Stromal cell-derived factor 2-like protein 1 (SDF2L1)

The protein contains 221 amino acids for an estimated molecular weight of 23598 Da.

 

No function (updated: Sept. 12, 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: 51

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The reference OMIM entry for this protein is 607551

Stromal cell-derived factor 2-like 1; sdf2l1
Sdf2-like 1

CLONING

While investigating radiation-induced gene expression in mouse hepatocellular carcinoma cells, Fukuda et al. (2001) isolated a clone showing similarity to Sdf2 (602934), and they obtained the full-length mouse cDNA. Using this cDNA as probe, they cloned SDF2L1 from a human testis cDNA library. The deduced human and mouse proteins contain 221 amino acids and share 88% sequence identity. SDF2L1 has an N-terminal hydrophobic signal sequence and an endoplasmic reticulum (ER) retention-like motif (HDEL) at the C terminus. SDF2 and SDF2L1 show significant similarity to the central hydrophilic regions of POMT1 (607423), POMT2 (607439), the O-mannosyltransferase family of S. cerevisiae and C. albicans, and the rt protein of Drosophila. Northern blot analysis detected ubiquitous expression of Sdf2l1 in mouse tissues, with strong expression in testis, ovary, and uterus, and weak expression in heart and skeletal muscle. Northern blot analysis of human tissues revealed strong expression in testis, moderate expression in pancreas, spleen, prostate, small intestine, and colon, and low expression in brain and skeletal muscle.

GENE FUNCTION

Fukuda et al. (2001) noted that several ER resident proteins are stress proteins that increase expression in an 'unfolded protein response' that is activated by disruption of protein synthesis or calcium homeostasis. They found that Sdf2l1 was upregulated in a mouse hepatocellular carcinoma cell line following treatment with tunicamycin, an N-linked glycosylation inhibitor, or with A23187, a calcium ionophore. Heat stress weakly increased Sdf2l1 expression, and cycloheximide, a protein synthesis inhibitor, had no effect.

GENE STRUCTURE

Fukuda et al. (2001) determined that the SDF2L1 gene contains 3 exons and spans about 2 kb.

MAPPING

By genomic sequence analysis, Fukuda et al. (2001) mapped the SDF2L1 gene to chromosome 22q11.2. ... More on the omim web site

Subscribe to this protein entry history

June 30, 2020: Protein entry updated
Automatic update: OMIM entry 607551 was added.

Feb. 23, 2019: Protein entry updated
Automatic update: comparative model was added.

Feb. 23, 2019: Protein entry updated
Automatic update: model status changed

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