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Protein

Periaxin

Gene

Prx

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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:23022068, PubMed:22764250). Recruits DRP2 to the Schwann cell plasma membrane (PubMed:11430802, PubMed:23022068, PubMed:22764250). Required for normal protein composition of the eye lens fiber cell plasma membrane and normal eye lens fiber cell morphology (PubMed:21745462).5 Publications

GO - Biological processi

  • peripheral nervous system myelin formation Source: UniProtKB
  • peripheral nervous system myelin maintenance Source: UniProtKB
  • regulation of RNA splicing Source: UniProtKB
  • sensory perception of pain Source: UniProtKB
  • transmission of nerve impulse Source: UniProtKB
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Periaxin
Gene namesi
Name:Prx
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:108176. Prx.

Subcellular locationi

  • Cell membrane 1 Publication
  • Cell junction 1 Publication

  • Note: Colocalizes with ACTB at tricellular junctions between eye lens fiber cells.1 Publication
Isoform 1 :
Isoform 2 :

GO - Cellular componenti

  • cell junction Source: UniProtKB-SubCell
  • cytoplasm Source: MGI
  • cytosol Source: UniProtKB
  • nucleus Source: MGI
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Disruption phenotypei

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).4 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000585641 – 1391PeriaxinAdd BLAST1391

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei7PhosphoserineBy similarity1
Modified residuei243PhosphoserineBy similarity1
Modified residuei848PhosphoserineBy similarity1
Modified residuei979PhosphoserineCombined sources1
Modified residuei1028PhosphoserineBy similarity1
Modified residuei1279PhosphoserineCombined sources1
Modified residuei1283PhosphoserineCombined sources1
Modified residuei1285PhosphoserineCombined sources1
Modified residuei1293PhosphoserineCombined sources1
Modified residuei1331PhosphoserineBy similarity1
Modified residuei1337PhosphoserineCombined sources1
Modified residuei1369PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO55103.
PaxDbiO55103.
PeptideAtlasiO55103.
PRIDEiO55103.

PTM databases

iPTMnetiO55103.
PhosphoSitePlusiO55103.

Expressioni

Tissue specificityi

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:9488714, PubMed:10671475, PubMed:10839370). Isoform 2 is detected in myelinating Schwann cells in sciatic nerve (at protein level) (PubMed:9488714, PubMed:10839370). Detected in sciatic nerve (PubMed:9488714, PubMed:10839370).6 Publications

Developmental stagei

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.1 Publication

Gene expression databases

BgeeiENSMUSG00000053198.
CleanExiMM_PRX.
ExpressionAtlasiO55103. baseline and differential.
GenevisibleiO55103. MM.

Interactioni

Subunit structurei

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).By similarity3 Publications

Protein-protein interaction databases

BioGridi202408. 1 interactor.
IntActiO55103. 2 interactors.
MINTiMINT-4108501.
STRINGi10090.ENSMUSP00000096241.

Structurei

3D structure databases

ProteinModelPortaliO55103.
SMRiO55103.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini16 – 99PDZPROSITE-ProRule annotationAdd BLAST84
Repeati432 – 43615
Repeati440 – 44425
Repeati448 – 45235
Repeati456 – 46045
Repeati464 – 46855
Repeati469 – 47365
Repeati474 – 47875
Repeati482 – 48685
Repeati487 – 49195
Repeati495 – 499105
Repeati500 – 504115
Repeati508 – 512125
Repeati513 – 51713; approximate5
Repeati521 – 525145
Repeati526 – 530155
Repeati534 – 538165
Repeati539 – 543175
Repeati547 – 551185
Repeati552 – 556195
Repeati560 – 564205
Repeati565 – 569215
Repeati573 – 577225
Repeati578 – 582235
Repeati583 – 587245
Repeati591 – 595255
Repeati596 – 600265
Repeati601 – 605275
Repeati609 – 613285
Repeati614 – 618295
Repeati619 – 623305
Repeati627 – 631315
Repeati632 – 636325
Repeati637 – 641335
Repeati645 – 649345
Repeati650 – 654355
Repeati655 – 659365
Repeati663 – 667375
Repeati671 – 675385
Repeati676 – 680395
Repeati684 – 688405
Repeati689 – 693415
Repeati697 – 701425
Repeati702 – 706435
Repeati707 – 711445
Repeati715 – 719455

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni432 – 71945 X 5 AA approximate tandem repeats of [LVMGIED]-[PQSKHARMI]-[EDKLVTR]-[LIVMAP]-[AQKHRPEVSD]; that may have a tripeptide spacer of [LVIDEA]-[PMSVI]-[KEATDQ]Add BLAST288

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi70 – 84Nuclear export signalBy similarityAdd BLAST15
Motifi118 – 196Nuclear localization signalAdd BLAST79

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi118 – 196Arg/Lys-rich (basic)Add BLAST79
Compositional biasi1044 – 1171Glu-rich (acidic)Add BLAST128
Compositional biasi1287 – 1291Poly-Glu5

Domaini

Has a remarkable domain of repetitive pentameric units sometimes followed by a tripeptide spacer, it may separate two functional basic and acidic domains.Curated
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.By similarity1 Publication
The Arg/Lys-rich basic domain functions as a tripartite nuclear localization signal.By similarity

Sequence similaritiesi

Belongs to the periaxin family.Curated
Contains 1 PDZ (DHR) domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG410II3A. Eukaryota.
ENOG410ZMDY. LUCA.
GeneTreeiENSGT00530000063716.
HOGENOMiHOG000168246.
HOVERGENiHBG031836.
InParanoidiO55103.
PhylomeDBiO55103.

Family and domain databases

Gene3Di2.30.42.10. 1 hit.
InterProiIPR001478. PDZ.
[Graphical view]
SMARTiSM00228. PDZ. 1 hit.
[Graphical view]
SUPFAMiSSF50156. SSF50156. 1 hit.
PROSITEiPS50106. PDZ. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O55103-1) [UniParc]FASTAAdd to basket
Also known as: L-periaxin

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.

« Hide

        10         20         30         40         50
MEARSRSAEE LRRAELVEII VETEAQTGVS GFNVAGGGKE GIFVRELRED
60 70 80 90 100
SPAAKSLSLQ EGDQLLSARV FFENFKYEDA LRLLQCAEPY KVSFCLKRTV
110 120 130 140 150
PTGDLALRPG TVSGYEMKGP RAKVAKLNIQ SLAPVKKKKM VTGALGTPAD
160 170 180 190 200
LAPVDVEFSF PKFSRLRRGL KAEAVKGPVP AAPARRRLQL PRLRVREVAE
210 220 230 240 250
EAQVARMAAA APPPRKAKAE AEAATGAGFT APQIELVGPR LPSAEVGVPQ
260 270 280 290 300
VSVPKGTPST EAASGFALHL PTLGLGAPAA PAVEPPATGI QVPQVELPTL
310 320 330 340 350
PSLPTLPTLP CLDTQEGAAV VKVPTLDVAA PSMGVDLALP GAEVEAQGEV
360 370 380 390 400
PEVALKMPRL SFPRFGIRGK EATEAKVVKG SPEAKAKGPR LRMPTFGLSL
410 420 430 440 450
LEPRPSGPEA VAESKLKLPT LKMPSFGIGV AGPEVKAPTG PEVKLPKVPE
460 470 480 490 500
VKLPKVPEAA IPDVQLPEVQ LPKMSDMKLP KIPEMVVPDV RLPEVQLPKV
510 520 530 540 550
PEMKVPEMKL PKWPEMAVPD VHLPDVQLPK VPEMKLPKVP EMAVPDVHLP
560 570 580 590 600
DVQLPKVPEM KLPEMKLPKV PEMAVPDVRL PEVQLPKVSE VKLPKMPEMA
610 620 630 640 650
VPDVHLPELQ LPKMSEVKLP KMPEMAVPDV RLPEVQLPKV SEMKLPKMPE
660 670 680 690 700
MTMPDIRLPE VQLPKVPDIK LPEMKLPEIK LPKVPDMAVP DVPLPELQLP
710 720 730 740 750
KVSDIRLPEM QVSQVPEVQL PKMPEMKLSK VPEVQRKSAG AEQAKGTEFS
760 770 780 790 800
FKLPKMTMPK LGKVGKPGEA SIEVPDKLMT LPCLQPEVGT EASHVGVPSL
810 820 830 840 850
SLPSVELDLP GALGLEGQVQ EAVPGKVEKP EGPRVAVGVG EVGFRVPSVE
860 870 880 890 900
IVTPQLPTVE VEKEQLEMVE MKVKPSSKFS LPKFGLSGPK AVKGEVEGPG
910 920 930 940 950
RATKLKVSKF TISLPKARAG TEAEAKGAGE AGLLPALDLS IPQLSLDAQL
960 970 980 990 1000
PSGKVEVADS KPKSSRFALP KFGVKGRDSE ADVLVAGEAE LEGKGWGWDG
1010 1020 1030 1040 1050
KVKMPKLKMP SFGLSRGKEA ETQDGRVSPG EKLEAIAGQL KIPAVELVTP
1060 1070 1080 1090 1100
GAQETEKVTS GVKPSGLQVS TTGQVVAEGQ ESVQRVSTLG ISLPQVELAS
1110 1120 1130 1140 1150
FGEAGPEIVA PSAEGTAGSR VQVPQVMLEL PGTQVAGGDL LVGEGIFKMP
1160 1170 1180 1190 1200
TVTVPQLELD VGLGHEAQAG EAAKSEGGIK LKLPTLGTGS RGEGVEPQGP
1210 1220 1230 1240 1250
EAQRTFHLSL PDVELTSPVS SHAEYQVVEG DGDGGHKLKV RLPLFGLAKA
1260 1270 1280 1290 1300
KEGIEVGEKV KSPKLRLPRV GFSQSESVSG EGSPSPEEEE EGSGEGASSR
1310 1320 1330 1340 1350
RGRVRVRLPR VGLASPSKVS KGQEGDATSK SPVGEKSPKF RFPRVSLSPK
1360 1370 1380 1390
ARSGSRDREE GGFRVRLPSV GFSETAVPGS TRIEGTQAAA I
Length:1,391
Mass (Da):147,688
Last modified:June 1, 1998 - v1
Checksum:iB16DF4E5C33D376C
GO
Isoform 2 (identifier: O55103-2) [UniParc]FASTAAdd to basket
Also known as: S-periaxin

The sequence of this isoform differs from the canonical sequence as follows:
     128-148: NIQSLAPVKKKKMVTGALGTP → VRVLSPVPVQDSPSDRVAAAP
     149-1391: Missing.

Show »
Length:148
Mass (Da):16,124
Checksum:i426D1148993E79B0
GO

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_004366128 – 148NIQSL…ALGTP → VRVLSPVPVQDSPSDRVAAA P in isoform 2. 1 PublicationAdd BLAST21
Alternative sequenceiVSP_004367149 – 1391Missing in isoform 2. 1 PublicationAdd BLAST1243

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ222968 mRNA. Translation: CAA11022.1.
AJ222969 mRNA. Translation: CAA11023.1.
CCDSiCCDS21023.1. [O55103-1]
CCDS39849.1. [O55103-2]
RefSeqiNP_062285.1. NM_019412.2. [O55103-2]
NP_932165.2. NM_198048.2.
UniGeneiMm.10119.

Genome annotation databases

EnsembliENSMUST00000108355; ENSMUSP00000103992; ENSMUSG00000053198. [O55103-2]
GeneIDi19153.
KEGGimmu:19153.
UCSCiuc009fwj.2. mouse. [O55103-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ222968 mRNA. Translation: CAA11022.1.
AJ222969 mRNA. Translation: CAA11023.1.
CCDSiCCDS21023.1. [O55103-1]
CCDS39849.1. [O55103-2]
RefSeqiNP_062285.1. NM_019412.2. [O55103-2]
NP_932165.2. NM_198048.2.
UniGeneiMm.10119.

3D structure databases

ProteinModelPortaliO55103.
SMRiO55103.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202408. 1 interactor.
IntActiO55103. 2 interactors.
MINTiMINT-4108501.
STRINGi10090.ENSMUSP00000096241.

PTM databases

iPTMnetiO55103.
PhosphoSitePlusiO55103.

Proteomic databases

MaxQBiO55103.
PaxDbiO55103.
PeptideAtlasiO55103.
PRIDEiO55103.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000108355; ENSMUSP00000103992; ENSMUSG00000053198. [O55103-2]
GeneIDi19153.
KEGGimmu:19153.
UCSCiuc009fwj.2. mouse. [O55103-2]

Organism-specific databases

CTDi57716.
MGIiMGI:108176. Prx.

Phylogenomic databases

eggNOGiENOG410II3A. Eukaryota.
ENOG410ZMDY. LUCA.
GeneTreeiENSGT00530000063716.
HOGENOMiHOG000168246.
HOVERGENiHBG031836.
InParanoidiO55103.
PhylomeDBiO55103.

Miscellaneous databases

PROiO55103.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000053198.
CleanExiMM_PRX.
ExpressionAtlasiO55103. baseline and differential.
GenevisibleiO55103. MM.

Family and domain databases

Gene3Di2.30.42.10. 1 hit.
InterProiIPR001478. PDZ.
[Graphical view]
SMARTiSM00228. PDZ. 1 hit.
[Graphical view]
SUPFAMiSSF50156. SSF50156. 1 hit.
PROSITEiPS50106. PDZ. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPRAX_MOUSE
AccessioniPrimary (citable) accession number: O55103
Secondary accession number(s): O55104
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 16, 2002
Last sequence update: June 1, 1998
Last modified: November 2, 2016
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.