FIP1_MOUSE
ID FIP1_MOUSE Reviewed; 581 AA.
AC Q9D824; Q8BWX7; Q99LH0; Q9DBB2;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Pre-mRNA 3'-end-processing factor FIP1;
DE AltName: Full=FIP1-like 1 protein;
GN Name=Fip1l1;
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1-558 (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Embryonic spinal cord, Liver, and Small intestine;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-479; THR-481; SER-483 AND
RP SER-487, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280 AND SER-479, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [5]
RP INTERACTION WITH AHCYL1 AND PAPOLA.
RX PubMed=19224921; DOI=10.1074/jbc.m807136200;
RA Kiefer H., Mizutani A., Iemura S., Natsume T., Ando H., Kuroda Y.,
RA Mikoshiba K.;
RT "Inositol 1,4,5-triphosphate receptor-binding protein released with
RT inositol 1,4,5-triphosphate (IRBIT) associates with components of the mRNA
RT 3' processing machinery in a phosphorylation-dependent manner and inhibits
RT polyadenylation.";
RL J. Biol. Chem. 284:10694-10705(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-84; SER-86; SER-88; SER-479;
RP THR-481; SER-483 AND SER-487, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Lung, Pancreas, 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).
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 (By similarity). Interacts with
CC AHCYL1 (when phosphorylated); the interaction is direct and associates
CC AHCYL1 with the CPSF complex and RNA (PubMed:19224921). Interacts with
CC PAPOLA; the interaction seems to be increased by the interaction with
CC AHCYL1 (PubMed:19224921). Interacts with NUDT21/CPSF5; this interaction
CC occurs in a RNA sequence-specific manner. Interacts (preferentially via
CC unphosphorylated form and Arg/Glu/Asp-rich domain) with CPSF6 (via
CC Arg/Ser-rich domain); this interaction mediates, at least in part, the
CC interaction between the CFIm and CPSF complexes and may be inhibited by
CC CPSF6 hyper-phosphorylation. Interacts (preferentially via
CC unphosphorylated form and Arg/Asp/Glu-rich domain) with CPSF7 (via
CC Arg/Ser-rich domain); this interaction mediates, at least in part, the
CC interaction between the CFIm and CPSF complexes and may be inhibited by
CC CPSF7 hyper-phosphorylation (By similarity).
CC {ECO:0000250|UniProtKB:Q6UN15, ECO:0000269|PubMed:19224921}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9D824-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9D824-2; Sequence=VSP_016734;
CC Name=3;
CC IsoId=Q9D824-3; Sequence=VSP_016734, VSP_016735;
CC Name=4;
CC IsoId=Q9D824-4; Sequence=VSP_016733, VSP_016735, VSP_016736;
CC -!- SIMILARITY: Belongs to the FIP1 family. {ECO:0000305}.
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DR EMBL; AK005061; BAB23785.1; -; mRNA.
DR EMBL; AK008561; BAB25745.1; -; mRNA.
DR EMBL; AK049672; BAC33867.1; -; mRNA.
DR EMBL; AK164105; BAE37629.1; -; mRNA.
DR EMBL; BC003263; AAH03263.1; -; mRNA.
DR CCDS; CCDS19346.1; -. [Q9D824-2]
DR CCDS; CCDS51520.1; -. [Q9D824-1]
DR CCDS; CCDS51521.1; -. [Q9D824-3]
DR RefSeq; NP_001153045.1; NM_001159573.1. [Q9D824-1]
DR RefSeq; NP_001153046.1; NM_001159574.1. [Q9D824-3]
DR RefSeq; NP_077145.2; NM_024183.5. [Q9D824-2]
DR AlphaFoldDB; Q9D824; -.
DR SMR; Q9D824; -.
DR BioGRID; 211797; 14.
DR IntAct; Q9D824; 3.
DR STRING; 10090.ENSMUSP00000109164; -.
DR iPTMnet; Q9D824; -.
DR PhosphoSitePlus; Q9D824; -.
DR EPD; Q9D824; -.
DR jPOST; Q9D824; -.
DR MaxQB; Q9D824; -.
DR PaxDb; Q9D824; -.
DR PeptideAtlas; Q9D824; -.
DR PRIDE; Q9D824; -.
DR ProteomicsDB; 271765; -. [Q9D824-1]
DR ProteomicsDB; 271766; -. [Q9D824-2]
DR ProteomicsDB; 271767; -. [Q9D824-3]
DR ProteomicsDB; 271768; -. [Q9D824-4]
DR DNASU; 66899; -.
DR Ensembl; ENSMUST00000080164; ENSMUSP00000079059; ENSMUSG00000029227. [Q9D824-2]
DR Ensembl; ENSMUST00000113534; ENSMUSP00000109162; ENSMUSG00000029227. [Q9D824-4]
DR Ensembl; ENSMUST00000113535; ENSMUSP00000109163; ENSMUSG00000029227. [Q9D824-3]
DR Ensembl; ENSMUST00000113536; ENSMUSP00000109164; ENSMUSG00000029227. [Q9D824-1]
DR GeneID; 66899; -.
DR KEGG; mmu:66899; -.
DR UCSC; uc008xtm.2; mouse. [Q9D824-4]
DR UCSC; uc008xtn.2; mouse. [Q9D824-2]
DR UCSC; uc008xto.2; mouse. [Q9D824-1]
DR UCSC; uc008xtp.2; mouse. [Q9D824-3]
DR CTD; 81608; -.
DR MGI; MGI:1914149; Fip1l1.
DR VEuPathDB; HostDB:ENSMUSG00000029227; -.
DR eggNOG; KOG1049; Eukaryota.
DR GeneTree; ENSGT00940000162578; -.
DR HOGENOM; CLU_035577_1_0_1; -.
DR InParanoid; Q9D824; -.
DR OMA; YYPRRED; -.
DR OrthoDB; 929913at2759; -.
DR PhylomeDB; Q9D824; -.
DR TreeFam; TF318610; -.
DR Reactome; R-MMU-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-MMU-72187; mRNA 3'-end processing.
DR Reactome; R-MMU-73856; RNA Polymerase II Transcription Termination.
DR Reactome; R-MMU-77595; Processing of Intronless Pre-mRNAs.
DR BioGRID-ORCS; 66899; 16 hits in 76 CRISPR screens.
DR ChiTaRS; Fip1l1; mouse.
DR PRO; PR:Q9D824; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9D824; protein.
DR Bgee; ENSMUSG00000029227; Expressed in primary oocyte and 260 other tissues.
DR ExpressionAtlas; Q9D824; baseline and differential.
DR Genevisible; Q9D824; MM.
DR GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
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 Alternative splicing; mRNA processing; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-binding.
FT CHAIN 1..581
FT /note="Pre-mRNA 3'-end-processing factor FIP1"
FT /id="PRO_0000215038"
FT REGION 1..332
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 211..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 320..581
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 428..581
FT /note="Sufficient for interaction with CPSF1 and CSTF3"
FT /evidence="ECO:0000250"
FT REGION 442..477
FT /note="Arg/Asp/Glu-rich domain"
FT /evidence="ECO:0000250|UniProtKB:Q6UN15"
FT REGION 478..535
FT /note="Sufficient for interaction with AHCYL1"
FT /evidence="ECO:0000269|PubMed:19224921"
FT COMPBIAS 231..268
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..389
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..432
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..548
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 84
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 88
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 280
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 411
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q6UN15"
FT MOD_RES 479
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 481
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 483
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 487
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 541
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6UN15"
FT VAR_SEQ 211
FT /note="T -> TAEDCTMEVTPGAEIQDGRFNLFK (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_016733"
FT VAR_SEQ 248..283
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016734"
FT VAR_SEQ 365..373
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_016735"
FT VAR_SEQ 487..581
FT /note="SDEERYRYREYAERGYERHRASREKEERHRERRHREKEETRHKSSRSNSRRR
FT HESEEGDSHRRHKHKKSKRSKEGKEAGSEPVPEQESTEAAPAE -> RFVGCAGP (in
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_016736"
SQ SEQUENCE 581 AA; 64959 MW; 2E8D6DF558168035 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
KTGLPPSRNS TSSQSQTSTA SRKASSSVGK WQDRYGRAES PDLRRLPGAI DVIGQTITIS
RVEGRRRANE NSNIQVLSDR SATEVDNNFS KPPPFFPPGA PPTHLPPPPF LPPPPTVSTA
PPLIPPPGIP ITVPPPGFPP PPGAPPPSLI PTIESGHSSG YDSRSARAFP YGNVAFPHLT
SSAPSWPSLV DTTKQWDYYA RREKDRDRDR ERDRDRERER DRDRERERTR ERERERDHSP
TPSVFNSDEE RYRYREYAER GYERHRASRE KEERHRERRH REKEETRHKS SRSNSRRRHE
SEEGDSHRRH KHKKSKRSKE GKEAGSEPVP EQESTEAAPA E
