Hemopexin (HPX)

The protein contains 462 amino acids for an estimated molecular weight of 51676 Da.

 

Binds heme and transports it to the liver for breakdown and iron recovery, after which the free hemopexin returns to the circulation. (updated: Oct. 10, 2018)

Protein identification was indicated in the following studies:

  1. Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
  2. D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.

Methods

The following articles were analysed to gather the proteome content of erythrocytes.

The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.

PublicationIdentification 1Uniprot mapping 2Not mapped /
Obsolete
TrEMBLSwiss-Prot
Goodman (2013)2289 (gene list)227853205992269
Lange (2014)123412347281224
Hegedus (2015)2638262202352387
Wilson (2016)165815281702911068
d'Alessandro (2017)18261817201815
Bryk (2017)20902060101081942
Chu (2018)18531804553621387

1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry

The compilation of older studies can be retrieved from the Red Blood Cell Collection database.

The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.

No sequence conservation computed yet.

Interpro domains
Total structural coverage: 0%
Model score: 0
No model available.

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VariantDescription
dbSNP:rs10839564
dbSNP:rs12117

No binding partner found

The reference OMIM entry for this protein is 142290

Hemopexin; hpx

DESCRIPTION

Hemopexin is a plasma beta-glycoprotein that specifically binds one heme with high affinity and transports it to hepatocytes for salvage of iron (summary by Takahashi et al., 1985).

CLONING

Takahashi et al. (1985) determined that human hemopexin consists of a single polypeptide chain of 439 amino acids and has a molecular mass of approximately 63 kD. Altruda et al. (1985) also determined the protein sequence of human hemopexin. Both groups noted that hemopexin is low in patients with hemolysis. Naylor et al. (1987) found that hemopexin mRNA was present at a low level in fetal liver, increased dramatically in adult liver, and was not detectable in other tissues.

GENE STRUCTURE

Altruda et al. (1988) demonstrated that the HPX gene spans approximately 12 kb and is interrupted by 9 exons. A direct correspondence between exons and the 10 repeating units in the protein was shown. The introns were not randomly placed; they fell in the middle of the region of amino acid sequence homology in strikingly similar locations in 6 of the 10 units and in a symmetric position in each half of the coding sequence. From these findings, Altruda et al. (1988) concluded that the gene evolved through intron-mediated duplications of a primordial sequence to a 5-exon cluster. A more recent gene duplication led to the present-day gene organization.

MAPPING

Cai and Law (1986) prepared a cDNA clone for hemopexin and, by Southern blot analysis of human/hamster hybrids containing different combinations of human chromosomes, assigned the hemopexin gene to human chromosome 11. Naylor et al. (1987) used a hemopexin cDNA clone to map the HPX gene to 11pter-p11 by somatic cell hybrid analysis. By means of in situ hybridization, Law et al. (1988) assigned the hemopexin gene to 11p15.5-p15.4, the same location as that of the beta-globin gene complex.

MOLECULAR GENETICS

Hemopexin has been found in the serum of all mammals studied and it is polymorphic in rabbits. Stewart and Lovrien (1971) found no electrophoretic polymorphism in humans. Polymorphism of hemopexin is known in the pig (Lush, 1966). By isoelectric focusing, Kamboh and Ferrell (1987) demonstrated polymorphism of HPX in US blacks but not in US whites. Data on gene frequencies of allelic variants were tabulated by Roychoudhury and Nei (1988). ... More on the omim web site

Subscribe to this protein entry history

June 30, 2020: Protein entry updated
Automatic update: OMIM entry 142290 was added.

Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).