O55103 · PRAX_MOUSE
- ProteinPeriaxin
- GenePrx
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1391 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Scaffolding protein that functions as part of a dystroglycan complex in Schwann cells, and as part of EZR and AHNAK-containing complexes in eye lens fiber cells (PubMed:11430802, PubMed:21745462, PubMed:22764250).
Required for the maintenance of the peripheral myelin sheath that is essential for normal transmission of nerve impulses and normal perception of sensory stimuli (PubMed:10839370).
Required for normal transport of MBP mRNA from the perinuclear to the paranodal regions (PubMed:15356632).
Required for normal remyelination after nerve injury (PubMed:10839370).
Required for normal elongation of Schwann cells and normal length of the internodes between the nodes of Ranvier. The demyelinated nodes of Ranvier permit saltatory transmission of nerve impulses; shorter internodes cause slower transmission of nerve impulses (PubMed:15356632, PubMed:23022068).
Required for the formation of appositions between the abaxonal surface of the myelin sheath and the Schwann cell plasma membrane; the Schwann cell cytoplasm is restricted to regions between these appositions (PubMed:15356632, PubMed:23022068).
Required for the formation of Cajal bands and of Schmidt-Lanterman incisures that correspond to short, cytoplasm-filled regions on myelinated nerves (PubMed:22764250, PubMed:23022068).
Recruits DRP2 to the Schwann cell plasma membrane (PubMed:11430802, PubMed:22764250, PubMed:23022068).
Required for normal protein composition of the eye lens fiber cell plasma membrane and normal eye lens fiber cell morphology (PubMed:21745462).
Required for the maintenance of the peripheral myelin sheath that is essential for normal transmission of nerve impulses and normal perception of sensory stimuli (PubMed:10839370).
Required for normal transport of MBP mRNA from the perinuclear to the paranodal regions (PubMed:15356632).
Required for normal remyelination after nerve injury (PubMed:10839370).
Required for normal elongation of Schwann cells and normal length of the internodes between the nodes of Ranvier. The demyelinated nodes of Ranvier permit saltatory transmission of nerve impulses; shorter internodes cause slower transmission of nerve impulses (PubMed:15356632, PubMed:23022068).
Required for the formation of appositions between the abaxonal surface of the myelin sheath and the Schwann cell plasma membrane; the Schwann cell cytoplasm is restricted to regions between these appositions (PubMed:15356632, PubMed:23022068).
Required for the formation of Cajal bands and of Schmidt-Lanterman incisures that correspond to short, cytoplasm-filled regions on myelinated nerves (PubMed:22764250, PubMed:23022068).
Recruits DRP2 to the Schwann cell plasma membrane (PubMed:11430802, PubMed:22764250, PubMed:23022068).
Required for normal protein composition of the eye lens fiber cell plasma membrane and normal eye lens fiber cell morphology (PubMed:21745462).
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | anchoring junction | |
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | nuclear speck | |
Cellular Component | nucleus | |
Cellular Component | plasma membrane | |
Biological Process | peripheral nervous system myelin formation | |
Biological Process | peripheral nervous system myelin maintenance | |
Biological Process | regulation of RNA splicing | |
Biological Process | sensory perception of pain | |
Biological Process | transmission of nerve impulse |
Names & Taxonomy
Protein names
- Recommended namePeriaxin
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionO55103
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Colocalizes with ACTB at tricellular junctions between eye lens fiber cells.
Isoform 1
Cell membrane ; Peripheral membrane protein
Isoform 2
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Mice are born at the expected Mendelian rate and appear grossly normal during the first six weeks of life. After six to nine months, they display pronounced unsteadiness of gait and difficulty in supporting themselves on their hindlimbs, weight loss due to an inability to feed and labored respiration (PubMed:10839370).
Their sensory, motor and vagus nerves show extensive demyelination with demyelinated segments surrounded by focal thickenings (PubMed:10839370, PubMed:18205176).
In contrast, the predominantly sensory saphenous nerves are extensively hypermyelinated, resulting in myelin sheath infolding and axon compression (PubMed:10839370).
At eight months, naked or thinly myelinated axons are common in sciatic nerve fibers (PubMed:10839370).
Already at six weeks, mutant mice display markedly increased sensitivity to noxious mechanical and thermal stimuli (PubMed:10839370).
Besides, four month old mutant mice display impaired remyelination after crush injury (PubMed:10839370).
Schwann cells from mutant mice display a reduced rate of elongation, leading to decreased distances between nodes of Ranvier and reduced velocity of the transmission of nerve impulses; this results in impaired motor skills on the RotaRod in three week old mice (PubMed:15356632).
Peripheral nerves show decreased conduction velocity, due to defects in the myelin sheath (PubMed:10839370).
Motor axons from five month old mice show an increased number of preterminal branches that arise from demyelinated regions close to the neuromuscular junction (PubMed:18205176).
In contrast, axon branching close to the neuromuscular junction appears normal in three week old mice (PubMed:18205176).
At the molecular level, gene disruption impairs formation of Cajal bands and location of Drp2 in patches that colocalize with appositions between the abaxonal surface of the myelin sheath and the Schwann cell plasma membrane (PubMed:15356632).
Cytoplasm from mutant Schwann cells forms a concentric ring under the cell membrane, instead of being strictly compartmentalized at Cajal bands (PubMed:15356632).
The transport of the mRNA coding for Mbp is impaired; the mRNA level is highest in the perinuclear region and does not accumulate in the paranodal region (PubMed:15356632).
Eye lenses from 90 day old mutant mice appear grossly normal at the macroscopic level, but display altered shape and organization of inner lens fiber cells, together with alteration in the membrane localization of Mip, Ezr and Ahnak (PubMed:21745462).
Their sensory, motor and vagus nerves show extensive demyelination with demyelinated segments surrounded by focal thickenings (PubMed:10839370, PubMed:18205176).
In contrast, the predominantly sensory saphenous nerves are extensively hypermyelinated, resulting in myelin sheath infolding and axon compression (PubMed:10839370).
At eight months, naked or thinly myelinated axons are common in sciatic nerve fibers (PubMed:10839370).
Already at six weeks, mutant mice display markedly increased sensitivity to noxious mechanical and thermal stimuli (PubMed:10839370).
Besides, four month old mutant mice display impaired remyelination after crush injury (PubMed:10839370).
Schwann cells from mutant mice display a reduced rate of elongation, leading to decreased distances between nodes of Ranvier and reduced velocity of the transmission of nerve impulses; this results in impaired motor skills on the RotaRod in three week old mice (PubMed:15356632).
Peripheral nerves show decreased conduction velocity, due to defects in the myelin sheath (PubMed:10839370).
Motor axons from five month old mice show an increased number of preterminal branches that arise from demyelinated regions close to the neuromuscular junction (PubMed:18205176).
In contrast, axon branching close to the neuromuscular junction appears normal in three week old mice (PubMed:18205176).
At the molecular level, gene disruption impairs formation of Cajal bands and location of Drp2 in patches that colocalize with appositions between the abaxonal surface of the myelin sheath and the Schwann cell plasma membrane (PubMed:15356632).
Cytoplasm from mutant Schwann cells forms a concentric ring under the cell membrane, instead of being strictly compartmentalized at Cajal bands (PubMed:15356632).
The transport of the mRNA coding for Mbp is impaired; the mRNA level is highest in the perinuclear region and does not accumulate in the paranodal region (PubMed:15356632).
Eye lenses from 90 day old mutant mice appear grossly normal at the macroscopic level, but display altered shape and organization of inner lens fiber cells, together with alteration in the membrane localization of Mip, Ezr and Ahnak (PubMed:21745462).
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000058564 | 1-1391 | Periaxin | |||
Sequence: MEARSRSAEELRRAELVEIIVETEAQTGVSGFNVAGGGKEGIFVRELREDSPAAKSLSLQEGDQLLSARVFFENFKYEDALRLLQCAEPYKVSFCLKRTVPTGDLALRPGTVSGYEMKGPRAKVAKLNIQSLAPVKKKKMVTGALGTPADLAPVDVEFSFPKFSRLRRGLKAEAVKGPVPAAPARRRLQLPRLRVREVAEEAQVARMAAAAPPPRKAKAEAEAATGAGFTAPQIELVGPRLPSAEVGVPQVSVPKGTPSTEAASGFALHLPTLGLGAPAAPAVEPPATGIQVPQVELPTLPSLPTLPTLPCLDTQEGAAVVKVPTLDVAAPSMGVDLALPGAEVEAQGEVPEVALKMPRLSFPRFGIRGKEATEAKVVKGSPEAKAKGPRLRMPTFGLSLLEPRPSGPEAVAESKLKLPTLKMPSFGIGVAGPEVKAPTGPEVKLPKVPEVKLPKVPEAAIPDVQLPEVQLPKMSDMKLPKIPEMVVPDVRLPEVQLPKVPEMKVPEMKLPKWPEMAVPDVHLPDVQLPKVPEMKLPKVPEMAVPDVHLPDVQLPKVPEMKLPEMKLPKVPEMAVPDVRLPEVQLPKVSEVKLPKMPEMAVPDVHLPELQLPKMSEVKLPKMPEMAVPDVRLPEVQLPKVSEMKLPKMPEMTMPDIRLPEVQLPKVPDIKLPEMKLPEIKLPKVPDMAVPDVPLPELQLPKVSDIRLPEMQVSQVPEVQLPKMPEMKLSKVPEVQRKSAGAEQAKGTEFSFKLPKMTMPKLGKVGKPGEASIEVPDKLMTLPCLQPEVGTEASHVGVPSLSLPSVELDLPGALGLEGQVQEAVPGKVEKPEGPRVAVGVGEVGFRVPSVEIVTPQLPTVEVEKEQLEMVEMKVKPSSKFSLPKFGLSGPKAVKGEVEGPGRATKLKVSKFTISLPKARAGTEAEAKGAGEAGLLPALDLSIPQLSLDAQLPSGKVEVADSKPKSSRFALPKFGVKGRDSEADVLVAGEAELEGKGWGWDGKVKMPKLKMPSFGLSRGKEAETQDGRVSPGEKLEAIAGQLKIPAVELVTPGAQETEKVTSGVKPSGLQVSTTGQVVAEGQESVQRVSTLGISLPQVELASFGEAGPEIVAPSAEGTAGSRVQVPQVMLELPGTQVAGGDLLVGEGIFKMPTVTVPQLELDVGLGHEAQAGEAAKSEGGIKLKLPTLGTGSRGEGVEPQGPEAQRTFHLSLPDVELTSPVSSHAEYQVVEGDGDGGHKLKVRLPLFGLAKAKEGIEVGEKVKSPKLRLPRVGFSQSESVSGEGSPSPEEEEEGSGEGASSRRGRVRVRLPRVGLASPSKVSKGQEGDATSKSPVGEKSPKFRFPRVSLSPKARSGSRDREEGGFRVRLPSVGFSETAVPGSTRIEGTQAAAI | ||||||
Modified residue | 7 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 243 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 848 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 979 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1028 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1279 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1283 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1285 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1293 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1331 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1337 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1369 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Detected in myelinating Schwann cells in intramuscular nerves in triangularis sterni (PubMed:18205176).
Detected in sciatic nerve (PubMed:11430802).
Detected in eye lens fiber cells (PubMed:21745462).
Isoform 1 is detected in myelinating Schwann cells in sciatic nerve (PubMed:10671475, PubMed:10839370, PubMed:9488714).
Isoform 2 is detected in myelinating Schwann cells in sciatic nerve (at protein level) (PubMed:10839370, PubMed:9488714).
Detected in sciatic nerve (PubMed:10839370, PubMed:9488714).
Detected in sciatic nerve (PubMed:11430802).
Detected in eye lens fiber cells (PubMed:21745462).
Isoform 1 is detected in myelinating Schwann cells in sciatic nerve (PubMed:10671475, PubMed:10839370, PubMed:9488714).
Isoform 2 is detected in myelinating Schwann cells in sciatic nerve (at protein level) (PubMed:10839370, PubMed:9488714).
Detected in sciatic nerve (PubMed:10839370, PubMed:9488714).
Developmental stage
Detected in embryonic eye lens; levels increase steadily from 10.5 dpc onto birth and continue to increase during the first three weeks after birth.
Gene expression databases
Interaction
Subunit
Homodimer (via PDZ domain) (By similarity).
Interacts with SCN10A. Found in a complex with SCN10A (By similarity).
Interacts with DRP2 (PubMed:22764250).
Identified in a dystroglycan complex that contains at least PRX, DRP2, UTRN, DMD and DAG1 (PubMed:11430802).
Detected in a complex composed of at least EZR, AHNAK, PPL and PRX (By similarity).
Identified in a complex with EZR, AHNAK, BFSP1, BFSP2, ANK2, PLEC, VIM and spectrin (PubMed:21745462).
Interacts with SCN10A. Found in a complex with SCN10A (By similarity).
Interacts with DRP2 (PubMed:22764250).
Identified in a dystroglycan complex that contains at least PRX, DRP2, UTRN, DMD and DAG1 (PubMed:11430802).
Detected in a complex composed of at least EZR, AHNAK, PPL and PRX (By similarity).
Identified in a complex with EZR, AHNAK, BFSP1, BFSP2, ANK2, PLEC, VIM and spectrin (PubMed:21745462).
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, motif, repeat, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 16-99 | PDZ | ||||
Sequence: LVEIIVETEAQTGVSGFNVAGGGKEGIFVRELREDSPAAKSLSLQEGDQLLSARVFFENFKYEDALRLLQCAEPYKVSFCLKRT | ||||||
Motif | 70-84 | Nuclear export signal | ||||
Sequence: VFFENFKYEDALRLL | ||||||
Motif | 118-196 | Nuclear localization signal | ||||
Sequence: KGPRAKVAKLNIQSLAPVKKKKMVTGALGTPADLAPVDVEFSFPKFSRLRRGLKAEAVKGPVPAAPARRRLQLPRLRVR | ||||||
Repeat | 432-436 | 1 | ||||
Sequence: GPEVK | ||||||
Region | 432-719 | 45 X 5 AA approximate tandem repeats of [LVMGIED]-[PQSKHARMI]-[EDKLVTR]-[LIVMAP]-[AQKHRPEVSD]; that may have a tripeptide spacer of [LVIDEA]-[PMSVI]-[KEATDQ] | ||||
Sequence: GPEVKAPTGPEVKLPKVPEVKLPKVPEAAIPDVQLPEVQLPKMSDMKLPKIPEMVVPDVRLPEVQLPKVPEMKVPEMKLPKWPEMAVPDVHLPDVQLPKVPEMKLPKVPEMAVPDVHLPDVQLPKVPEMKLPEMKLPKVPEMAVPDVRLPEVQLPKVSEVKLPKMPEMAVPDVHLPELQLPKMSEVKLPKMPEMAVPDVRLPEVQLPKVSEMKLPKMPEMTMPDIRLPEVQLPKVPDIKLPEMKLPEIKLPKVPDMAVPDVPLPELQLPKVSDIRLPEMQVSQVPEVQ | ||||||
Repeat | 440-444 | 2 | ||||
Sequence: GPEVK | ||||||
Repeat | 448-452 | 3 | ||||
Sequence: VPEVK | ||||||
Repeat | 456-460 | 4 | ||||
Sequence: VPEAA | ||||||
Repeat | 464-468 | 5 | ||||
Sequence: VQLPE | ||||||
Repeat | 469-473 | 6 | ||||
Sequence: VQLPK | ||||||
Repeat | 474-478 | 7 | ||||
Sequence: MSDMK | ||||||
Repeat | 482-486 | 8 | ||||
Sequence: IPEMV | ||||||
Repeat | 487-491 | 9 | ||||
Sequence: VPDVR | ||||||
Repeat | 495-499 | 10 | ||||
Sequence: VQLPK | ||||||
Repeat | 500-504 | 11 | ||||
Sequence: VPEMK | ||||||
Repeat | 508-512 | 12 | ||||
Sequence: MKLPK | ||||||
Repeat | 513-517 | 13; approximate | ||||
Sequence: WPEMA | ||||||
Repeat | 521-525 | 14 | ||||
Sequence: VHLPD | ||||||
Repeat | 526-530 | 15 | ||||
Sequence: VQLPK | ||||||
Repeat | 534-538 | 16 | ||||
Sequence: MKLPK | ||||||
Repeat | 539-543 | 17 | ||||
Sequence: VPEMA | ||||||
Repeat | 547-551 | 18 | ||||
Sequence: VHLPD | ||||||
Repeat | 552-556 | 19 | ||||
Sequence: VQLPK | ||||||
Repeat | 560-564 | 20 | ||||
Sequence: MKLPE | ||||||
Repeat | 565-569 | 21 | ||||
Sequence: MKLPK | ||||||
Repeat | 573-577 | 22 | ||||
Sequence: MAVPD | ||||||
Repeat | 578-582 | 23 | ||||
Sequence: VRLPE | ||||||
Repeat | 583-587 | 24 | ||||
Sequence: VQLPK | ||||||
Repeat | 591-595 | 25 | ||||
Sequence: VKLPK | ||||||
Repeat | 596-600 | 26 | ||||
Sequence: MPEMA | ||||||
Repeat | 601-605 | 27 | ||||
Sequence: VPDVH | ||||||
Repeat | 609-613 | 28 | ||||
Sequence: LQLPK | ||||||
Repeat | 614-618 | 29 | ||||
Sequence: MSEVK | ||||||
Repeat | 619-623 | 30 | ||||
Sequence: LPKMP | ||||||
Repeat | 627-631 | 31 | ||||
Sequence: VPDVR | ||||||
Repeat | 632-636 | 32 | ||||
Sequence: LPEVQ | ||||||
Repeat | 637-641 | 33 | ||||
Sequence: LPKVS | ||||||
Repeat | 645-649 | 34 | ||||
Sequence: LPKMP | ||||||
Repeat | 650-654 | 35 | ||||
Sequence: EMTMP | ||||||
Repeat | 655-659 | 36 | ||||
Sequence: DIRLP | ||||||
Repeat | 663-667 | 37 | ||||
Sequence: LPKVP | ||||||
Repeat | 671-675 | 38 | ||||
Sequence: LPEMK | ||||||
Repeat | 676-680 | 39 | ||||
Sequence: LPEIK | ||||||
Repeat | 684-688 | 40 | ||||
Sequence: VPDMA | ||||||
Repeat | 689-693 | 41 | ||||
Sequence: VPDVP | ||||||
Repeat | 697-701 | 42 | ||||
Sequence: LQLPK | ||||||
Repeat | 702-706 | 43 | ||||
Sequence: VSDIR | ||||||
Repeat | 707-711 | 44 | ||||
Sequence: LPEMQ | ||||||
Repeat | 715-719 | 45 | ||||
Sequence: VPEVQ | ||||||
Region | 1267-1366 | Disordered | ||||
Sequence: LPRVGFSQSESVSGEGSPSPEEEEEGSGEGASSRRGRVRVRLPRVGLASPSKVSKGQEGDATSKSPVGEKSPKFRFPRVSLSPKARSGSRDREEGGFRVR |
Domain
Has a remarkable domain of repetitive pentameric units sometimes followed by a tripeptide spacer, it may separate two functional basic and acidic domains.
The PDZ domain contains the signal for export from the nucleus (By similarity).
The N-terminal region including the PDZ domain is required for the formation of Cajal bands on myelinated nerves
The N-terminal region including the PDZ domain is required for the formation of Cajal bands on myelinated nerves
The Arg/Lys-rich basic domain functions as a tripartite nuclear localization signal.
Sequence similarities
Belongs to the periaxin family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
O55103-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- SynonymsL-periaxin
- Length1,391
- Mass (Da)147,688
- Last updated1998-06-01 v1
- ChecksumB16DF4E5C33D376C
O55103-2
- Name2
- SynonymsS-periaxin
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0U1RNK1 | A0A0U1RNK1_MOUSE | Prx | 1252 | ||
A0A5F8MQ58 | A0A5F8MQ58_MOUSE | Prx | 1525 | ||
Q6NVF7 | Q6NVF7_MOUSE | Prx | 1391 | ||
E9QQ57 | E9QQ57_MOUSE | Prx | 1391 |
Features
Showing features for alternative sequence.
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AJ222968 EMBL· GenBank· DDBJ | CAA11022.1 EMBL· GenBank· DDBJ | mRNA | ||
AJ222969 EMBL· GenBank· DDBJ | CAA11023.1 EMBL· GenBank· DDBJ | mRNA |