FIP1_PONAB
ID FIP1_PONAB Reviewed; 588 AA.
AC Q5RAA7;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 62.
DE RecName: Full=Pre-mRNA 3'-end-processing factor FIP1;
DE AltName: Full=FIP1-like 1 protein;
GN Name=FIP1L1;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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; CR859111; CAH91303.1; -; mRNA.
DR RefSeq; NP_001125772.1; NM_001132300.2.
DR AlphaFoldDB; Q5RAA7; -.
DR SMR; Q5RAA7; -.
DR STRING; 9601.ENSPPYP00000016499; -.
DR PRIDE; Q5RAA7; -.
DR GeneID; 100172699; -.
DR KEGG; pon:100172699; -.
DR CTD; 81608; -.
DR eggNOG; KOG1049; Eukaryota.
DR InParanoid; Q5RAA7; -.
DR Proteomes; UP000001595; Unplaced.
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 Pfam; PF05182; Fip1; 1.
PE 2: Evidence at transcript level;
KW mRNA processing; Nucleus; Phosphoprotein; Reference proteome; RNA-binding.
FT CHAIN 1..588
FT /note="Pre-mRNA 3'-end-processing factor FIP1"
FT /id="PRO_0000215039"
FT REGION 1..341
FT /note="Necessary for stimulating PAPOLA activity"
FT /evidence="ECO:0000250"
FT REGION 1..96
FT /note="Sufficient for interaction with PAPOLA"
FT /evidence="ECO:0000250"
FT REGION 1..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 122..228
FT /note="Sufficient for interaction with CPSF4"
FT /evidence="ECO:0000250"
FT REGION 223..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 334..588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 437..588
FT /note="Sufficient for interaction with CPSF1 and CSTF3"
FT /evidence="ECO:0000250"
FT REGION 451..484
FT /note="Arg/Asp/Glu-rich domain"
FT /evidence="ECO:0000250|UniProtKB:Q6UN15"
FT COMPBIAS 17..36
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..277
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..398
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..555
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 70
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D824"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D824"
FT MOD_RES 74
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D824"
FT MOD_RES 289
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D824"
FT MOD_RES 420
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q6UN15"
FT MOD_RES 486
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6UN15"
FT MOD_RES 488
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6UN15"
FT MOD_RES 490
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6UN15"
FT MOD_RES 494
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6UN15"
FT MOD_RES 548
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6UN15"
SQ SEQUENCE 588 AA; 65640 MW; F5503E59E29FA96A CRC64;
MSAGEVERLV SELSGGTGGD EEEEWLYGDE NEVERPEEEN ASANPPSGIE DETAENGVPK
PKVTETEDDS DSDSDDDEDD VHVTIGDIKT GAPQYGSYGT APVNLNIKTG GRVYGTTGTK
VKGVDLDAPG SINGVPLLEV DLDSFEDKPW RKPGADLSDY FNYGFNEDTW KAYCEKQKRI
RMGLEVIPVT STTNKITAED CTMEVTPGAE IQDGRFNLFK VQQGRTGNSE KETALPSAKA
EFTSPPSLFK TGLPPSRNST SSQSQTSTAS RKANSSVGKW QDRYGRAESP DLRRLPGAID
VIGQTITISR VEGRRRANEN SNIQVLSERS ATAVDNNFSK PPPFFPPGAP PTHLPPPPFL
PPPPTVSTAP PLIPPPGIPI TVPPPGFPPP PGAPPPSLIP TIESGHSSGY DSRSARAFPY
GNVAFPHLPG SAPSWPSLVD TSKQWDYYAR REKDRDRERD RDRERDRDRD RERERTRERE
RERDHSPTPS VFNSDEERYR YREYAERGYE RHRASREKEE RHRERRHREK EETRHKSSRS
NSRRRHESEE GDSHRRHKHK KSKRSKEGKE AGSEPAPEQE STEATPAE
