ID ASGR2_HUMAN Reviewed; 311 AA.
AC P07307; A6NLV8; A8MT12; D3DTM9; D3DTN0; O00448; Q03969;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 27-MAR-2024, entry version 213.
DE RecName: Full=Asialoglycoprotein receptor 2;
DE Short=ASGP-R 2;
DE Short=ASGPR 2;
DE AltName: Full=C-type lectin domain family 4 member H2;
DE AltName: Full=Hepatic lectin H2;
DE Short=HL-2;
GN Name=ASGR2; Synonyms=CLEC4H2;
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 1), AND VARIANT ARG-85.
RX PubMed=3863106; DOI=10.1073/pnas.82.19.6465;
RA Spiess M., Lodish H.F.;
RT "Sequence of a second human asialoglycoprotein receptor: conservation of
RT two receptor genes during evolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:6465-6469(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ARG-85.
RC TISSUE=Liver;
RX PubMed=1371982; DOI=10.1002/hep.1840150307;
RA Paietta E., Stockert R.J., Racevskis J.;
RT "Differences in the abundance of variably spliced transcripts for the
RT second asialoglycoprotein receptor polypeptide, H2, in normal and
RT transformed human liver.";
RL Hepatology 15:395-402(1992).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ARG-85.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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 [6]
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 [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-102.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-102 AND ASN-170.
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 [9]
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 [10]
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).
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: The functioning ligand-binding unit of this receptor is
CC thought to be at least a dimer. Interacts with LASS2.
CC {ECO:0000269|PubMed:11543633}.
CC -!- SUBUNIT: (Microbial infection) Interacts with hepatitis E virus capsid
CC protein ORF2. {ECO:0000269|PubMed:27155063}.
CC -!- INTERACTION:
CC P07307; Q96G23: CERS2; NbExp=3; IntAct=EBI-1172636, EBI-1057080;
CC P07307-3; Q08AM2: ADAM33; NbExp=3; IntAct=EBI-12808270, EBI-10225815;
CC P07307-3; Q15848: ADIPOQ; NbExp=3; IntAct=EBI-12808270, EBI-10827839;
CC P07307-3; Q9NVV5-2: AIG1; NbExp=3; IntAct=EBI-12808270, EBI-11957045;
CC P07307-3; P27449: ATP6V0C; NbExp=3; IntAct=EBI-12808270, EBI-721179;
CC P07307-3; O15155: BET1; NbExp=3; IntAct=EBI-12808270, EBI-749204;
CC P07307-3; P19397: CD53; NbExp=3; IntAct=EBI-12808270, EBI-6657396;
CC P07307-3; Q6ZS10: CLEC17A; NbExp=3; IntAct=EBI-12808270, EBI-11977093;
CC P07307-3; Q9BXN2-6: CLEC7A; NbExp=3; IntAct=EBI-12808270, EBI-11989440;
CC P07307-3; P54849: EMP1; NbExp=3; IntAct=EBI-12808270, EBI-4319440;
CC P07307-3; Q7L5A8: FA2H; NbExp=3; IntAct=EBI-12808270, EBI-11337888;
CC P07307-3; Q969F0: FATE1; NbExp=3; IntAct=EBI-12808270, EBI-743099;
CC P07307-3; P30519: HMOX2; NbExp=3; IntAct=EBI-12808270, EBI-712096;
CC P07307-3; Q01638-2: IL1RL1; NbExp=3; IntAct=EBI-12808270, EBI-12838366;
CC P07307-3; O43561-2: LAT; NbExp=3; IntAct=EBI-12808270, EBI-8070286;
CC P07307-3; Q9UIQ6-2: LNPEP; NbExp=3; IntAct=EBI-12808270, EBI-12133176;
CC P07307-3; Q8IX19: MCEMP1; NbExp=3; IntAct=EBI-12808270, EBI-2816356;
CC P07307-3; Q8IY49-2: MMD2; NbExp=3; IntAct=EBI-12808270, EBI-13349813;
CC P07307-3; Q5J8X5: MS4A13; NbExp=3; IntAct=EBI-12808270, EBI-12070086;
CC P07307-3; Q02297-10: NRG1; NbExp=3; IntAct=EBI-12808270, EBI-12842334;
CC P07307-3; Q9P0S3: ORMDL1; NbExp=3; IntAct=EBI-12808270, EBI-1054848;
CC P07307-3; P26678: PLN; NbExp=3; IntAct=EBI-12808270, EBI-692836;
CC P07307-3; Q04941: PLP2; NbExp=3; IntAct=EBI-12808270, EBI-608347;
CC P07307-3; Q01453: PMP22; NbExp=3; IntAct=EBI-12808270, EBI-2845982;
CC P07307-3; Q9NS64: RPRM; NbExp=3; IntAct=EBI-12808270, EBI-1052363;
CC P07307-3; Q96IW7: SEC22A; NbExp=3; IntAct=EBI-12808270, EBI-8652744;
CC P07307-3; P78382: SLC35A1; NbExp=3; IntAct=EBI-12808270, EBI-12870360;
CC P07307-3; Q8TB61: SLC35B2; NbExp=3; IntAct=EBI-12808270, EBI-1054782;
CC P07307-3; Q9BZL3: SMIM3; NbExp=3; IntAct=EBI-12808270, EBI-741850;
CC P07307-3; Q9UNK0: STX8; NbExp=3; IntAct=EBI-12808270, EBI-727240;
CC P07307-3; P02786: TFRC; NbExp=3; IntAct=EBI-12808270, EBI-355727;
CC P07307-3; Q9NV12: TMEM140; NbExp=3; IntAct=EBI-12808270, EBI-2844246;
CC P07307-3; Q9H2L4: TMEM60; NbExp=3; IntAct=EBI-12808270, EBI-2852148;
CC P07307-3; Q8N661: TMEM86B; NbExp=3; IntAct=EBI-12808270, EBI-2548832;
CC P07307-3; Q6ZT21: TMPPE; NbExp=3; IntAct=EBI-12808270, EBI-11724433;
CC P07307-3; Q8N609: TRAM1L1; NbExp=3; IntAct=EBI-12808270, EBI-11996766;
CC P07307-3; Q5TGU0: TSPO2; NbExp=3; IntAct=EBI-12808270, EBI-12195249;
CC P07307-3; Q9Y5Z9: UBIAD1; NbExp=3; IntAct=EBI-12808270, EBI-2819725;
CC P07307-3; O00526: UPK2; NbExp=3; IntAct=EBI-12808270, EBI-10179682;
CC P07307-3; O95183: VAMP5; NbExp=3; IntAct=EBI-12808270, EBI-10191195;
CC P07307-3; Q9UEU0: VTI1B; NbExp=3; IntAct=EBI-12808270, EBI-723716;
CC P07307-3; Q9Y548: YIPF1; NbExp=3; IntAct=EBI-12808270, EBI-7850136;
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P07307-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P07307-2; Sequence=VSP_003060;
CC Name=3;
CC IsoId=P07307-3; Sequence=VSP_003060, VSP_003061;
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_hum_Ctlect_216";
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DR EMBL; M11025; AAB59519.1; -; mRNA.
DR EMBL; U97197; AAB58308.1; -; mRNA.
DR EMBL; X55283; CAA38997.1; -; mRNA.
DR EMBL; AC120057; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471108; EAW90259.1; -; Genomic_DNA.
DR EMBL; CH471108; EAW90260.1; -; Genomic_DNA.
DR EMBL; CH471108; EAW90261.1; -; Genomic_DNA.
DR EMBL; CH471108; EAW90263.1; -; Genomic_DNA.
DR EMBL; BC017251; AAH17251.1; -; mRNA.
DR CCDS; CCDS11088.1; -. [P07307-3]
DR CCDS; CCDS32544.1; -. [P07307-1]
DR CCDS; CCDS45598.1; -. [P07307-2]
DR PIR; A25179; LNHU2A.
DR RefSeq; NP_001172.1; NM_001181.4.
DR RefSeq; NP_001188281.1; NM_001201352.1.
DR RefSeq; NP_550434.1; NM_080912.3.
DR RefSeq; NP_550435.1; NM_080913.3. [P07307-3]
DR RefSeq; NP_550436.1; NM_080914.2.
DR RefSeq; XP_005256705.1; XM_005256648.2.
DR RefSeq; XP_006721589.1; XM_006721526.1. [P07307-3]
DR RefSeq; XP_016880140.1; XM_017024651.1. [P07307-2]
DR RefSeq; XP_016880141.1; XM_017024652.1.
DR RefSeq; XP_016880142.1; XM_017024653.1.
DR AlphaFoldDB; P07307; -.
DR SMR; P07307; -.
DR BioGRID; 106925; 88.
DR IntAct; P07307; 64.
DR STRING; 9606.ENSP00000347140; -.
DR DrugBank; DB00025; Antihemophilic factor, human recombinant.
DR DrugBank; DB13998; Lonoctocog alfa.
DR DrugBank; DB13999; Moroctocog alfa.
DR GlyConnect; 1920; 9 N-Linked glycans (1 site).
DR GlyCosmos; P07307; 3 sites, 9 glycans.
DR GlyGen; P07307; 3 sites, 9 N-linked glycans (1 site).
DR iPTMnet; P07307; -.
DR PhosphoSitePlus; P07307; -.
DR SwissPalm; P07307; -.
DR BioMuta; ASGR2; -.
DR DMDM; 218511923; -.
DR CPTAC; CPTAC-1176; -.
DR jPOST; P07307; -.
DR MassIVE; P07307; -.
DR MaxQB; P07307; -.
DR PaxDb; 9606-ENSP00000347140; -.
DR PeptideAtlas; P07307; -.
DR ProteomicsDB; 51981; -. [P07307-1]
DR ProteomicsDB; 51982; -. [P07307-2]
DR ProteomicsDB; 51983; -. [P07307-3]
DR Antibodypedia; 2656; 327 antibodies from 30 providers.
DR DNASU; 433; -.
DR Ensembl; ENST00000254850.11; ENSP00000254850.7; ENSG00000161944.17. [P07307-3]
DR Ensembl; ENST00000355035.9; ENSP00000347140.5; ENSG00000161944.17. [P07307-1]
DR Ensembl; ENST00000446679.6; ENSP00000405844.2; ENSG00000161944.17. [P07307-2]
DR GeneID; 433; -.
DR KEGG; hsa:433; -.
DR UCSC; uc002gen.2; human. [P07307-1]
DR AGR; HGNC:743; -.
DR CTD; 433; -.
DR DisGeNET; 433; -.
DR GeneCards; ASGR2; -.
DR HGNC; HGNC:743; ASGR2.
DR HPA; ENSG00000161944; Tissue enriched (liver).
DR MIM; 108361; gene.
DR neXtProt; NX_P07307; -.
DR OpenTargets; ENSG00000161944; -.
DR PharmGKB; PA25043; -.
DR VEuPathDB; HostDB:ENSG00000161944; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000162310; -.
DR HOGENOM; CLU_049894_2_0_1; -.
DR InParanoid; P07307; -.
DR OMA; RTLTCQM; -.
DR OrthoDB; 3991783at2759; -.
DR PhylomeDB; P07307; -.
DR TreeFam; TF352155; -.
DR PathwayCommons; P07307; -.
DR Reactome; R-HSA-446203; Asparagine N-linked glycosylation.
DR SignaLink; P07307; -.
DR BioGRID-ORCS; 433; 11 hits in 1148 CRISPR screens.
DR ChiTaRS; ASGR2; human.
DR GenomeRNAi; 433; -.
DR Pharos; P07307; Tbio.
DR PRO; PR:P07307; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P07307; Protein.
DR Bgee; ENSG00000161944; Expressed in right lobe of liver and 122 other cell types or tissues.
DR ExpressionAtlas; P07307; baseline and differential.
DR Genevisible; P07307; HS.
DR GO; GO:0044322; C:endoplasmic reticulum quality control compartment; IDA:UniProtKB.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0004873; F:asialoglycoprotein receptor activity; TAS:UniProtKB.
DR GO; GO:0042806; F:fucose binding; IBA:GO_Central.
DR GO; GO:0005537; F:mannose binding; IBA:GO_Central.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; 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.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Disulfide bond; Endocytosis; Glycoprotein;
KW Host-virus interaction; Lectin; Lipoprotein; Membrane; Palmitate;
KW Phosphoprotein; Receptor; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..311
FT /note="Asialoglycoprotein receptor 2"
FT /id="PRO_0000046654"
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..311
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 176..302
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 5..8
FT /note="Endocytosis signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 1..16
FT /note="Polar 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 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19159218"
FT CARBOHYD 170
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 305
FT /note="N-linked (GlcNAc...) asparagine"
FT DISULFID 177..188
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 205..300
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 278..292
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT VAR_SEQ 24..42
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_003060"
FT VAR_SEQ 82..86
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_003061"
FT VARIANT 85
FT /note="G -> R (in dbSNP:rs2304978)"
FT /evidence="ECO:0000269|PubMed:1371982,
FT ECO:0000269|PubMed:3863106, ECO:0000269|Ref.4"
FT /id="VAR_068747"
SQ SEQUENCE 311 AA; 35092 MW; C86D2247FFF604DC CRC64;
MAKDFQDIQQ LSSEENDHPF HQGEGPGTRR LNPRRGNPFL KGPPPAQPLA QRLCSMVCFS
LLALSFNILL LVVICVTGSQ SEGHGGAQLQ AELRSLKEAF SNFSSSTLTE VQAISTHGGS
VGDKITSLGA KLEKQQQDLK ADHDALLFHL KHFPVDLRFV ACQMELLHSN GSQRTCCPVN
WVEHQGSCYW FSHSGKAWAE AEKYCQLENA HLVVINSWEE QKFIVQHTNP FNTWIGLTDS
DGSWKWVDGT DYRHNYKNWA VTQPDNWHGH ELGGSEDCVE VQPDGRWNDD FCLQVYRWVC
EKRRNATGEV A
//
