Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-10116-00393
Entry Name
UniProt Accession
Theoretical PI
5.09
Molecular Weight
35027.16
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Asialoglycoprotein receptor 2
Protein Synonyms/Alias
ASGP-R 2; ASGPR 2; Hepatic lectin R2/3; HL-2; rHL-2;
Gene Name
Asgr2
Gene Synonyms/Alias
Asgr-2;
Created Date
01-AUG-1988
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
54
Canonical
RPFPQRLCSKFRLSL
[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 58 Cytoplasmic.
Transmembrane: 59 79 Helical; Signal-anchor for type IImembrane protein.
Topological domain: 80 301 Extracellular.
Domain: 169 295 C-type lectin.
Protein Length
301 AA.
Protein Sequence
(Canonical)
MEKDFQDIQQ LDSEENDHQL IGDEEQGSHV QNLRTENPRW GGQPPSRPFP QRLCSKFRLS  60
LLALAFNILL LVVICVVSSQ SMQLQKEFWT LKETLSNFST TTLMEFKALD SHGGSRNDNL  120
TSWETILEKK QKDIKADHST LLFHLKHFPL DLRTLTCQLA FFLSNGTECC PVNWVEFGGS  180
CYWFSRDGLT WAEADQYCQM ENAHLLVINS REEQEFVVKH RGAFHIWIGL TDKDGSWKWV  240
DGTEYRSNFK NWAFTQPDNW QGHEEGGSED CAEILSDGLW NDNFCQQVNR WACERKRDIT  300
Y                                                                  301
FASTA
(Canonical)
>LipidDB-10116-00393|P08290
MEKDFQDIQQLDSEENDHQLIGDEEQGSHVQNLRTENPRWGGQPPSRPFPQRLCSKFRLS
LLALAFNILLLVVICVVSSQSMQLQKEFWTLKETLSNFSTTTLMEFKALDSHGGSRNDNL
TSWETILEKKQKDIKADHSTLLFHLKHFPLDLRTLTCQLAFFLSNGTECCPVNWVEFGGS
CYWFSRDGLTWAEADQYCQMENAHLLVINSREEQEFVVKHRGAFHIWIGLTDKDGSWKWV
DGTEYRSNFKNWAFTQPDNWQGHEEGGSEDCAEILSDGLWNDNFCQQVNRWACERKRDIT
Y
Gene Ontology
GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW
GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW
GO:0030282; P:bone mineralization; IEP:RGD
GO:0006897; P:endocytosis; IEA:UniProtKB-KW
GO:0009100; P:glycoprotein metabolic process; IEA:Ensembl
GO:0055088; P:lipid homeostasis; IEA:Ensembl
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