Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-00821
Entry Name
UniProt Accession
Theoretical PI
5.81
Molecular Weight
35092.21
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Asialoglycoprotein receptor 2
Protein Synonyms/Alias
ASGP-R 2; ASGPR 2; C-type lectin domain family 4 member H2; Hepatic lectin H2; HL-2;
Gene Name
ASGR2
Gene Synonyms/Alias
CLEC4H2;
Created Date
01-APR-1988
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
58
Canonical
QRLCSMVCFSLLALS
[1][2]
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]
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 58 Cytoplasmic.
Transmembrane: 59 79 Helical; Signal-anchor for type IImembrane protein.
Topological domain: 80 311 Extracellular.
Domain: 176 302 C-type lectin.
Motif: 5 8 Endocytosis signal.
Protein Length
311 AA.
Protein Sequence
(Canonical)
MAKDFQDIQQ LSSEENDHPF HQGEGPGTRR LNPRRGNPFL KGPPPAQPLA QRLCSMVCFS  60
LLALSFNILL LVVICVTGSQ SEGHGGAQLQ AELRSLKEAF SNFSSSTLTE VQAISTHGGS  120
VGDKITSLGA KLEKQQQDLK ADHDALLFHL KHFPVDLRFV ACQMELLHSN GSQRTCCPVN  180
WVEHQGSCYW FSHSGKAWAE AEKYCQLENA HLVVINSWEE QKFIVQHTNP FNTWIGLTDS  240
DGSWKWVDGT DYRHNYKNWA VTQPDNWHGH ELGGSEDCVE VQPDGRWNDD FCLQVYRWVC  300
EKRRNATGEV A                                                       311
FASTA
(Canonical)
>LipidDB-9606-00821|P07307
MAKDFQDIQQLSSEENDHPFHQGEGPGTRRLNPRRGNPFLKGPPPAQPLAQRLCSMVCFS
LLALSFNILLLVVICVTGSQSEGHGGAQLQAELRSLKEAFSNFSSSTLTEVQAISTHGGS
VGDKITSLGAKLEKQQQDLKADHDALLFHLKHFPVDLRFVACQMELLHSNGSQRTCCPVN
WVEHQGSCYWFSHSGKAWAEAEKYCQLENAHLVVINSWEEQKFIVQHTNPFNTWIGLTDS
DGSWKWVDGTDYRHNYKNWAVTQPDNWHGHELGGSEDCVEVQPDGRWNDDFCLQVYRWVC
EKRRNATGEVA
Gene Ontology
GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW
GO:0004873; F:asialoglycoprotein receptor activity; TAS:UniProtKB
GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW
GO:0030282; P:bone mineralization; IEA:Ensembl
GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc
GO:0009100; P:glycoprotein metabolic process; IEA:Ensembl
GO:0055088; P:lipid homeostasis; IEA:Ensembl
GO:0006898; P:receptor-mediated endocytosis; TAS:GOC
GO:0031647; P:regulation of protein stability; IEA:Ensembl
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