CPSF1_BOVIN
ID CPSF1_BOVIN Reviewed; 1444 AA.
AC Q10569;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Cleavage and polyadenylation specificity factor subunit 1;
DE AltName: Full=Cleavage and polyadenylation specificity factor 160 kDa subunit;
DE Short=CPSF 160 kDa subunit;
GN Name=CPSF1; Synonyms=CPSF160;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Thymus;
RX PubMed=7651824; DOI=10.1093/nar/23.14.2629;
RA Jenny A., Keller W.;
RT "Cloning of cDNAs encoding the 160 kDa subunit of the bovine cleavage and
RT polyadenylation specificity factor.";
RL Nucleic Acids Res. 23:2629-2635(1995).
RN [2]
RP CHARACTERIZATION.
RX PubMed=1756731; DOI=10.1002/j.1460-2075.1991.tb05002.x;
RA Keller W., Bienroth S., Lang K.M., Christofori G.;
RT "Cleavage and polyadenylation factor CPF specifically interacts with the
RT pre-mRNA 3' processing signal AAUAAA.";
RL EMBO J. 10:4241-4249(1991).
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. This subunit is involved in the RNA recognition step
CC of the polyadenylation reaction (By similarity). May play a role in eye
CC morphogenesis and the development of retinal ganglion cell projections
CC to the midbrain (By similarity). {ECO:0000250|UniProtKB:A0A0R4IC37,
CC ECO:0000250|UniProtKB:Q10570}.
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 FIP1L1, TENT2/GLD2 and SRRM1. Interacts with TUT1; the interaction
CC is direct and mediates the recruitment of the CPSF complex on the 3'UTR
CC of selected pre-mRNAs (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the CPSF1 family. {ECO:0000305}.
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DR EMBL; X83097; CAA58152.1; -; mRNA.
DR PIR; S57335; S57335.
DR RefSeq; NP_777145.1; NM_174720.3.
DR AlphaFoldDB; Q10569; -.
DR SMR; Q10569; -.
DR IntAct; Q10569; 1.
DR MINT; Q10569; -.
DR STRING; 9913.ENSBTAP00000011004; -.
DR PaxDb; Q10569; -.
DR PRIDE; Q10569; -.
DR GeneID; 282703; -.
DR KEGG; bta:282703; -.
DR CTD; 29894; -.
DR eggNOG; KOG1896; Eukaryota.
DR HOGENOM; CLU_002414_0_0_1; -.
DR InParanoid; Q10569; -.
DR OrthoDB; 360328at2759; -.
DR TreeFam; TF314322; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006378; P:mRNA polyadenylation; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR004871; Cleavage/polyA-sp_fac_asu_C.
DR InterPro; IPR018846; Cleavage/polyA-sp_fac_asu_N.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR Pfam; PF03178; CPSF_A; 1.
DR Pfam; PF10433; MMS1_N; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; mRNA processing; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-binding.
FT CHAIN 1..1444
FT /note="Cleavage and polyadenylation specificity factor
FT subunit 1"
FT /id="PRO_0000074386"
FT REGION 406..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 549..571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 716..778
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 902..924
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 894..909
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 411..426
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 902..919
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 757
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9EPU4"
FT MOD_RES 767
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q10570"
SQ SEQUENCE 1444 AA; 161214 MW; 226B3A4F9812E0FA CRC64;
MYAVYKQAHP PTGLEFSMYC NFFNNSERNL VVAGTSQLYV YRLNRDSEAP TKNDRSTDGK
AHREHREKLE LVASFSFFGN VMSMASVQLA GAKRDALLLS FKDAKLSVVE YDPGTHDLKT
LSLHYFEEPE LRDGFVQNVH TPRVRVDPDG RCAAMLIYGT RLVVLPFRRE SLAEEHEGLV
GEGQRSSFLP SYIIDVRALD EKLLNIVDLQ FLHGYYEPTL LILFEPNQTW PGRVAVRQDT
CSIVAISLNI TQKVHPVIWS LTSLPFDCTQ ALAVPKPIGG VVIFAVNSLL YLNQSVPPYG
VALNSLTTGT TAFPLRTQEG VRITLDCAQA AFISYDKMVI SLKGGEIYVL TLITDGMRSV
RAFHFDKAAA SVLTTSMVTM EPGYLFLGSR LGNSLLLKYT EKLQEPPAST AREAADKEEP
PSKKKRVDAT TGWSGSKSVP QDEVDEIEVY GSEAQSGTQL ATYSFEVCDS ILNIGPCANA
AMGEPAFLSE EFQNSPEPDL EIVVCSGYGK NGALSVLQKS IRPQVVTTFE LPGCYDMWTV
IAPVRKEQEE TLKGEGTEPE PGAPEAEDDG RRHGFLILSR EDSTMILQTG QEIMELDASG
FATQGPTVFA GNIGDNRYIV QVSPLGIRLL EGVNQLHFIP VDLGSPIVQC AVADPYVVIM
SAEGHVTMFL LKNDSYGGRH HRLALHKPPL HHQSKVITLC VYRDVSGMFT TESRLGGVRD
ELGGRGGPEA EGQGAETSPT VDDEEEMLYG DSGSLFSPSK EEARRSSQPP ADRDPAPFRA
EPTHWCLLVR ENGAMEIYQL PDWRLVFLVK NFPVGQRVLV DSSFGQPTTQ GEARKEEATR
QGELPLVKEV LLVALGSRQR RPYLLVHVDQ ELLIYEAFPH DSQLGQGNLK VRFKKVPHNI
NFREKKPKPS KKKAEGGSTE EGTGPRGRVA RFRYFEDIYG YSGVFICGPS PHWLLVTGRG
ALRLHPMGID GPIDSFAPFH NINCPRGFLY FNRQGELRIS VLPAYLSYDA PWPVRKIPLR
CTAHYVAYHV ESKVYAVATS TSTPCTRVPR MTGEEKEFET IERDERYVHP QQEAFCIQLI
SPVSWEAIPN ARIELEEWEH VTCMKTVSLR SEETVSGLKG YVAAGTCLMQ GEEVTCRGRI
LIMDVIEVVP EPGQPLTKNK FKVLYEKEQK GPVTALCHCN GHLVSAIGQK IFLWSLRASE
LTGMAFIDTQ LYIHQMISVK NFILAADVMK SISLLRYQEE SKTLSLVSRD AKPLEVYSVD
FMVDNAQLGF LVSDRDRNLM VYMYLPEAKE SFGGMRLLRR ADFHVGAHVN TFWRTPCRGA
AEGPSKKSVV WENKHITWFA TLDGGIGLLL PMQEKTYRRL LMLQNALTTM LPHHAGLNPR
AFRMLHVDRR VLQNAVRNVL DGELLNRYLY LSTMERGELA KKIGTTPDII LDDLLETDRV
TAHF