ID ASGR1_HUMAN Reviewed; 291 AA. AC P07306; I3L1X1; DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 27-MAR-2024, entry version 214. DE RecName: Full=Asialoglycoprotein receptor 1; DE Short=ASGP-R 1; DE Short=ASGPR 1; DE AltName: Full=C-type lectin domain family 4 member H1; DE AltName: Full=Hepatic lectin H1; DE Short=HL-1; GN Name=ASGR1; Synonyms=CLEC4H1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM H1A). RX PubMed=2982798; DOI=10.1016/s0021-9258(18)89497-2; RA Spiess M., Schwartz A.L., Lodish H.F.; RT "Sequence of human asialoglycoprotein receptor cDNA. An internal signal RT sequence for membrane insertion."; RL J. Biol. Chem. 260:1979-1982(1985). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM H1A). RX PubMed=3753585; DOI=10.1016/0092-8674(86)90496-4; RA Spiess M., Lodish H.F.; RT "An internal signal sequence: the asialoglycoprotein receptor membrane RT anchor."; RL Cell 44:177-185(1986). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM H1A). RA Wang H., Gao X., Li L., Lou H., Huang Y., Wang B., Han J.; RT "Human asialoglycoprotein receptor 1 gene is expressed in SH-SY5Y human RT neuroblastoma cells."; RL Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM H1B), ALTERNATIVE SPLICING, AND RP SUBCELLULAR LOCATION (ISOFORM H1B). RC TISSUE=Liver; RX PubMed=20886072; DOI=10.1371/journal.pone.0012934; RA Liu J., Hu B., Yang Y., Ma Z., Yu Y., Liu S., Wang B., Zhao X., Lu M., RA Yang D.; RT "A new splice variant of the major subunit of human asialoglycoprotein RT receptor encodes a secreted form in hepatocytes."; RL PLoS ONE 5:E12934-E12934(2010). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16625196; DOI=10.1038/nature04689; RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.; RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the RT human lineage."; RL Nature 440:1045-1049(2006). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM H1A). 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 [7] RP PALMITOYLATION AT CYS-36. 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 [8] RP INTERACTION WITH LASS2. RX PubMed=11543633; DOI=10.1006/geno.2001.6614; RA Pan H., Qin W.-X., Huo K.-K., Wan D.-F., Yu Y., Xu Z.-G., Hu Q.-D., RA Gu K.T., Zhou X.-M., Jiang H.-Q., Zhang P.-P., Huang Y., Li Y.-Y., RA Gu J.-R.; RT "Cloning, mapping, and characterization of a human homologue of the yeast RT longevity assurance gene LAG1."; RL Genomics 77:58-64(2001). RN [9] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-79 AND ASN-147. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of multiple RT enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16 AND SER-285, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [12] RP INTERACTION WITH HEPATITIS E VIRUS CAPSID PROTEIN ORF2 (MICROBIAL RP INFECTION). RX PubMed=27155063; DOI=10.1002/jmv.24570; RA Zhang L., Tian Y., Wen Z., Zhang F., Qi Y., Huang W., Zhang H., Wang Y.; RT "Asialoglycoprotein receptor facilitates infection of PLC/PRF/5 cells by RT HEV through interaction with ORF2."; RL J. Med. Virol. 88:2186-2195(2016). RN [13] {ECO:0007744|PDB:1DV8} RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 154-281. RX PubMed=10891274; DOI=10.1006/jmbi.2000.3853; RA Meier M., Bider M.D., Malashkevich V.N., Spiess M., Burkhard P.; RT "Crystal structure of the carbohydrate recognition domain of the H1 subunit RT of the asialoglycoprotein receptor."; RL J. Mol. Biol. 300:857-865(2000). 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:0000269|PubMed:11543633}. CC -!- SUBUNIT: (Microbial infection) Interacts with hepatitis E virus capsid CC protein ORF2. {ECO:0000269|PubMed:27155063}. CC -!- INTERACTION: CC P07306; Q8IVF2-3: AHNAK2; NbExp=3; IntAct=EBI-1172335, EBI-12078468; CC P07306; Q86WK6: AMIGO1; NbExp=3; IntAct=EBI-1172335, EBI-19125216; CC P07306; Q96BI3: APH1A; NbExp=3; IntAct=EBI-1172335, EBI-2606935; CC P07306; Q9UN42: ATP1B4; NbExp=3; IntAct=EBI-1172335, EBI-12894731; CC P07306; P62952: BLCAP; NbExp=3; IntAct=EBI-1172335, EBI-3895726; CC P07306; Q96G23: CERS2; NbExp=3; IntAct=EBI-1172335, EBI-1057080; CC P07306; O95471: CLDN7; NbExp=3; IntAct=EBI-1172335, EBI-740744; CC P07306; Q7Z7G2: CPLX4; NbExp=3; IntAct=EBI-1172335, EBI-18013275; CC P07306; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-1172335, EBI-6942903; CC P07306; P00387: CYB5R3; NbExp=3; IntAct=EBI-1172335, EBI-1046040; CC P07306; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-1172335, EBI-781551; CC P07306; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-1172335, EBI-18304435; CC P07306; P12314: FCGR1A; NbExp=3; IntAct=EBI-1172335, EBI-2869867; CC P07306; Q8TBE3: FNDC9; NbExp=3; IntAct=EBI-1172335, EBI-12142257; CC P07306; Q8TED1: GPX8; NbExp=3; IntAct=EBI-1172335, EBI-11721746; CC P07306; P31937: HIBADH; NbExp=3; IntAct=EBI-1172335, EBI-11427100; CC P07306; P24593: IGFBP5; NbExp=3; IntAct=EBI-1172335, EBI-720480; CC P07306; P43628: KIR2DL3; NbExp=3; IntAct=EBI-1172335, EBI-8632435; CC P07306; A8MZ59: LEUTX; NbExp=3; IntAct=EBI-1172335, EBI-17490413; CC P07306; Q8IX19: MCEMP1; NbExp=3; IntAct=EBI-1172335, EBI-2816356; CC P07306; O14524-2: NEMP1; NbExp=3; IntAct=EBI-1172335, EBI-10969203; CC P07306; Q13113: PDZK1IP1; NbExp=3; IntAct=EBI-1172335, EBI-716063; CC P07306; Q6ZMZ0: RNF19B; NbExp=3; IntAct=EBI-1172335, EBI-2466594; CC P07306; Q9NR31: SAR1A; NbExp=3; IntAct=EBI-1172335, EBI-3920694; CC P07306; Q14973: SLC10A1; NbExp=3; IntAct=EBI-1172335, EBI-3923031; CC P07306; Q9NQQ7-3: SLC35C2; NbExp=3; IntAct=EBI-1172335, EBI-17295964; CC P07306; Q9NPE6: SPAG4; NbExp=3; IntAct=EBI-1172335, EBI-10819434; CC P07306; Q96L08: SUSD3; NbExp=3; IntAct=EBI-1172335, EBI-18194029; CC P07306; Q9Y320: TMX2; NbExp=3; IntAct=EBI-1172335, EBI-6447886; CC P07306; Q9H7M9: VSIR; NbExp=3; IntAct=EBI-1172335, EBI-744988; CC -!- SUBCELLULAR LOCATION: [Isoform H1a]: Membrane; Single-pass type II CC membrane protein. CC -!- SUBCELLULAR LOCATION: [Isoform H1b]: Secreted CC {ECO:0000269|PubMed:20886072}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=H1a; CC IsoId=P07306-1; Sequence=Displayed; CC Name=H1b; Synonyms=sASGPR; CC IsoId=P07306-2; Sequence=VSP_044480; CC -!- TISSUE SPECIFICITY: Expressed exclusively in hepatic parenchymal cells. CC -!- PTM: Phosphorylated on a cytoplasmic Ser residue. CC -!- MISCELLANEOUS: Calcium is required for ligand binding. 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_hum_Ctlect_215"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M10058; AAA51785.1; -; mRNA. DR EMBL; AB070933; BAB83508.1; -; mRNA. DR EMBL; FJ410292; ACQ90237.1; -; mRNA. DR EMBL; AC120057; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC032130; AAH32130.1; -; mRNA. DR CCDS; CCDS11089.1; -. [P07306-1] DR CCDS; CCDS56017.1; -. [P07306-2] DR PIR; A22509; LNHU1. DR RefSeq; NP_001184145.1; NM_001197216.2. [P07306-2] DR RefSeq; NP_001662.1; NM_001671.4. [P07306-1] DR RefSeq; XP_011522163.1; XM_011523861.2. [P07306-1] DR PDB; 1DV8; X-ray; 2.30 A; A=154-281. DR PDB; 5JPV; X-ray; 1.90 A; A/B=148-291. DR PDB; 5JQ1; X-ray; 1.83 A; A/B=148-291. DR PDB; 6YAU; X-ray; 1.40 A; A=148-291. DR PDBsum; 1DV8; -. DR PDBsum; 5JPV; -. DR PDBsum; 5JQ1; -. DR PDBsum; 6YAU; -. DR AlphaFoldDB; P07306; -. DR SMR; P07306; -. DR BioGRID; 106924; 56. DR ELM; P07306; -. DR IntAct; P07306; 38. DR STRING; 9606.ENSP00000269299; -. DR BindingDB; P07306; -. DR ChEMBL; CHEMBL2084; -. DR DrugBank; DB13133; Von Willebrand factor human. DR UniLectin; P07306; -. DR GlyCosmos; P07306; 2 sites, No reported glycans. DR GlyGen; P07306; 2 sites. DR iPTMnet; P07306; -. DR PhosphoSitePlus; P07306; -. DR SwissPalm; P07306; -. DR BioMuta; ASGR1; -. DR DMDM; 126132; -. DR MassIVE; P07306; -. DR MaxQB; P07306; -. DR PaxDb; 9606-ENSP00000269299; -. DR PeptideAtlas; P07306; -. DR ProteomicsDB; 46770; -. DR ProteomicsDB; 51980; -. [P07306-1] DR ABCD; P07306; 3 sequenced antibodies. DR Antibodypedia; 2481; 526 antibodies from 33 providers. DR DNASU; 432; -. DR Ensembl; ENST00000269299.8; ENSP00000269299.3; ENSG00000141505.12. [P07306-1] DR Ensembl; ENST00000574388.5; ENSP00000459169.1; ENSG00000141505.12. [P07306-2] DR Ensembl; ENST00000619926.4; ENSP00000481182.1; ENSG00000141505.12. [P07306-2] DR GeneID; 432; -. DR KEGG; hsa:432; -. DR MANE-Select; ENST00000269299.8; ENSP00000269299.3; NM_001671.5; NP_001662.1. DR UCSC; uc021toy.3; human. [P07306-1] DR AGR; HGNC:742; -. DR CTD; 432; -. DR DisGeNET; 432; -. DR GeneCards; ASGR1; -. DR HGNC; HGNC:742; ASGR1. DR HPA; ENSG00000141505; Tissue enriched (liver). DR MIM; 108360; gene. DR neXtProt; NX_P07306; -. DR OpenTargets; ENSG00000141505; -. DR PharmGKB; PA25042; -. DR VEuPathDB; HostDB:ENSG00000141505; -. DR eggNOG; KOG4297; Eukaryota. DR GeneTree; ENSGT00940000161727; -. DR HOGENOM; CLU_049894_2_0_1; -. DR InParanoid; P07306; -. DR OMA; NGHQFSK; -. DR OrthoDB; 3991783at2759; -. DR PhylomeDB; P07306; -. DR TreeFam; TF352155; -. DR PathwayCommons; P07306; -. DR Reactome; R-HSA-446203; Asparagine N-linked glycosylation. DR SignaLink; P07306; -. DR BioGRID-ORCS; 432; 8 hits in 1145 CRISPR screens. DR ChiTaRS; ASGR1; human. DR EvolutionaryTrace; P07306; -. DR GenomeRNAi; 432; -. DR Pharos; P07306; Tbio. DR PRO; PR:P07306; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; P07306; Protein. DR Bgee; ENSG00000141505; Expressed in right lobe of liver and 92 other cell types or tissues. DR ExpressionAtlas; P07306; baseline and differential. DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0004873; F:asialoglycoprotein receptor activity; TAS:ProtInc. DR GO; GO:0042806; F:fucose binding; IBA:GO_Central. DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl. 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; IEA:Ensembl. DR GO; GO:0006898; P:receptor-mediated endocytosis; TAS:ProtInc. 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. DR Genevisible; P07306; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Calcium; Coiled coil; Disulfide bond; KW Endocytosis; Glycoprotein; Host-virus interaction; Lectin; Lipoprotein; KW Membrane; Metal-binding; Palmitate; Phosphoprotein; Receptor; KW Reference proteome; Secreted; Signal-anchor; Transmembrane; KW Transmembrane helix. FT CHAIN 1..291 FT /note="Asialoglycoprotein receptor 1" FT /id="PRO_0000046650" FT TOPO_DOM 1..40 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 41..61 FT /note="Helical; Signal-anchor for type II membrane protein" FT /evidence="ECO:0000305" FT TOPO_DOM 62..291 FT /note="Extracellular" FT /evidence="ECO:0000305" FT DOMAIN 161..278 FT /note="C-type lectin" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040" FT REGION 1..30 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 61..123 FT /evidence="ECO:0000255" FT MOTIF 5..8 FT /note="Endocytosis signal" FT /evidence="ECO:0000255" FT COMPBIAS 1..22 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 191 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT BINDING 197 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT BINDING 216 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT BINDING 240 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT BINDING 242 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT BINDING 243 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT BINDING 253 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT BINDING 253 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT BINDING 254 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT BINDING 265 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT BINDING 266 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT BINDING 278 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT MOD_RES 16 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 285 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT LIPID 36 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000269|PubMed:8943311" FT CARBOHYD 79 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT CARBOHYD 147 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT DISULFID 154..165 FT DISULFID 182..277 FT DISULFID 255..269 FT VAR_SEQ 24..63 FT /note="GPPPPQPLLQRLCSGPRLLLLSLGLSLLLLVVVCVIGSQN -> D (in FT isoform H1b)" FT /evidence="ECO:0000303|PubMed:20886072" FT /id="VSP_044480" FT STRAND 159..161 FT /evidence="ECO:0007829|PDB:6YAU" FT STRAND 164..168 FT /evidence="ECO:0007829|PDB:6YAU" FT HELIX 175..184 FT /evidence="ECO:0007829|PDB:6YAU" FT HELIX 195..205 FT /evidence="ECO:0007829|PDB:6YAU" FT STRAND 210..215 FT /evidence="ECO:0007829|PDB:6YAU" FT STRAND 248..251 FT /evidence="ECO:0007829|PDB:6YAU" FT STRAND 255..258 FT /evidence="ECO:0007829|PDB:6YAU" FT STRAND 264..267 FT /evidence="ECO:0007829|PDB:6YAU" FT STRAND 273..280 FT /evidence="ECO:0007829|PDB:6YAU" SQ SEQUENCE 291 AA; 33186 MW; 9B825527B2FC1FD0 CRC64; MTKEYQDLQH LDNEESDHHQ LRKGPPPPQP LLQRLCSGPR LLLLSLGLSL LLLVVVCVIG SQNSQLQEEL RGLRETFSNF TASTEAQVKG LSTQGGNVGR KMKSLESQLE KQQKDLSEDH SSLLLHVKQF VSDLRSLSCQ MAALQGNGSE RTCCPVNWVE HERSCYWFSR SGKAWADADN YCRLEDAHLV VVTSWEEQKF VQHHIGPVNT WMGLHDQNGP WKWVDGTDYE TGFKNWRPEQ PDDWYGHGLG GGEDCAHFTD DGRWNDDVCQ RPYRWVCETE LDKASQEPPL L //