ASGR2_RAT
ID ASGR2_RAT Reviewed; 301 AA.
AC P08290; Q5M8C9;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 4.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Asialoglycoprotein receptor 2;
DE Short=ASGP-R 2;
DE Short=ASGPR 2;
DE AltName: Full=Hepatic lectin R2/3;
DE Short=HL-2;
DE Short=rHL-2;
GN Name=Asgr2; Synonyms=Asgr-2;
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].
RX PubMed=3600647; DOI=10.1128/mcb.7.5.1841-1847.1987;
RA McPhaul M., Berg P.;
RT "Identification and characterization of cDNA clones encoding two homologous
RT proteins that are part of the asialoglycoprotein receptor.";
RL Mol. Cell. Biol. 7:1841-1847(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3597443; DOI=10.1016/s0021-9258(18)48008-8;
RA Halberg D.F., Wager R.E., Farrell D.C., Hildreth J., Quesenberry M.S.,
RA Loeb J.A., Holland E.C., Drickamer K.;
RT "Major and minor forms of the rat liver asialoglycoprotein receptor are
RT independent galactose-binding proteins. Primary structure and glycosylation
RT heterogeneity of minor receptor forms.";
RL J. Biol. Chem. 262:9828-9838(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=3234178; DOI=10.1089/dna.1988.7.721;
RA Sanford J.P., Elliott R.W., Doyle D.;
RT "Asialoglycoprotein receptor genes are linked on chromosome 11 in the
RT mouse.";
RL DNA 7:721-728(1988).
RN [4]
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 [5]
RP PROTEIN SEQUENCE OF 201-301.
RX PubMed=6319386; DOI=10.1016/s0021-9258(17)43524-1;
RA Drickamer K., Mamon J.F., Binns G., Leung J.O.;
RT "Primary structure of the rat liver asialoglycoprotein receptor. Structural
RT evidence for multiple polypeptide species.";
RL J. Biol. Chem. 259:770-778(1984).
RN [6]
RP PALMITOYLATION AT CYS-54.
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).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 -!- 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. RHL-2 and RHL-3
CC only differs in their carbohydrate structures.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=Hepatic asialoglycoprotein receptor subunit 2/3;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_rat_Ctlect_357";
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DR EMBL; M16347; AAA42038.1; -; mRNA.
DR EMBL; J02762; AAA41522.1; -; mRNA.
DR EMBL; X07636; CAA30476.1; -; mRNA.
DR EMBL; BC088099; AAH88099.1; -; mRNA.
DR PIR; B28462; LNRT2.
DR RefSeq; NP_058885.1; NM_017189.2.
DR RefSeq; XP_006246738.1; XM_006246676.3.
DR AlphaFoldDB; P08290; -.
DR SMR; P08290; -.
DR IntAct; P08290; 1.
DR STRING; 10116.ENSRNOP00000060474; -.
DR GlyGen; P08290; 3 sites.
DR iPTMnet; P08290; -.
DR PhosphoSitePlus; P08290; -.
DR SwissPalm; P08290; -.
DR PaxDb; P08290; -.
DR PRIDE; P08290; -.
DR Ensembl; ENSRNOT00000065370; ENSRNOP00000060474; ENSRNOG00000030726.
DR GeneID; 29403; -.
DR KEGG; rno:29403; -.
DR UCSC; RGD:2161; rat.
DR CTD; 433; -.
DR RGD; 2161; Asgr2.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000162310; -.
DR HOGENOM; CLU_049894_2_0_1; -.
DR InParanoid; P08290; -.
DR OMA; RTLTCQM; -.
DR OrthoDB; 1247924at2759; -.
DR PhylomeDB; P08290; -.
DR TreeFam; TF352155; -.
DR Reactome; R-RNO-446203; Asparagine N-linked glycosylation.
DR PRO; PR:P08290; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000030726; Expressed in liver and 15 other tissues.
DR ExpressionAtlas; P08290; baseline and differential.
DR Genevisible; P08290; RN.
DR GO; GO:0044322; C:endoplasmic reticulum quality control compartment; ISO:RGD.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0030246; F:carbohydrate binding; IBA:GO_Central.
DR GO; GO:0030282; P:bone mineralization; IEP:RGD.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0009100; P:glycoprotein metabolic process; ISO:RGD.
DR GO; GO:0055088; P:lipid homeostasis; ISO:RGD.
DR GO; GO:0031647; P:regulation of protein stability; ISO:RGD.
DR CDD; cd03590; CLECT_DC-SIGN_like; 1.
DR Gene3D; 3.10.100.10; -; 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 Pfam; PF00059; Lectin_C; 1.
DR SMART; SM00034; CLECT; 1.
DR SUPFAM; SSF56436; SSF56436; 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; Direct protein sequencing; Disulfide bond; Endocytosis;
KW Glycoprotein; Lectin; Lipoprotein; Membrane; Palmitate; Phosphoprotein;
KW Receptor; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..301
FT /note="Asialoglycoprotein receptor 2"
FT /id="PRO_0000046656"
FT TOPO_DOM 1..58
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 59..79
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 80..301
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 169..295
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT LIPID 54
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:8943311"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine"
FT DISULFID 170..181
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 198..293
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 271..285
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT CONFLICT 153
FT /note="R -> A (in Ref. 1; AAA42038)"
FT /evidence="ECO:0000305"
FT CONFLICT 202
FT /note="N -> I (in Ref. 1; AAA42038)"
FT /evidence="ECO:0000305"
FT CONFLICT 260
FT /note="W -> C (in Ref. 1; AAA42038 and 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 282..283
FT /note="DN -> ND (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 301 AA; 35027 MW; 21832FA713C3433C CRC64;
MEKDFQDIQQ LDSEENDHQL IGDEEQGSHV QNLRTENPRW GGQPPSRPFP QRLCSKFRLS
LLALAFNILL LVVICVVSSQ SMQLQKEFWT LKETLSNFST TTLMEFKALD SHGGSRNDNL
TSWETILEKK QKDIKADHST LLFHLKHFPL DLRTLTCQLA FFLSNGTECC PVNWVEFGGS
CYWFSRDGLT WAEADQYCQM ENAHLLVINS REEQEFVVKH RGAFHIWIGL TDKDGSWKWV
DGTEYRSNFK NWAFTQPDNW QGHEEGGSED CAEILSDGLW NDNFCQQVNR WACERKRDIT
Y
