PRAX_BOVIN
ID PRAX_BOVIN Reviewed; 1349 AA.
AC E1BM58;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 09-DEC-2015, sequence version 3.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=Periaxin {ECO:0000305};
GN Name=PRX;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT "A whole-genome assembly of the domestic cow, Bos taurus.";
RL Genome Biol. 10:R42.01-R42.10(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-127.
RC STRAIN=Friesian; TISSUE=Fetal brain;
RA Lehnert K., Ford C., Reid S.J., Bohm E., Sutherland G.T., Verkerk G.,
RA Walden A., Ward H.E., Pearson J.F., Snell R.G.;
RT "Generation of normalized libraries and expressed sequence tags from bovine
RT fetal brain.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP SUBUNIT, IDENTIFICATION IN A COMPLEX WITH EZR; AHNAK AND PPL, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=14625392; DOI=10.1242/jcs.00815;
RA Straub B.K., Boda J., Kuhn C., Schnoelzer M., Korf U., Kempf T., Spring H.,
RA Hatzfeld M., Franke W.W.;
RT "A novel cell-cell junction system: the cortex adhaerens mosaic of lens
RT fiber cells.";
RL J. Cell Sci. 116:4985-4995(2003).
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) (By similarity). Interacts with
CC SCN10A. Found in a complex with SCN10A (By similarity). Interacts with
CC DRP2. Identified in a dystroglycan complex that contains at least PRX,
CC DRP2, UTRN, DMD and DAG1 (By similarity). Detected in a complex
CC composed of at least EZR, AHNAK, PPL and PRX (PubMed:14625392).
CC Identified in a complex with EZR, AHNAK, BFSP1, BFSP2, ANK2, PLEC, VIM
CC and spectrin (By similarity). {ECO:0000250|UniProtKB:O55103,
CC ECO:0000250|UniProtKB:Q63425, ECO:0000250|UniProtKB:Q9BXM0}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q63425}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q63425}. Cell membrane
CC {ECO:0000250|UniProtKB:Q63425}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q63425}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q63425}. Cell junction, adherens junction
CC {ECO:0000305|PubMed:14625392}. Cell junction
CC {ECO:0000250|UniProtKB:O55103}. 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 (By similarity).
CC Associated with the cell membrane during myelination (By similarity).
CC Colocalizes with ACTB at tricellular junctions between eye lens fiber
CC cells (By similarity). {ECO:0000250|UniProtKB:O55103,
CC ECO:0000250|UniProtKB:Q63425}.
CC -!- TISSUE SPECIFICITY: Detected in eye lens (at protein level).
CC {ECO:0000269|PubMed:14625392}.
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:0000250|UniProtKB:Q63425}.
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 -!- SIMILARITY: Belongs to the periaxin family. {ECO:0000305}.
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DR EMBL; DAAA02047080; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DV920320; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_003587302.2; XM_003587254.4.
DR RefSeq; XP_015322984.1; XM_015467498.1.
DR AlphaFoldDB; E1BM58; -.
DR SMR; E1BM58; -.
DR CORUM; E1BM58; -.
DR STRING; 9913.ENSBTAP00000010183; -.
DR PaxDb; E1BM58; -.
DR Ensembl; ENSBTAT00000010183; ENSBTAP00000010183; ENSBTAG00000017333.
DR GeneID; 520296; -.
DR KEGG; bta:520296; -.
DR CTD; 57716; -.
DR VEuPathDB; HostDB:ENSBTAG00000017333; -.
DR VGNC; VGNC:33430; PRX.
DR eggNOG; ENOG502QS7Y; Eukaryota.
DR GeneTree; ENSGT00940000160366; -.
DR HOGENOM; CLU_252008_0_0_1; -.
DR InParanoid; E1BM58; -.
DR OMA; CRVQVPQ; -.
DR OrthoDB; 71329at2759; -.
DR TreeFam; TF350595; -.
DR Proteomes; UP000009136; Chromosome 18.
DR Bgee; ENSBTAG00000017333; Expressed in pigment epithelium of eye and 84 other tissues.
DR GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032287; P:peripheral nervous system myelin maintenance; IBA:GO_Central.
DR GO; GO:0043484; P:regulation of RNA splicing; IBA:GO_Central.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 1: Evidence at protein level;
KW Cell junction; Cell membrane; Cytoplasm; Membrane; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..1349
FT /note="Periaxin"
FT /id="PRO_0000434898"
FT DOMAIN 16..99
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REPEAT 402..406
FT /note="1"
FT /evidence="ECO:0000305"
FT REPEAT 410..414
FT /note="2"
FT /evidence="ECO:0000305"
FT REPEAT 418..422
FT /note="3"
FT /evidence="ECO:0000305"
FT REPEAT 426..430
FT /note="4"
FT /evidence="ECO:0000305"
FT REPEAT 431..435
FT /note="5"
FT /evidence="ECO:0000305"
FT REPEAT 436..440
FT /note="6"
FT /evidence="ECO:0000305"
FT REPEAT 444..448
FT /note="7"
FT /evidence="ECO:0000305"
FT REPEAT 452..456
FT /note="8"
FT /evidence="ECO:0000305"
FT REPEAT 457..461
FT /note="9"
FT /evidence="ECO:0000305"
FT REPEAT 462..466
FT /note="10"
FT /evidence="ECO:0000305"
FT REPEAT 467..471
FT /note="11"
FT /evidence="ECO:0000305"
FT REPEAT 472..476
FT /note="12"
FT /evidence="ECO:0000305"
FT REPEAT 477..481
FT /note="13"
FT /evidence="ECO:0000305"
FT REPEAT 485..489
FT /note="14"
FT /evidence="ECO:0000305"
FT REPEAT 493..497
FT /note="15"
FT /evidence="ECO:0000305"
FT REPEAT 501..505
FT /note="16"
FT /evidence="ECO:0000305"
FT REPEAT 506..510
FT /note="17"
FT /evidence="ECO:0000305"
FT REPEAT 514..518
FT /note="18"
FT /evidence="ECO:0000305"
FT REPEAT 519..523
FT /note="19"
FT /evidence="ECO:0000305"
FT REPEAT 524..528
FT /note="20"
FT /evidence="ECO:0000305"
FT REPEAT 532..536
FT /note="21"
FT /evidence="ECO:0000305"
FT REPEAT 537..549
FT /note="22"
FT /evidence="ECO:0000305"
FT REPEAT 553..557
FT /note="23"
FT /evidence="ECO:0000305"
FT REPEAT 558..562
FT /note="24"
FT /evidence="ECO:0000305"
FT REPEAT 563..567
FT /note="25"
FT /evidence="ECO:0000305"
FT REPEAT 571..575
FT /note="26"
FT /evidence="ECO:0000305"
FT REPEAT 576..580
FT /note="27"
FT /evidence="ECO:0000305"
FT REPEAT 589..593
FT /note="28"
FT /evidence="ECO:0000305"
FT REPEAT 594..598
FT /note="29"
FT /evidence="ECO:0000305"
FT REPEAT 599..603
FT /note="30"
FT /evidence="ECO:0000305"
FT REPEAT 612..616
FT /note="31"
FT /evidence="ECO:0000305"
FT REPEAT 617..621
FT /note="32"
FT /evidence="ECO:0000305"
FT REPEAT 622..626
FT /note="33"
FT /evidence="ECO:0000305"
FT REPEAT 630..634
FT /note="34"
FT /evidence="ECO:0000305"
FT REPEAT 635..639
FT /note="35"
FT /evidence="ECO:0000305"
FT REPEAT 643..647
FT /note="36"
FT /evidence="ECO:0000305"
FT REPEAT 648..652
FT /note="37"
FT /evidence="ECO:0000305"
FT REPEAT 653..657
FT /note="38"
FT /evidence="ECO:0000305"
FT REPEAT 661..665
FT /note="39"
FT /evidence="ECO:0000305"
FT REPEAT 669..673
FT /note="40"
FT /evidence="ECO:0000305"
FT REPEAT 674..678
FT /note="41"
FT /evidence="ECO:0000305"
FT REGION 402..678
FT /note="41 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 /evidence="ECO:0000305"
FT REGION 1207..1349
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 COMPBIAS 1207..1222
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63425"
FT MOD_RES 133
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63425"
FT MOD_RES 794
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63425"
FT MOD_RES 974
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63425"
FT MOD_RES 1236
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O55103"
FT MOD_RES 1240
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O55103"
FT MOD_RES 1242
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O55103"
FT MOD_RES 1289
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63425"
FT MOD_RES 1295
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O55103"
FT MOD_RES 1327
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O55103"
SQ SEQUENCE 1349 AA; 142695 MW; AE24F403249AA877 CRC64;
MEARSRSAEE LRRAELVEII VETEAQTGVS GINVAGGGKE GIFVRDLRED SPAARSLSLQ
EGDQLLSARV FFENFKYEDA LRLLQCAEPY KVSFCLKRTV PTGDLALRPG TVAGYEIKGP
RAKVAKLNIQ SLSPVKKKKM VMPGALGAPA DLAPVDVEFS FPKFSRLRRG LKAEAVEGPV
PAAPTRRRLQ LPRLRVREVA EEAQVARLAA AAPPPRKAKA EAEVAAGPRF TAPQVELVGP
RLPGAEVGVP QVPAPKREAA PAVEPAAVGI QVPQVELPSL PSLPALPTLP CLETREGAVA
VTVPTLDVAA PTVGVDLALP GAEVEPREEV PEVALKMPRL SFPRFGARAK EAAEAKVKGP
KLRMPTFGLS LLEPRPAVPE APESKLKLPT IKIPSFGIGV SPPEVKVPKG PEVKPPKVPE
VKLPKMPEPV LPEVRLPEVE LPKVSEMKLP KVPEMAVPEV RLPEVQLPKV PEMKLPEVKL
PKVPEMAVPE VHLPEVQLPK VPEMKLPEVK LPKVPEMAVP EVRLPEVQLP KVPEMKLPKV
PEMKCPEMKL PKVPEMAVPE VRLPEVQLPK VPEVKLPEVK LPEVKLPKVP EMAVPEVHLP
EVQLPKVSEM KVPDVKLPEV KLPEIKLPKV PEMVVPDVHL PQVHLPKVSE MRLPEVQAPK
VPEVHLPKAP EVKLPKAPEA QLKAARVEEA EGMDFGFKMP KMTLPKLGRA ESPSQGKPGE
AGAEVSGKLV TLPCLQPEVG SEARVGVPRL TLPSVELDLP GALGLEGQAA AAEVGKGEQA
EAAGVGEVAF RLPSVEIVTP QLPTLDEGQA EVTEAKVKLS SKFSLPKFGL SGPKVTKPEA
EGAGRAAKLK VSKFAISLPR ARVGTEVEAK GTEEAGLLPA LDLSIPQLSL DSHLPTGKAE
VAGADIKLKG PKFGLPKFGV RGRDTEAGEL VPGAAELEGK SRGWDGKVKM PKLKMPSFGL
ARGKEADISG GQVSPGEKPE STAVQLKIPE VELVTLGAQE EGRVEEEAAG SRGRLAGLQV
SPAKQVGTEA QDGGLRMPLG ISLPQVELTG FREATPGQQA ESSAPPAEGT AGYRVHVPQV
TLALPGAQAV GGELLVGEGV FKMPSVTVPQ LELDVGLSRE VQDGEAATSE GGLKLKVPTL
GARAGAGAEG PSDQSAGAER TFHLSLPDVE LSPPAVGTHA EYQVAEGEGD AGHKLKVRLP
RFGLARAKEG AEEGEKAKSP KLKLPHVGFS QSEAVSGEGS PSPEEEDVEG GGEGASGRRG
RVRVRLPRVG LAAPSKASRG QEGKAAPKSP SGEKSPKFRF PRVSLSPKTR GGSGDQDEGG
FRVRLPSVGF SETGPPGPTR MEGAQAAVI
