PRR23A

Last updated
PRR23A
Identifiers
Aliases PRR23A , proline rich 23A
External IDs MGI: 3645937 HomoloGene: 67036 GeneCards: PRR23A
Orthologs
SpeciesHumanMouse
Entrez

729627

623186

Ensembl

ENSG00000206260

ENSMUSG00000063058

UniProt

A6NEV1

D3YWX5

RefSeq (mRNA)

NM_001134659

NM_001134661

RefSeq (protein)

NP_001128131

NP_001128133

Location (UCSC) Chr 3: 139 – 139.01 Mb Chr 9: 98.74 – 98.74 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Proline-Rich Protein 23A is a protein that is encoded by the Proline-Rich 23A (PRR23A) gene.

Contents

Gene

Locus

The human PRR23A gene is on chromosome 3 at position 3q23 and is located on the antisense strand. [5] The gene is encoded from position 139,003,962 to 139,006,268. It consists on 1 exon and spans 2,307 base pairs. Other genes in the neighborhood include: FOXL2NB, FOXL2, PRR23B, and PRR23C. The FOXL2NB gene has tissue enriched expression in ovaries, and PRR23A has demonstrated expression in the ovary as well. [6] [7] Aliases for PRR23A include: Proline-Rich 23A, Proline-Rich Protein 23A, and UPF0572 Protein ENSP00000372650. [8] Two of those genes, PRR23B and PRR23C, are paralogs to PRR23A. [9]

Gene expression

PRR23A is primarily expressed at low levels in the brain and testis. [7] [10] There were also very low levels of PRR23A expression detected in ovary and bone marrow tissue. [7] Genes typically show high expression in the testis during RNA sequencing since it is a highly transcriptionally active tissue due to its function of sperm production. [11] However, some researchers have noted that this testis tissue expression of PRR23A may be legitimate since PRR23 family genes are thought to play a role in male reproduction. [9] [12] Furthermore, brain and testis tissue share biochemical characteristics and express a large number of common genes. [13] This may also explain why PRR23A expression has been found at similar levels within the brain and testis.

PRR23A Gene Expression Includes the Tissues that PRR23A RNA Transcript has Been Identified in Through RNA Sequencing Data [7]
TissueCerebellumChoroid PlexusWhite MatterCerebral CortexMedulla OblongataPonsThalamusAmygdalaHippocampal FormationMidbrainBasal GangliaHypothalamusSpinal CordTestisOvaryBone Marrow
RNA Abundance (nTPM)2.41.71.71.61.61.61.51.41.31.31.21.21.21.50.10.1

mRNA transcript

Since PRR23A consists of 1 exon, there are no alternative splicing products. [5] This also means that the 1 known isoform in humans has an mRNA sequence of 2,307 nucleotides which matches the length of the PRR23A gene. [14] mRNA typically contain a 5' UTR with a median length of 170 nucleotides in humans, but the human PRR23A mRNA sequence does not contain a 5' UTR. [14] [15] Instead, the FASTA sequence for human PRR23A begins with the start codon ATG. [14] Although, the 5' UTR is not translated, it plays a major regulatory role for the translation of coding sequence nucleotides to their amino acids that go on to form a protein structure. [16] Therefore, it is unlikely that human PRR23A does not have this region, and that its upstream 5' UTR sequence could be obtained through further sequencing research.

Protein

Human PRR23A consists of 266 amino acids, has a predicted molecular weight of 28.2 kDal, and a predicted basal isoelectric point of 4.57. [17] PRR23A, as its name implies, is enriched with the amino acid proline. Therefore, PRR23A belongs to the category of proteins called proline-rich proteins. PRR23A contains less asparagine, threonine, and lysine compared to other human proteins. [18] [17] This protein composition for PRR23A is generally conserved across species. [18] [19]

Human PRR23A Protein CompositionIncludes Percent Composition of Each Amino Acid for Human PRR23A and How that Percent Composition Compares to Other Human Proteins [18] [17]
Amino AcidPro

(P)

Ala

(A)

Leu

(L)

Ser

(S)

Glu

(E)

Gly

(G)

Val

(V)

Arg

(R)

Asp

(D)

Phe

(F)

Gln

(Q)

Ile

(I)

Cys

(C)

His

(H)

Thr

(T)

Lys

(K)

Met

(M)

Try

(Y)

Trp

(W)

Asn

(N)

Composition of Human PRR23A16.2%10.5%10.5%9.8%9.0%7.5%7.1%6.4%5.3%3.4%3.0%2.3%1.51.51.51.11.1%1.10.80%0.4
Composition of PRR23A Compared to Other Human Proteinsvery richaverageaverageaverageaverageaverageaverageaverageaverageaverageaverageaverageaverageaveragevery poorpooraverageaverageaveragevery poor

Secondary and tertiary structure

Human PRR23A is mainly a disordered protein with small stretches of beta strands and alpha helices forming. [17] [20] [21] [22] [23] [24] There are 2 known disordered regions at the beginning and the end of the protein. [17] There are 6 regions from the beginning-middle of the protein sequence that are predicted to form beta strands, and when folded into the tertiary structure are in the middle of the predicted protein structure. There is 1 possible transmembrane domain that is located in 1 of these beta strands. [18] [17] [20] [21] Some proteins can create transmembrane beta barrels when a beta sheet curls on itself to make a tube that goes through a membrane, so the PRR23A could exhibit this phenomenon [25] . There are 2 regions towards the end of the protein sequence that are predicted to form alpha helices, and when folded into a tertiary structure are in the middle of the predicted protein structure.

iCN3D Human PRR23A Protein Structure With Proline DistributionThe proline amino acids are highlighted in yellow. Predicted beta strands are shown in a green ribbon structure, and predicted alpha helices are shown in a red ribbon structure. The start of the protein is represented by pale green spheres, and the end of the protein is represented by pale red spheres PRR23A Protein Structure Proline Distribution.png
iCN3D Human PRR23A Protein Structure With Proline DistributionThe proline amino acids are highlighted in yellow. Predicted beta strands are shown in a green ribbon structure, and predicted alpha helices are shown in a red ribbon structure. The start of the protein is represented by pale green spheres, and the end of the protein is represented by pale red spheres
iCN3D Human PRR23A Protein StructureThe 6 predicted beta strands are shown in a green ribbon structure, and the 2 predicted alpha helices are shown in a red ribbon structure. The region of PRR23A that is predicted to be a transmembrane domain is highlighted in yellow PRR23A Protein Structure.png
iCN3D Human PRR23A Protein StructureThe 6 predicted beta strands are shown in a green ribbon structure, and the 2 predicted alpha helices are shown in a red ribbon structure. The region of PRR23A that is predicted to be a transmembrane domain is highlighted in yellow

Subcellular localization

Antibody detection in human stomach cells has shown that PRR23A localizes in the membrane and cytoplasm. [26] Further investigation of the PRR23A protein sequence has also identified a small transmembrane region towards the beginning of the protein, and signal sequences for the ER membrane, nucleus, and mitochondria. [18] [21]

Interacting proteins

PRR23A does not have very many known interactions. The most significant protein interactions for human PRR23A are DEFB106A and DEFB107A which have been determined though co-expression data and textmining. [27] Co-expression data has also shown that DEFB106A and DEFB107A interact with one another. This means that PRR23A, DEFB106A, and DEFB107A have been observed to be correlated in expression across a large number of experiments. DEFB105A, DEFB106B, IQCJ, FAM90A10P, SPAG11B, PRSS22, USP17L4, and USP17L7 are also thought to interact with PRR23A. The basis of these interactions were determined through textmining, so further experiments such as the yeast two-hybrid assay should be conducted to increase the confidence of these protein interactions.

Summary of PRR23A Protein InteractionsIncludes Info About DEFB106A, DEFB107A, DEFB105A, DEFB106B, IQCJ, FAM90A10P, SPAG11B, PRSS22, USP17L4, and USP17L7 [27] [28]
NameBasisFunction
DEFB106A

Beta-defensin 106A

Textmining and Co-expressionBelongs to the defensin family which are antimicrobial and cytotoxic peptides made by neutrophils. Associated with Diamond-Blackfan Anemia15, Mandibulofacial with Dysostosis, and Keratomalacia. Enables lipopolysaccharide binding, protein binding, heparin binding and CCR2 chemokine receptor binding
DEFB107A

Beta-defensin 107A

Textmining and Co-expressionBelongs to the defensin family which are antimicrobial and cytotoxic peptides made by neutrophils. Enables lipid binding
DEFB105A

Beta-defensin 105A

TextminingBelongs to the defensin family which are antimicrobial and cytotoxic peptides made by neutrophils. Associated with Familial Hypertrophic Cardiomyopathy 12, and Familial Hypertrophic Cardiomyopathy 6
DEFB106B

Beta-defensin  106B

TextminingBelongs to the defensin family which are antimicrobial and cytotoxic peptides made by neutrophils. Associated with Diamond-Blackfan Anemia15, Mandibulofacial with Dysostosis. Enables lipopolysaccharide binding, protein binding, heparin binding and CCR2 chemokine receptor binding
IQCJ

IQ motif containing J

TextminingNA
FAM90A10P

Putative protein FAM90A10P

TextminingBelongs to the FAM90 family
SPAG11B

Sperm associated antigen 11B

TextminingEncodes several androgen-dependent, epididymis-specific secretory proteins. Thought to be involved in sperm maturation. Associated with Small Intestine Lymphoma and Herpes Zoster Oticus
PRSS22

Serine protease 22

TextminingGene encodes a member of the trypsin family of serine-proteases. Preferentially cleaves the synthetic substrate H-D-Leu-Thr-Arg-pNA compared to tosyl-Gly-Pro-Arg-pNA. Enables serine-type endopeptidase activity and peptidase activator activity
USP17L4

Ubiquitin specific peptidase 17 like family member 4

TextminingPredicted to enable cysteine-type endopeptidase activity and thiol-dependent deubiquitinase
USP17L7

Ubiquitin specific peptidase 17 like family member 7

TextminingPredicted to enable cysteine-type endopeptidase activity and thiol-dependent deubiquitinase

Post-translational modifications

Post-translational modifications for human PRR23A include: phosphorylation, [29] [30] [31] [32] acetylation, [33] myristoylation, [32] sulfonation, [34] SUMOylation, [35] and glycosylation. [36] [37] The glycosylation site supports the identified transmembrane region and ER membrane subcellular localization of PRR23A since proteins that are glycosylated are typically membrane bound and expressed in the ER. [18] [21] [38]

Homology

Paralogs

There are 2 known paralogs of PRR23A: PRR23B and PRR23C. [9] [17] [39]

Summary of PRR23 Family Proteins Found in HumansSimilarity of Human PRR23B and PRR23C to PRR23A [17] [40] [41] [42]
ProteinAccession NumberSequence Length (Amino Acids)E-valueSequence Identity to Human PRR23A Protein (%)Sequence Similarity to Human PRR23A Protein (%)
PRR23A NP_001128131 2660100100
PRR23B NP_001013672 2655e-14689.891.4
PRR23C NP_001128129 2621e-11684.686.8

Orthologs

PRR23A orthologs are only found in placental mammals. [17] [39] No PRR23A orthologs have been identified in marsupials, monotremes, birds, reptiles, amphibians, fish, or invertebrates.

PRR23A OrthologsContains Some Select PRR23A Orthologs from Each Major Mammalian Group Where PRR23A is Present [5] [40] [39] [43]
Genus and SpeciesCommon NameTaxonomic GroupMedian Date of Divergence (Millions of Years Ago)Accession NumberSequence Length (Amino Acids)Sequence Identity to Human Protein (%)Sequence Similarity to Human Protein (%)
Homo sapiens Human Primates 0 NP_001128131 266100100
Macaca mulatta Rhesus Monkey Primates 28.8 XP_001113833 28283.385.5
Mus musculus Mouse Rodentia 87 NP_001128132 25841.353.1
Ochotona princeps American Pika Lagomorpha 87 XP_058513009 27639.750.8
Pteropus alecto Black Flying Fox Chiroptera 94 XP_006907257 2736369.2
Sturnira hondurensis Honduran Yellow-Shouldered Bat Chiroptera 94 XP_036917059 27056.964.1
Leptonychotes weddellii Weddell Seal Carnivora 94 XP_006734260 26053.161.7
Canis lupus familiaris Dog Carnivora 94 XP_038288414 2435359.8
Neophocaena asiaeorientalis asiaeorientalis Yangtze Finless Porpoise Cetacea 94 XP_024606498 2615361.9
Hippopotamus amphibius kiboko East African Hippopotamus Hippopotamidae 94 XP_057593770 26351.960.5
Equus caballus Horse Perissodactyla 94 XP_023477063 27959.668.1
Camelus ferus Wild Bactrian Camel Tylopoda 94 XP_032343448 25856.463.5
Phacochoerus africanus Common Warthog Suiformes 94 XP_047608137 26247.357.4
Moschus berezovskii Dwarf Musk Deer Ruminantia 94 XP_055276284 29145.254.2
Talpa occidentalis Spanish Mole Talpidae 94 XP_037382562 26454.164.4
Sorex araneus Common Shrew Soricidae 94 XP_054980762 21741.646.8
Erinaceus europaeus European Hedgehog Erinaceidae 94 XP_060039908 27427.840.6
Elephas maximus indicus Indian Elephant Proboscidea 99 XP_049726169 23553.458.6
Loxodonta africana African Savanna Elephant Proboscidea 99 XP_003420004 23553.458.6
Orycteropus afer afer Aardvark Tubulidentata 99 XP_007945733 24352.958

Evolution

PRR23A first appeared within placental mammals which evolved 78-129 million years ago. [39] [44] Then, placental mammals began to diversify into two the major lineages of Atlantogenata and Boreoeutheria which emerged 90-100 million years ago. [45] PRR23A orthologs can be found within both of these major lineages, and several subgroups that evolved as well. [39] [46] Despite PRR23A's recent emergence in the long run of evolutionary history, it is evolving at a very rapid rate. [47] [48] [19]

PRR23A Evolution from Placental MammalsGreen indicates presence and red indicates absence of PRR23A proteins within a group PRR23A Evolution from Placental Mammals.png
PRR23A Evolution from Placental MammalsGreen indicates presence and red indicates absence of PRR23A proteins within a group
PRR23A Presence in Organisms Evolved from Placental MammalsThe different colors indicate significant differences between the groups PRR23A Presence in Organisms Evolved from Placental Mammals.png
PRR23A Presence in Organisms Evolved from Placental MammalsThe different colors indicate significant differences between the groups
Rate of Evolution for PRR23A GeneShows the approximate date of divergence from humans for the species listed in the ortholog table above versus the corrected percent divergence (m) of the orthologous protein and the human protein for PRR23A, Cytochrome C, and Fibrinogen Alpha Chain. The slope of the lines corresponds to how fast the genes for the proteins included are evolving. Since PRR23A has a stepper slope (y=0.7456x) than Cytochrome C (y=0.3484x) and Fibrinogen Alpha (y=0.0638x), PRR23A is evolving rapidly Evolutionary Rate of PRR23A.png
Rate of Evolution for PRR23A GeneShows the approximate date of divergence from humans for the species listed in the ortholog table above versus the corrected percent divergence (m) of the orthologous protein and the human protein for PRR23A, Cytochrome C, and Fibrinogen Alpha Chain. The slope of the lines corresponds to how fast the genes for the proteins included are evolving. Since PRR23A has a stepper slope (y=0.7456x) than Cytochrome C (y=0.3484x) and Fibrinogen Alpha (y=0.0638x), PRR23A is evolving rapidly

Function

PRR23A has demonstrated gene expression within the testis through increased mRNA levels, and so have the other PRR23 family genes. [9] This expression indicates that PRR23A may have a role within the male reproductive system. The larger family of proline-rich proteins have a large range of functions including: energy provisions, antistress responses, calcium binding in saliva, structure support, and many others. [49] [50] One subgroup called small proline-rich proteins (SPRRs) are antimicrobial proteins that direct bacterial membrane disruption. [51]

Clinical significance and pathology

Epigenetic modifications of PRR23A have been shown to impact maternal early-pregnancy serum ferritin concentrations. [12] 2 CpG sites within human PRR23A have been identified: cg02806645 and cg06322988. When these locations are methylated, a decrease in serum ferritin concentrations during early-pregnancy was observed. Low levels of ferritin are a sign of iron deficiency which is especially important to monitor during pregnancy. [52] Therefore, the decreased expression of PRR23A though methylation silencing is associated with iron deficiency.

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  32. 1 2 "Motif Scan". myhits.sib.swiss. Retrieved 2023-12-15.
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