LAMP1_BOVIN
ID LAMP1_BOVIN Reviewed; 409 AA.
AC Q05204; A2VE82; A5D7M2; Q17QC6;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 132.
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=Chromaffin granule-associated membrane glycoprotein IIA;
DE AltName: CD_antigen=CD107a;
DE Flags: Precursor;
GN Name=LAMP1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus, and Hereford;
RC TISSUE=Fetal brain, Fetal liver, and Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2-409, AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Adrenal medulla;
RX PubMed=8496169; DOI=10.1016/s0021-9258(18)82093-2;
RA Hieber A.D., Christie D.L.;
RT "Characterization of glycoprotein II from bovine adrenal medullary
RT chromaffin granules. Identification of components representing the
RT secretory vesicle counterparts of the lysosomal-associated membrane
RT glycoproteins (lamp-1 and lamp-2).";
RL J. Biol. Chem. 268:11073-11078(1993).
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-linked glycans are
CC polylactosaminoglycans. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the LAMP family. {ECO:0000255|PROSITE-
CC ProRule:PRU00740}.
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DR EMBL; BC118436; AAI18437.1; -; mRNA.
DR EMBL; BC133619; AAI33620.1; -; mRNA.
DR EMBL; BC140610; AAI40611.1; -; mRNA.
DR EMBL; L09113; AAA30548.1; -; mRNA.
DR PIR; A46712; A46712.
DR RefSeq; NP_001068592.1; NM_001075124.2.
DR AlphaFoldDB; Q05204; -.
DR SMR; Q05204; -.
DR STRING; 9913.ENSBTAP00000042536; -.
DR PaxDb; Q05204; -.
DR PeptideAtlas; Q05204; -.
DR PRIDE; Q05204; -.
DR Ensembl; ENSBTAT00000045121; ENSBTAP00000042536; ENSBTAG00000010242.
DR GeneID; 281897; -.
DR KEGG; bta:281897; -.
DR CTD; 3916; -.
DR VEuPathDB; HostDB:ENSBTAG00000010242; -.
DR VGNC; VGNC:30775; LAMP1.
DR eggNOG; KOG4818; Eukaryota.
DR GeneTree; ENSGT00950000182899; -.
DR HOGENOM; CLU_055379_2_0_1; -.
DR InParanoid; Q05204; -.
DR OMA; NSYKCSA; -.
DR OrthoDB; 1042920at2759; -.
DR TreeFam; TF316339; -.
DR Reactome; R-BTA-6798695; Neutrophil degranulation.
DR Proteomes; UP000009136; Chromosome 12.
DR Bgee; ENSBTAG00000010242; Expressed in monocyte and 105 other tissues.
DR GO; GO:0044754; C:autolysosome; IEA:Ensembl.
DR GO; GO:0000421; C:autophagosome membrane; IEA:Ensembl.
DR GO; GO:0005901; C:caveola; IDA:AgBase.
DR GO; GO:0101004; C:cytolytic granule membrane; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0010008; C:endosome membrane; ISS:UniProtKB.
DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031902; C:late endosome membrane; IBA:GO_Central.
DR GO; GO:0005765; C:lysosomal membrane; IDA:AgBase.
DR GO; GO:0042470; C:melanosome; IEA:Ensembl.
DR GO; GO:0045121; C:membrane raft; IDA:AgBase.
DR GO; GO:0005771; C:multivesicular body; IEA:Ensembl.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0061474; C:phagolysosome membrane; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0042383; C:sarcolemma; IEA:Ensembl.
DR GO; GO:0008021; C:synaptic vesicle; IEA:Ensembl.
DR GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0072594; P:establishment of protein localization to organelle; IBA:GO_Central.
DR GO; GO:0090160; P:Golgi to lysosome transport; IEA:Ensembl.
DR GO; GO:0140507; P:granzyme-mediated programmed cell death signaling pathway; IEA:Ensembl.
DR GO; GO:0043323; P:positive regulation of natural killer cell degranulation; IEA:Ensembl.
DR GO; GO:0050821; P:protein stabilization; ISS:CAFA.
DR GO; GO:1902513; P:regulation of organelle transport along microtubule; IEA:Ensembl.
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..25
FT /evidence="ECO:0000250|UniProtKB:P14562"
FT CHAIN 26..409
FT /note="Lysosome-associated membrane glycoprotein 1"
FT /id="PRO_0000017107"
FT TOPO_DOM 26..374
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 375..398
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00740"
FT TOPO_DOM 399..409
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00740"
FT REGION 26..187
FT /note="First lumenal domain"
FT REGION 180..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 188..219
FT /note="Hinge"
FT REGION 220..374
FT /note="Second lumenal domain"
FT COMPBIAS 193..207
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 34
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 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 179
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 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 260
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 285
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 299
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 314
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 38..76
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00740"
FT DISULFID 151..187
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00740"
FT DISULFID 223..261
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00740"
FT DISULFID 330..367
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00740"
FT CONFLICT 2..7
FT /note="AAPGGA -> RPPAAP (in Ref. 2; AAA30548)"
FT /evidence="ECO:0000305"
SQ 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
