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 24-JAN-2024, entry version 213. 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}; 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; 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; 73. DR DIP; DIP-38339N; -. DR IntAct; P02790; 23. 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 GlyCosmos; P02790; 10 sites, 109 glycans. DR GlyGen; P02790; 12 sites, 105 N-linked glycans (5 sites), 9 O-linked glycans (6 sites). DR iPTMnet; P02790; -. DR PhosphoSitePlus; P02790; -. DR BioMuta; HPX; -. DR DMDM; 1708182; -. DR DOSAC-COBS-2DPAGE; P02790; -. DR REPRODUCTION-2DPAGE; IPI00022488; -. DR CPTAC; non-CPTAC-1131; -. DR EPD; P02790; -. DR jPOST; P02790; -. DR MassIVE; P02790; -. DR PaxDb; 9606-ENSP00000265983; -. DR PeptideAtlas; P02790; -. DR PRIDE; P02790; -. DR ProteomicsDB; 51598; -. DR Pumba; P02790; -. DR Antibodypedia; 23841; 591 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 AGR; HGNC:5171; -. 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; 5312290at2759; -. 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 1149 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 106 other cell types or tissues. DR ExpressionAtlas; P02790; baseline and differential. 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: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:0006879; P:intracellular iron ion homeostasis; TAS:ProtInc. 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 type II interferon-mediated signaling pathway; IEA:Ensembl. DR GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IEA:Ensembl. DR GO; GO:0060333; P:type II interferon-mediated signaling pathway; IEA:Ensembl. DR CDD; cd00094; HX; 2. DR Gene3D; 2.110.10.10; Hemopexin-like domain; 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 PANTHER; PTHR22917:SF9; HEMOPEXIN; 1. DR PANTHER; PTHR22917; HEMOPEXIN DOMAIN-CONTAINING PROTEIN; 1. DR Pfam; PF00045; Hemopexin; 5. DR PIRSF; PIRSF002551; Hemopexin_chordata; 1. DR SMART; SM00120; HX; 5. DR SUPFAM; SSF50923; Hemopexin-like domain; 2. DR PROSITE; PS00024; HEMOPEXIN; 2. DR PROSITE; PS51642; HEMOPEXIN_2; 8. DR SWISS-2DPAGE; P02790; -. DR Genevisible; P02790; HS. 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 //