| Tag |
Content |
LipidDB ID |
LipidDB-9606-00823 |
Entry Name |
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UniProt Accession |
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Theoretical PI |
5.28 |
Molecular Weight |
33186.03 |
Genbank Protein ID |
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Genbank Nucleotide ID |
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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]
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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
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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 |
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Pfam |
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SMART |
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PROSITE |
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PRINTS |
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