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Lysosome-associated membrane glycoprotein 1 (LAMP-1) (Lysosome-associated membrane protein 1) (CD107 antigen-like family member A) (Chromaffin granule-associated membrane glycoprotein IIA) (CD antigen CD107a)

 LAMP1_BOVIN             Reviewed;         409 AA.
Q05204; A2VE82; A5D7M2; Q17QC6;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
17-OCT-2006, sequence version 2.
05-JUL-2017, entry version 112.
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=Chromaffin granule-associated membrane glycoprotein IIA;
AltName: CD_antigen=CD107a;
Flags: Precursor;
Name=LAMP1;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Crossbred X Angus, and Hereford;
TISSUE=Fetal brain, Fetal liver, and Ileum;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 2-409, AND PARTIAL PROTEIN SEQUENCE.
TISSUE=Adrenal medulla;
PubMed=8496169;
Hieber A.D., Christie D.L.;
"Characterization of glycoprotein II from bovine adrenal medullary
chromaffin granules. Identification of components representing the
secretory vesicle counterparts of the lysosomal-associated membrane
glycoproteins (lamp-1 and lamp-2).";
J. Biol. Chem. 268:11073-11078(1993).
-!- 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-linked glycans are
polylactosaminoglycans. {ECO:0000250}.
-!- SIMILARITY: Belongs to the LAMP family. {ECO:0000255|PROSITE-
ProRule:PRU00740}.
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EMBL; BC118436; AAI18437.1; -; mRNA.
EMBL; BC133619; AAI33620.1; -; mRNA.
EMBL; BC140610; AAI40611.1; -; mRNA.
EMBL; L09113; AAA30548.1; -; mRNA.
PIR; A46712; A46712.
RefSeq; NP_001068592.1; NM_001075124.2.
UniGene; Bt.5330; -.
SMR; Q05204; -.
STRING; 9913.ENSBTAP00000042536; -.
PaxDb; Q05204; -.
PeptideAtlas; Q05204; -.
PRIDE; Q05204; -.
Ensembl; ENSBTAT00000045121; ENSBTAP00000042536; ENSBTAG00000010242.
GeneID; 281897; -.
KEGG; bta:281897; -.
CTD; 3916; -.
eggNOG; KOG4818; Eukaryota.
eggNOG; ENOG410XQ96; LUCA.
GeneTree; ENSGT00530000063068; -.
HOGENOM; HOG000230942; -.
HOVERGEN; HBG052303; -.
InParanoid; Q05204; -.
KO; K06528; -.
OMA; NGTACIM; -.
OrthoDB; EOG091G09EV; -.
TreeFam; TF316339; -.
Reactome; R-BTA-6798695; Neutrophil degranulation.
Proteomes; UP000009136; Chromosome 12.
Bgee; ENSBTAG00000010242; -.
GO; GO:0044754; C:autolysosome; IEA:Ensembl.
GO; GO:0005901; C:caveola; IDA:AgBase.
GO; GO:0044194; C:cytolytic granule; IEA:Ensembl.
GO; GO:0005829; C:cytosol; IEA:GOC.
GO; GO:0010008; C:endosome membrane; ISS:UniProtKB.
GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005765; C:lysosomal membrane; IDA:AgBase.
GO; GO:0042470; C:melanosome; IEA:Ensembl.
GO; GO:0045121; C:membrane raft; IDA:AgBase.
GO; GO:0005771; C:multivesicular body; IEA:Ensembl.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
GO; GO:0061474; C:phagolysosome membrane; IEA:Ensembl.
GO; GO:0042383; C:sarcolemma; IEA:Ensembl.
GO; GO:0008021; C:synaptic vesicle; IEA:Ensembl.
GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
GO; GO:0072594; P:establishment of protein localization to organelle; IEA:Ensembl.
GO; GO:0090160; P:Golgi to lysosome transport; IEA:Ensembl.
GO; GO:0008626; P:granzyme-mediated apoptotic signaling pathway; IEA:Ensembl.
GO; GO:0043323; P:positive regulation of natural killer cell degranulation; IEA:Ensembl.
GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
GO; GO:1902513; P:regulation of organelle transport along microtubule; IEA:Ensembl.
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.
1: Evidence at protein level;
Cell membrane; Complete proteome; Direct protein sequencing;
Disulfide bond; Endosome; Glycoprotein; Lysosome; Membrane;
Reference proteome; Signal; Transmembrane; Transmembrane helix.
SIGNAL 1 25 {ECO:0000250|UniProtKB:P14562}.
CHAIN 26 409 Lysosome-associated membrane glycoprotein
1.
/FTId=PRO_0000017107.
TOPO_DOM 26 374 Lumenal. {ECO:0000255}.
TRANSMEM 375 398 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00740}.
TOPO_DOM 399 409 Cytoplasmic. {ECO:0000255|PROSITE-
ProRule:PRU00740}.
REGION 26 187 First lumenal domain.
REGION 188 219 Hinge.
REGION 220 374 Second lumenal domain.
CARBOHYD 34 34 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 59 59 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 72 72 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 80 80 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 103 103 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 117 117 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 126 126 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 146 146 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 161 161 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 179 179 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 241 241 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 253 253 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 260 260 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 285 285 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 299 299 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 314 314 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 38 76 {ECO:0000255|PROSITE-ProRule:PRU00740}.
DISULFID 151 187 {ECO:0000255|PROSITE-ProRule:PRU00740}.
DISULFID 223 261 {ECO:0000255|PROSITE-ProRule:PRU00740}.
DISULFID 330 367 {ECO:0000255|PROSITE-ProRule:PRU00740}.
CONFLICT 2 7 AAPGGA -> RPPAAP (in Ref. 2; AAA30548).
{ECO:0000305}.
SEQUENCE 409 AA; 44153 MW; 36E955E7F1AB74F5 CRC64;
MAAPGGARRR PLLLLLFAGL VHGASAVFVV KNGNGTACIM ADFSATFLTS YDTRSGPQNK
SFELPAGAEV SNSSSCGKEN ASDSSLVITF GRGHTLTLIF TRNATRYEVQ LMRFAYNLSD
TDTFPNSSST GVKTVESATD IKADINKTYR CVSETQVNMD NVTVTLRDAA IQAYLSSSNF
SREETRCEQD LPTPTTPPQP APTPAPASPA VFRYNVSGSN GTCLLASMGL QLNVTYRRVD
NKTVTREFNV NPNKTTFGGN CSATLATLEL HSENLLLLAL QFVMNESSSR VFLQGVQLNL
TLPDAKEGSF TATNSSLRAL QATAGNSYKC NAEQRLRVTS SFSLNMFRVW LQAFRVDGDK
FGPVEECQLD ENSMLIPIAV GGALAGLVLI VLLAYLIGRK RSHAGYQTI


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