FIP1_RAT
ID FIP1_RAT Reviewed; 536 AA.
AC Q5U317;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Pre-mRNA 3'-end-processing factor FIP1;
DE AltName: Full=FIP1-like 1 protein;
GN Name=Fip1l1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88; SER-434; THR-436; SER-442
RP AND SER-496, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the cleavage and polyadenylation specificity
CC factor (CPSF) complex, composed of CPSF1, CPSF2, CPSF3, CPSF4 and
CC FIP1L1. Found in a complex with CPSF1, FIP1L1 and PAPOLA. Interacts
CC with CPSF1, CPSF4, CSTF2 and CSTF3. Interacts with AHCYL1 (when
CC phosphorylated); the interaction is direct and associates AHCYL1 with
CC the CPSF complex and RNA. Interacts with PAPOLA; the interaction seems
CC to be increased by the interaction with AHCYL1. Interacts with
CC NUDT21/CPSF5; this interaction occurs in a RNA sequence-specific
CC manner. Interacts (preferentially via unphosphorylated form and
CC Arg/Glu/Asp-rich domain) with CPSF6 (via Arg/Ser-rich domain); this
CC interaction mediates, at least in part, the interaction between the
CC CFIm and CPSF complexes and may be inhibited by CPSF6 hyper-
CC phosphorylation. Interacts (preferentially via unphosphorylated form
CC and Arg/Asp/Glu-rich domain) with CPSF7 (via Arg/Ser-rich domain); this
CC interaction mediates, at least in part, the interaction between the
CC CFIm and CPSF complexes and may be inhibited by CPSF7 hyper-
CC phosphorylation. {ECO:0000250|UniProtKB:Q6UN15,
CC ECO:0000250|UniProtKB:Q9D824}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the FIP1 family. {ECO:0000305}.
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DR EMBL; BC085767; AAH85767.1; -; mRNA.
DR RefSeq; NP_001008296.1; NM_001008295.1.
DR AlphaFoldDB; Q5U317; -.
DR SMR; Q5U317; -.
DR IntAct; Q5U317; 2.
DR STRING; 10116.ENSRNOP00000049728; -.
DR iPTMnet; Q5U317; -.
DR PhosphoSitePlus; Q5U317; -.
DR jPOST; Q5U317; -.
DR PaxDb; Q5U317; -.
DR PRIDE; Q5U317; -.
DR GeneID; 289582; -.
DR KEGG; rno:289582; -.
DR UCSC; RGD:1309336; rat.
DR CTD; 81608; -.
DR RGD; 1309336; Fip1l1.
DR VEuPathDB; HostDB:ENSRNOG00000002275; -.
DR eggNOG; KOG1049; Eukaryota.
DR HOGENOM; CLU_035577_1_0_1; -.
DR InParanoid; Q5U317; -.
DR OrthoDB; 929913at2759; -.
DR Reactome; R-RNO-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR Reactome; R-RNO-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-RNO-72187; mRNA 3'-end processing.
DR Reactome; R-RNO-73856; RNA Polymerase II Transcription Termination.
DR Reactome; R-RNO-77595; Processing of Intronless Pre-mRNAs.
DR PRO; PR:Q5U317; -.
DR Proteomes; UP000002494; Chromosome 14.
DR Bgee; ENSRNOG00000002275; Expressed in ovary and 20 other tissues.
DR ExpressionAtlas; Q5U317; baseline and differential.
DR Genevisible; Q5U317; RN.
DR GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006378; P:mRNA polyadenylation; IBA:GO_Central.
DR GO; GO:0098789; P:pre-mRNA cleavage required for polyadenylation; IBA:GO_Central.
DR InterPro; IPR007854; Fip1_dom.
DR Pfam; PF05182; Fip1; 1.
PE 1: Evidence at protein level;
KW mRNA processing; Nucleus; Phosphoprotein; Reference proteome; RNA-binding.
FT CHAIN 1..536
FT /note="Pre-mRNA 3'-end-processing factor FIP1"
FT /id="PRO_0000215040"
FT REGION 1..296
FT /note="Necessary for stimulating PAPOLA activity"
FT /evidence="ECO:0000250"
FT REGION 1..110
FT /note="Sufficient for interaction with PAPOLA"
FT /evidence="ECO:0000250"
FT REGION 1..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 136..219
FT /note="Sufficient for interaction with CPSF4"
FT /evidence="ECO:0000250"
FT REGION 212..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 300..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 383..536
FT /note="Sufficient for interaction with CPSF1 and CSTF3"
FT /evidence="ECO:0000250"
FT REGION 397..432
FT /note="Arg/Asp/Glu-rich domain"
FT /evidence="ECO:0000250|UniProtKB:Q6UN15"
FT COMPBIAS 300..344
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..387
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..503
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 84
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D824"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D824"
FT MOD_RES 88
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 366
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q6UN15"
FT MOD_RES 434
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 436
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 438
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6UN15"
FT MOD_RES 442
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 496
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 536 AA; 60188 MW; B608BE48974164C0 CRC64;
MSAGEVERLV ELSGGTGGDE EEEWLYGGPW DVHVHSDLAK DLDENEVERP EEENASANPP
SGIEEEAAEN GVAKPKVTET EDDSDSDSDD DEDDVHVTIG DIKTGAPQYG SYGTAPVNLN
IKAGGRVYGN TGTKVKGVDL DAPGSINGVP LLEVDLDSFE DKPWRKPGAD LSDYFNYGFN
EDTWKAYCEK QKRIRMGLEV IPVTSTTNKI TVQQGRTGNS EKEAALPSTK AEFTSPPSLF
KTGLPPSRRL PGAIDVIGQT ITISRVEGRR RANENSNIQV LSDRSATEVD NNFSKPPPFF
PPGAPPTHLP PPPFLPPPPT VSTAPPLIPP PGFPPPPGAP PPSLIPTIES GHSSGYDSRS
ARAFPYGNVA FPHLTSSAPS WPSLVDTTKQ WDYYARREKD RDRDRERDRD RERERDRDRE
RERTRERERE RDHSPTPSVF NSDEERYRYR EYAERGYERH RASREKEERH RERRHREKEE
TRHKSSRSNS RRRHESEEGD SHRRHKHKKS KRSKEGKEAG SEPVPEQEST EAAPAE
