Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-00823
Entry Name
UniProt Accession
Theoretical PI
5.28
Molecular Weight
33186.03
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Asialoglycoprotein receptor 1
Protein Synonyms/Alias
ASGP-R 1; ASGPR 1; C-type lectin domain family 4 member H1; Hepatic lectin H1; HL-1;
Gene Name
ASGR1
Gene Synonyms/Alias
CLEC4H1;
Created Date
01-APR-1988
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
36
Canonical
QPLLQRLCSGPRLLL
[1][2][3]
S-Palmitoylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Yik JH, Saxena A, Weigel JA, Weigel PH. Nonpalmitoylated humanasialoglycoprotein receptors recycle constitutively but are defective in coatedpit-mediated endocytosis, dissociation, and delivery of ligand to lysosomes. JBiol Chem. 2002 Oct 25;277(43):40844-52. Epub 2002 Aug 8.[PMID:12171918]
[2] Yik JH, Saxena A, Weigel JA, Weigel PH. Palmitoylation-defectiveasialoglycoprotein receptors are normal in their cellular distribution andability to bind ligand, but are defective in ligand uptake and degradation.Biochem Biophys Res Commun. 2002 Oct 4;297(4):980-6.[PMID:12359251]
[3] Yik JH, Weigel PH. The position of cysteine relative to the transmembranedomain is critical for palmitoylation of H1, the major subunit of the humanasialoglycoprotein receptor. J Biol Chem. 2002 Dec 6;277(49):47305-12. Epub 2002 Oct 4.[PMID:12370180]
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 40 Cytoplasmic.
Transmembrane: 41 61 Helical; Signal-anchor for type IImembrane protein.
Topological domain: 62 291 Extracellular.
Domain: 161 278 C-type lectin.
Motif: 5 8 Endocytosis signal.
Metal binding site: 191 191 Calcium 1; via carbonyl oxygen.
Metal binding site: 197 197 Calcium 1.
Metal binding site: 216 216 Calcium 2.
Metal binding site: 240 240 Calcium 3.
Metal binding site: 242 242 Calcium 3.
Metal binding site: 243 243 Calcium 2.
Metal binding site: 253 253 Calcium 2; via carbonyl oxygen.
Metal binding site: 253 253 Calcium 3.
Metal binding site: 254 254 Calcium 2.
Metal binding site: 265 265 Calcium 3.
Metal binding site: 266 266 Calcium 3.
Metal binding site: 278 278 Calcium 1.
Binding site: 240 240 Carbohydrate.
Binding site: 244 244 Carbohydrate.
Binding site: 253 253 Carbohydrate.
Protein Length
291 AA.
Protein Sequence
(Canonical)
MTKEYQDLQH LDNEESDHHQ LRKGPPPPQP LLQRLCSGPR LLLLSLGLSL LLLVVVCVIG  60
SQNSQLQEEL RGLRETFSNF TASTEAQVKG LSTQGGNVGR KMKSLESQLE KQQKDLSEDH  120
SSLLLHVKQF VSDLRSLSCQ MAALQGNGSE RTCCPVNWVE HERSCYWFSR SGKAWADADN  180
YCRLEDAHLV VVTSWEEQKF VQHHIGPVNT WMGLHDQNGP WKWVDGTDYE TGFKNWRPEQ  240
PDDWYGHGLG GGEDCAHFTD DGRWNDDVCQ RPYRWVCETE LDKASQEPPL L           291
FASTA
(Canonical)
>LipidDB-9606-00823|P07306
MTKEYQDLQHLDNEESDHHQLRKGPPPPQPLLQRLCSGPRLLLLSLGLSLLLLVVVCVIG
SQNSQLQEELRGLRETFSNFTASTEAQVKGLSTQGGNVGRKMKSLESQLEKQQKDLSEDH
SSLLLHVKQFVSDLRSLSCQMAALQGNGSERTCCPVNWVEHERSCYWFSRSGKAWADADN
YCRLEDAHLVVVTSWEEQKFVQHHIGPVNTWMGLHDQNGPWKWVDGTDYETGFKNWRPEQ
PDDWYGHGLGGGEDCAHFTDDGRWNDDVCQRPYRWVCETELDKASQEPPLL
Gene Ontology
GO:0005576; C:extracellular region; IEA:UniProtKB-KW
GO:0005887; C:integral component of plasma membrane; TAS:ProtInc
GO:0004873; F:asialoglycoprotein receptor activity; TAS:ProtInc
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; TAS:ProtInc
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