Anamorsin (CIAPIN1)

The protein contains 312 amino acids for an estimated molecular weight of 33582 Da.

 

Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery required for the maturation of extramitochondrial Fe-S proteins. Part of an electron transfer chain functioning in an early step of cytosolic Fe-S biogenesis, facilitating the de novo assembly of a [4Fe-4S] cluster on the scaffold complex NUBP1-NUBP2. Electrons are transferred to CIAPIN1 from NADPH via the FAD- and FMN-containing protein NDOR1 (PubMed:23596212). NDOR1-CIAPIN1 are also required for the assembly of the diferric tyrosyl radical cofactor of ribonucleotide reductase (RNR), probably by providing electrons for reduction during radical cofactor maturation in the catalytic small subunit (By similarity). Has anti-apoptotic effects in the cell. Involved in negative control of cell death upon cytokine withdrawal. Promotes development of hematopoietic cells (By similarity). (updated: Feb. 28, 2018)

Protein identification was indicated in the following studies:

  1. Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
  2. Lange and co-workers. (2014) Annotating N termini for the human proteome project: N termini and Nα-acetylation status differentiate stable cleaved protein species from degradation remnants in the human erythrocyte proteome. J Proteome Res. 13(4), 2028-2044.
  3. Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
  4. Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.

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: 56%
Model score: 27

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VariantDescription
dbSNP:rs11557672
dbSNP:rs11557674

The reference OMIM entry for this protein is 608943

Cytokine-induced apoptosis inhibitor 1; ciapin1
Anamorsin

DESCRIPTION

CIAPIN1 is a cytokine-induced inhibitor of apoptosis with no relation to apoptosis regulatory molecules of the BCL2 (151430) or CASP (see 147678) families. Expression of CIAPIN1 is dependent on growth factor stimulation (Shibayama et al., 2004).

CLONING

Using expression cloning with an IL3 (147740)-independent subline of an IL3-dependent mouse cell line, Shibayama et al. (2004) obtained a cDNA encoding Ciapin1, which they termed Anamorsin, meaning 'anti-death molecule' in Latin. By searching databases, Shibayama et al. (2004) identified human Anamorsin. The predicted 310-amino acid mouse protein has a calculated molecular mass of 37 kD and contains an N-terminal methyltransferase motif. Human and mouse Anamorsin share 82% amino acid identity. Northern blot analysis of human tissues revealed ubiquitous expression of Anamorsin, with particularly high levels in heart, liver, and pancreas. Immunofluorescence microscopy of mouse cells demonstrated that Anamorsin was localized in the cytoplasm exclusively.

GENE FUNCTION

Shibayama et al. (2004) found that expression of Anamorsin in mouse cells conferred resistance to apoptosis caused by IL3 deprivation. Addition of growth factors, such as EPO (133170), SCF (184745), TPO (600044), or IL3, all of which depend on RAS (190020) signaling, induced dose-dependent expression of Anamorsin in mouse cells. Based on these results and their findings in Anamorsin null mice, Shibayama et al. (2004) concluded that Anamorsin is critical in hematopoiesis and in the mediation of cytokine-induced antiapoptosis.

MAPPING

Loftus et al. (1999) identified the CIAPIN1 gene on chromosome 16.

ANIMAL MODEL

Shibayama et al. (2004) generated Anamorsin null mice, all of which died by late gestation due to a hematopoiesis defect in fetal liver. Myeloid, and particularly erythroid, colony formation was disrupted in these mice. Microarray analysis revealed reduced expression of Bclxl (600039) and Jak2 (147796) in fetal liver of Anamorsin null mice. ... More on the omim web site

Subscribe to this protein entry history

April 12, 2018: Protein entry updated
Automatic update: Entry updated from uniprot information.

Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated

Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated

Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated

March 16, 2016: Protein entry updated
Automatic update: OMIM entry 608943 was added.

Jan. 24, 2016: Protein entry updated
Automatic update: model status changed