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 27-MAR-2024, entry version 193. 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 -!- 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"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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. 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; 16. DR IntAct; Q9BXM0; 11. DR STRING; 9606.ENSP00000326018; -. DR iPTMnet; Q9BXM0; -. DR PhosphoSitePlus; Q9BXM0; -. DR BioMuta; PRX; -. DR DMDM; 317373270; -. DR jPOST; Q9BXM0; -. DR MassIVE; Q9BXM0; -. DR PaxDb; 9606-ENSP00000326018; -. DR PeptideAtlas; Q9BXM0; -. DR ProteomicsDB; 79452; -. [Q9BXM0-1] DR ProteomicsDB; 79453; -. [Q9BXM0-2] DR ProteomicsDB; 79454; -. [Q9BXM0-3] DR Antibodypedia; 959; 85 antibodies from 17 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 AGR; HGNC:13797; -. 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; RKFEMPK; -. DR OrthoDB; 3061191at2759; -. 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; 16 hits in 1160 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 182 other cell types or tissues. DR ExpressionAtlas; Q9BXM0; baseline and differential. 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 CDD; cd00992; PDZ_signaling; 1. DR Gene3D; 2.30.42.10; -; 1. DR InterPro; IPR001478; PDZ. DR InterPro; IPR036034; PDZ_sf. DR PANTHER; PTHR23348:SF42; PERIAXIN; 1. DR PANTHER; PTHR23348; PERIAXIN/AHNAK; 1. DR SMART; SM00228; PDZ; 1. DR SUPFAM; SSF50156; PDZ domain-like; 1. DR PROSITE; PS50106; PDZ; 1. DR Genevisible; Q9BXM0; HS. 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 with dysarthria, joints FT hypermobility and cerebellar signs; uncertain significance; FT 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 //