FIPS5_ARATH
ID FIPS5_ARATH Reviewed; 1196 AA.
AC F4KDH9; Q9FGU0;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 62.
DE RecName: Full=FIP1[V]-like protein {ECO:0000303|PubMed:16282318};
DE Short=AtFIP1(V) {ECO:0000303|PubMed:16282318};
DE AltName: Full=Factor interacting with poly(A) polymerase 1-like 5 {ECO:0000305};
DE Short=AtFIPS5 {ECO:0000303|PubMed:16282318};
DE AltName: Full=Protein HOMOLOG OF YEAST FIP1 [V] {ECO:0000305};
GN Name=FIPS5 {ECO:0000303|PubMed:16282318};
GN Synonyms=FIP1[V] {ECO:0000303|PubMed:16282318};
GN OrderedLocusNames=At5g58040 {ECO:0000312|Araport:AT5G58040};
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=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(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 FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH CSTF77; CPSF30; PAPS4;
RP CFIM25 AND PABN1, TISSUE SPECIFICITY, RNA-BINDING, AND 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 CPSF30.
RX PubMed=17576667; DOI=10.1093/nar/gkm457;
RA Addepalli B., Hunt A.G.;
RT "A novel endonuclease activity associated with the Arabidopsis ortholog of
RT the 30-kDa subunit of cleavage and polyadenylation specificity factor.";
RL Nucleic Acids Res. 35:4453-4463(2007).
RN [5]
RP INTERACTION WITH CFIS1; CFIS2; CSTF64; CSTF77; CPSF30; CSTF50; PABN1;
RP PABN2; PABN3; PAPS2; PAPS3; PAPS4 AND FIPS3, GENE 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).
RN [6]
RP INTERACTION WITH CSTF77.
RX PubMed=18221017; DOI=10.2174/092986608783330431;
RA Addepalli B., Hunt A.G.;
RT "The interaction between two Arabidopsis polyadenylation factor subunits
RT involves an evolutionarily-conserved motif and has implications for the
RT assembly and function of the polyadenylation complex.";
RL Protein Pept. Lett. 15:76-88(2008).
CC -!- FUNCTION: Essential gene (PubMed:16282318). Component of the cleavage
CC and polyadenylation specificity factor (CPSF) complex that plays a key
CC role in pre-mRNA 3'-end formation, recognizing the AAUAAA signal
CC sequence and interacting with poly(A) polymerase and other factors to
CC bring about cleavage and poly(A) addition. FIP1L1 contributes to
CC poly(A) site recognition and stimulates poly(A) addition. Binds to U-
CC rich RNA sequence elements surrounding the poly(A) site. May act to
CC tether poly(A) polymerase to the CPSF complex (By similarity).
CC {ECO:0000250|UniProtKB:Q6UN15, ECO:0000269|PubMed:16282318}.
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 CFIS1, CFIS2,
CC CPSF30, CSTF50, CSTF64, CSTF77, FIPS3, PABN1, PABN2, PABN3, PAPS4,
CC CFIM25 and PABN1. Binds RNA (PubMed:16282318, PubMed:17576667,
CC PubMed:18479511, PubMed:18221017). {ECO:0000250|UniProtKB:Q6UN15,
CC ECO:0000269|PubMed:16282318, ECO:0000269|PubMed:17576667,
CC ECO:0000269|PubMed:18221017, ECO:0000269|PubMed:18479511}.
CC -!- INTERACTION:
CC F4KDH9; Q94AF0: CFIS1; NbExp=3; IntAct=EBI-962489, EBI-962531;
CC F4KDH9; A9LNK9: CPSF30; NbExp=3; IntAct=EBI-962489, EBI-962511;
CC F4KDH9; F4KDH9: FIPS5; NbExp=2; IntAct=EBI-962489, EBI-962489;
CC F4KDH9; Q93VI4: PABN1; NbExp=3; IntAct=EBI-962489, EBI-962543;
CC F4KDH9; Q8VYW1: PAPS4; NbExp=3; IntAct=EBI-962489, EBI-962558;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q6UN15,
CC ECO:0000255|PROSITE-ProRule:PRU00768}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, stems, flower tissues and
CC roots. {ECO:0000269|PubMed:16282318}.
CC -!- DISRUPTION PHENOTYPE: Lethal. {ECO:0000269|PubMed:16282318}.
CC -!- SIMILARITY: Belongs to the FIP1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB10995.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB024029; BAB10995.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED96990.1; -; Genomic_DNA.
DR RefSeq; NP_200612.2; NM_125189.3.
DR AlphaFoldDB; F4KDH9; -.
DR SMR; F4KDH9; -.
DR BioGRID; 21160; 13.
DR IntAct; F4KDH9; 12.
DR STRING; 3702.AT5G58040.1; -.
DR iPTMnet; F4KDH9; -.
DR PaxDb; F4KDH9; -.
DR PRIDE; F4KDH9; -.
DR ProteomicsDB; 230595; -.
DR EnsemblPlants; AT5G58040.1; AT5G58040.1; AT5G58040.
DR GeneID; 835916; -.
DR Gramene; AT5G58040.1; AT5G58040.1; AT5G58040.
DR KEGG; ath:AT5G58040; -.
DR Araport; AT5G58040; -.
DR TAIR; locus:2155806; AT5G58040.
DR eggNOG; KOG1049; Eukaryota.
DR HOGENOM; CLU_006491_1_0_1; -.
DR InParanoid; F4KDH9; -.
DR OrthoDB; 173217at2759; -.
DR PRO; PR:F4KDH9; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; F4KDH9; baseline and differential.
DR Genevisible; F4KDH9; AT.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003723; F:RNA binding; IDA:TAIR.
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; 1.
DR Pfam; PF05182; Fip1; 1.
PE 1: Evidence at protein level;
KW mRNA processing; Nucleus; Reference proteome; Repeat; RNA-binding.
FT CHAIN 1..1196
FT /note="FIP1[V]-like protein"
FT /id="PRO_0000431327"
FT REGION 1..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 117..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 268..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 485..1174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 704..711
FT /note="Nuclear localization signal 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 734..741
FT /note="Nuclear localization signal 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 19..33
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..519
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..550
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..567
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..590
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..646
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 654..677
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 699..999
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1000..1030
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1031..1072
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1102..1160
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1196 AA; 133439 MW; FF928745DF43F32C CRC64;
MEEDDEFGDL YSDVLQPFQP PVVLPPPPPL PHRSIDLNLR SQDQDVSEPN SAPISRVSDN
DAVKLSTQDA TRQAIVDGGG DDKDMSFDIE EPDADSTPTI PGLFVTGALP GLATDRGVSQ
VTTRIEQQVG GGGDGGYGGQ GEGDDWDSDS EDDLQIVLND SSRNVMIGGA DRRSRMGDNE
DDDDEDDEDP LVIVADTDPN QPMEEQMWGE DGLQGIEGDG KDGGEAGKGS GPGGATGPPK
AGYSSHGYHP FHSQFKYVRP GAAPIPGGAA SVGGPSSGQV RPPANLGPMA GRGRGDWRPL
GMRNASAAQK GFHQPWGSNT AGRGLDFTLP SHKTIFEVDI DSFEEKPWRY PGVEMTDYFN
FGLNEESWKD YCKQLDQHRI QTTMQSRIRV YESGRTDQGY DPDLPPELAA ATGAQGVPVD
SSNLVKPDSV QGDSAKVPAN VRPTLPPGRP IPVETGSGER LPSIDTRAPR MRDLDAIIEI
VCQDSHEDEP SGENGTDQAD SSLPGENVPV ETSYVNNKRP DTESAEHSPA QDEPHKNLLK
KQDDEISRST DSGQSFRSSS PVGDRGTRSS SVDREDVGGE AGKDAEMGEE LKMSFTSPQS
AVQEDDGGES KTERSSESSK ARSGSHRDFQ QEEDVIQDKH SSRPANNRKQ YDNNAPHQSR
KNQDRGKEME RTRAASKGGR ENSNPHMELD STYIYSIASR EDFDKRKERD VDGAVWRRKE
DDPYSRRGGD EGSRKRDRED DPGFRQRGKM RENEIRSKDD QVPSRKHMDD AGMRNIYEPD
DHINKRRKDE EYLRRSRPEK NEISYGQRES MSRVKRERDD RLEHQKRDVQ HKIRDDFDDH
GSLRQRDDIY MQRDGNERLR ERDVLDKLKL PHEDGISARG RERQVAVRGH RGSEDRSSRM
KDEYKASDKE HVTKDTLRHA KQTKRRDYPG EESSSHHRGH EDFSARTDNI VNNEKKPRQE
RTGAKIDKFI DTLDGQRLQD RKHKDSRRKI KEQREGTESL SKQGEQNGSS VVTGSKGTND
ARNCRSEIPH QPNTAKRHKE NASSGDEIHD SKRGRTKLER WASHKEREDA VSAKSSSISS
KLEEKENNTN GRLSEPVHGS IGKSRDVTEE KIGHDLADTK DGSEKGPGDR HLDTVEKLKK
RSERFKLPMP TEKDTTGVKK MESETLPSAK IEGPVDSEGE YVWDERSCVR IGREYA
