ASGR2_MOUSE
ID ASGR2_MOUSE Reviewed; 301 AA.
AC P24721;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Asialoglycoprotein receptor 2;
DE Short=ASGP-R 2;
DE Short=ASGPR 2;
DE AltName: Full=Hepatic lectin 2;
DE Short=HL-2;
DE Short=mHL-2;
GN Name=Asgr2; Synonyms=Asgr-2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Liver;
RX PubMed=2223888; DOI=10.1016/0167-4781(90)90216-o;
RA Sanford J.P., Doyle D.;
RT "Mouse asialoglycoprotein receptor cDNA sequence: conservation of receptor
RT genes during mammalian evolution.";
RL Biochim. Biophys. Acta 1087:259-261(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; 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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=Hepatic asialoglycoprotein receptor subunit 2;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_mou_Ctlect_159";
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DR EMBL; X53042; CAA37211.1; -; mRNA.
DR EMBL; BC011197; AAH11197.1; -; mRNA.
DR CCDS; CCDS24934.1; -.
DR PIR; S13165; S13165.
DR RefSeq; NP_001300854.1; NM_001313925.1.
DR RefSeq; NP_001300855.1; NM_001313926.1.
DR RefSeq; NP_001300856.1; NM_001313927.1.
DR RefSeq; NP_031519.1; NM_007493.3.
DR AlphaFoldDB; P24721; -.
DR SMR; P24721; -.
DR STRING; 10090.ENSMUSP00000099632; -.
DR GlyGen; P24721; 3 sites.
DR iPTMnet; P24721; -.
DR PhosphoSitePlus; P24721; -.
DR SwissPalm; P24721; -.
DR jPOST; P24721; -.
DR MaxQB; P24721; -.
DR PaxDb; P24721; -.
DR PRIDE; P24721; -.
DR ProteomicsDB; 281919; -.
DR Antibodypedia; 2656; 306 antibodies from 30 providers.
DR DNASU; 11890; -.
DR Ensembl; ENSMUST00000102572; ENSMUSP00000099632; ENSMUSG00000040963.
DR GeneID; 11890; -.
DR KEGG; mmu:11890; -.
DR UCSC; uc007jtt.1; mouse.
DR CTD; 433; -.
DR MGI; MGI:88082; Asgr2.
DR VEuPathDB; HostDB:ENSMUSG00000040963; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000162310; -.
DR HOGENOM; CLU_049894_2_0_1; -.
DR InParanoid; P24721; -.
DR OMA; RTLTCQM; -.
DR OrthoDB; 1247924at2759; -.
DR PhylomeDB; P24721; -.
DR TreeFam; TF352155; -.
DR Reactome; R-MMU-446203; Asparagine N-linked glycosylation.
DR BioGRID-ORCS; 11890; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Asgr2; mouse.
DR PRO; PR:P24721; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P24721; protein.
DR Bgee; ENSMUSG00000040963; Expressed in liver and 48 other tissues.
DR ExpressionAtlas; P24721; baseline and differential.
DR Genevisible; P24721; MM.
DR GO; GO:0044322; C:endoplasmic reticulum quality control compartment; ISO:MGI.
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:MGI.
DR GO; GO:0030246; F:carbohydrate binding; IBA:GO_Central.
DR GO; GO:0030282; P:bone mineralization; IEA:Ensembl.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0009100; P:glycoprotein metabolic process; IMP:MGI.
DR GO; GO:0055088; P:lipid homeostasis; IMP:MGI.
DR GO; GO:0031647; P:regulation of protein stability; IMP:MGI.
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; Disulfide bond; Endocytosis; Glycoprotein; Lectin; Lipoprotein;
KW Membrane; Palmitate; Phosphoprotein; Receptor; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..301
FT /note="Asialoglycoprotein receptor 2"
FT /id="PRO_0000046655"
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..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..36
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08290"
FT LIPID 54
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 298
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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"
SQ SEQUENCE 301 AA; 34907 MW; 3A29F1AFBA68F298 CRC64;
MEKDCQDIQQ LDSEENDHQL SGDDEHGSHV QDPRIENPHW KGQPLSRPFP QRLCSTFRLS
LLALAFNILL LVVICVVSSQ SIQLQEEFRT LKETFSNFSS STLMEFGALD TLGGSTNAIL
TSWLAQLEEK QQQLKADHST LLFHLKHFPM DLRTLTCQLA YFQSNGTECC PVNWVEFGGS
CYWFSRDGLT WAEADQYCQL ENAHLLVINS REEQDFVVKH RSQFHIWIGL TDRDGSWKWV
DGTDYRSNYR NWAFTQPDNW QGHEQGGGED CAEILSDGHW NDNFCQQVNR WVCEKRRNIT
H
