PRAX_HUMAN
ID PRAX_HUMAN Reviewed; 1461 AA.
AC Q9BXM0; Q9BXL9; Q9HCF2;
DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 2.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Periaxin;
GN Name=PRX; Synonyms=KIAA1620;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, VARIANTS
RP THR-406; GLN-495; ALA-882; MET-921; GLU-935; ARG-1083; ARG-1132; LYS-1259;
RP GLU-1359 DEL AND CYS-1411, AND INVOLVEMENT IN DSS.
RX PubMed=11133365; DOI=10.1086/318208;
RA Boerkoel C.F., Takashima H., Stankiewicz P., Garcia C.A., Leber S.M.,
RA Rhee-Morris L., Lupski J.R.;
RT "Periaxin mutations cause recessive Dejerine-Sottas neuropathy.";
RL Am. J. Hum. Genet. 68:325-333(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT ALA-882.
RC TISSUE=Brain;
RX PubMed=10997877; DOI=10.1093/dnares/7.4.271;
RA Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:273-281(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ARG-1132.
RC TISSUE=PNS;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP DISEASE, AND TISSUE SPECIFICITY.
RX PubMed=11157804; DOI=10.1093/hmg/10.4.415;
RA Guilbot A., Williams A., Ravise N., Verny C., Brice A., Sherman D.L.,
RA Brophy P.J., LeGuern E., Delague V., Bareil C., Megarbane A., Claustres M.;
RT "A mutation in periaxin is responsible for CMT4F, an autosomal recessive
RT form of Charcot-Marie-Tooth disease.";
RL Hum. Mol. Genet. 10:415-421(2001).
RN [6]
RP SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF 81-LEU--LEU-83, AND NUCLEAR
RP EXPORT SIGNAL.
RX PubMed=24633211; DOI=10.1371/journal.pone.0091953;
RA Shi Y., Zhang L., Yang T.;
RT "Nuclear export of L-periaxin, mediated by its nuclear export signal in the
RT PDZ domain.";
RL PLoS ONE 9:E91953-E91953(2014).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 14-104, AND SUBUNIT.
RX PubMed=24675079; DOI=10.1074/jbc.m114.554816;
RA Han H., Kursula P.;
RT "Periaxin and AHNAK nucleoprotein 2 form intertwined homodimers through
RT domain swapping.";
RL J. Biol. Chem. 289:14121-14131(2014).
RN [8]
RP VARIANT CMT4F ASN-651.
RX PubMed=22847150; DOI=10.1007/s10048-012-0338-5;
RA Tokunaga S., Hashiguchi A., Yoshimura A., Maeda K., Suzuki T., Haruki H.,
RA Nakamura T., Okamoto Y., Takashima H.;
RT "Late-onset Charcot-Marie-Tooth disease 4F caused by periaxin gene
RT mutation.";
RL Neurogenetics 13:359-365(2012).
RN [9]
RP VARIANTS ALA-525 AND GLN-1335.
RX PubMed=24627108; DOI=10.1007/s00415-014-7289-8;
RA Schabhuettl M., Wieland T., Senderek J., Baets J., Timmerman V.,
RA De Jonghe P., Reilly M.M., Stieglbauer K., Laich E., Windhager R., Erwa W.,
RA Trajanoski S., Strom T.M., Auer-Grumbach M.;
RT "Whole-exome sequencing in patients with inherited neuropathies: outcome
RT and challenges.";
RL J. Neurol. 261:970-982(2014).
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:24675079). 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 (By similarity).
CC Identified in a complex with EZR, AHNAK, BFSP1, BFSP2, ANK2, PLEC, VIM
CC and spectrin (By similarity). {ECO:0000250|UniProtKB:E1BM58,
CC ECO:0000250|UniProtKB:O55103, ECO:0000250|UniProtKB:Q63425,
CC ECO:0000269|PubMed:24675079}.
CC -!- INTERACTION:
CC Q9BXM0; P16333: NCK1; NbExp=2; IntAct=EBI-1753064, EBI-389883;
CC Q9BXM0; Q9NYB0: TERF2IP; NbExp=2; IntAct=EBI-1753064, EBI-750109;
CC Q9BXM0; P07947: YES1; NbExp=4; IntAct=EBI-1753064, EBI-515331;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane
CC {ECO:0000250|UniProtKB:O55103}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:O55103}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:O55103}. Nucleus {ECO:0000269|PubMed:24633211}.
CC Cytoplasm {ECO:0000269|PubMed:24633211}. Note=Detected in the Schwann
CC cell nucleus prior to the onset of myelination. Detected in Schwann
CC cells at periaxonal myelin membranes. Associated with the cell membrane
CC during myelination. {ECO:0000250|UniProtKB:O55103}.
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=3;
CC Name=1; Synonyms=L-periaxin;
CC IsoId=Q9BXM0-1; Sequence=Displayed;
CC Name=2; Synonyms=S-periaxin;
CC IsoId=Q9BXM0-2; Sequence=VSP_004363, VSP_004364;
CC Name=3;
CC IsoId=Q9BXM0-3; Sequence=VSP_040352;
CC -!- TISSUE SPECIFICITY: Detected in spinal cord (PubMed:11133365). Isoform
CC 1 and isoform 2 are found in sciatic nerve and Schwann cells
CC (PubMed:11157804). {ECO:0000269|PubMed:11133365,
CC ECO:0000269|PubMed:11157804}.
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 (PubMed:24633211). The N-terminal region including the PDZ domain is
CC required for the formation of Cajal bands on myelinated nerves.
CC {ECO:0000250|UniProtKB:O55103, ECO:0000269|PubMed:24633211}.
CC -!- DISEASE: Dejerine-Sottas syndrome (DSS) [MIM:145900]: A severe
CC degenerating neuropathy of the demyelinating Charcot-Marie-Tooth
CC disease category, with onset by age 2 years. Characterized by motor and
CC sensory neuropathy with very slow nerve conduction velocities,
CC increased cerebrospinal fluid protein concentrations, hypertrophic
CC nerve changes, delayed age of walking as well as areflexia. There are
CC both autosomal dominant and autosomal recessive forms of Dejerine-
CC Sottas syndrome. {ECO:0000269|PubMed:11133365}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- DISEASE: Charcot-Marie-Tooth disease 4F (CMT4F) [MIM:614895]: A
CC recessive demyelinating form of Charcot-Marie-Tooth disease, a disorder
CC of the peripheral nervous system, characterized by progressive weakness
CC and atrophy, initially of the peroneal muscles and later of the distal
CC muscles of the arms. Charcot-Marie-Tooth disease is classified in two
CC main groups on the basis of electrophysiologic properties and
CC histopathology: primary peripheral demyelinating neuropathies
CC (designated CMT1 when they are dominantly inherited) and primary
CC peripheral axonal neuropathies (CMT2). Demyelinating neuropathies are
CC characterized by severely reduced nerve conduction velocities (less
CC than 38 m/sec), segmental demyelination and remyelination with onion
CC bulb formations on nerve biopsy, slowly progressive distal muscle
CC atrophy and weakness, absent deep tendon reflexes, and hollow feet. By
CC convention autosomal recessive forms of demyelinating Charcot-Marie-
CC Tooth disease are designated CMT4. CMT4F is characterized by distal
CC sensory impairment and distal muscle weakness and atrophy affecting the
CC lower more than the upper limbs. The age at onset is variable and can
CC range from childhood to adult years. When the onset is in infancy, the
CC phenotype is characterized as Dejerine-Sottas syndrome.
CC {ECO:0000269|PubMed:22847150}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the periaxin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB13446.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB13446.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Inherited peripheral neuropathies mutation db;
CC URL="https://uantwerpen.vib.be/CMTMutations";
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DR EMBL; AF321191; AAK19279.1; -; mRNA.
DR EMBL; AF321192; AAK19280.1; -; mRNA.
DR EMBL; AB046840; BAB13446.1; ALT_SEQ; mRNA.
DR EMBL; AC010271; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC067266; AAH67266.1; -; mRNA.
DR CCDS; CCDS12556.1; -. [Q9BXM0-2]
DR CCDS; CCDS33028.1; -. [Q9BXM0-1]
DR RefSeq; NP_066007.1; NM_020956.2. [Q9BXM0-2]
DR RefSeq; NP_870998.2; NM_181882.2. [Q9BXM0-1]
DR RefSeq; XP_011525473.1; XM_011527171.2. [Q9BXM0-1]
DR PDB; 4CMZ; X-ray; 2.70 A; A/B/C=14-104.
DR PDBsum; 4CMZ; -.
DR AlphaFoldDB; Q9BXM0; -.
DR SMR; Q9BXM0; -.
DR BioGRID; 121739; 12.
DR IntAct; Q9BXM0; 13.
DR STRING; 9606.ENSP00000326018; -.
DR iPTMnet; Q9BXM0; -.
DR PhosphoSitePlus; Q9BXM0; -.
DR BioMuta; PRX; -.
DR DMDM; 317373270; -.
DR jPOST; Q9BXM0; -.
DR MassIVE; Q9BXM0; -.
DR PaxDb; Q9BXM0; -.
DR PeptideAtlas; Q9BXM0; -.
DR PRIDE; Q9BXM0; -.
DR ProteomicsDB; 79452; -. [Q9BXM0-1]
DR ProteomicsDB; 79453; -. [Q9BXM0-2]
DR ProteomicsDB; 79454; -. [Q9BXM0-3]
DR Antibodypedia; 959; 68 antibodies from 16 providers.
DR DNASU; 57716; -.
DR Ensembl; ENST00000291825.11; ENSP00000291825.6; ENSG00000105227.16. [Q9BXM0-2]
DR Ensembl; ENST00000324001.8; ENSP00000326018.6; ENSG00000105227.16. [Q9BXM0-1]
DR Ensembl; ENST00000673881.1; ENSP00000501070.1; ENSG00000105227.16. [Q9BXM0-3]
DR Ensembl; ENST00000674773.1; ENSP00000502579.1; ENSG00000105227.16. [Q9BXM0-3]
DR GeneID; 57716; -.
DR KEGG; hsa:57716; -.
DR MANE-Select; ENST00000324001.8; ENSP00000326018.6; NM_181882.3; NP_870998.2.
DR UCSC; uc002onr.4; human. [Q9BXM0-1]
DR CTD; 57716; -.
DR DisGeNET; 57716; -.
DR GeneCards; PRX; -.
DR GeneReviews; PRX; -.
DR HGNC; HGNC:13797; PRX.
DR HPA; ENSG00000105227; Tissue enhanced (lung).
DR MalaCards; PRX; -.
DR MIM; 145900; phenotype.
DR MIM; 605725; gene.
DR MIM; 614895; phenotype.
DR neXtProt; NX_Q9BXM0; -.
DR OpenTargets; ENSG00000105227; -.
DR Orphanet; 99952; Charcot-Marie-Tooth disease type 4F.
DR Orphanet; 64748; Dejerine-Sottas syndrome.
DR PharmGKB; PA33843; -.
DR VEuPathDB; HostDB:ENSG00000105227; -.
DR eggNOG; ENOG502QS7Y; Eukaryota.
DR GeneTree; ENSGT00940000160366; -.
DR HOGENOM; CLU_1758219_0_0_1; -.
DR InParanoid; Q9BXM0; -.
DR OMA; CRVQVPQ; -.
DR OrthoDB; 1621899at2759; -.
DR PhylomeDB; Q9BXM0; -.
DR TreeFam; TF350595; -.
DR PathwayCommons; Q9BXM0; -.
DR Reactome; R-HSA-9619665; EGR2 and SOX10-mediated initiation of Schwann cell myelination. [Q9BXM0-1]
DR SignaLink; Q9BXM0; -.
DR BioGRID-ORCS; 57716; 14 hits in 1082 CRISPR screens.
DR ChiTaRS; PRX; human.
DR GeneWiki; PRX_(gene); -.
DR GenomeRNAi; 57716; -.
DR Pharos; Q9BXM0; Tbio.
DR PRO; PR:Q9BXM0; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9BXM0; protein.
DR Bgee; ENSG00000105227; Expressed in olfactory bulb and 180 other tissues.
DR ExpressionAtlas; Q9BXM0; baseline and differential.
DR Genevisible; Q9BXM0; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0008366; P:axon ensheathment; NAS:UniProtKB.
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 3D-structure; Alternative splicing; Cell junction; Cell membrane;
KW Charcot-Marie-Tooth disease; Cytoplasm; Dejerine-Sottas syndrome;
KW Disease variant; Membrane; Neurodegeneration; Neuropathy; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..1461
FT /note="Periaxin"
FT /id="PRO_0000058563"
FT DOMAIN 16..99
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REPEAT 431..435
FT /note="1"
FT REPEAT 439..443
FT /note="2"
FT REPEAT 447..451
FT /note="3"
FT REPEAT 455..459
FT /note="4"
FT REPEAT 463..467
FT /note="5"
FT REPEAT 468..472
FT /note="6"
FT REPEAT 473..477
FT /note="7"
FT REPEAT 481..485
FT /note="8"
FT REPEAT 486..490
FT /note="9"
FT REPEAT 494..498
FT /note="10"
FT REPEAT 499..503
FT /note="11"
FT REPEAT 507..511
FT /note="12"
FT REPEAT 512..516
FT /note="13"
FT REPEAT 520..524
FT /note="14"
FT REPEAT 525..529
FT /note="15"
FT REPEAT 533..537
FT /note="16"
FT REPEAT 538..542
FT /note="17"
FT REPEAT 546..550
FT /note="18"
FT REPEAT 551..555
FT /note="19"
FT REPEAT 559..563
FT /note="20"
FT REPEAT 564..568
FT /note="21"
FT REPEAT 572..576
FT /note="22"
FT REPEAT 577..581
FT /note="23"
FT REPEAT 582..586
FT /note="24"
FT REPEAT 590..594
FT /note="25"
FT REPEAT 595..599
FT /note="26"
FT REPEAT 600..604
FT /note="27"
FT REPEAT 608..612
FT /note="28"
FT REPEAT 613..617
FT /note="29"
FT REPEAT 618..622
FT /note="30"
FT REPEAT 626..630
FT /note="31"
FT REPEAT 631..635
FT /note="32"
FT REPEAT 636..640
FT /note="33"
FT REPEAT 644..648
FT /note="34"
FT REPEAT 649..653
FT /note="35"
FT REPEAT 654..658
FT /note="36"
FT REPEAT 662..666
FT /note="37"
FT REPEAT 670..674
FT /note="38"
FT REPEAT 675..679
FT /note="39"
FT REPEAT 683..687
FT /note="40"
FT REPEAT 688..692
FT /note="41"
FT REPEAT 696..700
FT /note="42"
FT REPEAT 701..705
FT /note="43"
FT REPEAT 706..710
FT /note="44"
FT REPEAT 714..718
FT /note="45"
FT REPEAT 719..723
FT /note="46"
FT REPEAT 724..728
FT /note="47"
FT REPEAT 732..736
FT /note="48"
FT REPEAT 737..741
FT /note="49"
FT REPEAT 742..746
FT /note="50"
FT REPEAT 750..754
FT /note="51"
FT REPEAT 755..759
FT /note="52"
FT REPEAT 760..764
FT /note="53"
FT REPEAT 771..775
FT /note="54"
FT REPEAT 779..783
FT /note="55"
FT REGION 431..783
FT /note="55 X 5 AA approximate tandem repeats of [LVMAG]-
FT [PSREQC]-[EDKL]-[LIVMAP]-[AQKHRPE]; that may have a
FT tripeptide spacer of [LV]-P-[KER]"
FT REGION 1318..1461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 70..84
FT /note="Nuclear export signal"
FT /evidence="ECO:0000305|PubMed:24633211"
FT MOTIF 118..196
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 1349..1363
FT /note="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 900
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63425"
FT MOD_RES 1082
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63425"
FT MOD_RES 1349
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O55103"
FT MOD_RES 1351
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O55103"
FT MOD_RES 1363
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O55103"
FT MOD_RES 1401
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63425"
FT MOD_RES 1407
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O55103"
FT MOD_RES 1439
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O55103"
FT VAR_SEQ 1..139
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10997877"
FT /id="VSP_040352"
FT VAR_SEQ 128..147
FT /note="NIQSLSPVKKKKMVPGALGV -> VRVLSPAPALDCPSDPVSAP (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:11133365"
FT /id="VSP_004363"
FT VAR_SEQ 148..1461
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11133365"
FT /id="VSP_004364"
FT VARIANT 406
FT /note="A -> T (in dbSNP:rs117336941)"
FT /evidence="ECO:0000269|PubMed:11133365"
FT /id="VAR_013056"
FT VARIANT 495
FT /note="E -> Q (in dbSNP:rs146789340)"
FT /evidence="ECO:0000269|PubMed:11133365"
FT /id="VAR_013057"
FT VARIANT 525
FT /note="V -> A (in dbSNP:rs149715830)"
FT /evidence="ECO:0000269|PubMed:24627108"
FT /id="VAR_073295"
FT VARIANT 651
FT /note="D -> N (in CMT4F; dbSNP:rs3814290)"
FT /evidence="ECO:0000269|PubMed:22847150"
FT /id="VAR_069093"
FT VARIANT 882
FT /note="V -> A (in dbSNP:rs268671)"
FT /evidence="ECO:0000269|PubMed:10997877,
FT ECO:0000269|PubMed:11133365"
FT /id="VAR_013058"
FT VARIANT 921
FT /note="I -> M (in dbSNP:rs268673)"
FT /evidence="ECO:0000269|PubMed:11133365"
FT /id="VAR_013059"
FT VARIANT 935
FT /note="K -> E"
FT /evidence="ECO:0000269|PubMed:11133365"
FT /id="VAR_013060"
FT VARIANT 1083
FT /note="P -> R (in dbSNP:rs3745202)"
FT /evidence="ECO:0000269|PubMed:11133365"
FT /id="VAR_013061"
FT VARIANT 1132
FT /note="G -> R (in dbSNP:rs268674)"
FT /evidence="ECO:0000269|PubMed:11133365,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_013062"
FT VARIANT 1259
FT /note="E -> K (in dbSNP:rs751742049)"
FT /evidence="ECO:0000269|PubMed:11133365"
FT /id="VAR_013063"
FT VARIANT 1335
FT /note="R -> Q (found in a patient with a complex hereditary
FT motor and sensory neuropathy form associated with
FT dysarthria, joints hypermobility and cerebellar signs;
FT unknown pathological significance; dbSNP:rs1384489319)"
FT /evidence="ECO:0000269|PubMed:24627108"
FT /id="VAR_073296"
FT VARIANT 1359
FT /note="Missing"
FT /evidence="ECO:0000269|PubMed:11133365"
FT /id="VAR_013064"
FT VARIANT 1411
FT /note="R -> C (in dbSNP:rs533966999)"
FT /evidence="ECO:0000269|PubMed:11133365"
FT /id="VAR_013065"
FT MUTAGEN 81..83
FT /note="LRL->QRQ: Nearly abolishes export from the nucleus."
FT /evidence="ECO:0000269|PubMed:24633211"
FT STRAND 18..22
FT /evidence="ECO:0007829|PDB:4CMZ"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:4CMZ"
FT STRAND 32..38
FT /evidence="ECO:0007829|PDB:4CMZ"
FT STRAND 41..47
FT /evidence="ECO:0007829|PDB:4CMZ"
FT HELIX 52..56
FT /evidence="ECO:0007829|PDB:4CMZ"
FT STRAND 64..71
FT /evidence="ECO:0007829|PDB:4CMZ"
FT HELIX 77..87
FT /evidence="ECO:0007829|PDB:4CMZ"
FT STRAND 90..99
FT /evidence="ECO:0007829|PDB:4CMZ"
SQ SEQUENCE 1461 AA; 154905 MW; 41F00C50B1DC3C7A CRC64;
MEARSRSAEE LRRAELVEII VETEAQTGVS GINVAGGGKE GIFVRELRED SPAARSLSLQ
EGDQLLSARV FFENFKYEDA LRLLQCAEPY KVSFCLKRTV PTGDLALRPG TVSGYEIKGP
RAKVAKLNIQ SLSPVKKKKM VPGALGVPAD LAPVDVEFSF PKFSRLRRGL KAEAVKGPVP
AAPARRRLQL PRLRVREVAE EAQAARLAAA APPPRKAKVE AEVAAGARFT APQVELVGPR
LPGAEVGVPQ VSAPKAAPSA EAAGGFALHL PTLGLGAPAP PAVEAPAVGI QVPQVELPAL
PSLPTLPTLP CLETREGAVS VVVPTLDVAA PTVGVDLALP GAEVEARGEA PEVALKMPRL
SFPRFGARAK EVAEAKVAKV SPEARVKGPR LRMPTFGLSL LEPRPAAPEV VESKLKLPTI
KMPSLGIGVS GPEVKVPKGP EVKLPKAPEV KLPKVPEAAL PEVRLPEVEL PKVSEMKLPK
VPEMAVPEVR LPEVELPKVS EMKLPKVPEM AVPEVRLPEV QLLKVSEMKL PKVPEMAVPE
VRLPEVQLPK VSEMKLPEVS EVAVPEVRLP EVQLPKVPEM KVPEMKLPKV PEMKLPEMKL
PEVQLPKVPE MAVPDVHLPE VQLPKVPEMK LPEMKLPEVK LPKVPEMAVP DVHLPEVQLP
KVPEMKLPKM PEMAVPEVRL PEVQLPKVSE MKLPKVPEMA VPDVHLPEVQ LPKVCEMKVP
DMKLPEIKLP KVPEMAVPDV HLPEVQLPKV SEIRLPEMQV PKVPDVHLPK APEVKLPRAP
EVQLKATKAE QAEGMEFGFK MPKMTMPKLG RAESPSRGKP GEAGAEVSGK LVTLPCLQPE
VDGEAHVGVP SLTLPSVELD LPGALGLQGQ VPAAKMGKGE RVEGPEVAAG VREVGFRVPS
VEIVTPQLPA VEIEEGRLEM IETKVKPSSK FSLPKFGLSG PKVAKAEAEG AGRATKLKVS
KFAISLPKAR VGAEAEAKGA GEAGLLPALD LSIPQLSLDA HLPSGKVEVA GADLKFKGPR
FALPKFGVRG RDTEAAELVP GVAELEGKGW GWDGRVKMPK LKMPSFGLAR GKEAEVQGDR
ASPGEKAEST AVQLKIPEVE LVTLGAQEEG RAEGAVAVSG MQLSGLKVST AGQVVTEGHD
AGLRMPPLGI SLPQVELTGF GEAGTPGQQA QSTVPSAEGT AGYRVQVPQV TLSLPGAQVA
GGELLVGEGV FKMPTVTVPQ LELDVGLSRE AQAGEAATGE GGLRLKLPTL GARARVGGEG
AEEQPPGAER TFCLSLPDVE LSPSGGNHAE YQVAEGEGEA GHKLKVRLPR FGLVRAKEGA
EEGEKAKSPK LRLPRVGFSQ SEMVTGEGSP SPEEEEEEEE EGSGEGASGR RGRVRVRLPR
VGLAAPSKAS RGQEGDAAPK SPVREKSPKF RFPRVSLSPK ARSGSGDQEE GGLRVRLPSV
GFSETGAPGP ARMEGAQAAA V
