FIP37_ARATH
ID FIP37_ARATH Reviewed; 330 AA.
AC Q9ZSZ8;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 119.
DE RecName: Full=FKBP12-interacting protein of 37 kDa {ECO:0000305};
DE Short=FIP-37 {ECO:0000305};
DE AltName: Full=Immunophilin-interacting protein AtFIP37 {ECO:0000303|PubMed:9807817};
DE AltName: Full=Protein WTAP homolog {ECO:0000303|PubMed:28503769};
GN Name=FIP37 {ECO:0000303|PubMed:9807817};
GN OrderedLocusNames=At3g54170 {ECO:0000312|Araport:AT3G54170};
GN ORFNames=F24B22.130 {ECO:0000312|EMBL:CAB70991.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH FKBP12.
RC STRAIN=cv. Columbia;
RX PubMed=9807817; DOI=10.1046/j.1365-313x.1998.00248.x;
RA Faure J.-D., Gingerich D., Howell S.H.;
RT "An Arabidopsis immunophilin, AtFKBP12, binds to AtFIP37 (FKBP interacting
RT protein) in an interaction that is disrupted by FK506.";
RL Plant J. 15:783-789(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=15047892; DOI=10.1104/pp.103.028050;
RA Vespa L., Vachon G., Berger F., Perazza D., Faure J.-D., Herzog M.;
RT "The immunophilin-interacting protein AtFIP37 from Arabidopsis is essential
RT for plant development and is involved in trichome endoreduplication.";
RL Plant Physiol. 134:1283-1292(2004).
RN [6]
RP INTERACTION WITH MTA.
RX PubMed=18505803; DOI=10.1105/tpc.108.058883;
RA Zhong S., Li H., Bodi Z., Button J., Vespa L., Herzog M., Fray R.G.;
RT "MTA is an Arabidopsis messenger RNA adenosine methylase and interacts with
RT a homolog of a sex-specific splicing factor.";
RL Plant Cell 20:1278-1288(2008).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [8]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, HOMODIMERIZATION,
RP INTERACTION WITH MTA AND VIR, AND SUBCELLULAR LOCATION.
RX PubMed=28503769; DOI=10.1111/nph.14586;
RA Ruzicka K., Zhang M., Campilho A., Bodi Z., Kashif M., Saleh M.,
RA Eeckhout D., El-Showk S., Li H., Zhong S., De Jaeger G., Mongan N.P.,
RA Hejatko J., Helariutta Y., Fray R.G.;
RT "A mRNA methylation in Arabidopsis reveals a role for the conserved E3
RT ubiquitin ligase HAKAI.";
RL New Phytol. 215:157-172(2017).
CC -!- FUNCTION: Probable regulatory subunit of the N6-methyltransferase
CC complex, a multiprotein complex that mediates N6-methyladenosine (m6A)
CC methylation at the 5'-[AG]GAC-3' consensus sites of some mRNAs
CC (PubMed:15047892, PubMed:28503769). Associates with MTA, MTB, VIR and
CC HAKAI to form the m6A writer complex which is essential for adenosine
CC methylation at specific mRNA sequences (PubMed:28503769). N6-
CC methyladenosine (m6A) plays a role in mRNA stability, processing,
CC translation efficiency and editing (PubMed:15047892, PubMed:28503769).
CC Essential protein required during endosperm development and
CC embryogenesis. Involved in endoreduplication, especially in trichomes.
CC May play a role in splicing events (PubMed:15047892).
CC {ECO:0000269|PubMed:15047892, ECO:0000269|PubMed:28503769}.
CC -!- SUBUNIT: Forms homodimers (PubMed:28503769). Interacts with MTA/EMB1706
CC (PubMed:18505803, PubMed:28503769). Interacts with FKBP12; interaction
CC is inhibited by the immunosuppressive drug FK506 (PubMed:9807817).
CC Interacts with VIR (PubMed:28503769). Associates with MTA, MTB, VIR and
CC HAKAI to form the m6A writer complex which is essential for adenosine
CC methylation at specific mRNA sequences (PubMed:28503769).
CC {ECO:0000269|PubMed:18505803, ECO:0000269|PubMed:28503769,
CC ECO:0000269|PubMed:9807817}.
CC -!- INTERACTION:
CC Q9ZSZ8; Q17TI5: BRX; NbExp=4; IntAct=EBI-1641243, EBI-4426649;
CC Q9ZSZ8; Q8LGG0: FKBP12; NbExp=3; IntAct=EBI-1641243, EBI-1641228;
CC Q9ZSZ8; O82486: MTA; NbExp=5; IntAct=EBI-1641243, EBI-1797380;
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:15047892,
CC ECO:0000269|PubMed:28503769}. Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:28503769}. Note=Nuclear with a speckled
CC distribution pattern. {ECO:0000269|PubMed:15047892}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed with higher levels in
CC primary and lateral roots, leaves, trichomes, and in pollen grains (at
CC protein level). {ECO:0000269|PubMed:15047892}.
CC -!- DISRUPTION PHENOTYPE: Embryogenesis arrest at the midglobular stage.
CC {ECO:0000269|PubMed:15047892}.
CC -!- SIMILARITY: Belongs to the fl(2)d family. {ECO:0000305}.
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DR EMBL; AF084570; AAC72922.1; -; mRNA.
DR EMBL; AL132957; CAB70991.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79195.1; -; Genomic_DNA.
DR EMBL; AY063940; AAL36296.1; -; mRNA.
DR EMBL; AY113943; AAM44991.1; -; mRNA.
DR PIR; T47576; T47576.
DR RefSeq; NP_190985.1; NM_115277.5.
DR AlphaFoldDB; Q9ZSZ8; -.
DR SMR; Q9ZSZ8; -.
DR BioGRID; 9901; 12.
DR IntAct; Q9ZSZ8; 10.
DR STRING; 3702.AT3G54170.1; -.
DR iPTMnet; Q9ZSZ8; -.
DR PaxDb; Q9ZSZ8; -.
DR PRIDE; Q9ZSZ8; -.
DR ProteomicsDB; 232081; -.
DR EnsemblPlants; AT3G54170.1; AT3G54170.1; AT3G54170.
DR GeneID; 824584; -.
DR Gramene; AT3G54170.1; AT3G54170.1; AT3G54170.
DR KEGG; ath:AT3G54170; -.
DR Araport; AT3G54170; -.
DR TAIR; locus:2080275; AT3G54170.
DR eggNOG; KOG2991; Eukaryota.
DR HOGENOM; CLU_061667_0_0_1; -.
DR InParanoid; Q9ZSZ8; -.
DR OMA; NCKDNLA; -.
DR OrthoDB; 1384625at2759; -.
DR PhylomeDB; Q9ZSZ8; -.
DR PRO; PR:Q9ZSZ8; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9ZSZ8; baseline and differential.
DR Genevisible; Q9ZSZ8; AT.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0043621; F:protein self-association; IPI:TAIR.
DR GO; GO:0010073; P:meristem maintenance; IMP:TAIR.
DR GO; GO:0080009; P:mRNA methylation; IMP:TAIR.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0001510; P:RNA methylation; IMP:TAIR.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR InterPro; IPR033757; WTAP.
DR PANTHER; PTHR15217; PTHR15217; 1.
DR Pfam; PF17098; Wtap; 1.
PE 1: Evidence at protein level;
KW Acetylation; Coiled coil; mRNA processing; mRNA splicing; Nucleus;
KW Reference proteome.
FT CHAIN 1..330
FT /note="FKBP12-interacting protein of 37 kDa"
FT /id="PRO_0000087258"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 56..308
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 330 AA; 37215 MW; 6B4070D5AD332004 CRC64;
MEFSSQDDDF GGDDSAANAT RASGNRRSFG DLEDDEDDIF GSTTVAPGVR TGMILSLRGS
LKNCKDDLAS CQNELESAKT EIQKWKSAFQ NESFVPAGKS PEPRFLIDYI QNLKSSEKSL
KEQLEIAKRK EASCIVQYAK REQEMAELKS AVRDLKSQLK PASMQARRLL LDPAIHEEFS
RLKNLVEEKD KKIKELQDNI AAVTFTPQSK NGKMLMAKCR TLQEENEEIG HQAAEGKIHE
LAIKLAMQKS QNAELRSQFE GLYKHMEELT NDVERSNETV IILQEKLEEK EKEIERVKKG
LEIVSELVGD KKDEVDEIDE DAKEEIAGGE
