Tetranectin (CLEC3B)

The protein contains 202 amino acids for an estimated molecular weight of 22537 Da.

 

Tetranectin binds to plasminogen and to isolated kringle 4. May be involved in the packaging of molecules destined for exocytosis. (updated: Oct. 10, 2018)

Protein identification was indicated in the following studies:

  1. 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: 68%
Model score: 0
No model available.

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VariantDescription
empty
empty
dbSNP:rs13963

No binding partner found

The reference OMIM entry for this protein is 187520

Tetranectin; tna

DESCRIPTION

Tetranectin, a tetrameric protein isolated from human plasma, has 4 identical and noncovalently bound polypeptide chains, each of 181 amino acid residues. It has a specific binding affinity for sulfated polysaccharides and the kringle 4 of plasminogen. The plasma concentration of tetranectin is reduced in patients with various malignancies (summary by Berglund and Petersen, 1992).

CLONING

Using a mixture of degenerate oligonucleotide probes, Berglund and Petersen (1992) isolated the gene for human tetranectin from a genomic library. The gene is about 12 kb and contains 2 intervening sequences. It encodes a 202-residue pretetranectin, with a signal peptide of 21 amino acid residues followed by the tetranectin sequence of 181 amino acid residues. Northern blot analysis demonstrated tetranectin mRNA in all 8 tissues tested, with the highest concentration in lung. Southern blot analysis demonstrated hybridization to 2 genes, but it was not determined whether these were allelic or nonallelic. Holtet et al. (1997) observed that tetranectin is, in fact, a homotrimer.

GENE STRUCTURE

Berglund and Petersen (1992) determined that the TNA gene spans about 12 kb and contains 3 exons.

MAPPING

Ibaraki et al. (1995) characterized mouse tetranectin and mapped the gene (Tna) to distal mouse chromosome 9 by analysis of 2 sets of multilocus crosses. By PCR analysis of a panel of somatic cell hybrids containing cytogenetically defined regions of chromosome 3, Durkin et al. (1997) mapped the TNA gene to chromosome 3p22-p21.3. They quoted work by others indicating that the TNA cDNA sequence had been placed 175 cR from the most distal chromosome 3p marker on the radiation hybrid map of the Whitehead Institute/MIT Center for Genome Research.

GENE FUNCTION

Tetranectin is a plasminogen-binding protein that is induced during the mineralization phase of osteogenesis (Wewer et al., 1994). Thus, tetranectin is a candidate gene for human disorders affecting bone and connective tissue. ... More on the omim web site

Subscribe to this protein entry history

June 30, 2020: Protein entry updated
Automatic update: OMIM entry 187520 was added.

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