.
PROSITE; PS51407; LAMP_3; 1.
2: Evidence at transcript level;
Cell membrane; Disulfide bond; Endosome; Glycoprotein; Lysosome;
Membrane; Signal; Transmembrane; Transmembrane helix.
SIGNAL 1 21 {ECO:0000250|UniProtKB:P14562}.
CHAIN 22 407 Lysosome-associated membrane glycoprotein
1.
/FTId=PRO_0000017108.
TOPO_DOM 22 371 Lumenal. {ECO:0000255}.
TRANSMEM 372 395 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00740}.
TOPO_DOM 396 407 Cytoplasmic. {ECO:0000255|PROSITE-
ProRule:PRU00740}.
REGION 22 189 First lumenal domain.
REGION 190 219 Hinge.
REGION 220 371 Second lumenal domain.
CARBOHYD 32 32 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 40 40 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 57 57 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 72 72 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 79 79 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 98 98 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 102 102 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 116 116 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 125 125 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 145 145 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 160 160 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 178 178 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 215 215 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 220 220 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 233 233 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 241 241 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 253 253 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 283 283 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 297 297 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 304 304 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 312 312 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 36 75 {ECO:0000255|PROSITE-ProRule:PRU00740}.
DISULFID 150 186 {ECO:0000255|PROSITE-ProRule:PRU00740}.
DISULFID 223 260 {ECO:0000255|PROSITE-ProRule:PRU00740}.
DISULFID 328 365 {ECO:0000255|PROSITE-ProRule:PRU00740}.
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


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