ID LAMP1_CHICK Reviewed; 414 AA. AC P05300; DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1988, sequence version 1. DT 27-MAR-2024, entry version 136. DE RecName: Full=Lysosome-associated membrane glycoprotein 1 {ECO:0000303|PubMed:32999035}; DE Short=LAMP-1 {ECO:0000303|PubMed:32999035}; DE Short=Lysosome-associated membrane protein 1; DE AltName: Full=Lysosome membrane glycoprotein LEP100 {ECO:0000303|PubMed:3339090}; DE Flags: Precursor; GN Name=LAMP1; OS Gallus gallus (Chicken). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae; OC Phasianinae; Gallus. OX NCBI_TaxID=9031; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Brain; RX PubMed=3339090; DOI=10.1083/jcb.106.1.61; RA Fambrough D.M., Takeyasu K., Lippincott-Schwarz J., Siegel N.R.; RT "Structure of LEP100, a glycoprotein that shuttles between lysosomes and RT the plasma membrane, deduced from the nucleotide sequence of the encoding RT cDNA."; RL J. Cell Biol. 106:61-67(1988). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2250003; DOI=10.1016/s0021-9258(17)45315-4; RA Zot A.S., Fambrough D.M.; RT "Structure of a gene for a lysosomal membrane glycoprotein (LEP100). RT Housekeeping gene with unexpected exon organization."; RL J. Biol. Chem. 265:20988-20995(1990). RN [3] RP SUBCELLULAR LOCATION. RX PubMed=2871029; DOI=10.1083/jcb.102.5.1593; RA Lippincott-Schwartz J., Fambrough D.M.; RT "Lysosomal membrane dynamics: structure and interorganellar movement of a RT major lysosomal membrane glycoprotein."; RL J. Cell Biol. 102:1593-1605(1986). RN [4] RP SUBCELLULAR LOCATION. RX PubMed=3107839; DOI=10.1016/0092-8674(87)90543-5; RA Lippincott-Schwartz J., Fambrough D.M.; RT "Cycling of the integral membrane glycoprotein, LEP100, between plasma RT membrane and lysosomes: kinetic and morphological analysis."; RL Cell 49:669-677(1987). RN [5] RP FUNCTION (MICROBIAL INFECTION). RX PubMed=32999035; DOI=10.1128/jvi.01001-20; RA Boodhoo N., Kamble N., Behboudi S.; RT "De Novo Cholesterol Biosynthesis and Its Trafficking in LAMP-1-Positive RT Vesicles Are Involved in Replication and Spread of Marek's Disease Virus."; RL J. Virol. 94:0-0(2020). CC -!- FUNCTION: Lysosomal membrane glycoprotein which plays an important role CC in lysosome biogenesis, lysosomal pH regulation, autophagy and CC cholesterol homeostasis. {ECO:0000250|UniProtKB:P11279}. CC -!- FUNCTION: (Microbial infection) Plays an essential role in efficient CC replication and spread of Marek's disease virus, by facilitating viral CC cell-to-cell spread. {ECO:0000269|PubMed:32999035}. CC -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:2871029, CC ECO:0000269|PubMed:3107839}; Single-pass type I membrane protein CC {ECO:0000255}. Endosome membrane {ECO:0000269|PubMed:2871029, CC ECO:0000269|PubMed:3107839}; 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:0000269|PubMed:2871029, ECO:0000269|PubMed:3107839}; Single-pass CC type I membrane 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 (PubMed:2871029, PubMed:3107839). Colocalizes CC with OSBPL1A at the late endosome (PubMed:3107839). CC {ECO:0000269|PubMed:2871029, ECO:0000269|PubMed:3107839}. CC -!- SIMILARITY: Belongs to the LAMP family. {ECO:0000255|PROSITE- CC ProRule:PRU00740}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X07775; CAA30601.1; -; mRNA. DR EMBL; M59365; AAA65947.1; -; Genomic_DNA. DR EMBL; M59361; AAA65947.1; JOINED; Genomic_DNA. DR EMBL; M59362; AAA65947.1; JOINED; Genomic_DNA. DR EMBL; M59363; AAA65947.1; JOINED; Genomic_DNA. DR EMBL; M59364; AAA65947.1; JOINED; Genomic_DNA. DR PIR; A38331; A38331. DR RefSeq; NP_990614.2; NM_205283.2. DR AlphaFoldDB; P05300; -. DR SMR; P05300; -. DR STRING; 9031.ENSGALP00000052871; -. DR GlyCosmos; P05300; 17 sites, No reported glycans. DR PaxDb; 9031-ENSGALP00000027119; -. DR GeneID; 396220; -. DR KEGG; gga:396220; -. DR CTD; 3916; -. DR VEuPathDB; HostDB:geneid_396220; -. DR eggNOG; KOG4818; Eukaryota. DR InParanoid; P05300; -. DR PhylomeDB; P05300; -. DR PRO; PR:P05300; -. DR Proteomes; UP000000539; Unassembled WGS sequence. DR GO; GO:0101004; C:cytolytic granule membrane; ISS:UniProtKB. DR GO; GO:0010008; C:endosome membrane; IDA:UniProtKB. DR GO; GO:0031902; C:late endosome membrane; IBA:GO_Central. DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB. DR GO; GO:0016020; C:membrane; IDA:AgBase. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0008200; F:ion channel inhibitor activity; ISS:UniProtKB. DR GO; GO:0072594; P:establishment of protein localization to organelle; IBA:GO_Central. DR GO; GO:0007042; P:lysosomal lumen acidification; ISS:UniProtKB. 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:SF28; FI04419P; 1. DR PANTHER; PTHR11506; LYSOSOME-ASSOCIATED MEMBRANE GLYCOPROTEIN; 1. DR Pfam; PF01299; Lamp; 2. DR Pfam; PF21222; Lamp2_2nd; 1. DR PRINTS; PR00336; LYSASSOCTDMP. DR PROSITE; PS00310; LAMP_1; 1. 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 Reference proteome; Signal; Transmembrane; Transmembrane helix. FT SIGNAL 1..18 FT CHAIN 19..414 FT /note="Lysosome-associated membrane glycoprotein 1" FT /id="PRO_0000017109" FT TOPO_DOM 19..379 FT /note="Lumenal" FT /evidence="ECO:0000255" FT TRANSMEM 380..403 FT /note="Helical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00740" FT TOPO_DOM 404..414 FT /note="Cytoplasmic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00740" FT REGION 19..181 FT /note="First lumenal domain" FT REGION 182..224 FT /note="Hinge" FT REGION 186..213 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 225..379 FT /note="Second lumenal domain" FT COMPBIAS 186..210 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CARBOHYD 33 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 58 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 71 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 90 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 108 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 154 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 159 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 168 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 174 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 225 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 238 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 259 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 289 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 301 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 319 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 29..67 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00740" FT DISULFID 142..178 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00740" FT DISULFID 228..266 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00740" FT DISULFID 335..372 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00740" FT CONFLICT 3 FT /note="G -> R (in Ref. 2; AAA65947)" FT /evidence="ECO:0000305" FT CONFLICT 148 FT /note="V -> I (in Ref. 2; AAA65947)" FT /evidence="ECO:0000305" FT CONFLICT 325 FT /note="S -> L (in Ref. 2; AAA65947)" FT /evidence="ECO:0000305" FT CONFLICT 369 FT /note="M -> V (in Ref. 2; AAA65947)" FT /evidence="ECO:0000305" SQ SEQUENCE 414 AA; 44670 MW; 3D18941BAEA9372C CRC64; MGGAARAVLL GFLQASSSFD VRDSTGKVCI IANLTVAFSV EYKSSGQKQF AHFFLPQNAT SQSHSSCGEG NTSHPILALS FGAGHLISLN FSKTLDKYQV EELTFHYNLS DETLFPNATE GKVMVATQKS VIQARIGTEY RCINSKYVRM KHVNITFSNV TLEAYPTNDT FSANKTECRE DMVSTTTVAP TTPKHATSQV PTTSPAPTAA PSSPAVGKYN VTGANGTCVL ASMGLQLNIT YVKKDEKMGL DLLNFIPHNT SASGMCESTS AFLNLAFEKT KITFHFVLNA SSEKFFLQGV NVSTTLPSEA KAPTFEASND SMSESRATVG NSYKCSAEEN FQVTDKALVN VFNVQVQAFK VDGDKFGAME ECQLDENNML IPIIVGAALA GLVLIVLIAY LIGRKRSHAG YQTI //