C11orf54

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Identifiers
Aliases
External IDs	GeneCards: [1]
Orthologs
Species	Human	Mouse
Entrez	n/a	n/a
Ensembl	n/a	n/a
UniProt	n/a	n/a
RefSeq (mRNA)	n/a	n/a
RefSeq (protein)	n/a	n/a
Location (UCSC)	n/a	n/a
PubMed search	n/a	n/a
Wikidata
View/Edit Human

Chromosome 11 open reading frame 54 (C11orf54) is a protein that in humans is encoded by the C11orf54 gene. The "Homo sapiens" gene, C11orf54 is also known as PTD012 and PTOD12. C11orf54 exhibits hydrolase activity on p-nitrophenyl acetate and acts on ester bonds, though the overall function is still not fully understood by the scientific community. The protein is highly conserved with the most distant homolog found is in bacteria.

Gene

C11orf54 is located on chromosome 11 at 11q21. Common aliases of the gene are PTD012 and PT0D12. The gene consists 13 exons and spans 23730 bp. C11orf54 is flanked by TAF1D and MED17.

Gene neighborhood for C11orf54

mRNA

The protein ester hydrolase c11orf54 exists as a monomer and is composed of 315 amino acids. There are 6 isoforms for C11orf54. See table 1.

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Variant	Isoform	Length (bp)	Accession Number
1	ester hydrolase C11orf54 isoform a	2726	NM_001286067.1
2	ester hydrolase C11orf54 isoform a	2589	NM_001286068.1
3	ester hydrolase C11orf54 isoform a	2594	NM_001286069.1
4	ester hydrolase C11orf54 isoform b	2444	NM_014039.3
5	ester hydrolase C11orf54 isoform c	2442	NM_001286070.1
6	ester hydrolase C11orf54 isoform d	2417	NM_001286071.1

The amino acid sequence contains the Domain of Uknown Function 1907. Found in this transcript is the HxHxxxxxxxxxH motif which coordinates the zinc ion involved in the hydrolase activity. An LR nest motif is found at lys262 and Arg263. The LR nest motif forms hydrogen bonds between the NH groups and anions; an acetate anion is coordinated with the LR nest.

Protein

Primary sequence

Table 2 shows the different characteristics of the protein sequence throughout humans and other orthologs.}}</ref>

Organism	Molecular Weight (kiloDalton)	Isoelectric point	High Bias Amino Acids	Repeats
Human	35.1	5.9	F	AEFS
Mouse	35.0	5.9	H	None
13 Lined Ground Squirrel	35.1	6.0	F,H	PAEF
Giant Panda	35.2	6.5	F	PAEF

Secondary structure

The protein of C11orf54 exists as a monomer in solution. The protein assumes a globular shape of 20 beta strands and 4 alpha helices, containing 9 antiparallel beta strands forming a beta screw region. The β-screw region of C11orf54 has structural similarity to the cyclic adenosine 3′,5′-monophosphate (cAMP) binding domain of the regulatory subunit of protein kinase A. A zinc ion is bound to the HxHxxxxxxxxxH motif found in the sequence.

Subcellular localization

C11orf54 is predicted to be localized 60.9% in the cytoplasm, 21.7% in the nucleus, 13.0% mitochondrial and 4.3% in the Golgi Apparatus.

Expression & post translational modifications

File:Post-Transcriptional Modifications to C11orf54 protein.png

Image 1: Post-Transcriptional Modifications to C11orf54 protein

See image one. The protein is highly expressed in the kidneys and moderately expressed in the adrenal gland, colon, liver, testis and thyroid gland.

Homology

Paralogs

There are no paralogs for C11orf54.

Orthologs

The protein Ester Hydrolase C11orf54 has many orthologs (see table.) It is highly conserved (60-100% identity) in mammals, reptiles, birds, and fish. The protein is moderately conserved (30-59.99% identity) in invertebrates, amphibia, Cnidaria, Mollusca, fungi and bacteria. It is not conserved in archaea. The most distant orthologs are bacteria. Figure 2 shows the unrooted phylogenetic tree of a few of C11orf54’s orthologs.

Species	Common Name	Class	Accession Number	Percent Identity	Divergence (MYA median)
Microtus ochrogaster	Prairie Vole	mammalia	XP_005346877.1	87.0	88
Chelonia mydas	Green Sea Turtle	reptilia	XP_007069537.1	72.8	320
Xenopus tropicalis	Burmese Python	reptilia	XP_007434894.1	70.9	320
Python bivittatus	Red Junglefowl	Ave	NP_001264206.1	73.4	320
Gallus gallus	Common Cuckoo	Ave	XP_009564677.1	72.5	320
Cuculus canorus	Southern Platyfish	Actinopterygii	XP_005800827.1	65.2	432
Xiphophorus maculatus	Zebrafish	Actinopterygii	NP_997781.1	62.4	432
Danio rerio	Acorn Worm	Enteropneusta	XP_002738479.1	55.6	627
Saccoglossus kowalevskii	Atlantic Horseshoe Crab	Merostomata	XP_013785734.1	56.6	758
Limulus polyphemus	Western Clawed Frog	Amphibia	XP_012812415.1	55.1	353
Crassostrea gigas	Pacific Oyster	Bivalvia	XP_011412414.1	50.0	758
Tribolium castaneum	Red Flour Beetle	Insecta	XP_968861.1	49.0	758
Drosophila bipectinata	Fruitfly	Insecta	XP_017103988.1	46.0	758
Megachile rotundata	Alfalfa leafcutter bee	Insecta	XP_003702672.1	44.8	758
Zymoseptoria brevis	fungi	Dothideomycetes	KJX93246.1	36.5	1150
Cladophialophora carrionii	fungi	Dothideomycetes	OCT48531.1	35.8	1150
Alternaria alternata	fungi	Dothideomycetes	XP_018384285.1	36.2	1150
Candidatus Pelagibacter ubique	bacteria	Bacteria	WP_075504325.1	34.5	4090
Pelagibacteraceae bacterium	bacteria	Bacteria	OCW82973.1	34.1	4090

Function

C11orf54's coordination with a zinc ion through three histidines and an acetate anion is likely to point to a function of the protein being an enzymatic reaction as an ester hydrolase. The protein has a high turnover number when reacted with p-nitrophenyl acetate (0.042 sec−1) as compared to a 1 sec−1 turnover rate found in another enzyme (bovine carbonic anhydrase II) that reacts with p-nitrophenyl acetate.

Interacting Proteins

Protein Name	Abbreviation
Ubiquitin C	UBC
Collagen, type IV, alpha 3	COL4A3
Thyroid Hormone Receptor Interactor 13	TRIP13
DEAD (Asp-Glu-Ala-Asp) box polypeptide 60-like	DDX60L
Glutamine-fructose-6-phosphate transaminase 2	GFPT2
Superkiller viralicidic activity 2-like (S. cerevisiae)	SKIV2L
OTU domain, ubiquitin aldehyde binding 1	OTUB1

Further reading

• Maruyama K, Sugano S (January 1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (October 1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
• Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Böcher M, Blöcker H, Bauersachs S, Blum H, Lauber J, Düsterhöft A, Beyer A, Köhrer K, Strack N, Mewes HW, Ottenwälder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A (March 2001). "Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs". Genome Research. 11 (3): 422–35. doi:10.1101/gr.GR1547R. PMC 311072. PMID 11230166.
• Simpson JC, Wellenreuther R, Poustka A, Pepperkok R, Wiemann S (September 2000). "Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing". EMBO Reports. 1 (3): 287–92. doi:10.1093/embo-reports/kvd058. PMC 1083732. PMID 11256614.
• Wan D, Gong Y, Qin W, Zhang P, Li J, Wei L, Zhou X, Li H, Qiu X, Zhong F, He L, Yu J, Yao G, Jiang H, Qian L, Yu Y, Shu H, Chen X, Xu H, Guo M, Pan Z, Chen Y, Ge C, Yang S, Gu J (November 2004). "Large-scale cDNA transfection screening for genes related to cancer development and progression". Proceedings of the National Academy of Sciences of the United States of America. 101 (44): 15724–9. doi:10.1073/pnas.0404089101. PMC 524842. PMID 15498874.
• Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (October 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.

External links

• Human C11orf54 genome location and C11orf54 gene details page in the UCSC Genome Browser.