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   24-JAN-2024, entry version 139.
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, 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; 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   GlyCosmos; Q05204; 18 sites, No reported glycans.
DR   PaxDb; 9913-ENSBTAP00000042536; -.
DR   PeptideAtlas; Q05204; -.
DR   Ensembl; ENSBTAT00000045121.4; ENSBTAP00000042536.3; ENSBTAG00000010242.6.
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; CQMDQNQ; -.
DR   OrthoDB; 5404772at2759; -.
DR   TreeFam; TF316339; -.
DR   Reactome; R-BTA-6798695; Neutrophil degranulation.
DR   Proteomes; UP000009136; Chromosome 12.
DR   Bgee; ENSBTAG00000010242; Expressed in monocyte and 105 other cell types or 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: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:0008200; F:ion channel inhibitor activity; ISS:UniProtKB.
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:0007042; P:lysosomal lumen acidification; ISS:UniProtKB.
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   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:SF35; LYSOSOME-ASSOCIATED MEMBRANE GLYCOPROTEIN 5; 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   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
//