LAMP1_CHICK
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 03-AUG-2022, entry version 129.
DE RecName: Full=Lysosome-associated membrane glycoprotein 1;
DE Short=LAMP-1;
DE Short=Lysosome-associated membrane protein 1;
DE AltName: Full=Lysosome membrane glycoprotein LEP100;
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, autophagy, and cholesterol homeostasis.
CC Presents carbohydrate ligands to selectins. Also implicated in tumor
CC cell metastasis. {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: Cell 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}. Lysosome 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}. Cytolytic granule
CC membrane {ECO:0000250|UniProtKB:P11279}; Single-pass type I membrane
CC protein {ECO:0000255}. Note=This protein shuttles between lysosomes,
CC endosomes, and the plasma membrane (PubMed:2871029, PubMed:3107839).
CC Colocalizes 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}.
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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.ENSGALP00000027119; -.
DR PaxDb; P05300; -.
DR GeneID; 396220; -.
DR KEGG; gga:396220; -.
DR CTD; 3916; -.
DR VEuPathDB; HostDB:geneid_396220; -.
DR eggNOG; KOG4818; Eukaryota.
DR InParanoid; P05300; -.
DR OrthoDB; 1042920at2759; -.
DR PhylomeDB; P05300; -.
DR PRO; PR:P05300; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0101004; C:cytolytic granule membrane; ISS:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; IDA:UniProtKB.
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:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:AgBase.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0072594; P:establishment of protein localization to organelle; IBA:GO_Central.
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; 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
