ID ASGR1_RAT Reviewed; 284 AA.
AC P02706;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 27-MAR-2024, entry version 168.
DE RecName: Full=Asialoglycoprotein receptor 1;
DE Short=ASGP-R 1;
DE Short=ASGPR 1;
DE AltName: Full=Hepatic lectin 1;
DE Short=HL-1;
DE Short=rHL-1;
GN Name=Asgr1; Synonyms=Asgr-1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=6095287; DOI=10.1073/pnas.81.23.7338;
RA Holland E.C., Leung J.O., Drickamer K.;
RT "Rat liver asialoglycoprotein receptor lacks a cleavable NH2-terminal
RT signal sequence.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:7338-7342(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2995379; DOI=10.1016/s0021-9258(17)38902-0;
RA Leung J.O., Holland E.C., Drickamer K.;
RT "Characterization of the gene encoding the major rat liver
RT asialoglycoprotein receptor.";
RL J. Biol. Chem. 260:12523-12527(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 12-284.
RX PubMed=2945599; DOI=10.1007/bf01114949;
RA Watts C.;
RT "Isolation and expression of cDNA clones for a rat liver asialoglycoprotein
RT receptor.";
RL Biosci. Rep. 6:527-534(1986).
RN [5]
RP PALMITOYLATION AT CYS-35.
RX PubMed=8943311; DOI=10.1074/jbc.271.50.32454;
RA Zeng F.Y., Weigel P.H.;
RT "Fatty acylation of the rat and human asialoglycoprotein receptors. A
RT conserved cytoplasmic cysteine residue is acylated in all receptor
RT subunits.";
RL J. Biol. Chem. 271:32454-32460(1996).
CC -!- FUNCTION: Mediates the endocytosis of plasma glycoproteins to which the
CC terminal sialic acid residue on their complex carbohydrate moieties has
CC been removed. The receptor recognizes terminal galactose and N-
CC acetylgalactosamine units. After ligand binding to the receptor, the
CC resulting complex is internalized and transported to a sorting
CC organelle, where receptor and ligand are disassociated. The receptor
CC then returns to the cell membrane surface.
CC -!- SUBUNIT: Interacts with LASS2. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed exclusively in hepatic parenchymal cells.
CC -!- PTM: Phosphorylated on a cytoplasmic Ser residue. {ECO:0000250}.
CC -!- MISCELLANEOUS: Calcium is required for ligand binding.
CC -!- MISCELLANEOUS: Two types of rat hepatic lectin have been identified,
CC RHL-1 and RHL-2/3, having a relative abundance of 4:1.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=Hepatic asialoglycoprotein receptor subunit 1;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_rat_Ctlect_00128";
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DR EMBL; K02817; AAA42037.1; -; Genomic_DNA.
DR EMBL; BC088154; AAH88154.1; -; mRNA.
DR EMBL; M21770; AAA40764.1; -; mRNA.
DR PIR; A92497; LNRTL.
DR RefSeq; NP_036635.1; NM_012503.2.
DR RefSeq; XP_006246641.1; XM_006246579.1.
DR AlphaFoldDB; P02706; -.
DR SMR; P02706; -.
DR IntAct; P02706; 1.
DR STRING; 10116.ENSRNOP00000025254; -.
DR GlyCosmos; P02706; 3 sites, No reported glycans.
DR GlyGen; P02706; 3 sites.
DR iPTMnet; P02706; -.
DR PhosphoSitePlus; P02706; -.
DR SwissPalm; P02706; -.
DR PaxDb; 10116-ENSRNOP00000025254; -.
DR Ensembl; ENSRNOT00000025254.6; ENSRNOP00000025254.3; ENSRNOG00000018693.8.
DR Ensembl; ENSRNOT00055056898; ENSRNOP00055046997; ENSRNOG00055032882.
DR Ensembl; ENSRNOT00060052761; ENSRNOP00060043859; ENSRNOG00060030352.
DR Ensembl; ENSRNOT00065047528; ENSRNOP00065039000; ENSRNOG00065027557.
DR GeneID; 24210; -.
DR KEGG; rno:24210; -.
DR UCSC; RGD:2160; rat.
DR AGR; RGD:2160; -.
DR CTD; 432; -.
DR RGD; 2160; Asgr1.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000161727; -.
DR InParanoid; P02706; -.
DR OMA; NGHQFSK; -.
DR OrthoDB; 3991783at2759; -.
DR PhylomeDB; P02706; -.
DR TreeFam; TF352155; -.
DR Reactome; R-RNO-446203; Asparagine N-linked glycosylation.
DR PRO; PR:P02706; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000018693; Expressed in liver and 12 other cell types or tissues.
DR Genevisible; P02706; RN.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0004873; F:asialoglycoprotein receptor activity; IDA:RGD.
DR GO; GO:0042806; F:fucose binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0005537; F:mannose binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031668; P:cellular response to extracellular stimulus; ISO:RGD.
DR CDD; cd03590; CLECT_DC-SIGN_like; 1.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR018378; C-type_lectin_CS.
DR InterPro; IPR033989; CD209-like_CTLD.
DR InterPro; IPR016187; CTDL_fold.
DR PANTHER; PTHR22803:SF155; C-TYPE LECTIN DOMAIN CONTAINING 10A; 1.
DR PANTHER; PTHR22803; MANNOSE, PHOSPHOLIPASE, LECTIN RECEPTOR RELATED; 1.
DR Pfam; PF00059; Lectin_C; 1.
DR Pfam; PF03954; Lectin_N; 1.
DR SMART; SM00034; CLECT; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE 1: Evidence at protein level;
KW Calcium; Coiled coil; Disulfide bond; Endocytosis; Glycoprotein; Lectin;
KW Lipoprotein; Membrane; Metal-binding; Palmitate; Phosphoprotein; Receptor;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..284
FT /note="Asialoglycoprotein receptor 1"
FT /id="PRO_0000046653"
FT TOPO_DOM 1..39
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 40..60
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 61..284
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 160..277
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT COILED 58..122
FT /evidence="ECO:0000255"
FT MOTIF 5..8
FT /note="Endocytosis signal"
FT /evidence="ECO:0000255"
FT BINDING 190
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 196
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 215
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 239
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 241
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 242
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 252
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 252
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 253
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 264
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 265
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 277
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT LIPID 35
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:8943311"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 153..164
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 181..276
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 254..268
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT CONFLICT 61
FT /note="Q -> R (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 284 AA; 32849 MW; 5D973A09458900BA CRC64;
MTKDYQDFQH LDNENDHHQL QRGPPPAPRL LQRLCSGFRL FLLSLGLSIL LLVVVCVITS
QNSQLREDLR VLRQNFSNFT VSTEDQVKAL TTQGERVGRK MKLVESQLEK HQEDLREDHS
RLLLHVKQLV SDVRSLSCQM AALRGNGSER ICCPINWVEY EGSCYWFSSS VKPWTEADKY
CQLENAHLVV VTSWEEQRFV QQHMGPLNTW IGLTDQNGPW KWVDGTDYET GFKNWRPGQP
DDWYGHGLGG GEDCAHFTTD GHWNDDVCRR PYRWVCETEL GKAN
//
