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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
 
 
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