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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
 
 
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