ID RIF1_MOUSE Reviewed; 2419 AA. AC Q6PR54; Q6T8D9; Q7TPD8; Q8BTU2; Q8C408; Q9CS77; DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2005, sequence version 2. DT 02-SEP-2026, entry version 156. DE RecName: Full=Telomere-associated protein RIF1 {ECO:0000305}; DE AltName: Full=Rap1-interacting factor 1 homolog {ECO:0000305|PubMed:15042697}; DE Short=mRif1 {ECO:0000303|PubMed:15042697}; GN Name=Rif1 {ECO:0000312|MGI:MGI:1098622}; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH TRF2, SUBCELLULAR RP LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE. RC STRAIN=129/Sv; RX PubMed=15042697; DOI=10.1002/dvdy.10471; RA Adams I.R., McLaren A.; RT "Identification and characterisation of mRif1: a mouse telomere-associated RT protein highly expressed in germ cells and embryo-derived pluripotent stem RT cells."; RL Dev. Dyn. 229:733-744(2004). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). RA Silvermann J., Takai H., Buonomo S.B.C., Eisenhaber F., de Lange T.; RT "ATM-mediated S-phase checkpoint function for hRif1."; RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 416-1011; 1061-1556 AND RP 1859-2419. RC STRAIN=C57BL/6J; TISSUE=Liver, and Thymus; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1860-2419. RC STRAIN=C57BL/6J; TISSUE=Brain; 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-385; SER-391; SER-1407; RP SER-1457; SER-1528; SER-1538; SER-1540; SER-1550; SER-1565; SER-1683 AND RP SER-2144, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Lung, Spleen, and Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [6] RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND INTERACTION WITH RP TP53BP1. RX PubMed=23333305; DOI=10.1016/j.molcel.2013.01.002; RA Chapman J.R., Barral P., Vannier J.B., Borel V., Steger M., Tomas-Loba A., RA Sartori A.A., Adams I.R., Batista F.D., Boulton S.J.; RT "RIF1 is essential for 53BP1-dependent nonhomologous end joining and RT suppression of DNA double-strand break resection."; RL Mol. Cell 49:858-871(2013). RN [7] RP FUNCTION. RX PubMed=23333306; DOI=10.1016/j.molcel.2013.01.001; RA Escribano-Diaz C., Orthwein A., Fradet-Turcotte A., Xing M., Young J.T., RA Tkac J., Cook M.A., Rosebrock A.P., Munro M., Canny M.D., Xu D., RA Durocher D.; RT "A cell cycle-dependent regulatory circuit composed of 53BP1-RIF1 and RT BRCA1-CtIP controls DNA repair pathway choice."; RL Mol. Cell 49:872-883(2013). RN [8] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH TP53BP1. RX PubMed=23306437; DOI=10.1126/science.1231573; RA Zimmermann M., Lottersberger F., Buonomo S.B., Sfeir A., de Lange T.; RT "53BP1 regulates DSB repair using Rif1 to control 5' end resection."; RL Science 339:700-704(2013). RN [9] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH TP53BP1. RX PubMed=23306439; DOI=10.1126/science.1230624; RA Di Virgilio M., Callen E., Yamane A., Zhang W., Jankovic M., Gitlin A.D., RA Feldhahn N., Resch W., Oliveira T.Y., Chait B.T., Nussenzweig A., RA Casellas R., Robbiani D.F., Nussenzweig M.C.; RT "Rif1 prevents resection of DNA breaks and promotes immunoglobulin class RT switching."; RL Science 339:711-715(2013). CC -!- FUNCTION: Key regulator of TP53BP1 that plays a key role in the repair CC of double-strand DNA breaks (DSBs) in response to DNA damage: acts by CC promoting non-homologous end joining (NHEJ)-mediated repair of DSBs CC (PubMed:23306437, PubMed:23306439, PubMed:23333305). In response to DNA CC damage, interacts with ATM-phosphorylated TP53BP1 (PubMed:23306437, CC PubMed:23306439, PubMed:23333305). Interaction with TP53BP1 leads to CC dissociate the interaction between NUDT16L1/TIRR and TP53BP1, thereby CC unmasking the tandem Tudor-like domain of TP53BP1 and allowing CC recruitment to DNA DSBs (By similarity). Once recruited to DSBs, RIF1 CC and TP53BP1 act by promoting NHEJ-mediated repair of DSBs CC (PubMed:23306437, PubMed:23333305). In the same time, RIF1 and TP53BP1 CC specifically counteract the function of BRCA1 by blocking DSBs CC resection via homologous recombination (HR) during G1 phase CC (PubMed:23306437, PubMed:23333305). Also required for immunoglobulin CC class-switch recombination (CSR) during antibody genesis, a process CC that involves the generation of DNA DSBs (PubMed:23306439, CC PubMed:23333305, PubMed:23333306). Promotes NHEJ of dysfunctional CC telomeres (PubMed:23333305). {ECO:0000250|UniProtKB:Q5UIP0, CC ECO:0000269|PubMed:23306437, ECO:0000269|PubMed:23306439, CC ECO:0000269|PubMed:23333305, ECO:0000269|PubMed:23333306}. CC -!- SUBUNIT: Interacts with TP53BP1 (when phosphorylated by ATM) CC (PubMed:23306437, PubMed:23306439, PubMed:23333305). May interact with CC TRF2 (PubMed:15042697). Interacts with SHLD2 (By similarity). Interacts CC with ERCC6 (via WHD region) (By similarity). Interacts with ASTE1 (By CC similarity). {ECO:0000250|UniProtKB:Q5UIP0, CC ECO:0000269|PubMed:23306437, ECO:0000269|PubMed:23306439, CC ECO:0000269|PubMed:23333305, ECO:0000305|PubMed:15042697}. CC -!- INTERACTION: CC Q6PR54; Q80Z64: Nanog; NbExp=5; IntAct=EBI-2312621, EBI-2312517; CC Q6PR54; Q61066: Nr0b1; NbExp=2; IntAct=EBI-2312621, EBI-2312665; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15042697}. Chromosome CC {ECO:0000269|PubMed:23306437, ECO:0000269|PubMed:23306439, CC ECO:0000269|PubMed:23333305}. Chromosome, telomere CC {ECO:0000269|PubMed:15042697}. Cytoplasm, cytoskeleton, spindle CC {ECO:0000250|UniProtKB:Q5UIP0}. Note=Exhibits ATM- and TP53BP1- CC dependent localization to uncapped or aberrant telomeres and to DNA CC double strand breaks (DSBs). Following interaction with TP53BP1, CC recruited to sites of DNA damage, such as DSBs (PubMed:23306437, CC PubMed:23306439, PubMed:23333305). Localizes to microtubules of the CC midzone of the mitotic spindle during anaphase, and to condensed CC chromosomes in telophase (By similarity). While the majority of the CC protein appears nuclear and distinct from normal telomere structures, a CC small fraction may bind to telomeres in embryonic stem cells CC (PubMed:15042697). {ECO:0000250|UniProtKB:Q5UIP0, CC ECO:0000269|PubMed:15042697, ECO:0000269|PubMed:23306437, CC ECO:0000269|PubMed:23306439, ECO:0000269|PubMed:23333305}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q6PR54-1; Sequence=Displayed; CC Name=2; CC IsoId=Q6PR54-2; Sequence=VSP_014433; CC Name=3; CC IsoId=Q6PR54-3; Sequence=VSP_014432; CC -!- TISSUE SPECIFICITY: Expressed in Sertoli cells, prospermatagonia, early CC primary spermatocytes, and in oocytes at all stages of their growth. CC Expressed in embryonic stem (ES) and embryonic germ (EG) cells: CC expression is lost upon differentiation. {ECO:0000269|PubMed:15042697}. CC -!- DEVELOPMENTAL STAGE: Found in the nucleus of germinal-vesicle (GV) CC stage oocytes prior to fertilization. Accumulates in the male and CC female pronucleus after fertilization. Expressed in the nuclei of all CC blastomeres from the two cell stage to the compacted morula stage, CC although absent from the polar body and inner cell mass (ICM). Found in CC the nuclei of polar and mural trophectoderm cells from 3.5 dpc, and at CC high levels in the epiblast from 5.5 dpc to 7.5 dpc. Expressed by CC primitive germ cells (PGCs) in both male and female from 9.5 dpc to CC 13.5 dpc, at which point expression declines. A low level is observed CC in Sertoli cells of the testis at 17.5 dpc. CC {ECO:0000269|PubMed:15042697}. CC -!- DISRUPTION PHENOTYPE: Embryonic lethality in inbred 129/Ola and outbred CC MF1 mouse strains: 7.5 dpc embryos display significant developmental CC retardation (PubMed:23333305). Female-specific lethality in a CD1 CC strain background, while males survive (PubMed:23333305). Surviving CC males grow normally, are fertile, but are subject to infections due to CC defects in the immune response (PubMed:23333305). Surviving males are CC severely compromised for TP53BP1-dependent class-switch recombination CC (CSR) and fusion of dysfunctional telomeres (PubMed:23333305). CC {ECO:0000269|PubMed:23333305}. CC -!- MISCELLANEOUS: [Isoform 3]: May be due to a competing acceptor splice CC site. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the RIF1 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAB30843.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAC38846.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA.; Evidence={ECO:0000305}; CC Sequence=BAC40506.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={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; AY428571; AAR87833.2; -; mRNA. DR EMBL; AY585206; AAS94124.1; -; mRNA. DR EMBL; AK017618; BAB30843.1; ALT_INIT; mRNA. DR EMBL; AK083291; BAC38846.1; ALT_SEQ; mRNA. DR EMBL; AK088688; BAC40506.1; ALT_SEQ; mRNA. DR EMBL; BC055320; AAH55320.1; -; mRNA. DR CCDS; CCDS50583.1; -. [Q6PR54-3] DR RefSeq; NP_001342343.1; NM_001355414.1. [Q6PR54-3] DR RefSeq; NP_001342344.1; NM_001355415.1. [Q6PR54-1] DR RefSeq; NP_780447.4; NM_175238.6. [Q6PR54-3] DR RefSeq; XP_011237438.1; XM_011239136.3. [Q6PR54-2] DR AlphaFoldDB; Q6PR54; -. DR BioGRID; 206234; 18. DR DIP; DIP-54907N; -. DR FunCoup; Q6PR54; 4008. DR IntAct; Q6PR54; 7. DR MINT; Q6PR54; -. DR STRING; 10090.ENSMUSP00000108313; -. DR GlyGen; Q6PR54; 1 site. DR iPTMnet; Q6PR54; -. DR PhosphoSitePlus; Q6PR54; -. DR SwissPalm; Q6PR54; -. DR jPOST; Q6PR54; -. DR PaxDb; 10090-ENSMUSP00000108313; -. DR PeptideAtlas; Q6PR54; -. DR ProteomicsDB; 253284; -. [Q6PR54-1] DR ProteomicsDB; 253285; -. [Q6PR54-2] DR ProteomicsDB; 253286; -. [Q6PR54-3] DR Pumba; Q6PR54; -. DR Antibodypedia; 33653; 140 antibodies from 29 providers. DR DNASU; 51869; -. DR Ensembl; ENSMUST00000112693.10; ENSMUSP00000108313.3; ENSMUSG00000036202.17. [Q6PR54-3] DR GeneID; 51869; -. DR KEGG; mmu:51869; -. DR UCSC; uc008jqq.1; mouse. [Q6PR54-3] DR UCSC; uc008jqr.1; mouse. [Q6PR54-1] DR UCSC; uc008jqt.1; mouse. [Q6PR54-2] DR AGR; MGI:1098622; -. DR CTD; 55183; -. DR MGI; MGI:1098622; Rif1. DR VEuPathDB; HostDB:ENSMUSG00000036202; -. DR eggNOG; ENOG502QV6C; Eukaryota. DR GeneTree; ENSGT00390000012204; -. DR HOGENOM; CLU_000989_0_0_1; -. DR InParanoid; Q6PR54; -. DR OMA; NMRSTDY; -. DR Reactome; R-MMU-5693571; Nonhomologous End-Joining (NHEJ). DR BioGRID-ORCS; 51869; 18 hits in 115 CRISPR screens. DR PRO; PR:Q6PR54; -. DR Proteomes; UP000000589; Chromosome 2. DR RNAct; Q6PR54; protein. DR Bgee; ENSMUSG00000036202; Expressed in spermatocyte and 262 other cell types or tissues. DR ExpressionAtlas; Q6PR54; baseline and differential. DR GO; GO:0000785; C:chromatin; IMP:BHF-UCL. DR GO; GO:0005694; C:chromosome; EXP:UniProtKB. DR GO; GO:0000781; C:chromosome, telomeric region; IDA:MGI. DR GO; GO:0140445; C:chromosome, telomeric repeat region; IDA:BHF-UCL. DR GO; GO:0000793; C:condensed chromosome; ISO:GO_Central. DR GO; GO:0001939; C:female pronucleus; IDA:MGI. DR GO; GO:0001940; C:male pronucleus; IDA:MGI. DR GO; GO:0031965; C:nuclear membrane; ISO:GO_Central. DR GO; GO:0005654; C:nucleoplasm; ISO:GO_Central. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0005886; C:plasma membrane; ISO:GO_Central. DR GO; GO:0035861; C:site of double-strand break; IDA:UniProtKB. DR GO; GO:0051233; C:spindle midzone; ISO:GO_Central. DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI. DR GO; GO:0006974; P:DNA damage response; ISS:UniProtKB. DR GO; GO:2000042; P:negative regulation of double-strand break repair via homologous recombination; IMP:UniProtKB. DR GO; GO:0045814; P:negative regulation of gene expression, epigenetic; IDA:BHF-UCL. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:BHF-UCL. DR GO; GO:2001034; P:positive regulation of double-strand break repair via nonhomologous end joining; IMP:UniProtKB. DR GO; GO:0045830; P:positive regulation of isotype switching; IMP:UniProtKB. DR GO; GO:0019827; P:stem cell population maintenance; IMP:MGI. DR GO; GO:0031509; P:subtelomeric heterochromatin formation; IMP:BHF-UCL. DR GO; GO:0000723; P:telomere maintenance; IMP:BHF-UCL. DR GO; GO:0043247; P:telomere maintenance in response to DNA damage; ISO:GO_Central. DR CDD; cd14267; Rif1_CTD_C-II_like; 1. DR FunFam; 1.25.10.10:FF:000255; Telomere-associated protein RIF1 isoform 1; 1. DR InterPro; IPR016024; ARM-type_fold. DR InterPro; IPR022031; Rif1_N. DR PANTHER; PTHR22928; TELOMERE-ASSOCIATED PROTEIN RIF1; 1. DR PANTHER; PTHR22928:SF3; TELOMERE-ASSOCIATED PROTEIN RIF1; 1. DR Pfam; PF12231; Rif1_N; 1. DR SUPFAM; SSF48371; ARM repeat; 1. PE 1: Evidence at protein level; KW Alternative splicing; Cell cycle; Chromosome; Cytoplasm; Cytoskeleton; KW DNA damage; DNA repair; Nucleus; Phosphoprotein; Reference proteome; KW Telomere. FT CHAIN 1..2419 FT /note="Telomere-associated protein RIF1" FT /id="PRO_0000097334" FT REGION 1..24 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 373..408 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1184..1594 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1613..1637 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1812..1836 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1882..2419 FT /note="Interaction with condensed chromosomes in telophase" FT /evidence="ECO:0000250" FT REGION 1890..1914 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1929..1983 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2119..2394 FT /note="Interaction with ERCC6" FT /evidence="ECO:0000250|UniProtKB:Q5UIP0" FT REGION 2182..2212 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 373..385 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1184..1198 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1199..1217 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1228..1255 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1263..1272 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1289..1302 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1323..1345 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1416..1455 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1457..1467 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1507..1516 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1525..1537 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1551..1560 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1572..1581 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2189..2212 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 385 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 391 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 779 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q5UIP0" FT MOD_RES 976 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q5UIP0" FT MOD_RES 1005 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q5UIP0" FT MOD_RES 1044 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q5UIP0" FT MOD_RES 1215 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q5UIP0" FT MOD_RES 1231 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q5UIP0" FT MOD_RES 1233 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q5UIP0" FT MOD_RES 1407 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1439 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q5UIP0" FT MOD_RES 1457 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1498 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q5UIP0" FT MOD_RES 1504 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q5UIP0" FT MOD_RES 1528 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1538 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1540 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1542 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q5UIP0" FT MOD_RES 1550 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1562 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q5UIP0" FT MOD_RES 1565 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1680 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q5UIP0" FT MOD_RES 1683 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1780 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q5UIP0" FT MOD_RES 1784 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q5UIP0" FT MOD_RES 1842 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q5UIP0" FT MOD_RES 1931 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q5UIP0" FT MOD_RES 2094 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q5UIP0" FT MOD_RES 2109 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q5UIP0" FT MOD_RES 2121 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q5UIP0" FT MOD_RES 2125 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q5UIP0" FT MOD_RES 2144 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 2153 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q5UIP0" FT MOD_RES 2208 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q5UIP0" FT MOD_RES 2287 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q5UIP0" FT MOD_RES 2341 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q5UIP0" FT MOD_RES 2413 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q5UIP0" FT MOD_RES 2419 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q5UIP0" FT VAR_SEQ 167 FT /note="I -> ISHWFLHC (in isoform 3)" FT /evidence="ECO:0000303|Ref.2" FT /id="VSP_014432" FT VAR_SEQ 2198..2223 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_014433" FT CONFLICT 211 FT /note="M -> V (in Ref. 1; AAR87833)" FT /evidence="ECO:0000305" FT CONFLICT 548 FT /note="M -> V (in Ref. 1; AAR87833)" FT /evidence="ECO:0000305" FT CONFLICT 586 FT /note="F -> L (in Ref. 1; AAR87833 and 3; BAC40506)" FT /evidence="ECO:0000305" FT CONFLICT 592 FT /note="E -> G (in Ref. 1; AAR87833 and 3; BAC40506)" FT /evidence="ECO:0000305" FT CONFLICT 596 FT /note="E -> G (in Ref. 1; AAR87833 and 3; BAC40506)" FT /evidence="ECO:0000305" FT CONFLICT 717 FT /note="S -> A (in Ref. 1; AAR87833 and 3; BAC40506)" FT /evidence="ECO:0000305" FT CONFLICT 743 FT /note="V -> A (in Ref. 1; AAR87833 and 3; BAC40506)" FT /evidence="ECO:0000305" FT CONFLICT 802 FT /note="K -> E (in Ref. 3; BAC40506)" FT /evidence="ECO:0000305" FT CONFLICT 959 FT /note="I -> S (in Ref. 1; AAR87833 and 3; BAC40506)" FT /evidence="ECO:0000305" FT CONFLICT 1066 FT /note="K -> R (in Ref. 3; BAB30843)" FT /evidence="ECO:0000305" FT CONFLICT 1122 FT /note="M -> T (in Ref. 1; AAR87833)" FT /evidence="ECO:0000305" FT CONFLICT 1179 FT /note="L -> M (in Ref. 1; AAR87833)" FT /evidence="ECO:0000305" FT CONFLICT 1238 FT /note="I -> M (in Ref. 1; AAR87833)" FT /evidence="ECO:0000305" FT CONFLICT 1527 FT /note="A -> R (in Ref. 3; BAB30843)" FT /evidence="ECO:0000305" FT CONFLICT 1584 FT /note="A -> S (in Ref. 1; AAR87833)" FT /evidence="ECO:0000305" FT CONFLICT 1671 FT /note="N -> T (in Ref. 1; AAR87833)" FT /evidence="ECO:0000305" FT CONFLICT 1772 FT /note="V -> L (in Ref. 1; AAR87833)" FT /evidence="ECO:0000305" FT CONFLICT 1798 FT /note="P -> S (in Ref. 1; AAR87833)" FT /evidence="ECO:0000305" FT CONFLICT 1897 FT /note="V -> I (in Ref. 1; AAR87833)" FT /evidence="ECO:0000305" FT CONFLICT 1918 FT /note="E -> D (in Ref. 1; AAR87833)" FT /evidence="ECO:0000305" FT CONFLICT 1997 FT /note="L -> F (in Ref. 1; AAR87833)" FT /evidence="ECO:0000305" FT CONFLICT 2018 FT /note="F -> L (in Ref. 1; AAR87833)" FT /evidence="ECO:0000305" FT CONFLICT 2024 FT /note="M -> T (in Ref. 1; AAR87833)" FT /evidence="ECO:0000305" FT CONFLICT 2052 FT /note="N -> K (in Ref. 1; AAR87833)" FT /evidence="ECO:0000305" FT CONFLICT 2114 FT /note="Missing (in Ref. 1; AAR87833)" FT /evidence="ECO:0000305" FT CONFLICT 2394 FT /note="E -> G (in Ref. 1; AAR87833)" FT /evidence="ECO:0000305" SQ SEQUENCE 2419 AA; 266228 MW; 016A1A4CEF25B8F9 CRC64; MTAPGRSPLE PLLETWEDPS VPPGEQTDAY LTLTSRMTGE EGKEVIAEIE KNLSRLYTVL KAHISSQNSE LSSAALQALG FCLYNPRITS GLSEANIQEL LLTLNGIIKS SDKNVCTRAL WVISKQTFPA ELVSKMVSSI IDSLEVILSK GEIHSAVVDF EALNVIIRLI EQAPVQMGEE SVRWAKLVIP LVVHSAQKVH LRGATALEMG MPLLLQKQQE IALITEHLMT TKLISELQKL FKNKNETYVL KLWPLFVKLL GKTLHRSGSF INSLLQLEEL GFRSGTPMIK KIAFIAWKSL IDNFALNPDI LCSAKRLKLL MQPLSSIHVR TETLALTKLE VWWYLLMRLG PQLPANFEQV CVPLIQSTIS VDSIPSPQGN SSRGSASPGL SPLTPGHKGA SPYGSPRGNL SSNTGGMAAI PSIQLLGLEM MLHFLLGPEV LSFAKQHKIV LSLEPLEHPL ISSPSFFSKY AHTLITAVHD SFVSVGKDAS DAVVSAIWKE LISLVKSVTE AGNRKEKSGS EVLTLLLKSL ENIVKSEVFP VSKTLVLMEI TVKGLPPKVL GSPAYQVANM DILNGTPALF LIQLIFNNNL LECGVEDEKF FLNLETLVGC VLSGPTSPLA FSDSVLTVIN QNAKQLVNKE HLWRMWSMIV SPLTDVIHQT NEVNQGDALE HNFSAIYGAL TLPINHIFSA QTFPTGTMKA LLKTWSELYR AFTRCASLVA TAEENLCCEE LSSKIMCSLE DEVLSDLLFL DRISHIIIVM VDCIDFSPYN KKYQPKIKSP QRSSDWSRKK KEPLGKLASL FKLIVKVIDT FHTLSLKETF SDTLLAIGNS IISMLSNVFG HISLPSMIRE IFATFTRPLA LLYENSKLDE APKVYTSLNN KLEKLLGEIV ACLQFSYLGA YDSELLEHLS PLLCVIFLHK NKQIRKQSAL LWNATFAKAT ALVYPEELKP ILRQAKQKIL LLLPGLENVE MMDESSEPYS ESTENSQLNV KISGMERKSS GKRDSILAHT KDKKKKVKLS AKLKLESSSP KIKSGKLLEE EKSTDFVFIP PEGKETKARV LTEHQKEVLK TKRCDIPALY NNLDASQDTL FSAQFSQEES MESLTLTEKP KEDAKIIKEE QMESTIFIHQ DAPENCGIDE HSENASLPNC GGSVAETNPE TLITGFDARK EVLISSKILS AESSSSTETS VVSSSSVSNA TFSGTPPQPT SRRQTFITLE KFDGSETRPF SPSPLNNISS TVTVRNNQDN TTNTDMPPKA RKREVTNSKS DSENLANAGK KSSRRWSKAE QSVTKKSKPS LTSEQEEHSS ENNSPDLLSP TEHVSENDDH PSEATLEHKD GDPKPAVENA SLEDLTTEEK NVGINMESKE STASVVARTE QIVNEDSQAA ALAPNPKTLR RSSRRRSEAV DSCSDSQERE SGQQKKERRK EEEKIISKSP LRIKDDKLPT QKLTDESPIQ ENLTEKGNTL PERTSGEPSV NAEIDQNRRK PDLENVSSEG GGGTLDNLDK SSEKPLRGRT RYQTRRASQG LISAVENSES DSSEAKEEVS RKKRSGKWKN RSSDSVDIEE QEEKKAEEEV MKTANQTLDG QAVPDVDVNA AAQVCEKSTN NNRVILQDSA GPADSLQAPP KGEEKSKINK CVDSSFVSLP VPESNLRTRN ASKRLLYKQD NDSNVRVSDS SLSPEKFTQV ECQHKRSRRV RRSKSCDCCG EKSQSQEKSF IGLKNTESYA IKSVEKKKTD LQVPETAPET REARDHAETK LAGEEPLVNF HVGLKEENCT TGDSVKSEAE LQEASLPPEI VTVKEKTYDT DASEAVSEIQ GPCSENHSPA EDPGLSECKD ISQKQLSENG ELDISDVGKA CKVIAGSSPE GVETMELNVR NDAFVAADSE KSTQMDVSVD VATEEDNKKD ECEAVTTEVN VEGVATEDFN SGMDLSDTPI PVSKDVETEH AASGEIEGES NESDSGSCEE MNKEMGSHKA QMSTEIDSAR VKETDILASA SKSEEALIGR LDVNTQSFVS DIEMSSGERT VNCKTETSIE LNKLDEAKLS GNEATVGNDT LQEVCFTSEK VEKLPQCLLV QVASELGAES NTTSPEKLEL DSFGSVNESP SGMQQARCVW SPLASPSTSI LKRGLKRSQE DEISPVNKIR RVSFADPIYQ AGLADDIDRR CSVVRSHSSN SSPIIKSVKT SPTSHSKHNT TSAKGFLSPG SQSSKFKSPK KCLITEMAQE SMLSPTESVY PALVNCAASV DIILPQITSN MWARGLGQLI RAKNIKTIGD LSTLTASEIK TLPIRSPKVF NVKKALRVYH EQQMKSRGLE EIPIFDISEK AVNGVESRTV STDEERFASD LIEPVTLDTP LSKNLVAQIS ALALQLDSED LYSYTGSQLF EMHEKLGTMA NSIIRNLQSR WRSPAHENS //