CAF16_YEAST
ID CAF16_YEAST Reviewed; 289 AA.
AC P43569; D6VTK2;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=CCR4-associated factor 16;
GN Name=CAF16; OrderedLocusNames=YFL028C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7670463; DOI=10.1038/ng0795-261;
RA Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S.,
RA Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H.,
RA Eki T.;
RT "Analysis of the nucleotide sequence of chromosome VI from Saccharomyces
RT cerevisiae.";
RL Nat. Genet. 10:261-268(1995).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP INTERACTION WITH CCR4 AND SSN2.
RX PubMed=11113136; DOI=10.1074/jbc.m009112200;
RA Liu H.-Y., Chiang Y.-C., Pan J., Chen J., Salvadore C., Audino D.C.,
RA Badarinarayana V., Palaniswamy V., Anderson B., Denis C.L.;
RT "Characterization of CAF4 and CAF16 reveals a functional connection between
RT the CCR4-NOT complex and a subset of SRB proteins of the RNA polymerase II
RT holoenzyme.";
RL J. Biol. Chem. 276:7541-7548(2001).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- SUBUNIT: Interacts with CCR4 and SSN2. {ECO:0000269|PubMed:11113136}.
CC -!- INTERACTION:
CC P43569; P39954: SAH1; NbExp=3; IntAct=EBI-22808, EBI-16451;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 1620 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR EMBL; D50617; BAA09210.1; -; Genomic_DNA.
DR EMBL; BK006940; DAA12412.1; -; Genomic_DNA.
DR PIR; S56226; S56226.
DR RefSeq; NP_116625.1; NM_001179938.1.
DR AlphaFoldDB; P43569; -.
DR SMR; P43569; -.
DR BioGRID; 31118; 55.
DR DIP; DIP-5946N; -.
DR IntAct; P43569; 3.
DR STRING; 4932.YFL028C; -.
DR CarbonylDB; P43569; -.
DR MaxQB; P43569; -.
DR PaxDb; P43569; -.
DR PRIDE; P43569; -.
DR EnsemblFungi; YFL028C_mRNA; YFL028C; YFL028C.
DR GeneID; 850516; -.
DR KEGG; sce:YFL028C; -.
DR SGD; S000001866; CAF16.
DR VEuPathDB; FungiDB:YFL028C; -.
DR eggNOG; KOG2355; Eukaryota.
DR GeneTree; ENSGT00390000009359; -.
DR HOGENOM; CLU_057592_3_0_1; -.
DR InParanoid; P43569; -.
DR OMA; LMEEVFQ; -.
DR BioCyc; YEAST:G3O-30432-MON; -.
DR PRO; PR:P43569; -.
DR Proteomes; UP000002311; Chromosome VI.
DR RNAct; P43569; protein.
DR GO; GO:0030014; C:CCR4-NOT complex; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISS:SGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:SGD.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..289
FT /note="CCR4-associated factor 16"
FT /id="PRO_0000093464"
FT DOMAIN 7..249
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 41..48
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 289 AA; 33090 MW; 2250CC15F9CE1354 CRC64;
MVSQFAIEVR NLTYKFKESS DPSVVDINLQ IPWNTRSLVV GANGAGKSTL LKLLSGKHLC
LDGKILVNGL DPFSPLSMNQ VDDDESVEDS TNYQTTTYLG TEWCHMSIIN RDIGVLELLK
SIGFDHFRER GERLVRILDI DVRWRMHRLS DGQKRRVQLA MGLLKPWRVL LLDEVTVDLD
VIARARLLEF LKWETETRRC SVVYATHIFD GLAKWPNQVY HMKSGKIVDN LDYQKDVEFS
EVVNAKVNGQ VAFENDNNKV VISKVNSLHP LALEWLKRDN QIPDKEIGI
