HEMO_HUMAN
ID HEMO_HUMAN Reviewed; 462 AA.
AC P02790; B2R957;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 205.
DE RecName: Full=Hemopexin;
DE AltName: Full=Beta-1B-glycoprotein;
DE Flags: Precursor;
GN Name=HPX;
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 [GENOMIC DNA].
RX PubMed=2842511; DOI=10.1007/bf02138368;
RA Altruda F., Poli V., Restagno G., Silengo L.;
RT "Structure of the human hemopexin gene and evidence for intron-mediated
RT evolution.";
RL J. Mol. Evol. 27:102-108(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary gland;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2-462.
RX PubMed=3220477; DOI=10.1016/0888-7543(88)90158-9;
RA Law M.L., Cai G.Y., Hartz J.A., Jones C., Kao F.T.;
RT "The hemopexin gene maps to the same location as the beta-globin gene
RT cluster on human chromosome 11.";
RL Genomics 3:48-52(1988).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 22-462.
RX PubMed=2989777; DOI=10.1093/nar/13.11.3841;
RA Altruda F., Poli V., Restagno G., Argos P., Cortese R., Silengo L.;
RT "The primary structure of human hemopexin deduced from cDNA sequence:
RT evidence for internal, repeating homology.";
RL Nucleic Acids Res. 13:3841-3859(1985).
RN [5]
RP PROTEIN SEQUENCE OF ACTIVE PROTEIN.
RX PubMed=3855550; DOI=10.1073/pnas.82.1.73;
RA Takahashi N., Takahashi Y., Putnam F.W.;
RT "Complete amino acid sequence of human hemopexin, the heme-binding protein
RT of serum.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:73-77(1985).
RN [6]
RP PROTEIN SEQUENCE OF 24-255.
RX PubMed=6510521; DOI=10.1016/0014-5793(84)80603-1;
RA Frantikova V., Borvak J., Kluh I., Moravek L.;
RT "Amino acid sequence of the N-terminal region of human hemopexin.";
RL FEBS Lett. 178:213-216(1984).
RN [7]
RP PARTIAL PROTEIN SEQUENCE, AND GLYCOSYLATION AT THR-24; ASN-64; ASN-64;
RP ASN-187; ASN-240; ASN-246 AND ASN-453.
RX PubMed=6371807; DOI=10.1073/pnas.81.7.2021;
RA Takahashi N., Takahashi Y., Putnam F.W.;
RT "Structure of human hemopexin: O-glycosyl and N-glycosyl sites and unusual
RT clustering of tryptophan residues.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:2021-2025(1984).
RN [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-187 AND ASN-453.
RC TISSUE=Bile;
RX PubMed=15084671; DOI=10.1074/mcp.m400015-mcp200;
RA Kristiansen T.Z., Bunkenborg J., Gronborg M., Molina H., Thuluvath P.J.,
RA Argani P., Goggins M.G., Maitra A., Pandey A.;
RT "A proteomic analysis of human bile.";
RL Mol. Cell. Proteomics 3:715-728(2004).
RN [9]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-187; ASN-240 AND ASN-246.
RC TISSUE=Plasma;
RX PubMed=14760718; DOI=10.1002/pmic.200300556;
RA Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.;
RT "Screening for N-glycosylated proteins by liquid chromatography mass
RT spectrometry.";
RL Proteomics 4:454-465(2004).
RN [10]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-64 AND ASN-187.
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 [11]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-187 AND ASN-453.
RC TISSUE=Saliva;
RX PubMed=16740002; DOI=10.1021/pr050492k;
RA Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T., Loo J.A.;
RT "Identification of N-linked glycoproteins in human saliva by glycoprotein
RT capture and mass spectrometry.";
RL J. Proteome Res. 5:1493-1503(2006).
RN [12]
RP INTERACTION WITH HEPATITIS E VIRUS/HEV ORF3 PROTEIN (MICROBIAL INFECTION).
RX PubMed=18211098; DOI=10.1021/bi7016552;
RA Ratra R., Kar-Roy A., Lal S.K.;
RT "The ORF3 protein of hepatitis E virus interacts with hemopexin by means of
RT its 26 amino acid N-terminal hydrophobic domain II.";
RL Biochemistry 47:1957-1969(2008).
RN [13]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-187 AND ASN-453.
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 [14]
RP GLYCOSYLATION AT ASN-187 AND ASN-453.
RX PubMed=19139490; DOI=10.1074/mcp.m800504-mcp200;
RA Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B.,
RA Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L.,
RA Ying W.T., He S.M., Qian X.H.;
RT "A strategy for precise and large scale identification of core fucosylated
RT glycoproteins.";
RL Mol. Cell. Proteomics 8:913-923(2009).
RN [15]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT THR-24; ASN-64; ASN-187 AND
RP ASN-453, AND STRUCTURE OF CARBOHYDRATES.
RC TISSUE=Cerebrospinal fluid;
RX PubMed=19838169; DOI=10.1038/nmeth.1392;
RA Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E., Brinkmalm G.,
RA Larson G.;
RT "Enrichment of glycopeptides for glycan structure and attachment site
RT identification.";
RL Nat. Methods 6:809-811(2009).
RN [16]
RP INTERACTION WITH FLVCR1.
RX PubMed=20610401; DOI=10.1074/jbc.m110.119131;
RA Yang Z., Philips J.D., Doty R.T., Giraudi P., Ostrow J.D., Tiribelli C.,
RA Smith A., Abkowitz J.L.;
RT "Kinetics and specificity of feline leukemia virus subgroup C receptor
RT (FLVCR) export function and its dependence on hemopexin.";
RL J. Biol. Chem. 285:28874-28882(2010).
RN [17]
RP GLYCOSYLATION AT THR-29, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=23234360; DOI=10.1021/pr300963h;
RA Halim A., Ruetschi U., Larson G., Nilsson J.;
RT "LC-MS/MS characterization of O-glycosylation sites and glycan structures
RT of human cerebrospinal fluid glycoproteins.";
RL J. Proteome Res. 12:573-584(2013).
RN [18]
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).
CC -!- FUNCTION: Binds heme and transports it to the liver for breakdown and
CC iron recovery, after which the free hemopexin returns to the
CC circulation.
CC -!- SUBUNIT: Interacts with FLVCR1. {ECO:0000269|PubMed:20610401}.
CC -!- SUBUNIT: (Microbial infection) Interacts with hepatitis E virus/HEV
CC protein ORF3. {ECO:0000269|PubMed:18211098}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.
CC -!- PTM: N- and O-glycosylated. O-glycosylated with core 1 or possibly core
CC 8 glycans. O-glycosylation in the 30-40 region is minor compared to
CC glycosylation at Thr-24 and Thr-29. {ECO:0000269|PubMed:14760718,
CC ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:16335952,
CC ECO:0000269|PubMed:16740002, ECO:0000269|PubMed:19139490,
CC ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169,
CC ECO:0000269|PubMed:23234360, ECO:0000269|PubMed:6371807}.
CC -!- MISCELLANEOUS: The isolated N-terminal domain binds one heme. The full-
CC length protein also binds one heme, but at a different site. The
CC physiological significance of this is not clear (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the hemopexin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA26382.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M36803; AAA58678.1; -; Genomic_DNA.
DR EMBL; M36796; AAA58678.1; JOINED; Genomic_DNA.
DR EMBL; M36799; AAA58678.1; JOINED; Genomic_DNA.
DR EMBL; M36800; AAA58678.1; JOINED; Genomic_DNA.
DR EMBL; M36801; AAA58678.1; JOINED; Genomic_DNA.
DR EMBL; M36802; AAA58678.1; JOINED; Genomic_DNA.
DR EMBL; AK313648; BAG36404.1; -; mRNA.
DR EMBL; J03048; AAA52704.1; -; mRNA.
DR EMBL; X02537; CAA26382.1; ALT_INIT; mRNA.
DR CCDS; CCDS7763.1; -.
DR PIR; I56456; OQHU.
DR RefSeq; NP_000604.1; NM_000613.2.
DR AlphaFoldDB; P02790; -.
DR SASBDB; P02790; -.
DR SMR; P02790; -.
DR BioGRID; 109500; 69.
DR DIP; DIP-38339N; -.
DR IntAct; P02790; 21.
DR MINT; P02790; -.
DR STRING; 9606.ENSP00000265983; -.
DR DrugBank; DB00080; Daptomycin.
DR DrugBank; DB14533; Zinc chloride.
DR DrugBank; DB14548; Zinc sulfate, unspecified form.
DR CarbonylDB; P02790; -.
DR GlyConnect; 757; 84 N-Linked glycans (5 sites), 3 O-Linked glycans (2 sites).
DR GlyGen; P02790; 11 sites, 97 N-linked glycans (5 sites), 8 O-linked glycans (5 sites).
DR iPTMnet; P02790; -.
DR PhosphoSitePlus; P02790; -.
DR BioMuta; HPX; -.
DR DMDM; 1708182; -.
DR DOSAC-COBS-2DPAGE; P02790; -.
DR REPRODUCTION-2DPAGE; IPI00022488; -.
DR SWISS-2DPAGE; P02790; -.
DR CPTAC; non-CPTAC-1131; -.
DR EPD; P02790; -.
DR jPOST; P02790; -.
DR MassIVE; P02790; -.
DR PaxDb; P02790; -.
DR PeptideAtlas; P02790; -.
DR PRIDE; P02790; -.
DR ProteomicsDB; 51598; -.
DR Antibodypedia; 23841; 567 antibodies from 38 providers.
DR DNASU; 3263; -.
DR Ensembl; ENST00000265983.8; ENSP00000265983.3; ENSG00000110169.12.
DR GeneID; 3263; -.
DR KEGG; hsa:3263; -.
DR MANE-Select; ENST00000265983.8; ENSP00000265983.3; NM_000613.3; NP_000604.1.
DR UCSC; uc001mdg.3; human.
DR CTD; 3263; -.
DR DisGeNET; 3263; -.
DR GeneCards; HPX; -.
DR HGNC; HGNC:5171; HPX.
DR HPA; ENSG00000110169; Tissue enriched (liver).
DR MIM; 142290; gene.
DR neXtProt; NX_P02790; -.
DR OpenTargets; ENSG00000110169; -.
DR PharmGKB; PA29441; -.
DR VEuPathDB; HostDB:ENSG00000110169; -.
DR eggNOG; KOG1565; Eukaryota.
DR GeneTree; ENSGT00390000009178; -.
DR HOGENOM; CLU_061713_0_0_1; -.
DR InParanoid; P02790; -.
DR OMA; CSSAMRW; -.
DR OrthoDB; 792317at2759; -.
DR PhylomeDB; P02790; -.
DR TreeFam; TF331201; -.
DR PathwayCommons; P02790; -.
DR Reactome; R-HSA-2168880; Scavenging of heme from plasma.
DR SignaLink; P02790; -.
DR SIGNOR; P02790; -.
DR BioGRID-ORCS; 3263; 9 hits in 1070 CRISPR screens.
DR ChiTaRS; HPX; human.
DR GeneWiki; Hemopexin; -.
DR GenomeRNAi; 3263; -.
DR Pharos; P02790; Tbio.
DR PRO; PR:P02790; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; P02790; protein.
DR Bgee; ENSG00000110169; Expressed in right lobe of liver and 104 other tissues.
DR ExpressionAtlas; P02790; baseline and differential.
DR Genevisible; P02790; HS.
DR GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0071682; C:endocytic vesicle lumen; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0015232; F:heme transmembrane transporter activity; TAS:ProtInc.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006879; P:cellular iron ion homeostasis; TAS:ProtInc.
DR GO; GO:0042168; P:heme metabolic process; IBA:GO_Central.
DR GO; GO:0015886; P:heme transport; TAS:ProtInc.
DR GO; GO:0020027; P:hemoglobin metabolic process; IEA:Ensembl.
DR GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0002925; P:positive regulation of humoral immune response mediated by circulating immunoglobulin; IEA:Ensembl.
DR GO; GO:0002639; P:positive regulation of immunoglobulin production; IEA:Ensembl.
DR GO; GO:0060335; P:positive regulation of interferon-gamma-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IEA:Ensembl.
DR GO; GO:0007260; P:tyrosine phosphorylation of STAT protein; IEA:Ensembl.
DR CDD; cd00094; HX; 2.
DR Gene3D; 2.110.10.10; -; 2.
DR InterPro; IPR016358; Hemopexin.
DR InterPro; IPR000585; Hemopexin-like_dom.
DR InterPro; IPR036375; Hemopexin-like_dom_sf.
DR InterPro; IPR018487; Hemopexin-like_repeat.
DR InterPro; IPR018486; Hemopexin_CS.
DR Pfam; PF00045; Hemopexin; 5.
DR PIRSF; PIRSF002551; Hemopexin_chordata; 1.
DR SMART; SM00120; HX; 5.
DR SUPFAM; SSF50923; SSF50923; 2.
DR PROSITE; PS00024; HEMOPEXIN; 2.
DR PROSITE; PS51642; HEMOPEXIN_2; 8.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Heme;
KW Host-virus interaction; Iron; Metal-binding; Reference proteome; Repeat;
KW Secreted; Signal; Transport.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:3855550,
FT ECO:0000269|PubMed:6510521"
FT CHAIN 24..462
FT /note="Hemopexin"
FT /evidence="ECO:0000269|PubMed:3855550"
FT /id="PRO_0000021406"
FT REPEAT 53..93
FT /note="Hemopexin 1"
FT REPEAT 94..139
FT /note="Hemopexin 2"
FT REPEAT 140..184
FT /note="Hemopexin 3"
FT REPEAT 185..231
FT /note="Hemopexin 4"
FT REPEAT 259..304
FT /note="Hemopexin 5"
FT REPEAT 305..352
FT /note="Hemopexin 6"
FT REPEAT 357..396
FT /note="Hemopexin 7"
FT REPEAT 400..450
FT /note="Hemopexin 8"
FT REGION 29..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 30..40
FT /note="O-glycosylated at one site"
FT BINDING 79
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 150
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 236
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 293
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT CARBOHYD 24
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:19838169,
FT ECO:0000269|PubMed:6371807, ECO:0000269|PubMed:6510521"
FT CARBOHYD 29
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:23234360"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:6371807"
FT CARBOHYD 187
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:14760718,
FT ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:16740002, ECO:0000269|PubMed:19139490,
FT ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169,
FT ECO:0000269|PubMed:6371807"
FT CARBOHYD 240
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:14760718,
FT ECO:0000269|PubMed:6371807, ECO:0000269|PubMed:6510521"
FT CARBOHYD 246
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:14760718,
FT ECO:0000269|PubMed:6371807, ECO:0000269|PubMed:6510521"
FT CARBOHYD 453
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:15084671,
FT ECO:0000269|PubMed:16740002, ECO:0000269|PubMed:19139490,
FT ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169,
FT ECO:0000269|PubMed:6371807"
FT DISULFID 50..231
FT /evidence="ECO:0000269|PubMed:3855550"
FT DISULFID 149..154
FT /evidence="ECO:0000269|PubMed:3855550"
FT DISULFID 188..200
FT /evidence="ECO:0000269|PubMed:3855550"
FT DISULFID 257..460
FT /evidence="ECO:0000269|PubMed:3855550"
FT DISULFID 366..408
FT /evidence="ECO:0000269|PubMed:3855550"
FT DISULFID 418..435
FT /evidence="ECO:0000269|PubMed:3855550"
FT VARIANT 52
FT /note="D -> N (in dbSNP:rs10839564)"
FT /id="VAR_047137"
FT VARIANT 83
FT /note="R -> W (in dbSNP:rs12117)"
FT /id="VAR_033990"
FT CONFLICT 411
FT /note="K -> R (in Ref. 2; BAG36404)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 462 AA; 51676 MW; 054B44D0603763B8 CRC64;
MARVLGAPVA LGLWSLCWSL AIATPLPPTS AHGNVAEGET KPDPDVTERC SDGWSFDATT
LDDNGTMLFF KGEFVWKSHK WDRELISERW KNFPSPVDAA FRQGHNSVFL IKGDKVWVYP
PEKKEKGYPK LLQDEFPGIP SPLDAAVECH RGECQAEGVL FFQGDREWFW DLATGTMKER
SWPAVGNCSS ALRWLGRYYC FQGNQFLRFD PVRGEVPPRY PRDVRDYFMP CPGRGHGHRN
GTGHGNSTHH GPEYMRCSPH LVLSALTSDN HGATYAFSGT HYWRLDTSRD GWHSWPIAHQ
WPQGPSAVDA AFSWEEKLYL VQGTQVYVFL TKGGYTLVSG YPKRLEKEVG TPHGIILDSV
DAAFICPGSS RLHIMAGRRL WWLDLKSGAQ ATWTELPWPH EKVDGALCME KSLGPNSCSA
NGPGLYLIHG PNLYCYSDVE KLNAAKALPQ PQNVTSLLGC TH
