STOX1_HUMAN
ID STOX1_HUMAN Reviewed; 989 AA.
AC Q6ZVD7; A2A3Q9; A5D6Y7; B0QZA4; B0QZA5; B0QZA6; Q4F8Q6; Q5I946; Q5I947;
AC Q5I948; Q5VX38; Q5VX39; Q6ZRY3; Q96LR3; Q96LS0;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Storkhead-box protein 1;
DE AltName: Full=Winged-helix domain-containing protein;
GN Name=STOX1; Synonyms=C10orf24;
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 A; B AND C), ALTERNATIVE SPLICING,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, VARIANTS PEE4 PRO-18 AND ILE-825,
RP AND VARIANTS HIS-153 AND ASP-608.
RC TISSUE=Placenta;
RX PubMed=15806103; DOI=10.1038/ng1541;
RA van Dijk M., Mulders J., Poutsma A., Koenst A.A.M., Lachmeijer A.M.A.,
RA Dekker G.A., Blankenstein M.A., Oudejans C.B.M.;
RT "Maternal segregation of the Dutch preeclampsia locus at 10q22 with a new
RT member of the winged helix gene family.";
RL Nat. Genet. 37:514-519(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 512-989 (ISOFORM A), AND VARIANT HIS-153.
RC TISSUE=Pancreas;
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-104.
RA van Dijk M., Oudejans C.B.M., Mol A.J.M.;
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 74-989 (ISOFORM A), AND VARIANT
RP ASP-608.
RC TISSUE=Amygdala, Brain, and Prostate;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP FUNCTION.
RX PubMed=22995177; DOI=10.1016/j.neulet.2012.09.017;
RA van Abel D., Abdulhamid O., Scheper W., van Dijk M., Oudejans C.B.;
RT "STOX1A induces phosphorylation of tau proteins at epitopes
RT hyperphosphorylated in Alzheimer's disease.";
RL Neurosci. Lett. 528:104-109(2012).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=22253775; DOI=10.1371/journal.pone.0029769;
RA Abel D.V., Abdul-Hamid O., Dijk M.V., Oudejans C.B.;
RT "Transcription factor STOX1A promotes mitotic entry by binding to the CCNB1
RT promotor.";
RL PLoS ONE 7:E29769-E29769(2012).
RN [8]
RP FUNCTION.
RX PubMed=24738702; DOI=10.1089/ars.2013.5661;
RA Doridot L., Chatre L., Ducat A., Vilotte J.L., Lombes A., Mehats C.,
RA Barbaux S., Calicchio R., Ricchetti M., Vaiman D.;
RT "Nitroso-redox balance and mitochondrial homeostasis are regulated by
RT STOX1, a pre-eclampsia-associated gene.";
RL Antioxid. Redox Signal. 21:819-834(2014).
RN [9]
RP VARIANT HIS-153.
RX PubMed=27535533; DOI=10.1038/nature19057;
RG Exome Aggregation Consortium;
RA Lek M., Karczewski K.J., Minikel E.V., Samocha K.E., Banks E., Fennell T.,
RA O'Donnell-Luria A.H., Ware J.S., Hill A.J., Cummings B.B., Tukiainen T.,
RA Birnbaum D.P., Kosmicki J.A., Duncan L.E., Estrada K., Zhao F., Zou J.,
RA Pierce-Hoffman E., Berghout J., Cooper D.N., Deflaux N., DePristo M.,
RA Do R., Flannick J., Fromer M., Gauthier L., Goldstein J., Gupta N.,
RA Howrigan D., Kiezun A., Kurki M.I., Moonshine A.L., Natarajan P.,
RA Orozco L., Peloso G.M., Poplin R., Rivas M.A., Ruano-Rubio V., Rose S.A.,
RA Ruderfer D.M., Shakir K., Stenson P.D., Stevens C., Thomas B.P., Tiao G.,
RA Tusie-Luna M.T., Weisburd B., Won H.H., Yu D., Altshuler D.M.,
RA Ardissino D., Boehnke M., Danesh J., Donnelly S., Elosua R., Florez J.C.,
RA Gabriel S.B., Getz G., Glatt S.J., Hultman C.M., Kathiresan S., Laakso M.,
RA McCarroll S., McCarthy M.I., McGovern D., McPherson R., Neale B.M.,
RA Palotie A., Purcell S.M., Saleheen D., Scharf J.M., Sklar P.,
RA Sullivan P.F., Tuomilehto J., Tsuang M.T., Watkins H.C., Wilson J.G.,
RA Daly M.J., MacArthur D.G.;
RT "Analysis of protein-coding genetic variation in 60,706 humans.";
RL Nature 536:285-291(2016).
CC -!- FUNCTION: Involved in regulating the levels of reactive oxidative
CC species and reactive nitrogen species and in mitochondrial homeostasis
CC in the placenta (PubMed:24738702). Required for regulation of inner ear
CC epithelial cell proliferation via the AKT signaling pathway (By
CC similarity). {ECO:0000250|UniProtKB:B2RQL2,
CC ECO:0000269|PubMed:24738702}.
CC -!- FUNCTION: [Isoform A]: Involved in cell cycle regulation by binding to
CC the CCNB1 promoter, up-regulating its expression and promoting mitotic
CC entry (PubMed:22253775). Induces phosphorylation of MAPT/tau
CC (PubMed:22995177). {ECO:0000269|PubMed:22253775,
CC ECO:0000269|PubMed:22995177}.
CC -!- INTERACTION:
CC Q6ZVD7; P78563-4: ADARB1; NbExp=3; IntAct=EBI-3923644, EBI-12002366;
CC Q6ZVD7; Q8N9N5-2: BANP; NbExp=3; IntAct=EBI-3923644, EBI-11524452;
CC Q6ZVD7; Q9H8Y8: GORASP2; NbExp=4; IntAct=EBI-3923644, EBI-739467;
CC Q6ZVD7; Q13952-2: NFYC; NbExp=3; IntAct=EBI-3923644, EBI-11956831;
CC Q6ZVD7; P14859-6: POU2F1; NbExp=3; IntAct=EBI-3923644, EBI-11526590;
CC Q6ZVD7; Q01974: ROR2; NbExp=3; IntAct=EBI-3923644, EBI-6422642;
CC -!- SUBCELLULAR LOCATION: [Isoform A]: Cytoplasm
CC {ECO:0000269|PubMed:22253775}. Nucleus {ECO:0000269|PubMed:22253775}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000269|PubMed:22253775}. Note=In epithelial cells, diffusely
CC expressed in the cytoplasm, particularly in peri-membrane cortical
CC regions (By similarity). Concentrated at centrosomes during metaphase
CC (PubMed:22253775). {ECO:0000250|UniProtKB:B2RQL2,
CC ECO:0000269|PubMed:22253775}.
CC -!- SUBCELLULAR LOCATION: [Isoform B]: Nucleus.
CC -!- SUBCELLULAR LOCATION: [Isoform C]: Nucleus, nucleolus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=A;
CC IsoId=Q6ZVD7-1; Sequence=Displayed;
CC Name=B;
CC IsoId=Q6ZVD7-2; Sequence=VSP_016228, VSP_016229;
CC Name=C;
CC IsoId=Q6ZVD7-3; Sequence=VSP_016226, VSP_016227;
CC -!- TISSUE SPECIFICITY: Expressed in placenta, including the invasive
CC extravillus trophoblast cells. {ECO:0000269|PubMed:15806103}.
CC -!- DISEASE: Pre-eclampsia/eclampsia 4 (PEE4) [MIM:609404]: A hypertensive
CC disorder of pregnancy characterized by new hypertension (blood pressure
CC 140/90 or greater) presenting after 20 weeks' gestation with clinically
CC relevant proteinuria. It impacts 2 individuals, the mother and her
CC child, both of whom can be severely affected. Preeclampsia is one of
CC the causes of maternal mortality and morbidity worldwide.
CC {ECO:0000269|PubMed:15806103}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH63627.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB71600.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB71607.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC85925.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC87173.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY842014; AAW48524.1; -; mRNA.
DR EMBL; AY842015; AAW48525.1; -; mRNA.
DR EMBL; AY842016; AAW48526.1; -; mRNA.
DR EMBL; AY842017; AAW48527.1; -; mRNA.
DR EMBL; AL359844; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL391539; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC063627; AAH63627.1; ALT_INIT; mRNA.
DR EMBL; BC140011; AAI40012.1; -; mRNA.
DR EMBL; DQ099680; AAZ07992.1; -; Genomic_DNA.
DR EMBL; AK057864; BAB71600.1; ALT_INIT; mRNA.
DR EMBL; AK057891; BAB71607.1; ALT_INIT; mRNA.
DR EMBL; AK124681; BAC85925.1; ALT_INIT; mRNA.
DR EMBL; AK127878; BAC87173.1; ALT_INIT; mRNA.
DR CCDS; CCDS41535.1; -. [Q6ZVD7-1]
DR CCDS; CCDS44416.1; -. [Q6ZVD7-3]
DR CCDS; CCDS44417.1; -. [Q6ZVD7-2]
DR RefSeq; NP_001123631.1; NM_001130159.2. [Q6ZVD7-2]
DR RefSeq; NP_001123632.1; NM_001130160.2. [Q6ZVD7-3]
DR RefSeq; NP_001123633.1; NM_001130161.2. [Q6ZVD7-1]
DR RefSeq; NP_689922.3; NM_152709.4. [Q6ZVD7-1]
DR AlphaFoldDB; Q6ZVD7; -.
DR SMR; Q6ZVD7; -.
DR BioGRID; 128569; 14.
DR IntAct; Q6ZVD7; 10.
DR STRING; 9606.ENSP00000298596; -.
DR iPTMnet; Q6ZVD7; -.
DR PhosphoSitePlus; Q6ZVD7; -.
DR BioMuta; STOX1; -.
DR DMDM; 82592525; -.
DR MassIVE; Q6ZVD7; -.
DR PaxDb; Q6ZVD7; -.
DR PeptideAtlas; Q6ZVD7; -.
DR PRIDE; Q6ZVD7; -.
DR ProteomicsDB; 68406; -. [Q6ZVD7-1]
DR ProteomicsDB; 68407; -. [Q6ZVD7-2]
DR ProteomicsDB; 68408; -. [Q6ZVD7-3]
DR Antibodypedia; 51097; 76 antibodies from 20 providers.
DR DNASU; 219736; -.
DR Ensembl; ENST00000298596.11; ENSP00000298596.6; ENSG00000165730.16. [Q6ZVD7-1]
DR Ensembl; ENST00000399162.2; ENSP00000382115.2; ENSG00000165730.16. [Q6ZVD7-3]
DR Ensembl; ENST00000399165.8; ENSP00000382118.4; ENSG00000165730.16. [Q6ZVD7-2]
DR Ensembl; ENST00000399169.8; ENSP00000382121.4; ENSG00000165730.16. [Q6ZVD7-1]
DR GeneID; 219736; -.
DR KEGG; hsa:219736; -.
DR MANE-Select; ENST00000298596.11; ENSP00000298596.6; NM_152709.5; NP_689922.3.
DR UCSC; uc001joq.5; human. [Q6ZVD7-1]
DR CTD; 219736; -.
DR DisGeNET; 219736; -.
DR GeneCards; STOX1; -.
DR HGNC; HGNC:23508; STOX1.
DR HPA; ENSG00000165730; Tissue enhanced (brain, choroid plexus).
DR MalaCards; STOX1; -.
DR MIM; 609397; gene.
DR MIM; 609404; phenotype.
DR neXtProt; NX_Q6ZVD7; -.
DR OpenTargets; ENSG00000165730; -.
DR Orphanet; 275555; Preeclampsia.
DR PharmGKB; PA134883643; -.
DR VEuPathDB; HostDB:ENSG00000165730; -.
DR eggNOG; KOG3897; Eukaryota.
DR GeneTree; ENSGT00520000055589; -.
DR HOGENOM; CLU_306723_0_0_1; -.
DR InParanoid; Q6ZVD7; -.
DR OMA; DQLVKHY; -.
DR OrthoDB; 494782at2759; -.
DR PhylomeDB; Q6ZVD7; -.
DR TreeFam; TF337253; -.
DR PathwayCommons; Q6ZVD7; -.
DR SignaLink; Q6ZVD7; -.
DR BioGRID-ORCS; 219736; 13 hits in 1074 CRISPR screens.
DR ChiTaRS; STOX1; human.
DR GenomeRNAi; 219736; -.
DR Pharos; Q6ZVD7; Tbio.
DR PRO; PR:Q6ZVD7; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q6ZVD7; protein.
DR Bgee; ENSG00000165730; Expressed in bronchial epithelial cell and 137 other tissues.
DR ExpressionAtlas; Q6ZVD7; baseline and differential.
DR Genevisible; Q6ZVD7; HS.
DR GO; GO:0005938; C:cell cortex; IEA:Ensembl.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0001650; C:fibrillar center; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0071500; P:cellular response to nitrosative stress; IMP:UniProtKB.
DR GO; GO:0048839; P:inner ear development; IEA:Ensembl.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB.
DR GO; GO:1904031; P:positive regulation of cyclin-dependent protein kinase activity; IMP:UniProtKB.
DR GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; IMP:UniProtKB.
DR GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IMP:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR GO; GO:1904120; P:positive regulation of otic vesicle morphogenesis; IEA:Ensembl.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IMP:UniProtKB.
DR GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; IMP:UniProtKB.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0010468; P:regulation of gene expression; IMP:UniProtKB.
DR GO; GO:1901858; P:regulation of mitochondrial DNA metabolic process; IMP:UniProtKB.
DR GO; GO:0051881; P:regulation of mitochondrial membrane potential; IMP:UniProtKB.
DR GO; GO:0010821; P:regulation of mitochondrion organization; IMP:UniProtKB.
DR GO; GO:1902882; P:regulation of response to oxidative stress; IMP:UniProtKB.
DR GO; GO:0061418; P:regulation of transcription from RNA polymerase II promoter in response to hypoxia; IMP:UniProtKB.
DR InterPro; IPR019391; Storkhead-box_winged-helix.
DR InterPro; IPR040126; STOX1/2.
DR PANTHER; PTHR22437; PTHR22437; 1.
DR Pfam; PF10264; Stork_head; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Cell cycle; Cell division; Cytoplasm;
KW Cytoskeleton; Disease variant; DNA-binding; Mitosis; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..989
FT /note="Storkhead-box protein 1"
FT /id="PRO_0000072281"
FT REGION 327..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 389..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 497..556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 631..651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 926..948
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..523
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..556
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..651
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 932..948
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 156..169
FT /note="IAIPSEDILYTTLG -> HRVWDLIIQSFWMD (in isoform C)"
FT /evidence="ECO:0000303|PubMed:15806103"
FT /id="VSP_016226"
FT VAR_SEQ 170..989
FT /note="Missing (in isoform C)"
FT /evidence="ECO:0000303|PubMed:15806103"
FT /id="VSP_016227"
FT VAR_SEQ 222..227
FT /note="VSMESC -> DTESGI (in isoform B)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:15806103"
FT /id="VSP_016228"
FT VAR_SEQ 228..989
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:15806103"
FT /id="VSP_016229"
FT VARIANT 18
FT /note="R -> P (in PEE4; dbSNP:rs556362193)"
FT /evidence="ECO:0000269|PubMed:15806103"
FT /id="VAR_023784"
FT VARIANT 153
FT /note="Y -> H (in dbSNP:rs1341667)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:15806103, ECO:0000269|PubMed:27535533"
FT /id="VAR_023785"
FT VARIANT 608
FT /note="E -> D (in dbSNP:rs10509305)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15806103"
FT /id="VAR_023786"
FT VARIANT 825
FT /note="N -> I (in PEE4; dbSNP:rs41278532)"
FT /evidence="ECO:0000269|PubMed:15806103"
FT /id="VAR_023787"
FT VARIANT 863
FT /note="A -> T (in dbSNP:rs7904300)"
FT /id="VAR_051388"
SQ SEQUENCE 989 AA; 110962 MW; 5F1E70504F081AC7 CRC64;
MARPVQLAPG SLALVLCRLE AQKAAGAAEE PGGRAVFRAF RRANARCFWN ARLARAASRL
AFQGWLRRGV LLVRAPPACL QVLRDAWRRR ALRPPRGFRI RAVGDVFPVQ MNPITQSQFV
PLGEVLCCAI SDMNTAQIVV TQESLLERLM KHYPGIAIPS EDILYTTLGT LIKERKIYHT
GEGYFIVTPQ TYFITNTTTQ ENKRMLPSDE SRLMPASMTY LVSMESCAES AQENAAPISH
CQSCQCFRDM HTQDVQEAPV AAEVTRKSHR GLGESVSWVQ NGAVSVSAEH HICESTKPLP
YTRDKEKGKK FGFSLLWRSL SRKEKPKTEH SSFSAQFPPE EWPVRDEDDL DNIPRDVEHE
IIKRINPILT VDNLIKHTVL MQKYEEQKKY NSQGTSTDML TIGHKYPSKE GVKKRQGLSA
KPQGQGHSRR DRHKARNQGS EFQPGSIRLE KHPKLPATQP IPRIKSPNEM VGQKPLGEIT
TVLGSHLIYK KRISNPFQGL SHRGSTISKG HKIQKTSDLK PSQTGPKEKP FQKPRSLDSS
RIFDGKAKEP YAEQPNDKME AESIYINDPT VKPINDDFRG HLFSHPQQSM LQNDGKCCPF
MESMLRYEVY GGENEVIPEV LRKSHSHFDK LGETKQTPHS LPSRGASFSD RTPSACRLVD
NTIHQFQNLG LLDYPVGVNP LRQAARQDKD SEELLRKGFV QDAETTSLEN EQLSNDDQAL
YQNEVEDDDG ACSSLYLEED DISENDDLRQ MLPGHSQYSF TGGSQGNHLG KQKVIERSLT
EYNSTMERVE SQVLKRNECY KPTGLHATPG ESQEPNLSAE SCGLNSGAQF GFNYEEEPSV
AKCVQASAPA DERIFDYYSA RKASFEAEVI QDTIGDTGKK PASWSQSPQN QEMRKHFPQK
FQLFNTSHMP VLAQDVQYEH SHLEGTENHS MAGDSGIDSP RTQSLGSNNS VILDGLKRRQ
NFLQNVEGTK SSQPLTSNSL LPLTPVINV
