CA120_YEAS7
ID CA120_YEAS7 Reviewed; 1060 AA.
AC A6ZRG7;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=CCR4-NOT transcriptional complex subunit CAF120;
DE AltName: Full=120 kDa CCR4-associated factor;
GN Name=CAF120; ORFNames=SCY_4528;
OS Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=307796;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJM789;
RX PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA Steinmetz L.M.;
RT "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT strain YJM789.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
CC -!- FUNCTION: Acts as component of the CCR4-NOT core complex, which in the
CC nucleus seems to be a general transcription factor, and in the
CC cytoplasm the major mRNA deadenylase involved in mRNA turnover. The NOT
CC protein subcomplex negatively regulates the basal and activated
CC transcription of many genes. Preferentially affects TC-type TATA
CC element-dependent transcription. Could directly or indirectly inhibit
CC component(s) of the general transcription machinery (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Subunit of the 1.0 MDa CCR4-NOT core complex that contains
CC CCR4, CAF1, CAF120, NOT1, NOT2, NOT3, NOT4, NOT5, CAF40 and CAF130. In
CC the complex interacts with NOT1. The core complex probably is part of a
CC less characterized 1.9 MDa CCR4-NOT complex (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Bud neck {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CAF120 family. {ECO:0000305}.
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DR EMBL; AAFW02000067; EDN62549.1; -; Genomic_DNA.
DR AlphaFoldDB; A6ZRG7; -.
DR PRIDE; A6ZRG7; -.
DR EnsemblFungi; EDN62549; EDN62549; SCY_4528.
DR HOGENOM; CLU_006977_1_0_1; -.
DR Proteomes; UP000007060; Unassembled WGS sequence.
DR GO; GO:0005935; C:cellular bud neck; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR Pfam; PF00169; PH; 1.
DR SMART; SM00233; PH; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 3: Inferred from homology;
KW Activator; Cytoplasm; Nucleus; Phosphoprotein; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..1060
FT /note="CCR4-NOT transcriptional complex subunit CAF120"
FT /id="PRO_0000324853"
FT DOMAIN 75..204
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 465..588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 718..742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 801..1060
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 466..481
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..507
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..574
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 718..737
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 829..887
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 897..949
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 997..1011
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1012..1060
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 491
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53836"
FT MOD_RES 510
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53836"
FT MOD_RES 518
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53836"
FT MOD_RES 538
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53836"
FT MOD_RES 556
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53836"
FT MOD_RES 871
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53836"
FT MOD_RES 885
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53836"
SQ SEQUENCE 1060 AA; 118264 MW; DE63F0674733D498 CRC64;
MRIFSGDNKV VDSPASNPGL MSPSNFGGDF GSRLKVNVTS KKKLNDSSPT SPMESSPVSP
ELVPILTLLN AHTHRRYHEG VFLILQDLNN NGTHAARKWK DVYGVLLGTQ LALWDAKELA
EFTDPSCPVS EKKLKEVASK PTYINLTDAT LRTLDNSDNI VMECGKNLTN ALVVSTTLKN
RYFLQFGNKE SFNAWNSAIR LCLYECSSLQ EAYTGAFISS RGAKLGDIRI LLTNRKYDYK
DWVSVRFGAG MPWKRCYAVI SQSSSKKKGH FGEINLYEND KKVKKNHAMA TIVEAKALYA
VYPSSPKLID SSTIIKVVGS VKFEKKESAQ EKDVFIMPEK HQAVPSYDTI IRFLIPAMDT
FKLYGRPEKL LSSKNDPHSL LFGLPVLPHI YYLEVEDLLP LTNSVSSLHW SNNEWKEHIS
DILQRKIAQG YCGCNSTSNI TSPLPSPFLG SADLFERADG VLSPKLSYGS KSSSNNSSKN
SLPKRERVKL SSSSEQDLNN SDSPSIKRES PPLVISESPH KVHTPTDASF RTRVTEGSPY
AKQRHPKAFA SSVNDSPSDR AKSRTVPYNN NDRKATTPEK FERGETSCGK NVDESLKKVR
NMKLEIPESN FDKFMTDKNL LSVDSKSSNE KKLSVESDLS AIYEKYSNGP FGHTEGLNGS
SDETYLRFQR ASVHSESNYN SRKSFTPSDF SNGNEEEHAV LQELNSLTQR INELGMESIN
SNSDSDRING SYSQVDFDNN NDEDDMNLFD PDFMAQDQLR AEERDYNKDD RTPLAKVPAA
FQSTGLGITP DDDIERQYIT EHRSRHEVPK RSPEKPSNPL EIGNPYAKPG TRLNTTHTHS
KTDRSITPQR GQPVPSGQQI SSYVQPANIN SPNKMYGANN SAMGSPRNPK TRAPPGPYNQ
GWNNRPSPSN IYQRPHPSDT QPQAYHLPGN PYSTGNRPNM QAQYHPQQVP MPIPQQPNRP
YQPYAMNTHM GSPGGYAGAA PPFQPANVNY NTRPQQPWPT PNSPSAHYRP PPNLNQPQNG
SAGYYRPPAP QLQNSQARPQ KKDGFSQFMP SATTKNPYAQ
