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P02790 (HEMO_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 146. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Hemopexin
Alternative name(s):
Beta-1B-glycoprotein
Gene names
Name:HPX
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length462 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binds heme and transports it to the liver for breakdown and iron recovery, after which the free hemopexin returns to the circulation.

Subunit structure

Interacts with HEV ORF3 protein. Interacts with FLVCR1. Ref.12 Ref.16

Subcellular location

Secreted.

Tissue specificity

Expressed by the liver and secreted in plasma.

Post-translational modification

N- and O-glycosylated. O-glycosylated with core 1 or possibly core 8 glycans. O-glycosylation in the 30-40 region is minor compared to glycosylation at Thr-24 and Thr-29. Ref.7 Ref.14 Ref.17

Miscellaneous

The isolated N-terminal domain binds one heme. The full-length protein also binds one heme, but at a different site. The physiological significance of this is not clear By similarity.

Sequence similarities

Belongs to the hemopexin family.

Contains 8 hemopexin repeats.

Sequence caution

The sequence CAA26382.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processHost-virus interaction
Transport
   Cellular componentSecreted
   Coding sequence diversityPolymorphism
   DomainRepeat
Signal
   LigandHeme
Iron
Metal-binding
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcellular iron ion homeostasis

Traceable author statement Ref.5. Source: ProtInc

heme metabolic process

Inferred from electronic annotation. Source: Ensembl

heme transport

Traceable author statement Ref.5. Source: ProtInc

hemoglobin metabolic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of humoral immune response mediated by circulating immunoglobulin

Inferred from electronic annotation. Source: Ensembl

positive regulation of immunoglobulin production

Inferred from electronic annotation. Source: Ensembl

positive regulation of interferon-gamma-mediated signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of tyrosine phosphorylation of Stat1 protein

Inferred from electronic annotation. Source: Ensembl

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentblood microparticle

Inferred from direct assay PubMed 22516433. Source: UniProt

endocytic vesicle lumen

Traceable author statement. Source: Reactome

extracellular region

Non-traceable author statement PubMed 14718574. Source: UniProtKB

extracellular space

Inferred from direct assay PubMed 19433579. Source: MGI

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

   Molecular_functionheme transporter activity

Traceable author statement Ref.5. Source: ProtInc

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Ref.6
Chain24 – 462439Hemopexin Ref.5
PRO_0000021406

Regions

Repeat53 – 9341Hemopexin 1
Repeat94 – 13946Hemopexin 2
Repeat140 – 18445Hemopexin 3
Repeat185 – 23147Hemopexin 4
Repeat259 – 30446Hemopexin 5
Repeat305 – 35248Hemopexin 6
Repeat357 – 39640Hemopexin 7
Repeat400 – 45051Hemopexin 8
Region30 – 4011O-glycosylated at one site

Sites

Metal binding791Iron (heme 1 axial ligand) By similarity
Metal binding1501Iron (heme 1 axial ligand) By similarity
Metal binding2361Iron (heme 2 axial ligand) By similarity
Metal binding2931Iron (heme 2 axial ligand) By similarity

Amino acid modifications

Glycosylation241O-linked (GalNAc...) Ref.6 Ref.7 Ref.15
Glycosylation291O-linked (GalNAc...) Ref.17
Glycosylation641N-linked (GlcNAc...) (complex) Ref.7 Ref.10 Ref.15
Glycosylation1871N-linked (GlcNAc...) (complex) Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.13 Ref.14 Ref.15
Glycosylation2401N-linked (GlcNAc...) Ref.6 Ref.7 Ref.9
Glycosylation2461N-linked (GlcNAc...) Ref.6 Ref.7 Ref.9
Glycosylation4531N-linked (GlcNAc...) (complex) Ref.7 Ref.8 Ref.11 Ref.13 Ref.14 Ref.15
Disulfide bond50 ↔ 231 Ref.5
Disulfide bond149 ↔ 154 Ref.5
Disulfide bond188 ↔ 200 Ref.5
Disulfide bond257 ↔ 460 Ref.5
Disulfide bond366 ↔ 408 Ref.5
Disulfide bond418 ↔ 435 Ref.5

Natural variations

Natural variant521D → N.
Corresponds to variant rs10839564 [ dbSNP | Ensembl ].
VAR_047137
Natural variant831R → W.
Corresponds to variant rs12117 [ dbSNP | Ensembl ].
VAR_033990

Experimental info

Sequence conflict4111K → R in BAG36404. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P02790 [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: 054B44D0603763B8

FASTA46251,676
        10         20         30         40         50         60 
MARVLGAPVA LGLWSLCWSL AIATPLPPTS AHGNVAEGET KPDPDVTERC SDGWSFDATT 

        70         80         90        100        110        120 
LDDNGTMLFF KGEFVWKSHK WDRELISERW KNFPSPVDAA FRQGHNSVFL IKGDKVWVYP 

       130        140        150        160        170        180 
PEKKEKGYPK LLQDEFPGIP SPLDAAVECH RGECQAEGVL FFQGDREWFW DLATGTMKER 

       190        200        210        220        230        240 
SWPAVGNCSS ALRWLGRYYC FQGNQFLRFD PVRGEVPPRY PRDVRDYFMP CPGRGHGHRN 

       250        260        270        280        290        300 
GTGHGNSTHH GPEYMRCSPH LVLSALTSDN HGATYAFSGT HYWRLDTSRD GWHSWPIAHQ 

       310        320        330        340        350        360 
WPQGPSAVDA AFSWEEKLYL VQGTQVYVFL TKGGYTLVSG YPKRLEKEVG TPHGIILDSV 

       370        380        390        400        410        420 
DAAFICPGSS RLHIMAGRRL WWLDLKSGAQ ATWTELPWPH EKVDGALCME KSLGPNSCSA 

       430        440        450        460 
NGPGLYLIHG PNLYCYSDVE KLNAAKALPQ PQNVTSLLGC TH 

« Hide

References

« Hide 'large scale' references
[1]"Structure of the human hemopexin gene and evidence for intron-mediated evolution."
Altruda F., Poli V., Restagno G., Silengo L.
J. Mol. Evol. 27:102-108(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Mammary gland.
[3]"The hemopexin gene maps to the same location as the beta-globin gene cluster on human chromosome 11."
Law M.L., Cai G.Y., Hartz J.A., Jones C., Kao F.T.
Genomics 3:48-52(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-462.
[4]"The primary structure of human hemopexin deduced from cDNA sequence: evidence for internal, repeating homology."
Altruda F., Poli V., Restagno G., Argos P., Cortese R., Silengo L.
Nucleic Acids Res. 13:3841-3859(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 22-462.
[5]"Complete amino acid sequence of human hemopexin, the heme-binding protein of serum."
Takahashi N., Takahashi Y., Putnam F.W.
Proc. Natl. Acad. Sci. U.S.A. 82:73-77(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF ACTIVE PROTEIN.
[6]"Amino acid sequence of the N-terminal region of human hemopexin."
Frantikova V., Borvak J., Kluh I., Moravek L.
FEBS Lett. 178:213-216(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 24-255.
[7]"Structure of human hemopexin: O-glycosyl and N-glycosyl sites and unusual clustering of tryptophan residues."
Takahashi N., Takahashi Y., Putnam F.W.
Proc. Natl. Acad. Sci. U.S.A. 81:2021-2025(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE, GLYCOSYLATION AT THR-24; ASN-64; ASN-64; ASN-187; ASN-240; ASN-246 AND ASN-453.
[8]"A proteomic analysis of human bile."
Kristiansen T.Z., Bunkenborg J., Gronborg M., Molina H., Thuluvath P.J., Argani P., Goggins M.G., Maitra A., Pandey A.
Mol. Cell. Proteomics 3:715-728(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-187 AND ASN-453.
Tissue: Bile.
[9]"Screening for N-glycosylated proteins by liquid chromatography mass spectrometry."
Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.
Proteomics 4:454-465(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-187; ASN-240 AND ASN-246.
Tissue: Plasma.
[10]"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-64 AND ASN-187.
Tissue: Plasma.
[11]"Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry."
Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T., Loo J.A.
J. Proteome Res. 5:1493-1503(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-187 AND ASN-453.
Tissue: Saliva.
[12]"The ORF3 protein of hepatitis E virus interacts with hemopexin by means of its 26 amino acid N-terminal hydrophobic domain II."
Ratra R., Kar-Roy A., Lal S.K.
Biochemistry 47:1957-1969(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HEV ORF3 PROTEIN.
[13]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-187 AND ASN-453.
Tissue: Liver.
[14]"A strategy for precise and large scale identification of core fucosylated glycoproteins."
Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.
Mol. Cell. Proteomics 8:913-923(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-187 AND ASN-453.
[15]"Enrichment of glycopeptides for glycan structure and attachment site identification."
Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E., Brinkmalm G., Larson G.
Nat. Methods 6:809-811(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT THR-24; ASN-64; ASN-187 AND ASN-453, STRUCTURE OF CARBOHYDRATES.
Tissue: Cerebrospinal fluid.
[16]"Kinetics and specificity of feline leukemia virus subgroup C receptor (FLVCR) export function and its dependence on hemopexin."
Yang Z., Philips J.D., Doty R.T., Giraudi P., Ostrow J.D., Tiribelli C., Smith A., Abkowitz J.L.
J. Biol. Chem. 285:28874-28882(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FLVCR1.
[17]"LC-MS/MS characterization of O-glycosylation sites and glycan structures of human cerebrospinal fluid glycoproteins."
Halim A., Ruetschi U., Larson G., Nilsson J.
J. Proteome Res. 12:573-584(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT THR-29, IDENTIFICATION BY MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M36803 expand/collapse EMBL AC list , M36796, M36799, M36800, M36801, M36802 Genomic DNA. Translation: AAA58678.1.
AK313648 mRNA. Translation: BAG36404.1.
J03048 mRNA. Translation: AAA52704.1.
X02537 mRNA. Translation: CAA26382.1. Different initiation.
PIROQHU. I56456.
RefSeqNP_000604.1. NM_000613.2.
XP_005252940.1. XM_005252883.1.
UniGeneHs.426485.

3D structure databases

ProteinModelPortalP02790.
SMRP02790. Positions 48-462.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109500. 3 interactions.
DIPDIP-38339N.
IntActP02790. 3 interactions.
STRING9606.ENSP00000265983.

Protein family/group databases

TCDB1.C.39.8.3. the membrane attack complex/perforin (macpf) family.

PTM databases

PhosphoSiteP02790.

Polymorphism databases

DMDM1708182.

2D gel databases

DOSAC-COBS-2DPAGEP02790.
REPRODUCTION-2DPAGEIPI00022488.
SWISS-2DPAGEP02790.

Proteomic databases

PaxDbP02790.
PeptideAtlasP02790.
PRIDEP02790.

Protocols and materials databases

DNASU3263.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000265983; ENSP00000265983; ENSG00000110169.
GeneID3263.
KEGGhsa:3263.
UCSCuc001mdg.2. human.

Organism-specific databases

CTD3263.
GeneCardsGC11M006452.
HGNCHGNC:5171. HPX.
HPACAB016725.
MIM142290. gene.
neXtProtNX_P02790.
PharmGKBPA29441.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG251805.
HOGENOMHOG000112887.
HOVERGENHBG005956.
InParanoidP02790.
OMAAVECHRG.
OrthoDBEOG7Q8CN5.
PhylomeDBP02790.
TreeFamTF331201.

Enzyme and pathway databases

ReactomeREACT_160300. Binding and Uptake of Ligands by Scavenger Receptors.

Gene expression databases

BgeeP02790.
CleanExHS_HPX.
GenevestigatorP02790.

Family and domain databases

Gene3D2.110.10.10. 2 hits.
InterProIPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR016358. Hemopexin_chordata.
IPR018486. Hemopexin_CS.
[Graphical view]
PfamPF00045. Hemopexin. 5 hits.
[Graphical view]
PIRSFPIRSF002551. Hemopexin_chordata. 1 hit.
SMARTSM00120. HX. 5 hits.
[Graphical view]
SUPFAMSSF50923. SSF50923. 2 hits.
PROSITEPS00024. HEMOPEXIN. 2 hits.
PS51642. HEMOPEXIN_2. 8 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSHPX. human.
GeneWikiHemopexin.
GenomeRNAi3263.
NextBio12957.
PROP02790.
SOURCESearch...

Entry information

Entry nameHEMO_HUMAN
AccessionPrimary (citable) accession number: P02790
Secondary accession number(s): B2R957
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 146 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM