ASGR1_HUMAN
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 03-AUG-2022, entry version 205.
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";
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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; 54.
DR ELM; P07306; -.
DR IntAct; P07306; 38.
DR STRING; 9606.ENSP00000269299; -.
DR BindingDB; P07306; -.
DR ChEMBL; CHEMBL2084; -.
DR UniLectin; P07306; -.
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; P07306; -.
DR PeptideAtlas; P07306; -.
DR PRIDE; P07306; -.
DR ProteomicsDB; 46770; -.
DR ProteomicsDB; 51980; -. [P07306-1]
DR ABCD; P07306; 3 sequenced antibodies.
DR Antibodypedia; 2481; 475 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 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; CAHFTPD; -.
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 1067 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 90 other tissues.
DR ExpressionAtlas; P07306; baseline and differential.
DR Genevisible; P07306; HS.
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:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0004873; F:asialoglycoprotein receptor activity; TAS:ProtInc.
DR GO; GO:0030246; F:carbohydrate binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
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; -; 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 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
