FIPS3_ARATH
ID FIPS3_ARATH Reviewed; 997 AA.
AC F4JC20; Q9C834; Q9C904;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=FIP1[III]-like protein {ECO:0000303|PubMed:16282318};
DE Short=AtFIP1(III) {ECO:0000303|PubMed:16282318};
DE AltName: Full=Factor interacting with poly(A) polymerase-like 3 {ECO:0000305};
DE Short=AtFIPS3 {ECO:0000303|PubMed:16282318};
DE AltName: Full=Protein HOMOLOG OF YEAST FIP1 [III] {ECO:0000305};
GN Name=FIPS3 {ECO:0000303|PubMed:16282318};
GN OrderedLocusNames=At3g66652 {ECO:0000312|Araport:AT3G66652};
GN ORFNames=F5E6.1 {ECO:0000312|EMBL:AAG51321.1},
GN T8E24.6 {ECO:0000312|EMBL:AAG50995.1};
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 {ECO:0000312|Proteomes:UP000006548};
RN [1]
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 [2]
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 [3]
RP GENE FAMILY.
RX PubMed=16282318; DOI=10.1074/jbc.m510964200;
RA Forbes K.P., Addepalli B., Hunt A.G.;
RT "An Arabidopsis Fip1 homolog interacts with RNA and provides conceptual
RT links with a number of other polyadenylation factor subunits.";
RL J. Biol. Chem. 281:176-186(2006).
RN [4]
RP INTERACTION WITH CLPS5; CSTF64; CPSF30; FIPS5; PCFS1 AND PAPS4, GENE
RP FAMILY, AND NOMENCLATURE.
RX PubMed=18479511; DOI=10.1186/1471-2164-9-220;
RA Hunt A.G., Xu R., Addepalli B., Rao S., Forbes K.P., Meeks L.R., Xing D.,
RA Mo M., Zhao H., Bandyopadhyay A., Dampanaboina L., Marion A.,
RA Von Lanken C., Li Q.Q.;
RT "Arabidopsis mRNA polyadenylation machinery: comprehensive analysis of
RT protein-protein interactions and gene expression profiling.";
RL BMC Genomics 9:220-220(2008).
CC -!- FUNCTION: Component of the cleavage and polyadenylation specificity
CC factor (CPSF) complex that plays a key role in pre-mRNA 3'-end
CC formation, recognizing the AAUAAA signal sequence and interacting with
CC poly(A) polymerase and other factors to bring about cleavage and
CC poly(A) addition. FIP1L1 contributes to poly(A) site recognition and
CC stimulates poly(A) addition. Binds to U-rich RNA sequence elements
CC surrounding the poly(A) site. May act to tether poly(A) polymerase to
CC the CPSF complex. {ECO:0000250|UniProtKB:Q6UN15}.
CC -!- SUBUNIT: Component of the cleavage and polyadenylation specificity
CC factor (CPSF) complex (By similarity). Forms a complex with cleavage
CC and polyadenylation specificity factor (CPSF) subunits CLPS5, FIPS5,
CC PAPS4, PCFS1, CSTF64 and CPSF30 (PubMed:18479511).
CC {ECO:0000250|UniProtKB:Q6UN15, ECO:0000269|PubMed:18479511}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q6UN15,
CC ECO:0000255|PROSITE-ProRule:PRU00768}.
CC -!- SIMILARITY: Belongs to the FIP1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG50995.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAG51321.1; Type=Erroneous gene model prediction; 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; AC020580; AAG51321.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC036106; AAG50995.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE74427.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74428.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM64486.1; -; Genomic_DNA.
DR RefSeq; NP_001189830.1; NM_001202901.2.
DR RefSeq; NP_001326511.1; NM_001340220.1.
DR RefSeq; NP_187318.2; NM_111542.2.
DR AlphaFoldDB; F4JC20; -.
DR SMR; F4JC20; -.
DR BioGRID; 5181; 6.
DR IntAct; F4JC20; 6.
DR STRING; 3702.AT3G66652.2; -.
DR iPTMnet; F4JC20; -.
DR PaxDb; F4JC20; -.
DR PRIDE; F4JC20; -.
DR ProteomicsDB; 230579; -.
DR EnsemblPlants; AT3G66652.1; AT3G66652.1; AT3G66652.
DR EnsemblPlants; AT3G66652.2; AT3G66652.2; AT3G66652.
DR EnsemblPlants; AT3G66652.3; AT3G66652.3; AT3G66652.
DR GeneID; 819846; -.
DR Gramene; AT3G66652.1; AT3G66652.1; AT3G66652.
DR Gramene; AT3G66652.2; AT3G66652.2; AT3G66652.
DR Gramene; AT3G66652.3; AT3G66652.3; AT3G66652.
DR KEGG; ath:AT3G66652; -.
DR Araport; AT3G66652; -.
DR TAIR; locus:2084259; AT3G66652.
DR eggNOG; KOG1049; Eukaryota.
DR HOGENOM; CLU_006791_0_0_1; -.
DR InParanoid; F4JC20; -.
DR OMA; GWRNNKE; -.
DR OrthoDB; 173217at2759; -.
DR PRO; PR:F4JC20; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; F4JC20; baseline and differential.
DR Genevisible; F4JC20; AT.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR InterPro; IPR007854; Fip1_dom.
DR InterPro; IPR044976; FIPS3/FIPS5-like.
DR PANTHER; PTHR36884; PTHR36884; 3.
DR Pfam; PF05182; Fip1; 1.
PE 1: Evidence at protein level;
KW Coiled coil; mRNA processing; Nucleus; Reference proteome; RNA-binding.
FT CHAIN 1..997
FT /note="FIP1[III]-like protein"
FT /id="PRO_0000431326"
FT REGION 250..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 534..553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 880..900
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 930..963
FT /evidence="ECO:0000255"
FT MOTIF 397..404
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 250..270
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..306
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..343
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..359
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..427
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..466
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 997 AA; 115371 MW; CF2E90C72B0E4219 CRC64;
MDSTDDDFGD LYVDDAKFQA TDAFESECAT NSGEDKGFEE TVKSDSEGEV KKFDVVAKDS
SPCDDDDCAM NLTEADEESE FSDSDDDLNI VLKDDDSKAL PASCVFNTNF GGYEASKASS
FQRRWTRNAS ANNACIDPSL GMSQYRYSFP NPWSRTPFDV NLDVLEKKPW RDPGTDTSDF
FNFGLNEQSW KDYCKPLGRA IEVRGGTLER IPSADLRRPR DPDPGVVIQI PVTNDVEELP
VRTPEKARCI TSNEASRSDV SHSYGSKDLN SVYGSPKDEA FVGCQEENAG SFSGEKSLPT
ENCCSREATP SDKEMLEKEK EESVCNSDET DPSSVERESS LGDRIRLSPT SSSSVGINEE
SDDYETESLK DSATDDQREV STPPQEARLA EHEAISIKRG EDSGTMHSRH RRSHEDSSKR
HCGRAGYARY VKDASPTPDP GRGKKVGSLQ GLYRDSNKNW QNGPPITLER DETEGKGVHY
YREKSHGRLN SSVDHDRHRE HRFGWRNNKE SSLGRGFDHS NSYKCGTHLK EYTSRSSFDL
NQRNSRSSFK EEDDRYGWHH RERKYVHERS PIRAYENYKE RNGCDWLREP YYEDCIPITD
MDYRYRSENS SAHAIHNLKH SPENDLYCRR RGGYDYNLHR DRYEDGVHRV ESRIPFELAY
REMRSFAEVE MREYQGYKRH EEFSEIEKRH HYIHDWHLDR FVSEEDGYKY RIQDGWSSPS
LSLRDSWYTK EAKGDFRRDD TRDFRTPEAY DSQNNHFHKA APRDGWTQNL GRSHNVSVKD
RLQYDADWVG PDRGRYNMAD DMQCSMREVS NSEHPSYTDE IFVRDIRVPT HNRMATKQRF
GYLQSHIHEN DERHHRSKKL RGDGHAFIKR QDHVDLAGRQ GKVSNQSKKR FSNGGDTIEQ
QDVQKPRKLM GKSEEKAMQN RDINDKEEGE IIEEVKGVEI DNERIQESLK KMEKRRERFK
GTKLAVEATF KSQTELRAKA DVTNQQRPVR KRRWCAS
