XRN1_HUMAN
ID XRN1_HUMAN Reviewed; 1706 AA.
AC Q8IZH2; Q4G0S3; Q68D88; Q6AI24; Q6MZS8; Q86WS7; Q8N8U4; Q9UF39;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=5'-3' exoribonuclease 1;
DE EC=3.1.13.-;
DE AltName: Full=Strand-exchange protein 1 homolog;
GN Name=XRN1 {ECO:0000312|HGNC:HGNC:30654};
GN Synonyms=SEP1 {ECO:0000312|HGNC:HGNC:30654};
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] (ISOFORM 1), INDUCTION BY GDNF, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Neuroblastoma;
RX PubMed=14580940; DOI=10.1016/s0306-4522(03)00487-1;
RA Shimoyama Y., Morikawa Y., Ichihara M., Kodama Y., Fukuda N., Hayashi H.,
RA Morinaga T., Iwashita T., Murakumo Y., Takahashi M.;
RT "Identification of human SEP1 as a glial cell line-derived neurotrophic
RT factor-inducible protein and its expression in the nervous system.";
RL Neuroscience 121:899-906(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Fetal kidney, Small intestine, and Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Brain, and Testis;
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 [LARGE SCALE MRNA] OF 1-473 (ISOFORMS 1/2).
RC TISSUE=Mesangial cell;
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 [5]
RP ALTERNATIVE SPLICING (ISOFORM 2), AND SUBCELLULAR LOCATION.
RX PubMed=9802570; DOI=10.1093/dnares/5.4.241;
RA Sato Y., Shimamoto A., Shobuike T., Sugimoto M., Ikeda H., Kuroda S.,
RA Furuichi Y.;
RT "Cloning and characterization of human Sep1 (hSEP1) gene and cytoplasmic
RT localization of its product.";
RL DNA Res. 5:241-246(1998).
RN [6]
RP IDENTIFICATION IN A MRNP COMPLEX WITH UPF1; UPF2 AND UPF3B.
RX PubMed=14527413; DOI=10.1016/s1097-2765(03)00349-6;
RA Lejeune F., Li X., Maquat L.E.;
RT "Nonsense-mediated mRNA decay in mammalian cells involves decapping,
RT deadenylating, and exonucleolytic activities.";
RL Mol. Cell 12:675-687(2003).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=12515382;
RA Ingelfinger D., Arndt-Jovin D.J., Luehrmann R., Achsel T.;
RT "The human LSm1-7 proteins colocalize with the mRNA-degrading enzymes
RT Dcp1/2 and Xrnl in distinct cytoplasmic foci.";
RL RNA 8:1489-1501(2002).
RN [8]
RP POTENTIAL TUMOR SUPPRESSION ROLE IN OSTEOGENIC SARCOMA, AND TISSUE
RP SPECIFICITY.
RX PubMed=12426100; DOI=10.1016/s0378-1119(02)00929-0;
RA Zhang K., Dion N., Fuchs B., Damron T., Gitelis S., Irwin R., O'Connor M.,
RA Schwartz H., Scully S.P., Rock M.G., Bolander M.E., Sarkar G.;
RT "The human homolog of yeast SEP1 is a novel candidate tumor suppressor gene
RT in osteogenic sarcoma.";
RL Gene 298:121-127(2002).
RN [9]
RP INTERACTION WITH ZFP36L1.
RX PubMed=15687258; DOI=10.1101/gad.1282305;
RA Lykke-Andersen J., Wagner E.;
RT "Recruitment and activation of mRNA decay enzymes by two ARE-mediated decay
RT activation domains in the proteins TTP and BRF-1.";
RL Genes Dev. 19:351-361(2005).
RN [10]
RP FUNCTION IN HISTONE MRNA DEGRADATION ACTIVITY.
RX PubMed=18172165; DOI=10.1101/gad.1622708;
RA Mullen T.E., Marzluff W.F.;
RT "Degradation of histone mRNA requires oligouridylation followed by
RT decapping and simultaneous degradation of the mRNA both 5' to 3' and 3' to
RT 5'.";
RL Genes Dev. 22:50-65(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP INTERACTION WITH ZC3HAV1.
RX PubMed=21876179; DOI=10.1073/pnas.1101676108;
RA Zhu Y., Chen G., Lv F., Wang X., Ji X., Xu Y., Sun J., Wu L., Zheng Y.T.,
RA Gao G.;
RT "Zinc-finger antiviral protein inhibits HIV-1 infection by selectively
RT targeting multiply spliced viral mRNAs for degradation.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:15834-15839(2011).
RN [14]
RP INTERACTION WITH DIS3L2.
RX PubMed=23756462; DOI=10.1038/emboj.2013.135;
RA Lubas M., Damgaard C.K., Tomecki R., Cysewski D., Jensen T.H.,
RA Dziembowski A.;
RT "Exonuclease hDIS3L2 specifies an exosome-independent 3'-5' degradation
RT pathway of human cytoplasmic mRNA.";
RL EMBO J. 32:1855-1868(2013).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1645, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [16]
RP INTERACTION WITH TRIM71.
RX PubMed=23125361; DOI=10.1093/nar/gks1032;
RA Loedige I., Gaidatzis D., Sack R., Meister G., Filipowicz W.;
RT "The mammalian TRIM-NHL protein TRIM71/LIN-41 is a repressor of mRNA
RT function.";
RL Nucleic Acids Res. 41:518-532(2013).
RN [17]
RP INTERACTION WITH DHX34.
RX PubMed=25220460; DOI=10.1016/j.celrep.2014.08.020;
RA Hug N., Caceres J.F.;
RT "The RNA helicase DHX34 activates NMD by promoting a transition from the
RT surveillance to the decay-inducing complex.";
RL Cell Rep. 8:1845-1856(2014).
RN [18]
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 [19]
RP INTERACTION WITH YTHDC2.
RX PubMed=29033321; DOI=10.1016/j.molcel.2017.09.021;
RA Wojtas M.N., Pandey R.R., Mendel M., Homolka D., Sachidanandam R.,
RA Pillai R.S.;
RT "Regulation of m6A transcripts by the 3'-5' RNA helicase YTHDC2 is
RT essential for a successful meiotic program in the mammalian germline.";
RL Mol. Cell 68:374-387(2017).
CC -!- FUNCTION: Major 5'-3' exoribonuclease involved in mRNA decay. Required
CC for the 5'-3'-processing of the G4 tetraplex-containing DNA and RNA
CC substrates. The kinetic of hydrolysis is faster for G4 RNA tetraplex
CC than for G4 DNA tetraplex and monomeric RNA tetraplex. Binds to RNA and
CC DNA (By similarity). Plays a role in replication-dependent histone mRNA
CC degradation. May act as a tumor suppressor protein in osteogenic
CC sarcoma (OGS). {ECO:0000250|UniProtKB:P97789,
CC ECO:0000269|PubMed:18172165}.
CC -!- SUBUNIT: Found in a mRNP complex with UPF1, UPF2, UPF3B and XRN1
CC (PubMed:14527413). Associates with alpha and beta tubulins (By
CC similarity). Interacts with DIS3L2 (PubMed:23756462). Interacts with
CC ZC3HAV1 in an RNA-dependent manner (PubMed:21876179). Interacts with
CC ZFP36L1 (PubMed:15687258). Interacts with TRIM71 (via NHL repeats) in
CC an RNA-dependent manner (PubMed:23125361). Interacts with YTHDC2 (via
CC ANK repeats) (PubMed:29033321). Interacts with DHX34; the interaction
CC is RNA-independent (PubMed:25220460). {ECO:0000250|UniProtKB:P97789,
CC ECO:0000269|PubMed:14527413, ECO:0000269|PubMed:15687258,
CC ECO:0000269|PubMed:21876179, ECO:0000269|PubMed:23125361,
CC ECO:0000269|PubMed:23756462, ECO:0000269|PubMed:25220460,
CC ECO:0000269|PubMed:29033321}.
CC -!- INTERACTION:
CC Q8IZH2; Q6P2E9: EDC4; NbExp=4; IntAct=EBI-372406, EBI-1006038;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12515382,
CC ECO:0000269|PubMed:14580940, ECO:0000269|PubMed:9802570}. Note=Discrete
CC foci at the inner surface of the cell membrane.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8IZH2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8IZH2-2; Sequence=VSP_016694, VSP_016695;
CC Name=3;
CC IsoId=Q8IZH2-3; Sequence=VSP_016692, VSP_016693;
CC -!- TISSUE SPECIFICITY: Expressed in heart, brain, pancreas, spleen,
CC testis, osteogenic sarcoma (OGS) biopsy and primary cell lines.
CC {ECO:0000269|PubMed:12426100}.
CC -!- INDUCTION: By GDNF/glial cell line-derived neurotrophic factor.
CC {ECO:0000269|PubMed:14580940}.
CC -!- MISCELLANEOUS: Down-regulated in OGS biopsy.
CC -!- SIMILARITY: Belongs to the 5'-3' exonuclease family. {ECO:0000305}.
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DR EMBL; AY137776; AAN11306.1; -; mRNA.
DR EMBL; AL133623; CAB63749.1; -; mRNA.
DR EMBL; BX640905; CAE45950.1; -; mRNA.
DR EMBL; CR627396; CAH10490.1; -; mRNA.
DR EMBL; CR749518; CAH18332.1; -; mRNA.
DR EMBL; BC039314; AAH39314.1; -; mRNA.
DR EMBL; BC048104; AAH48104.1; -; mRNA.
DR EMBL; AK096177; BAC04718.1; -; mRNA.
DR CCDS; CCDS3123.1; -. [Q8IZH2-1]
DR CCDS; CCDS63801.1; -. [Q8IZH2-2]
DR CCDS; CCDS75028.1; -. [Q8IZH2-3]
DR PIR; T43461; T43461.
DR RefSeq; NP_001269786.1; NM_001282857.1. [Q8IZH2-2]
DR RefSeq; NP_001269788.1; NM_001282859.1. [Q8IZH2-3]
DR RefSeq; NP_061874.3; NM_019001.4. [Q8IZH2-1]
DR AlphaFoldDB; Q8IZH2; -.
DR SMR; Q8IZH2; -.
DR BioGRID; 119970; 238.
DR CORUM; Q8IZH2; -.
DR DIP; DIP-31174N; -.
DR IntAct; Q8IZH2; 72.
DR MINT; Q8IZH2; -.
DR STRING; 9606.ENSP00000264951; -.
DR MoonDB; Q8IZH2; Predicted.
DR GlyGen; Q8IZH2; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q8IZH2; -.
DR PhosphoSitePlus; Q8IZH2; -.
DR BioMuta; XRN1; -.
DR DMDM; 74714582; -.
DR EPD; Q8IZH2; -.
DR jPOST; Q8IZH2; -.
DR MassIVE; Q8IZH2; -.
DR MaxQB; Q8IZH2; -.
DR PaxDb; Q8IZH2; -.
DR PeptideAtlas; Q8IZH2; -.
DR PRIDE; Q8IZH2; -.
DR ProteomicsDB; 71350; -. [Q8IZH2-1]
DR ProteomicsDB; 71351; -. [Q8IZH2-2]
DR ProteomicsDB; 71352; -. [Q8IZH2-3]
DR Antibodypedia; 33491; 104 antibodies from 25 providers.
DR DNASU; 54464; -.
DR Ensembl; ENST00000264951.8; ENSP00000264951.4; ENSG00000114127.11. [Q8IZH2-1]
DR Ensembl; ENST00000392981.7; ENSP00000376707.2; ENSG00000114127.11. [Q8IZH2-2]
DR Ensembl; ENST00000463916.5; ENSP00000418404.1; ENSG00000114127.11. [Q8IZH2-3]
DR GeneID; 54464; -.
DR KEGG; hsa:54464; -.
DR MANE-Select; ENST00000392981.7; ENSP00000376707.2; NM_001282857.2; NP_001269786.1. [Q8IZH2-2]
DR UCSC; uc003eus.4; human. [Q8IZH2-1]
DR CTD; 54464; -.
DR DisGeNET; 54464; -.
DR GeneCards; XRN1; -.
DR HGNC; HGNC:30654; XRN1.
DR HPA; ENSG00000114127; Low tissue specificity.
DR MIM; 607994; gene.
DR neXtProt; NX_Q8IZH2; -.
DR OpenTargets; ENSG00000114127; -.
DR PharmGKB; PA134878471; -.
DR VEuPathDB; HostDB:ENSG00000114127; -.
DR eggNOG; KOG2045; Eukaryota.
DR GeneTree; ENSGT00670000098080; -.
DR HOGENOM; CLU_001581_3_0_1; -.
DR OMA; VASWPWF; -.
DR OrthoDB; 685597at2759; -.
DR PhylomeDB; Q8IZH2; -.
DR TreeFam; TF105757; -.
DR PathwayCommons; Q8IZH2; -.
DR Reactome; R-HSA-430039; mRNA decay by 5' to 3' exoribonuclease.
DR Reactome; R-HSA-450385; Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA.
DR Reactome; R-HSA-450513; Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA.
DR SignaLink; Q8IZH2; -.
DR BioGRID-ORCS; 54464; 468 hits in 1103 CRISPR screens.
DR ChiTaRS; XRN1; human.
DR GenomeRNAi; 54464; -.
DR Pharos; Q8IZH2; Tbio.
DR PRO; PR:Q8IZH2; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q8IZH2; protein.
DR Bgee; ENSG00000114127; Expressed in epithelial cell of pancreas and 187 other tissues.
DR ExpressionAtlas; Q8IZH2; baseline and differential.
DR Genevisible; Q8IZH2; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000932; C:P-body; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0045202; C:synapse; IEA:Ensembl.
DR GO; GO:0004534; F:5'-3' exoribonuclease activity; IMP:BHF-UCL.
DR GO; GO:0051880; F:G-quadruplex DNA binding; ISS:BHF-UCL.
DR GO; GO:0002151; F:G-quadruplex RNA binding; ISS:BHF-UCL.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0070034; F:telomerase RNA binding; IC:BHF-UCL.
DR GO; GO:0071409; P:cellular response to cycloheximide; IEA:Ensembl.
DR GO; GO:1905795; P:cellular response to puromycin; IEA:Ensembl.
DR GO; GO:0071044; P:histone mRNA catabolic process; IMP:UniProtKB.
DR GO; GO:0032211; P:negative regulation of telomere maintenance via telomerase; IC:BHF-UCL.
DR GO; GO:0017148; P:negative regulation of translation; IEA:Ensembl.
DR GO; GO:0071028; P:nuclear mRNA surveillance; IMP:UniProtKB.
DR GO; GO:0000956; P:nuclear-transcribed mRNA catabolic process; IMP:UniProtKB.
DR GO; GO:0033574; P:response to testosterone; IEA:Ensembl.
DR GO; GO:0090503; P:RNA phosphodiester bond hydrolysis, exonucleolytic; ISS:BHF-UCL.
DR GO; GO:0016075; P:rRNA catabolic process; IMP:UniProtKB.
DR InterPro; IPR027073; 5_3_exoribonuclease.
DR InterPro; IPR016494; 5_3_exoribonuclease_1.
DR InterPro; IPR004859; Put_53exo.
DR InterPro; IPR041385; SH3_12.
DR InterPro; IPR040992; XRN1_D1.
DR InterPro; IPR041106; XRN1_D2_D3.
DR InterPro; IPR041412; Xrn1_helical.
DR PANTHER; PTHR12341; PTHR12341; 1.
DR PANTHER; PTHR12341:SF7; PTHR12341:SF7; 1.
DR Pfam; PF18129; SH3_12; 1.
DR Pfam; PF18332; XRN1_D1; 1.
DR Pfam; PF18334; XRN1_D2_D3; 1.
DR Pfam; PF17846; XRN_M; 1.
DR Pfam; PF03159; XRN_N; 1.
DR PIRSF; PIRSF006743; Exonuclease_Xnr1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; DNA-binding; Exonuclease; Hydrolase;
KW Nuclease; Phosphoprotein; Reference proteome; RNA-binding;
KW Tumor suppressor.
FT CHAIN 1..1706
FT /note="5'-3' exoribonuclease 1"
FT /id="PRO_0000071392"
FT REGION 1619..1706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1619..1693
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1348
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97789"
FT MOD_RES 1645
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 449..459
FT /note="DDFLADQAACY -> EYVFANAFILK (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_016692"
FT VAR_SEQ 460..1706
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_016693"
FT VAR_SEQ 1354
FT /note="M -> MK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_016694"
FT VAR_SEQ 1540..1552
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_016695"
FT VARIANT 674
FT /note="S -> G (in dbSNP:rs35214510)"
FT /id="VAR_053000"
FT VARIANT 1259
FT /note="V -> A (in dbSNP:rs35902661)"
FT /id="VAR_053001"
FT CONFLICT 48
FT /note="D -> G (in Ref. 2; CAE45950)"
FT /evidence="ECO:0000305"
FT CONFLICT 55
FT /note="I -> T (in Ref. 4; BAC04718)"
FT /evidence="ECO:0000305"
FT CONFLICT 113
FT /note="K -> E (in Ref. 2; CAH18332)"
FT /evidence="ECO:0000305"
FT CONFLICT 142
FT /note="R -> K (in Ref. 3; AAH48104)"
FT /evidence="ECO:0000305"
FT CONFLICT 148
FT /note="K -> E (in Ref. 2; CAH18332)"
FT /evidence="ECO:0000305"
FT CONFLICT 572
FT /note="Missing (in Ref. 2; CAB63749)"
FT /evidence="ECO:0000305"
FT CONFLICT 722
FT /note="L -> I (in Ref. 2; CAE45950)"
FT /evidence="ECO:0000305"
FT CONFLICT 834
FT /note="K -> R (in Ref. 2; CAH18332)"
FT /evidence="ECO:0000305"
FT CONFLICT 1250
FT /note="Q -> R (in Ref. 2; CAH18332)"
FT /evidence="ECO:0000305"
FT CONFLICT 1463
FT /note="L -> F (in Ref. 2; CAE45950)"
FT /evidence="ECO:0000305"
FT CONFLICT 1686
FT /note="S -> P (in Ref. 2; CAH18332)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1706 AA; 194107 MW; D06A76208DE78698 CRC64;
MGVPKFYRWI SERYPCLSEV VKEHQIPEFD NLYLDMNGII HQCSHPNDDD VHFRISDDKI
FTDIFHYLEV LFRIIKPRKV FFMAVDGVAP RAKMNQQRGR RFRSAKEAED KIKKAIEKGE
TLPTEARFDS NCITPGTEFM ARLHEHLKYF VNMKISTDKS WQGVTIYFSG HETPGEGEHK
IMEFIRSEKA KPDHDPNTRH CLYGLDADLI MLGLTSHEAH FSLLREEVRF GGKKTQRVCA
PEETTFHLLH LSLMREYIDY EFSVLKEKIT FKYDIERIID DWILMGFLVG NDFIPHLPHL
HINHDALPLL YGTYVTILPE LGGYINESGH LNLPRFEKYL VKLSDFDREH FSEVFVDLKW
FESKVGNKYL NEAAGVAAEE ARNYKEKKKL KGQENSLCWT ALDKNEGEMI TSKDNLEDET
EDDDLFETEF RQYKRTYYMT KMGVDVVSDD FLADQAACYV QAIQWILHYY YHGVQSWSWY
YPYHYAPFLS DIHNISTLKI HFELGKPFKP FEQLLAVLPA ASKNLLPACY QHLMTNEDSP
IIEYYPPDFK TDLNGKQQEW EAVVLIPFID EKRLLEAMET CNHSLKKEER KRNQHSECLM
CWYDRDTEFI YPSPWPEKFP AIERCCTRYK IISLDAWRVD INKNKITRID QKALYFCGFP
TLKHIRHKFF LKKSGVQVFQ QSSRGENMML EILVDAESDE LTVENVASSV LGKSVFVNWP
HLEEARVVAV SDGETKFYLE EPPGTQKLYS GRTAPPSKVV HLGDKEQSNW AKEVQGISEH
YLRRKGIIIN ETSAVVYAQL LTGRKYQINQ NGEVRLEKQW SKQVVPFVYQ TIVKDIRAFD
SRFSNIKTLD DLFPLRSMVF MLGTPYYGCT GEVQDSGDVI TEGRIRVIFS IPCEPNLDAL
IQNQHKYSIK YNPGYVLASR LGVSGYLVSR FTGSIFIGRG SRRNPHGDHK ANVGLNLKFN
KKNEEVPGYT KKVGSEWMYS SAAEQLLAEY LERAPELFSY IAKNSQEDVF YEDDIWPGEN
ENGAEKVQEI ITWLKGHPVS TLSRSSCDLQ ILDAAIVEKI EEEVEKCKQR KNNKKVRVTV
KPHLLYRPLE QQHGVIPDRD AEFCLFDRVV NVRENFSVPV GLRGTIIGIK GANREADVLF
EVLFDEEFPG GLTIRCSPGR GYRLPTSALV NLSHGSRSET GNQKLTAIVK PQPAVHQHSS
SSSVSSGHLG ALNHSPQSLF VPTQVPTKDD DEFCNIWQSL QGSGKMQYFQ PTIQEKGAVL
PQEISQVNQH HKSGFNDNSV KYQQRKHDPH RKFKEECKSP KAECWSQKMS NKQPNSGIEN
FLASLNISKE NEVQSSHHGE PPSEEHLSPQ SFAMGTRMLK EILKIDGSNT VDHKNEIKQI
ANEIPVSSNR RDEYGLPSQP KQNKKLASYM NKPHSANEYH NVQSMDNMCW PAPSQIPPVS
TPVTELSRIC SLVGMPQPDF SFLRMPQTMT VCQVKLSNGL LVHGPQCHSE NEAKEKAALF
ALQQLGSLGM NFPLPSQVFA NYPSAVPPGT IPPAFPPPTG WDHYGSNYAL GAANIMPSSS
HLFGSMPWGP SVPVPGKPFH HTLYSGTMPM AGGIPGGVHN QFIPLQVTKK RVANKKNFEN
KEAQSSQATP VQTSQPDSSN IVKVSPRESS SASLKSSPIA QPASSFQVET ASQGHSISHH
KSTPISSSRR KSRKLAVNFG VSKPSE
