PRUN2_HUMAN
ID PRUN2_HUMAN Reviewed; 3088 AA.
AC Q8WUY3; B3KYC4; B4DQH8; O15073; Q58A63; Q5JUB6; Q5T304; Q5T476; Q6T2V6;
AC Q6T2V7; Q8N665;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 3.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Protein prune homolog 2;
DE AltName: Full=BNIP2 motif-containing molecule at the C-terminal region 1;
GN Name=PRUNE2; Synonyms=BMCC1, BNIPXL, C9orf65, KIAA0367;
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 [LARGE SCALE MRNA] (ISOFORM 5).
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC TISSUE=Hypothalamus;
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 [MRNA] OF 253-3088 (ISOFORM 1), FUNCTION, INDUCTION,
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC TISSUE=Neuroblastoma;
RX PubMed=16288218; DOI=10.1038/sj.onc.1209225;
RA Machida T., Fujita T., Ooo M.L., Ohira M., Isogai E., Mihara M., Hirato J.,
RA Tomotsune D., Hirata T., Fujimori M., Adachi W., Nakagawara A.;
RT "Increased expression of proapoptotic BMCC1, a novel gene with the BNIP2
RT and Cdc42GAP homology (BCH) domain, is associated with favorable prognosis
RT in human neuroblastomas.";
RL Oncogene 25:1931-1942(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2265-3088 (ISOFORMS 3 AND 4).
RC TISSUE=Brain, and Kidney;
RA Soh J.K.U., Zhou Y.T., Low B.C.;
RT "BNIPXL, an extra long member of the BNIP-2 family.";
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2265-3088 (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=9205841; DOI=10.1093/dnares/4.2.141;
RA Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VII. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 4:141-150(1997).
RN [7]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [9]
RP GENE REGULATION.
RX PubMed=19760627; DOI=10.1002/pros.21040;
RA Salagierski M., Verhaegh G.W., Jannink S.A., Smit F.P., Hessels D.,
RA Schalken J.A.;
RT "Differential expression of PCA3 and its overlapping PRUNE2 transcript in
RT prostate cancer.";
RL Prostate 70:70-78(2010).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [12]
RP VARIANT LYS-806.
RX PubMed=23033978; DOI=10.1056/nejmoa1206524;
RA de Ligt J., Willemsen M.H., van Bon B.W., Kleefstra T., Yntema H.G.,
RA Kroes T., Vulto-van Silfhout A.T., Koolen D.A., de Vries P., Gilissen C.,
RA del Rosario M., Hoischen A., Scheffer H., de Vries B.B., Brunner H.G.,
RA Veltman J.A., Vissers L.E.;
RT "Diagnostic exome sequencing in persons with severe intellectual
RT disability.";
RL N. Engl. J. Med. 367:1921-1929(2012).
CC -!- FUNCTION: May play an important role in regulating differentiation,
CC survival and aggressiveness of the tumor cells.
CC {ECO:0000269|PubMed:16288218}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16288218}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q8WUY3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8WUY3-2; Sequence=VSP_039341;
CC Name=3; Synonyms=BNIPXL-alpha;
CC IsoId=Q8WUY3-3; Sequence=VSP_039341, VSP_039342;
CC Name=4; Synonyms=BNIPXL-beta;
CC IsoId=Q8WUY3-4; Sequence=VSP_039341, VSP_039342, VSP_039343;
CC Name=5;
CC IsoId=Q8WUY3-5; Sequence=VSP_039339, VSP_039340;
CC -!- TISSUE SPECIFICITY: A high level of expression seen in the nervous
CC system (brain, cerebellum and spinal cord) as well as adrenal gland.
CC Expressed at high levels in noneuroblastoma, rhabdomyosarcoma, melanoma
CC and some osteosarcoma cell lines, whereas at only low levels in cancer
CC cell lines of liver, breast, thyroid and colon. Expression is
CC significantly higher in favorable tumors than aggressive ones.
CC {ECO:0000269|PubMed:16288218}.
CC -!- DEVELOPMENTAL STAGE: Induced during the G1 phase of the cell cycle.
CC -!- INDUCTION: Down-regulated after NGF-induced differentiation, and up-
CC regulated during the NGF-depletion-induced apoptosis.
CC {ECO:0000269|PubMed:16288218}.
CC -!- MISCELLANEOUS: PRUNE2/BMCC1 and PCA3, one of the most prostate cancer
CC specific markers are overlapping genes in reverse orientation. However,
CC they do not appear to be coregulated.
CC -!- SIMILARITY: Belongs to the PPase class C family. Prune subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH22571.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH22571.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
CC Sequence=AAR15150.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAR15151.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAD93351.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK298805; BAG60940.1; -; mRNA.
DR EMBL; AL161626; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL359314; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL390239; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC022571; AAH22571.1; ALT_SEQ; mRNA.
DR EMBL; AB050197; BAD93351.1; ALT_INIT; mRNA.
DR EMBL; AY439213; AAR15150.1; ALT_INIT; mRNA.
DR EMBL; AY439214; AAR15151.1; ALT_INIT; mRNA.
DR EMBL; AB002365; BAA20822.2; -; mRNA.
DR CCDS; CCDS47982.1; -. [Q8WUY3-1]
DR RefSeq; NP_001294976.1; NM_001308047.1.
DR RefSeq; NP_001294977.1; NM_001308048.1.
DR RefSeq; NP_001294978.1; NM_001308049.1.
DR RefSeq; NP_001294979.1; NM_001308050.1. [Q8WUY3-5]
DR RefSeq; NP_001294980.1; NM_001308051.1.
DR RefSeq; NP_056040.2; NM_015225.2. [Q8WUY3-1]
DR RefSeq; XP_011516625.1; XM_011518323.1. [Q8WUY3-2]
DR SMR; Q8WUY3; -.
DR BioGRID; 127687; 27.
DR ELM; Q8WUY3; -.
DR IntAct; Q8WUY3; 15.
DR MINT; Q8WUY3; -.
DR STRING; 9606.ENSP00000365908; -.
DR iPTMnet; Q8WUY3; -.
DR PhosphoSitePlus; Q8WUY3; -.
DR BioMuta; PRUNE2; -.
DR DMDM; 298286907; -.
DR EPD; Q8WUY3; -.
DR jPOST; Q8WUY3; -.
DR MassIVE; Q8WUY3; -.
DR MaxQB; Q8WUY3; -.
DR PaxDb; Q8WUY3; -.
DR PeptideAtlas; Q8WUY3; -.
DR PRIDE; Q8WUY3; -.
DR ProteomicsDB; 74722; -. [Q8WUY3-1]
DR ProteomicsDB; 74723; -. [Q8WUY3-2]
DR ProteomicsDB; 74724; -. [Q8WUY3-3]
DR ProteomicsDB; 74725; -. [Q8WUY3-4]
DR ProteomicsDB; 74726; -. [Q8WUY3-5]
DR Antibodypedia; 27288; 114 antibodies from 28 providers.
DR DNASU; 158471; -.
DR Ensembl; ENST00000376718.8; ENSP00000365908.3; ENSG00000106772.19. [Q8WUY3-1]
DR GeneID; 158471; -.
DR KEGG; hsa:158471; -.
DR MANE-Select; ENST00000376718.8; ENSP00000365908.3; NM_015225.3; NP_056040.2.
DR UCSC; uc010mpk.4; human. [Q8WUY3-1]
DR CTD; 158471; -.
DR DisGeNET; 158471; -.
DR GeneCards; PRUNE2; -.
DR HGNC; HGNC:25209; PRUNE2.
DR HPA; ENSG00000106772; Tissue enhanced (brain).
DR MIM; 610691; gene.
DR neXtProt; NX_Q8WUY3; -.
DR OpenTargets; ENSG00000106772; -.
DR PharmGKB; PA162400198; -.
DR VEuPathDB; HostDB:ENSG00000106772; -.
DR eggNOG; KOG4129; Eukaryota.
DR GeneTree; ENSGT00940000154422; -.
DR HOGENOM; CLU_227259_0_0_1; -.
DR InParanoid; Q8WUY3; -.
DR OMA; WMDAKQP; -.
DR OrthoDB; 1545660at2759; -.
DR PhylomeDB; Q8WUY3; -.
DR TreeFam; TF323914; -.
DR PathwayCommons; Q8WUY3; -.
DR SignaLink; Q8WUY3; -.
DR BioGRID-ORCS; 158471; 12 hits in 1079 CRISPR screens.
DR ChiTaRS; PRUNE2; human.
DR GeneWiki; PRUNE2; -.
DR GenomeRNAi; 158471; -.
DR Pharos; Q8WUY3; Tbio.
DR PRO; PR:Q8WUY3; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q8WUY3; protein.
DR Bgee; ENSG00000106772; Expressed in dorsal root ganglion and 198 other tissues.
DR ExpressionAtlas; Q8WUY3; baseline and differential.
DR Genevisible; Q8WUY3; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016462; F:pyrophosphatase activity; IEA:InterPro.
DR GO; GO:0006915; P:apoptotic process; IBA:GO_Central.
DR CDD; cd00170; SEC14; 1.
DR Gene3D; 3.10.310.20; -; 1.
DR Gene3D; 3.40.525.10; -; 1.
DR InterPro; IPR022181; Bcl2-/adenovirus-E1B.
DR InterPro; IPR001251; CRAL-TRIO_dom.
DR InterPro; IPR036865; CRAL-TRIO_dom_sf.
DR InterPro; IPR038763; DHH_sf.
DR InterPro; IPR004097; DHHA2.
DR InterPro; IPR038222; DHHA2_dom_sf.
DR Pfam; PF12496; BNIP2; 1.
DR Pfam; PF13716; CRAL_TRIO_2; 1.
DR Pfam; PF02833; DHHA2; 1.
DR SMART; SM01131; DHHA2; 1.
DR SMART; SM00516; SEC14; 1.
DR SUPFAM; SSF52087; SSF52087; 1.
DR SUPFAM; SSF64182; SSF64182; 1.
DR PROSITE; PS50191; CRAL_TRIO; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Apoptosis; Cytoplasm; Manganese;
KW Metal-binding; Reference proteome.
FT CHAIN 1..3088
FT /note="Protein prune homolog 2"
FT /id="PRO_0000089701"
FT DOMAIN 2895..3056
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00056"
FT REGION 433..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 490..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 673..759
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 771..795
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 846..909
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 952..1080
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1192..1211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1231..1371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1413..1452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1472..1491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1515..1585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1632..1698
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1741..1768
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1782..1813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2089..2114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2173..2215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2240..2260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2492..2542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2589..2667
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2687..2710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2814..2833
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2841..2875
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 109..111
FT /note="DHH motif"
FT /evidence="ECO:0000250"
FT COMPBIAS 500..515
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 543..558
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 561..582
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 608..628
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 682..696
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 724..738
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 884..898
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 952..979
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 980..1004
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1005..1028
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1034..1048
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1049..1068
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1257..1279
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1318..1345
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1353..1370
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1632..1668
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1676..1691
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1747..1768
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1792..1813
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2178..2207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2240..2259
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2509..2542
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2589..2604
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2615..2633
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2853..2867
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT VAR_SEQ 1..2736
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_039339"
FT VAR_SEQ 2737..2759
FT /note="PDTEMEEETEFLELGTRISRPNG -> MLKSCSRASFSPSVRKPPLILRR
FT (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_039340"
FT VAR_SEQ 2852
FT /note="H -> HE (in isoform 2, isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:9205841, ECO:0000303|Ref.5"
FT /id="VSP_039341"
FT VAR_SEQ 2909
FT /note="G -> GGLR (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_039342"
FT VAR_SEQ 3051..3088
FT /note="LDEELREASEAAKTSCLYNDPEMSSMEKDIDLKLKEKP -> Y (in
FT isoform 4)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_039343"
FT VARIANT 806
FT /note="E -> K (in dbSNP:rs375315668)"
FT /evidence="ECO:0000269|PubMed:23033978"
FT /id="VAR_069436"
FT CONFLICT 1675
FT /note="P -> S (in Ref. 4; BAD93351)"
FT /evidence="ECO:0000305"
FT CONFLICT 2401
FT /note="L -> I (in Ref. 5; AAR15150/AAR15151)"
FT /evidence="ECO:0000305"
FT CONFLICT 2511
FT /note="S -> P (in Ref. 4; BAD93351 and 6; BAA20822)"
FT /evidence="ECO:0000305"
FT CONFLICT 2618
FT /note="S -> G (in Ref. 4; BAD93351 and 6; BAA20822)"
FT /evidence="ECO:0000305"
FT CONFLICT 2711..2715
FT /note="Missing (in Ref. 4; BAD93351, 5; AAR15150/AAR15151
FT and 6; BAA20822)"
FT /evidence="ECO:0000305"
FT CONFLICT 2721
FT /note="N -> S (in Ref. 4; BAD93351 and 6; BAA20822)"
FT /evidence="ECO:0000305"
FT CONFLICT 2737
FT /note="P -> S (in Ref. 4; BAD93351 and 6; BAA20822)"
FT /evidence="ECO:0000305"
FT CONFLICT 2857
FT /note="N -> T (in Ref. 5; AAR15150/AAR15151)"
FT /evidence="ECO:0000305"
FT CONFLICT 2889
FT /note="E -> D (in Ref. 5; AAR15150/AAR15151)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 3088 AA; 340635 MW; 8C946594BAACB10A CRC64;
MEEFLQRAKS KLNRSKRLEK VHVVIGPKSC DLDSLISTFT YAYFLDKVSP PGVLCLPVLN
IPRTEFNYFT ETRFILEELN ISESFHIFRD EINLHQLNDE GKLSITLVGS SVLASEDKTL
ESAVVKVINP VEQSDANVEF RESSSSLVLK EILQEAPELI TEQLAHRLRG SILFKWMTME
SEKISEKQEE ILSILEEKFP NLPPREDIIN VLQETQFSAQ GLSIEQTMLK DLKELSDGEI
KVAISTVSMN LENCLFHSNI TSDLKAFTDK FGFDVLILFS SYLSEEQQPR RQIAVYSENM
ELCSQICCEL EECQNPCLEL EPFDCGCDEI LVYQQEDPSV TCDQVVLVVK EVINRRCPEM
VSNSRTSSTE AVAGSAPLSQ GSSGIMELYG SDIEPQPSSV NFIENPPDLN DSNQAQVDAN
VDLVSPDSGL ATIRSSRSSK ESSVFLSDDS PVGEGAGPHH TLLPGLDSYS PIPEGAVAEE
HAWSGEHGEH FDLFNFDPAP MASGQSQQSS HSADYSPADD FFPNSDLSEG QLPAGPEGLD
GMGTNMSNYS SSSLLSGAGK DSLVEHDEEF VQRQDSPRDN SERNLSLTDF VGDESPSPER
LKNTGKRIPP TPMNSLVESS PSTEEPASLY TEDMTQKATD TGHMGPPQTH ARCSSWWGGL
EIDSKNIADA WSSSEQESVF QSPESWKEHK PSSIDRRASD SVFQPKSLEF TKSGPWESEF
GQPELGSNDI QDKNEESLPF QNLPMEKSPL PNTSPQGTNH LIEDFASLWH SGRSPTAMPE
PWGNPTDDGE PAAVAPFPAW SAFGKEDHDE ALKNTWNLHP TSSKTPSVRD PNEWAMAKSG
FAFSSSELLD NSPSEINNEA APEIWGKKNN DSRDHIFAPG NPSSDLDHTW TNSKPPKEDQ
NGLVDPKTRG KVYEKVDSWN LFEENMKKGG SDVLVPWEDS FLSYKCSDYS ASNLGEDSVP
SPLDTNYSTS DSYTSPTFAG DEKETEHKPF AKEEGFESKD GNSTAEETDI PPQSLQQSSR
NRISSGPGNL DMWASPHTDN SSEINTTHNL DENELKTEHT DGKNISMEDD VGESSQSSYD
DPSMMQLYNE TNRQLTLLHS STNSRQTAPD SLDLWNRVIL EDTQSTATIS DMDNDLDWDD
CSGGAAIPSD GQTEGYMAEG SEPETRFTVR QLEPWGLEYQ EANQVDWELP ASDEHTKDSA
PSEHHTLNEK SGQLIANSIW DSVMRDKDMS SFMLPGSSHI TDSEQRELPP EIPSHSANVK
DTHSPDAPAA SGTSESEALI SHLDKQDTER ETLQSDAASL ATRLENPGYF PHPDPWKGHG
DGQSESEKEA QGATDRGHLD EEEVIASGVE NASGISEKGQ SDQELSSLVA SEHQEICIKS
GKISSLAVTF SPQTEEPEEV LEYEEGSYNL DSRDVQTGMS ADNLQPKDTH EKHLMSQRNS
GETTETSDGM NFTKYVSVPE KDLEKTEECN FLEPENVGGG PPHRVPRSLD FGDVPIDSDV
HVSSTCSEIT KNLDVKGSEN SLPGAGSSGN FDRDTISSEY THSSASSPEL NDSSVALSSW
GQQPSSGYQE ENQGNWSEQN HQESELITTD GQVEIVTKVK DLEKNRINEF EKSFDRKTPT
FLEIWNDSVD GDSFSSLSSP ETGKYSEHSG THQESNLIAS YQEKNEHDIS ATVQPEDARV
ISTSSGSDDD SVGGEESIEE EIQVANCHVA EDESRAWDSL NESNKFLVTA DPKSENIYDY
LDSSEPAENE NKSNPFCDNQ QSSPDPWTFS PLTETEMQIT AVEKEKRSSP ETGTTGDVAW
QISPKASFPK NEDNSQLEML GFSADSTEWW KASPQEGRLI ESPFERELSD SSGVLEINSS
VHQNASPWGV PVQGDIEPVE THYTNPFSDN HQSPFLEGNG KNSHEQLWNI QPRQPDPDAD
KFSQLVKLDQ IKEKDSREQT FVSAAGDELT PETPTQEQCQ DTMLPVCDHP DTAFTHAEEN
SCVTSNVSTN EGQETNQWEQ EKSYLGEMTN SSIATENFPA VSSPTQLIMK PGSEWDGSTP
SEDSRGTFVP DILHGNFQEG GQLASAAPDL WIDAKKPFSL KADGENPDIL THCEHDSNSQ
ASDSPDICHD SEAKQETEKH LSACMGPEVE SSELCLTEPE IDEEPIYEPG REFVPSNAEL
DSENATVLPP IGYQADIKGS SQPASHKGSP EPSEINGDNS TGLQVSEKGA SPDMAPILEP
VDRRIPRIEN VATSIFVTHQ EPTPEGDGSW ISDSFSPESQ PGARALFDGD PHLSTENPAL
VPDALLASDT CLDISEAAFD HSFSDASGLN TSTGTIDDMS KLTLSEGHPE TPVDGDLGKQ
DICSSEASWG DFEYDVMGQN IDEDLLREPE HFLYGGDPPL EEDSLKQSLA PYTPPFDLSY
LTEPAQSAET IEEAGSPEDE SLGCRAAEIV LSALPDRRSE GNQAETKNRL PGSQLAVLHI
REDPESVYLP VGAGSNILSP SNVDWEVETD NSDLPAGGDI GPPNGASKEI SELEEEKTIP
TKEPEQIKSE YKEERCTEKN EDRHALHMDY ILVNREENSH SKPETCEERE SIAELELYVG
SKETGLQGTQ LASFPDTCQP ASLNERKGLS AEKMSSKSDT RSSFESPAQD QSWMFLGHSE
VGDPSLDARD SGPGWSGKTV EPFSELGLGE GPQLQILEEM KPLESLALEE ASGPVSQSQK
SKSRGRAGPD AVTLQAVTHD NEWEMLSPQP VQKNMIPDTE MEEETEFLEL GTRISRPNGL
LSEDVGMDIP FEEGVLSPSA ADMRPEPPNS LDLNDTHPRR IKLTAPNINL SLDQSEGSIL
SDDNLDSPDE IDINVDELDT PDEADSFEYT GHDPTANKDS GQESESIPEY TAEEEREDNR
LWRTVVIGEQ EQRIDMKVIE PYRRVISHGG YYGDGLNAII VFAACFLPDS SRADYHYVME
NLFLYVISTL ELMVAEDYMI VYLNGATPRR RMPGLGWMKK CYQMIDRRLR KNLKSFIIVH
PSWFIRTILA VTRPFISSKF SSKIKYVNSL SELSGLIPMD CIHIPESIIK LDEELREASE
AAKTSCLYND PEMSSMEKDI DLKLKEKP
