GenomeNet

Database: UniProt
Entry: PAX6_RAT
LinkDB: PAX6_RAT
Original site: PAX6_RAT 
ID   PAX6_RAT                Reviewed;         422 AA.
AC   P63016; A1A5N7; P32117; P70601; Q62222; Q64037; Q6QHS5; Q701Q8;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   31-AUG-2004, sequence version 1.
DT   27-MAR-2024, entry version 155.
DE   RecName: Full=Paired box protein Pax-6;
DE   AltName: Full=Oculorhombin;
GN   Name=Pax6; Synonyms=Pax-6, Sey;
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 5A), SUBCELLULAR LOCATION,
RP   DEVELOPMENTAL STAGE, AND ALTERNATIVE SPLICING.
RC   STRAIN=Sprague-Dawley; TISSUE=Brain;
RX   PubMed=24952136; DOI=10.1016/j.gene.2014.06.032;
RA   Wei F., Li M., Cheng S.Y., Wen L., Liu M.H., Shuai J.;
RT   "Cloning, expression, and functional characterization of the rat Pax6 5a
RT   orthologous splicing variant.";
RL   Gene 547:169-174(2014).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Gimlich R., Arnold G.S., Wawersik S., Maas R., Wong G.;
RT   "Pax-6 is required for pancreatic islet development.";
RL   Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5A).
RC   STRAIN=New England Deaconess Hospital, and Sprague-Dawley;
RA   Karkour A., Wolf G.M., Walther R.;
RL   Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Heart;
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   PARTIAL NUCLEOTIDE SEQUENCE [MRNA], AND INVOLVEMENT IN SEY.
RC   STRAIN=Sprague-Dawley; TISSUE=Embryo;
RX   PubMed=7981749; DOI=10.1038/ng0493-299;
RA   Matsuo T., Osumi-Yamashita N., Noji S., Ohuchi H., Koyama E., Myokai F.,
RA   Matsuo N., Taniguchi S., Doi H., Iseki S., Ninomiya Y., Fujiwara M.,
RA   Wantanabe T., Eto K.;
RT   "A mutation in the Pax-6 gene in rat small eye is associated with impaired
RT   migration of midbrain crest cells.";
RL   Nat. Genet. 3:299-304(1993).
RN   [6]
RP   FUNCTION.
RX   PubMed=11880342; DOI=10.1242/dev.129.6.1327;
RA   Takahashi M., Osumi N.;
RT   "Pax6 regulates specification of ventral neurone subtypes in the hindbrain
RT   by establishing progenitor domains.";
RL   Development 129:1327-1338(2002).
RN   [7]
RP   INDUCTION.
RX   PubMed=24114637; DOI=10.5114/fn.2013.37704;
RA   Steliga A., Waskow M., Karwacki Z., Wojcik S., Lietzau G., Klejbor I.,
RA   Kowianski P.;
RT   "Transcription factor Pax6 is expressed by astroglia after transient brain
RT   ischemia in the rat model.";
RL   Folia Neuropathol. 51:203-213(2013).
CC   -!- FUNCTION: Transcription factor with important functions in the
CC       development of the eye, nose, central nervous system and pancreas.
CC       Required for the differentiation of pancreatic islet alpha cells.
CC       Competes with PAX4 in binding to a common element in the glucagon,
CC       insulin and somatostatin promoters (By similarity). Regulates
CC       specification of the ventral neuron subtypes by establishing the
CC       correct progenitor domains. Acts as a transcriptional repressor of
CC       NFATC1-mediated gene expression (By similarity). {ECO:0000250,
CC       ECO:0000250|UniProtKB:P63015, ECO:0000269|PubMed:11880342}.
CC   -!- SUBUNIT: Interacts with MAF and MAFB (By similarity). Interacts with
CC       TRIM11; this interaction leads to ubiquitination and proteasomal
CC       degradation, as well as inhibition of transactivation, possibly in part
CC       by preventing PAX6 binding to consensus DNA sequences (By similarity).
CC       Interacts with TLE6/GRG6 (By similarity).
CC       {ECO:0000250|UniProtKB:P63015}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P63015}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 1]: Nucleus {ECO:0000255|PROSITE-
CC       ProRule:PRU00108, ECO:0000255|PROSITE-ProRule:PRU00381,
CC       ECO:0000269|PubMed:24952136}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 5a]: Nucleus
CC       {ECO:0000269|PubMed:24952136}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P63016-1; Sequence=Displayed;
CC       Name=5a; Synonyms=Pax6-5a {ECO:0000303|PubMed:24952136};
CC         IsoId=P63016-2; Sequence=VSP_011531;
CC   -!- DEVELOPMENTAL STAGE: [Isoform 1]: Expressed in the embryonic headfolds
CC       and to a lesser extent in the trunk of neurula at 10 dpc.
CC       {ECO:0000269|PubMed:24952136}.
CC   -!- DEVELOPMENTAL STAGE: [Isoform 5a]: Expressed in the embryonic headfolds
CC       and to a lesser extent in the trunk of neurula at 10 dpc.
CC       {ECO:0000269|PubMed:24952136}.
CC   -!- INDUCTION: Up-regulated in response to transient cerebral ischemia in
CC       cerebral cortex, striatum and subcortical white matter fibers in the
CC       ischemic region starting from 24 hours after initiating the ischemia.
CC       {ECO:0000269|PubMed:24114637}.
CC   -!- PTM: Ubiquitinated by TRIM11, leading to ubiquitination and proteasomal
CC       degradation. {ECO:0000250}.
CC   -!- DISEASE: Note=Defects in Pax6 are the cause of a condition known as
CC       small eye (Sey) which results in the complete lack of eyes and nasal
CC       primordia. {ECO:0000269|PubMed:7981749}.
CC   -!- SIMILARITY: Belongs to the paired homeobox family. {ECO:0000305}.
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; U69644; AAB09042.1; -; mRNA.
DR   EMBL; AJ627631; CAF29075.1; -; mRNA.
DR   EMBL; AY540905; AAS48919.1; -; mRNA.
DR   EMBL; AY540906; AAS48920.1; -; mRNA.
DR   EMBL; BC128741; AAI28742.1; -; mRNA.
DR   EMBL; S74393; AAB32671.1; ALT_TERM; mRNA.
DR   PIR; S36166; S36166.
DR   RefSeq; NP_037133.1; NM_013001.2. [P63016-1]
DR   RefSeq; XP_006234695.1; XM_006234633.3. [P63016-2]
DR   RefSeq; XP_006234696.1; XM_006234634.3. [P63016-2]
DR   RefSeq; XP_006234697.1; XM_006234635.3. [P63016-2]
DR   RefSeq; XP_006234698.1; XM_006234636.3. [P63016-2]
DR   RefSeq; XP_017446983.1; XM_017591494.1.
DR   RefSeq; XP_017446984.1; XM_017591495.1.
DR   AlphaFoldDB; P63016; -.
DR   SMR; P63016; -.
DR   BioGRID; 247541; 1.
DR   STRING; 10116.ENSRNOP00000071013; -.
DR   PhosphoSitePlus; P63016; -.
DR   PaxDb; 10116-ENSRNOP00000006302; -.
DR   Ensembl; ENSRNOT00000005882.6; ENSRNOP00000005882.3; ENSRNOG00000004410.9. [P63016-1]
DR   Ensembl; ENSRNOT00000089525.2; ENSRNOP00000071013.2; ENSRNOG00000004410.9. [P63016-2]
DR   Ensembl; ENSRNOT00055039364; ENSRNOP00055031943; ENSRNOG00055022908. [P63016-1]
DR   Ensembl; ENSRNOT00060003572; ENSRNOP00060002461; ENSRNOG00060002262. [P63016-1]
DR   Ensembl; ENSRNOT00065025746; ENSRNOP00065020235; ENSRNOG00065015473. [P63016-1]
DR   GeneID; 25509; -.
DR   KEGG; rno:25509; -.
DR   UCSC; RGD:3258; rat. [P63016-1]
DR   AGR; RGD:3258; -.
DR   CTD; 5080; -.
DR   RGD; 3258; Pax6.
DR   eggNOG; KOG0849; Eukaryota.
DR   GeneTree; ENSGT00940000155391; -.
DR   InParanoid; P63016; -.
DR   OrthoDB; 5398393at2759; -.
DR   PhylomeDB; P63016; -.
DR   TreeFam; TF320146; -.
DR   PRO; PR:P63016; -.
DR   Proteomes; UP000002494; Chromosome 3.
DR   Bgee; ENSRNOG00000004410; Expressed in cerebellum and 8 other cell types or tissues.
DR   ExpressionAtlas; P63016; baseline and differential.
DR   Genevisible; P63016; RN.
DR   GO; GO:0000785; C:chromatin; IDA:BHF-UCL.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; ISO:RGD.
DR   GO; GO:0003682; F:chromatin binding; ISO:RGD.
DR   GO; GO:0031490; F:chromatin DNA binding; ISO:RGD.
DR   GO; GO:0070410; F:co-SMAD binding; ISO:RGD.
DR   GO; GO:0003677; F:DNA binding; ISO:RGD.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:RGD.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; ISO:RGD.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:BHF-UCL.
DR   GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:RGD.
DR   GO; GO:0003690; F:double-stranded DNA binding; IDA:RGD.
DR   GO; GO:0035035; F:histone acetyltransferase binding; ISO:RGD.
DR   GO; GO:0071837; F:HMG box domain binding; ISO:RGD.
DR   GO; GO:0003680; F:minor groove of adenine-thymine-rich DNA binding; IDA:RGD.
DR   GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR   GO; GO:0070412; F:R-SMAD binding; ISO:RGD.
DR   GO; GO:0003723; F:RNA binding; ISO:RGD.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:BHF-UCL.
DR   GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; ISO:RGD.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:RGD.
DR   GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:RGD.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB.
DR   GO; GO:0001221; F:transcription coregulator binding; ISO:RGD.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD.
DR   GO; GO:0048856; P:anatomical structure development; IBA:GO_Central.
DR   GO; GO:0009952; P:anterior/posterior pattern specification; ISO:RGD.
DR   GO; GO:0048708; P:astrocyte differentiation; IMP:RGD.
DR   GO; GO:0007411; P:axon guidance; ISO:RGD.
DR   GO; GO:0007409; P:axonogenesis; ISO:RGD.
DR   GO; GO:0001568; P:blood vessel development; ISO:RGD.
DR   GO; GO:0007420; P:brain development; ISO:RGD.
DR   GO; GO:0043010; P:camera-type eye development; ISO:RGD.
DR   GO; GO:0030154; P:cell differentiation; ISO:RGD.
DR   GO; GO:0045165; P:cell fate commitment; ISO:RGD.
DR   GO; GO:0001709; P:cell fate determination; ISO:RGD.
DR   GO; GO:0008283; P:cell population proliferation; ISO:RGD.
DR   GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; IEP:RGD.
DR   GO; GO:0071333; P:cellular response to glucose stimulus; IEP:RGD.
DR   GO; GO:0032869; P:cellular response to insulin stimulus; IEP:RGD.
DR   GO; GO:1990830; P:cellular response to leukemia inhibitory factor; ISO:RGD.
DR   GO; GO:0071380; P:cellular response to prostaglandin E stimulus; IEP:RGD.
DR   GO; GO:0071466; P:cellular response to xenobiotic stimulus; IEP:RGD.
DR   GO; GO:0021549; P:cerebellum development; IEP:RGD.
DR   GO; GO:0021987; P:cerebral cortex development; ISO:RGD.
DR   GO; GO:0021796; P:cerebral cortex regionalization; ISO:RGD.
DR   GO; GO:0006338; P:chromatin remodeling; ISO:RGD.
DR   GO; GO:0021902; P:commitment of neuronal cell to specific neuron type in forebrain; ISO:RGD.
DR   GO; GO:0061303; P:cornea development in camera-type eye; ISO:RGD.
DR   GO; GO:0080111; P:DNA demethylation; ISO:RGD.
DR   GO; GO:0006306; P:DNA methylation; ISO:RGD.
DR   GO; GO:0009950; P:dorsal/ventral axis specification; ISO:RGD.
DR   GO; GO:0009953; P:dorsal/ventral pattern formation; ISO:RGD.
DR   GO; GO:0048596; P:embryonic camera-type eye morphogenesis; ISO:RGD.
DR   GO; GO:0002064; P:epithelial cell development; IMP:RGD.
DR   GO; GO:0000132; P:establishment of mitotic spindle orientation; ISO:RGD.
DR   GO; GO:0042462; P:eye photoreceptor cell development; ISO:RGD.
DR   GO; GO:0030900; P:forebrain development; ISO:RGD.
DR   GO; GO:0021798; P:forebrain dorsal/ventral pattern formation; ISO:RGD.
DR   GO; GO:0021905; P:forebrain-midbrain boundary formation; ISO:RGD.
DR   GO; GO:0010467; P:gene expression; ISO:RGD.
DR   GO; GO:0002067; P:glandular epithelial cell differentiation; ISO:RGD.
DR   GO; GO:0042593; P:glucose homeostasis; ISO:RGD.
DR   GO; GO:0021986; P:habenula development; ISO:RGD.
DR   GO; GO:0030902; P:hindbrain development; IDA:RGD.
DR   GO; GO:1901142; P:insulin metabolic process; IMP:RGD.
DR   GO; GO:0022027; P:interkinetic nuclear migration; IMP:RGD.
DR   GO; GO:0061072; P:iris morphogenesis; ISO:RGD.
DR   GO; GO:0030216; P:keratinocyte differentiation; ISO:RGD.
DR   GO; GO:0032808; P:lacrimal gland development; ISO:RGD.
DR   GO; GO:0098598; P:learned vocalization behavior or vocal learning; IMP:RGD.
DR   GO; GO:0002088; P:lens development in camera-type eye; ISO:RGD.
DR   GO; GO:0050680; P:negative regulation of epithelial cell proliferation; ISO:RGD.
DR   GO; GO:2000178; P:negative regulation of neural precursor cell proliferation; ISO:RGD.
DR   GO; GO:0007406; P:negative regulation of neuroblast proliferation; ISO:RGD.
DR   GO; GO:0045665; P:negative regulation of neuron differentiation; ISO:RGD.
DR   GO; GO:0001933; P:negative regulation of protein phosphorylation; ISO:RGD.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR   GO; GO:0007399; P:nervous system development; ISO:RGD.
DR   GO; GO:0001755; P:neural crest cell migration; IMP:RGD.
DR   GO; GO:0061351; P:neural precursor cell proliferation; IMP:RGD.
DR   GO; GO:0007405; P:neuroblast proliferation; ISO:RGD.
DR   GO; GO:0030182; P:neuron differentiation; ISO:RGD.
DR   GO; GO:0001764; P:neuron migration; IMP:RGD.
DR   GO; GO:0021772; P:olfactory bulb development; IMP:RGD.
DR   GO; GO:0061034; P:olfactory bulb mitral cell layer development; IMP:RGD.
DR   GO; GO:0021778; P:oligodendrocyte cell fate specification; ISO:RGD.
DR   GO; GO:0021543; P:pallium development; ISO:RGD.
DR   GO; GO:0003322; P:pancreatic A cell development; IMP:BHF-UCL.
DR   GO; GO:0003310; P:pancreatic A cell differentiation; IMP:RGD.
DR   GO; GO:0021983; P:pituitary gland development; ISO:RGD.
DR   GO; GO:0042660; P:positive regulation of cell fate specification; IMP:RGD.
DR   GO; GO:1904798; P:positive regulation of core promoter binding; ISS:UniProtKB.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISS:UniProtKB.
DR   GO; GO:0030858; P:positive regulation of epithelial cell differentiation; ISO:RGD.
DR   GO; GO:0010628; P:positive regulation of gene expression; IMP:BHF-UCL.
DR   GO; GO:0120008; P:positive regulation of glutamatergic neuron differentiation; IMP:RGD.
DR   GO; GO:1902895; P:positive regulation of miRNA transcription; ISO:RGD.
DR   GO; GO:0002052; P:positive regulation of neuroblast proliferation; ISO:RGD.
DR   GO; GO:2001224; P:positive regulation of neuron migration; IGI:RGD.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
DR   GO; GO:0033365; P:protein localization to organelle; ISO:RGD.
DR   GO; GO:0003002; P:regionalization; ISO:RGD.
DR   GO; GO:0009786; P:regulation of asymmetric cell division; ISO:RGD.
DR   GO; GO:0030334; P:regulation of cell migration; ISO:RGD.
DR   GO; GO:0010468; P:regulation of gene expression; ISO:RGD.
DR   GO; GO:0050767; P:regulation of neurogenesis; IMP:RGD.
DR   GO; GO:0045664; P:regulation of neuron differentiation; IDA:RGD.
DR   GO; GO:0010975; P:regulation of neuron projection development; IGI:RGD.
DR   GO; GO:0048505; P:regulation of timing of cell differentiation; ISO:RGD.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:RGD.
DR   GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR   GO; GO:0009611; P:response to wounding; ISO:RGD.
DR   GO; GO:0060041; P:retina development in camera-type eye; IEP:RGD.
DR   GO; GO:0021593; P:rhombomere morphogenesis; IMP:RGD.
DR   GO; GO:0007435; P:salivary gland morphogenesis; ISO:RGD.
DR   GO; GO:1904937; P:sensory neuron migration; IMP:RGD.
DR   GO; GO:0023019; P:signal transduction involved in regulation of gene expression; ISO:RGD.
DR   GO; GO:0007224; P:smoothened signaling pathway; ISO:RGD.
DR   GO; GO:0021510; P:spinal cord development; IEP:RGD.
DR   GO; GO:0021978; P:telencephalon regionalization; ISO:RGD.
DR   GO; GO:0006366; P:transcription by RNA polymerase II; ISO:RGD.
DR   GO; GO:0003309; P:type B pancreatic cell differentiation; IMP:RGD.
DR   GO; GO:0021517; P:ventral spinal cord development; ISO:RGD.
DR   CDD; cd00086; homeodomain; 1.
DR   CDD; cd00131; PAX; 1.
DR   Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 2.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR017970; Homeobox_CS.
DR   InterPro; IPR001356; Homeobox_dom.
DR   InterPro; IPR043182; PAIRED_DNA-bd_dom.
DR   InterPro; IPR001523; Paired_dom.
DR   InterPro; IPR043565; PAX_fam.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   PANTHER; PTHR45636:SF21; PAIRED BOX PROTEIN PAX-6; 1.
DR   PANTHER; PTHR45636; PAIRED BOX PROTEIN PAX-6-RELATED-RELATED; 1.
DR   Pfam; PF00046; Homeodomain; 1.
DR   Pfam; PF00292; PAX; 1.
DR   PRINTS; PR00027; PAIREDBOX.
DR   SMART; SM00389; HOX; 1.
DR   SMART; SM00351; PAX; 1.
DR   SUPFAM; SSF46689; Homeodomain-like; 2.
DR   PROSITE; PS00027; HOMEOBOX_1; 1.
DR   PROSITE; PS50071; HOMEOBOX_2; 1.
DR   PROSITE; PS00034; PAIRED_1; 1.
DR   PROSITE; PS51057; PAIRED_2; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Developmental protein; Differentiation; DNA-binding;
KW   Homeobox; Nucleus; Paired box; Reference proteome; Transcription;
KW   Transcription regulation; Ubl conjugation.
FT   CHAIN           1..422
FT                   /note="Paired box protein Pax-6"
FT                   /id="PRO_0000050187"
FT   DNA_BIND        4..130
FT                   /note="Paired"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00381"
FT   DNA_BIND        210..269
FT                   /note="Homeobox"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT   REGION          7..63
FT                   /note="PAI subdomain"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00381"
FT   REGION          82..130
FT                   /note="RED subdomain"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00381"
FT   REGION          157..201
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          269..311
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          345..422
FT                   /note="Required for suppression of NFATC1-mediated
FT                   transcription"
FT                   /evidence="ECO:0000250|UniProtKB:P63015"
FT   COMPBIAS        167..199
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        276..311
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         47
FT                   /note="Q -> QTHADAKVQVLDSEN (in isoform 5a)"
FT                   /evidence="ECO:0000269|PubMed:24952136, ECO:0000303|Ref.2"
FT                   /id="VSP_011531"
FT   CONFLICT        159
FT                   /note="R -> C (in Ref. 2; CAF29075)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        183
FT                   /note="Q -> G (in Ref. 5; AAB32671)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   422 AA;  46754 MW;  B0B2E5C176A518FE CRC64;
     MQNSHSGVNQ LGGVFVNGRP LPDSTRQKIV ELAHSGARPC DISRILQVSN GCVSKILGRY
     YETGSIRPRA IGGSKPRVAT PEVVSKIAQY KRECPSIFAW EIRDRLLSEG VCTNDNIPSV
     SSINRVLRNL ASEKQQMGAD GMYDKLRMLN GQTGSWGTRP GWYPGTSVPG QPTQDGCQQQ
     EGQGENTNSI SSNGEDSDEA QMRLQLKRKL QRNRTSFTQE QIEALEKEFE RTHYPDVFAR
     ERLAAKIDLP EARIQVWFSN RRAKWRREEK LRNQRRQASN TPSHIPISSS FSTSVYQPIP
     QPTTPVSSFT SGSMLGRTDT ALTNTYSALP PMPSFTMANN LPMQPPVPSQ TSSYSCMLPT
     SPSVNGRSYD TYTPPHMQTH MNSQPMGTSG TTSTGLISPG VSVPVQVPGS EPDMSQYWPR
     LQ
//
DBGET integrated database retrieval system