Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-10116-00676
Entry Name
UniProt Accession
Theoretical PI
5.77
Molecular Weight
32848.88
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Asialoglycoprotein receptor 1
Protein Synonyms/Alias
ASGP-R 1; ASGPR 1; Hepatic lectin 1; HL-1; rHL-1;
Gene Name
Asgr1
Gene Synonyms/Alias
Asgr-1;
Created Date
21-JUL-1986
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
35
Canonical
PRLLQRLCSGFRLFL
[1]
S-Palmitoylation
Organism
Rattus norvegicus (Rat)
NCBI Taxa ID
10116
Reference
[1] Zeng FY, Weigel PH. Fatty acylation of the rat and human asialoglycoproteinreceptors. A conserved cytoplasmic cysteine residue is acylated in all receptorsubunits. J Biol Chem. 1996 Dec 13;271(50):32454-60.[PMID:8943311]
Functional Description
Mediates the endocytosis of plasma glycoproteins to which the terminal sialic acid residue on their complex carbohydrate moieties has been removed. The receptor recognizes terminal galactose and N-acetylgalactosamine units. After ligand binding to the receptor, the resulting complex is internalized and transported to a sorting organelle, where receptor and ligand are disassociated. The receptor then returns to the cell membrane surface.
Sequence Annotation
Topological domain: 1 39 Cytoplasmic.
Transmembrane: 40 60 Helical; Signal-anchor for type IImembrane protein.
Topological domain: 61 284 Extracellular.
Domain: 160 277 C-type lectin.
Motif: 5 8 Endocytosis signal.
Metal binding site: 190 190 Calcium 1; via carbonyl oxygen.
Metal binding site: 196 196 Calcium 1.
Metal binding site: 215 215 Calcium 2.
Metal binding site: 239 239 Calcium 3.
Metal binding site: 241 241 Calcium 3.
Metal binding site: 242 242 Calcium 2.
Metal binding site: 252 252 Calcium 2; via carbonyl oxygen.
Metal binding site: 252 252 Calcium 3.
Metal binding site: 253 253 Calcium 2.
Metal binding site: 264 264 Calcium 3.
Metal binding site: 265 265 Calcium 3.
Metal binding site: 277 277 Calcium 1.
Binding site: 239 239 Carbohydrate.
Binding site: 243 243 Carbohydrate.
Binding site: 252 252 Carbohydrate.
Protein Length
284 AA.
Protein Sequence
(Canonical)
MTKDYQDFQH LDNENDHHQL QRGPPPAPRL LQRLCSGFRL FLLSLGLSIL LLVVVCVITS  60
QNSQLREDLR VLRQNFSNFT VSTEDQVKAL TTQGERVGRK MKLVESQLEK HQEDLREDHS  120
RLLLHVKQLV SDVRSLSCQM AALRGNGSER ICCPINWVEY EGSCYWFSSS VKPWTEADKY  180
CQLENAHLVV VTSWEEQRFV QQHMGPLNTW IGLTDQNGPW KWVDGTDYET GFKNWRPGQP  240
DDWYGHGLGG GEDCAHFTTD GHWNDDVCRR PYRWVCETEL GKAN                   284
FASTA
(Canonical)
>LipidDB-10116-00676|P02706
MTKDYQDFQHLDNENDHHQLQRGPPPAPRLLQRLCSGFRLFLLSLGLSILLLVVVCVITS
QNSQLREDLRVLRQNFSNFTVSTEDQVKALTTQGERVGRKMKLVESQLEKHQEDLREDHS
RLLLHVKQLVSDVRSLSCQMAALRGNGSERICCPINWVEYEGSCYWFSSSVKPWTEADKY
CQLENAHLVVVTSWEEQRFVQQHMGPLNTWIGLTDQNGPWKWVDGTDYETGFKNWRPGQP
DDWYGHGLGGGEDCAHFTTDGHWNDDVCRRPYRWVCETELGKAN
Gene Ontology
GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW
GO:0004873; F:asialoglycoprotein receptor activity; IDA:RGD
GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW
GO:0046872; F:metal ion binding; IEA:UniProtKB-KW
GO:0031668; P:cellular response to extracellular stimulus; IEA:Ensembl
GO:0006898; P:receptor-mediated endocytosis; IDA:GOC
Interpro
InterPro; IPR001304; C-type_lectin
InterPro; IPR016186; C-type_lectin-like
InterPro; IPR018378; C-type_lectin_CS
InterPro; IPR016187; C-type_lectin_fold
InterPro; IPR005640; Lectin_N
Pfam
Pfam; PF00059; Lectin_C;
Pfam; PF03954; Lectin_N;
SMART
SMART; SM00034; CLECT;
PROSITE
PROSITE; PS00615; C_TYPE_LECTIN_1;
PROSITE; PS50041; C_TYPE_LECTIN_2;
PRINTS