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   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.
DR   Genevisible; P07307; HS.
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
//