PRAX_RAT
ID PRAX_RAT Reviewed; 1383 AA.
AC Q63425;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2002, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Periaxin {ECO:0000303|PubMed:8155317};
GN Name=Prx;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=Wistar;
RX PubMed=8155317; DOI=10.1016/0896-6273(94)90208-9;
RA Gillespie C.S., Sherman D.L., Blair G.E., Brophy P.J.;
RT "Periaxin, a novel protein of myelinating Schwann cells with a possible
RT role in axonal ensheathment.";
RL Neuron 12:497-508(1994).
RN [2]
RP SEQUENCE REVISION TO 1364-1371.
RA Brophy P.J.;
RL Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=9488714; DOI=10.1074/jbc.273.10.5794;
RA Dytrych L., Sherman D.L., Gillespie C.S., Brophy P.J.;
RT "Two PDZ domain proteins encoded by the murine periaxin gene are the result
RT of alternative intron retention and are differentially targeted in Schwann
RT cells.";
RL J. Biol. Chem. 273:5794-5800(1998).
RN [4]
RP PROTEIN SEQUENCE OF 1019-1033, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA Lubec G., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [5]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DOMAIN.
RX PubMed=10671475; DOI=10.1074/jbc.275.7.4537;
RA Sherman D.L., Brophy P.J.;
RT "A tripartite nuclear localization signal in the PDZ-domain protein L-
RT periaxin.";
RL J. Biol. Chem. 275:4537-4540(2000).
RN [6]
RP INTERACTION WITH DRP2, SUBUNIT, TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RX PubMed=11430802; DOI=10.1016/s0896-6273(01)00327-0;
RA Sherman D.L., Fabrizi C., Gillespie C.S., Brophy P.J.;
RT "Specific disruption of a Schwann cell dystrophin-related protein complex
RT in a demyelinating neuropathy.";
RL Neuron 30:677-687(2001).
RN [7]
RP INTERACTION WITH SCN10A, AND IDENTIFICATION IN A COMPLEX WITH SCN10A.
RX PubMed=12591166; DOI=10.1016/s0169-328x(02)00661-7;
RA Malik-Hall M., Poon W.-Y.L., Baker M.D., Wood J.N., Okuse K.;
RT "Sensory neuron proteins interact with the intracellular domains of sodium
RT channel NaV1.8.";
RL Brain Res. Mol. Brain Res. 110:298-304(2003).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7; SER-133; SER-243; SER-838;
RP SER-1020; SER-1323; SER-1329 AND SER-1361, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Scaffolding protein that functions as part of a dystroglycan
CC complex in Schwann cells, and as part of EZR and AHNAK-containing
CC complexes in eye lens fiber cells. Required for the maintenance of the
CC peripheral myelin sheath that is essential for normal transmission of
CC nerve impulses and normal perception of sensory stimuli. Required for
CC normal transport of MBP mRNA from the perinuclear to the paranodal
CC regions. Required for normal remyelination after nerve injury. Required
CC for normal elongation of Schwann cells and normal length of the
CC internodes between the nodes of Ranvier. The demyelinated nodes of
CC Ranvier permit saltatory transmission of nerve impulses; shorter
CC internodes cause slower transmission of nerve impulses. Required for
CC the formation of appositions between the abaxonal surface of the myelin
CC sheath and the Schwann cell plasma membrane; the Schwann cell cytoplasm
CC is restricted to regions between these appositions. Required for the
CC formation of Cajal bands and of Schmidt-Lanterman incisures that
CC correspond to short, cytoplasm-filled regions on myelinated nerves.
CC Recruits DRP2 to the Schwann cell plasma membrane. Required for normal
CC protein composition of the eye lens fiber cell plasma membrane and
CC normal eye lens fiber cell morphology. {ECO:0000250|UniProtKB:O55103}.
CC -!- SUBUNIT: Homodimer (via PDZ domain) (PubMed:11430802). Interacts with
CC SCN10A. Found in a complex with SCN10A (PubMed:12591166). Interacts
CC with DRP2 (PubMed:11430802). Identified in a dystroglycan complex that
CC contains at least PRX, DRP2, UTRN, DMD and DAG1 (By similarity).
CC Detected in a complex composed of at least EZR, AHNAK, PPL and PRX (By
CC similarity). Identified in a complex with EZR, AHNAK, BFSP1, BFSP2,
CC ANK2, PLEC, VIM and spectrin (By similarity).
CC {ECO:0000250|UniProtKB:E1BM58, ECO:0000250|UniProtKB:O55103,
CC ECO:0000250|UniProtKB:Q9BXM0, ECO:0000269|PubMed:11430802,
CC ECO:0000269|PubMed:12591166}.
CC -!- INTERACTION:
CC Q63425; Q62968: Scn10a; NbExp=2; IntAct=EBI-1800492, EBI-1800320;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Nucleus
CC {ECO:0000269|PubMed:10671475}. Cytoplasm {ECO:0000269|PubMed:10671475,
CC ECO:0000269|PubMed:8155317}. Cell membrane
CC {ECO:0000269|PubMed:10671475, ECO:0000269|PubMed:11430802,
CC ECO:0000269|PubMed:8155317}; Peripheral membrane protein {ECO:0000305};
CC Cytoplasmic side {ECO:0000305}. Note=Detected in the Schwann cell
CC nucleus prior to the onset of myelination (By similarity). Detected in
CC Schwann cells at periaxonal myelin membranes (PubMed:8155317,
CC PubMed:10671475, PubMed:11430802). Associated with the cell membrane
CC during myelination (By similarity). {ECO:0000250|UniProtKB:O55103,
CC ECO:0000269|PubMed:10671475, ECO:0000269|PubMed:11430802,
CC ECO:0000269|PubMed:8155317}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm
CC {ECO:0000250|UniProtKB:O55103}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O55103}.
CC Cell junction {ECO:0000250|UniProtKB:O55103}. Note=Colocalizes with
CC ACTB at tricellular junctions between eye lens fiber cells.
CC {ECO:0000250|UniProtKB:O55103}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=L-periaxin;
CC IsoId=Q63425-1; Sequence=Displayed;
CC Name=2; Synonyms=S-periaxin;
CC IsoId=Q63425-2; Sequence=VSP_004368, VSP_004369;
CC -!- TISSUE SPECIFICITY: Detected in sciatic nerve and in trigeminal nerve
CC Schwann cells (PubMed:11430802). Detected in myelinating Schwann cells
CC in sciatic nerve (at protein level) (PubMed:8155317, PubMed:10671475).
CC {ECO:0000269|PubMed:10671475, ECO:0000269|PubMed:11430802,
CC ECO:0000269|PubMed:8155317}.
CC -!- DEVELOPMENTAL STAGE: mRNA and protein levels peak in the sciatic nerve
CC between posnatal days 8 and 20; thereafter they decline precipitously.
CC {ECO:0000269|PubMed:8155317}.
CC -!- DOMAIN: Has a remarkable domain of repetitive pentameric units
CC sometimes followed by a tripeptide spacer, it may separate two
CC functional basic and acidic domains. {ECO:0000305}.
CC -!- DOMAIN: The Arg/Lys-rich basic domain functions as a tripartite nuclear
CC localization signal. {ECO:0000269|PubMed:10671475}.
CC -!- DOMAIN: The PDZ domain contains the signal for export from the nucleus
CC (By similarity). The N-terminal region including the PDZ domain is
CC required for the formation of Cajal bands on myelinated nerves (By
CC similarity). {ECO:0000250|UniProtKB:O55103,
CC ECO:0000250|UniProtKB:Q9BXM0}.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the periaxin family. {ECO:0000305}.
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DR EMBL; Z29649; CAA82757.2; -; mRNA.
DR PIR; I58157; I58157.
DR RefSeq; NP_076466.2; NM_023976.2. [Q63425-1]
DR AlphaFoldDB; Q63425; -.
DR SMR; Q63425; -.
DR IntAct; Q63425; 3.
DR STRING; 10116.ENSRNOP00000024771; -.
DR iPTMnet; Q63425; -.
DR PhosphoSitePlus; Q63425; -.
DR PaxDb; Q63425; -.
DR PRIDE; Q63425; -.
DR GeneID; 78960; -.
DR KEGG; rno:78960; -.
DR UCSC; RGD:619960; rat. [Q63425-1]
DR CTD; 57716; -.
DR RGD; 619960; Prx.
DR eggNOG; ENOG502QS7Y; Eukaryota.
DR InParanoid; Q63425; -.
DR PhylomeDB; Q63425; -.
DR PRO; PR:Q63425; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0043209; C:myelin sheath; IDA:RGD.
DR GO; GO:0016607; C:nuclear speck; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0008366; P:axon ensheathment; IEP:RGD.
DR GO; GO:0021675; P:nerve development; IEP:RGD.
DR GO; GO:0032290; P:peripheral nervous system myelin formation; ISO:RGD.
DR GO; GO:0032287; P:peripheral nervous system myelin maintenance; ISO:RGD.
DR GO; GO:0043484; P:regulation of RNA splicing; IBA:GO_Central.
DR GO; GO:0019233; P:sensory perception of pain; ISO:RGD.
DR GO; GO:0019226; P:transmission of nerve impulse; ISO:RGD.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR Pfam; PF00595; PDZ; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell junction; Cell membrane; Cytoplasm;
KW Direct protein sequencing; Membrane; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..1383
FT /note="Periaxin"
FT /id="PRO_0000058565"
FT DOMAIN 16..99
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REPEAT 432..436
FT /note="1"
FT REPEAT 440..444
FT /note="2"
FT REPEAT 448..452
FT /note="3"
FT REPEAT 456..460
FT /note="4"
FT REPEAT 461..465
FT /note="5"
FT REPEAT 466..470
FT /note="6"
FT REPEAT 474..478
FT /note="7"
FT REPEAT 482..486
FT /note="8"
FT REPEAT 487..491
FT /note="9"
FT REPEAT 492..496
FT /note="10"
FT REPEAT 497..501
FT /note="11"
FT REPEAT 502..506
FT /note="12"
FT REPEAT 507..511
FT /note="13"
FT REPEAT 515..519
FT /note="14"
FT REPEAT 523..527
FT /note="15"
FT REPEAT 531..535
FT /note="16"
FT REPEAT 536..540
FT /note="17"
FT REPEAT 544..548
FT /note="18"
FT REPEAT 549..553
FT /note="19"
FT REPEAT 554..558
FT /note="20"
FT REPEAT 562..566
FT /note="21"
FT REPEAT 567..571
FT /note="22"
FT REPEAT 575..579
FT /note="23"
FT REPEAT 580..584
FT /note="24"
FT REPEAT 585..589
FT /note="25"
FT REPEAT 593..597
FT /note="26"
FT REPEAT 601..605
FT /note="27"
FT REPEAT 606..610
FT /note="28"
FT REPEAT 611..615
FT /note="29"
FT REPEAT 619..623
FT /note="30"
FT REPEAT 627..631
FT /note="31"
FT REPEAT 632..636
FT /note="32"
FT REPEAT 637..641
FT /note="33"
FT REPEAT 645..649
FT /note="34"
FT REPEAT 653..657
FT /note="35"
FT REPEAT 658..662
FT /note="36"
FT REPEAT 663..667
FT /note="37"
FT REPEAT 671..675
FT /note="38"
FT REPEAT 676..680
FT /note="39"
FT REPEAT 684..688
FT /note="40"
FT REPEAT 689..693
FT /note="41"
FT REPEAT 694..698
FT /note="42"
FT REPEAT 699..703
FT /note="43"
FT REPEAT 705..709
FT /note="44"
FT REPEAT 713..717
FT /note="45"
FT REPEAT 718..722
FT /note="46"
FT REGION 432..722
FT /note="46 X 5 AA approximate tandem repeats of [LVMGIE]-
FT [PSM]-[EDKA]-[LIVMA]-[AQKHPRT]; that may have a tripeptide
FT spacer of [ALKD]-[IPV]-[KPH]"
FT REGION 1251..1383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 70..84
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250|UniProtKB:Q9BXM0"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 133
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 243
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 838
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 971
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O55103"
FT MOD_RES 1020
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1271
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O55103"
FT MOD_RES 1275
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O55103"
FT MOD_RES 1277
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O55103"
FT MOD_RES 1285
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O55103"
FT MOD_RES 1323
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1329
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1361
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT VAR_SEQ 128..147
FT /note="NIQSLSPVKKKKMVIGTLGT -> VRVLSPVPVQDSPSDAVAAP (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:9488714"
FT /id="VSP_004368"
FT VAR_SEQ 148..1383
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9488714"
FT /id="VSP_004369"
SQ SEQUENCE 1383 AA; 146400 MW; FF6593BCFA23A437 CRC64;
MEARSRSAEE LRRAELVEII VETEAQTGVS GFNVAGGGKE GIFVRELRED SPAAKSLSLQ
EGDQLLSARV FFENFKYEDA LRLLQCAEPY KVSFCLKRTV PTGDLALRPG TVSGYEMKGP
RAKVAKLNIQ SLSPVKKKKM VIGTLGTPAD LAPVDVEFSF PKFSRLRRGL KADAVKGPVP
AAPARRRLQL PRLRVREVAE EAQVARMAAA APPSRKAKSE AEVATGAGFT APQIELVGPR
LPSAEVGVPK VSVPKGTPST EAASGFALHL PTLGLGAPAA PAVEPPTTGI QVPQVELPTL
PSLPTLPTLP CLDTQEGAAV VKVPTLDVAA PSVEVDLALP GAEVEAQGEV PEVALKMPRL
SFPRFGVRGK EATEAKVVKG SPEAKAKGPR LRMPTFGLSL LESRPSGPEV AAESKLKLPT
LKMPSFGISV AGPEVKAPKG PEVKLPKVPE IKLPKAPEAA IPDVQLPEVQ LPKMSDMKLP
KIPEMAVPDV HLPEVKLPKV PEMKVPEMKL PKIPEMAVPD VHLPDIQLPK VPEMKLPDMK
LPKVPEMAVP DVHLPDIQLP KVPEMKLPDM KLPKVPEMAV PDVRIPEVQL PKVSEVKLPK
IPDMAVPDVR LPELQLPKMS EVKLPKIPDM AVPDVRLPEV QLPKVSELKL PKVPEMTMPD
IRLPEVQLPK VPDIKLPEIK LPKVPEMAVP DVPLPELQLP KVPQVPDVHL PKVPEMKLPK
VPEAQRKSAG AEQAEKTEFS FKLPKMTVPK LGKVTKPGEA GIEVPDKLLI LPCLQPEVGT
EVARVGVPSL SLPSVELDLP GALGLEGQVQ EAVSGKVEKP EGPRVAVGTG EAGFRVPSVE
IVNPQLPTVE VKKEQLEMVE MKVKPTSKFS LPKFGLSGPK AVKAEVEGPG RATKLKVSKF
AISLPRARAG TDADAKGAGE AGLLPALDLS IPQLSLDAQL PSGKVEVAGA ESKPKGSRFA
LPKFGAKGRD SEADVLVAGE AELEGKGWGW DGKVKMPKLK MPSFGLSRGK EAEIQDGRVS
PGEKLEAIAG QLKIPEVELV TPGAQETEKV TSGVKPSGLQ VSTTRQVVAE GQEGAQRVSS
LGISLPQVEL ASFGEAGPEI AAPSAEGTVG SRIQVPQVML ELPGTQVAGG DLLVGEGIFK
MPTVTVPQLE LDVGLGHEAQ AGETAKSEGG LKLKLPTLGA GGKGEGAEAQ SPEAQHTFHI
SLPDVELTSP VSSHAEYQVV EGDGDGGHKL KVRLPLFGLA RAKEGIETGE KVKSPKLRLP
RVGFSQSESA SGEGSPSPEE EEEGSGEGAS GRRGRVRVRL PRVGLASPSK GSKGQEGDAA
SKSPVGEKSP KFRFPRVSLS PKARSGSKDR EEGGFRVRLP SVGFSETAAP GSARIEGTQA
AAI
