AZF1_YEAST
ID AZF1_YEAST Reviewed; 914 AA.
AC P41696; D6W2H2;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Asparagine-rich zinc finger protein AZF1;
GN Name=AZF1; OrderedLocusNames=YOR113W; ORFNames=O3244, YOR3244W;
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 [GENOMIC DNA].
RC STRAIN=SC167;
RX PubMed=7975891; DOI=10.1002/yea.320100604;
RA Broehl S., Lisowsky T., Riemen G., Michaelis G.;
RT "A new nuclear suppressor system for a mitochondrial RNA polymerase mutant
RT identifies an unusual zinc-finger protein and a polyglutamine domain
RT protein in Saccharomyces cerevisiae.";
RL Yeast 10:719-731(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8904341;
RX DOI=10.1002/(sici)1097-0061(19960315)12:3<281::aid-yea904>3.0.co;2-o;
RA Wiemann S., Rechmann S., Benes V., Voss H., Schwager C., Vlcek C.,
RA Stegemann J., Zimmermann J., Erfle H., Paces V., Ansorge W.;
RT "Sequencing and analysis of 51 kb on the right arm of chromosome XV from
RT Saccharomyces cerevisiae reveals 30 open reading frames.";
RL Yeast 12:281-288(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9200815;
RX DOI=10.1002/(sici)1097-0061(19970615)13:7<655::aid-yea120>3.0.co;2-i;
RA Voss H., Benes V., Andrade M.A., Valencia A., Rechmann S., Teodoru C.,
RA Schwager C., Paces V., Sander C., Ansorge W.;
RT "DNA sequencing and analysis of 130 kb from yeast chromosome XV.";
RL Yeast 13:655-672(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [5]
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 [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61; SER-286 AND SER-325, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Potential transcription factor; suppressor for a
CC mitochondrial RNA polymerase mutant.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- MISCELLANEOUS: Present with 556 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z26253; CAA81212.1; -; Genomic_DNA.
DR EMBL; X90518; CAA62111.1; -; Genomic_DNA.
DR EMBL; X94335; CAA64033.1; -; Genomic_DNA.
DR EMBL; Z75021; CAA99311.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10888.1; -; Genomic_DNA.
DR PIR; S46593; S46593.
DR RefSeq; NP_014756.3; NM_001183532.3.
DR AlphaFoldDB; P41696; -.
DR SMR; P41696; -.
DR BioGRID; 34509; 181.
DR IntAct; P41696; 10.
DR MINT; P41696; -.
DR STRING; 4932.YOR113W; -.
DR iPTMnet; P41696; -.
DR MaxQB; P41696; -.
DR PaxDb; P41696; -.
DR PRIDE; P41696; -.
DR EnsemblFungi; YOR113W_mRNA; YOR113W; YOR113W.
DR GeneID; 854280; -.
DR KEGG; sce:YOR113W; -.
DR SGD; S000005639; AZF1.
DR VEuPathDB; FungiDB:YOR113W; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00530000068109; -.
DR HOGENOM; CLU_010433_0_0_1; -.
DR InParanoid; P41696; -.
DR OMA; YCHKCFT; -.
DR BioCyc; YEAST:G3O-33642-MON; -.
DR PRO; PR:P41696; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P41696; protein.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:SGD.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:SGD.
DR GO; GO:0043565; F:sequence-specific DNA binding; HDA:SGD.
DR GO; GO:0071322; P:cellular response to carbohydrate stimulus; IMP:SGD.
DR GO; GO:0060237; P:regulation of fungal-type cell wall organization; IMP:SGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:SGD.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 4.
DR SMART; SM00355; ZnF_C2H2; 4.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE 1: Evidence at protein level;
KW DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..914
FT /note="Asparagine-rich zinc finger protein AZF1"
FT /id="PRO_0000046802"
FT ZN_FING 593..615
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 621..643
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 649..671
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 677..702
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 93..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 138..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 326..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 743..812
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 853..877
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..229
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..275
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..348
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..411
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 753..812
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 853..872
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 61
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 286
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 325
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 914 AA; 101170 MW; BA1898DAB68AD050 CRC64;
MPPPTAQFMG PTQAGQNESQ NQSSGEAGEQ NQEHGQGPTP ILNQSQPASS QPQHQQQRNE
SISYYTNFNQ PRYSTDASIN SFLNISDNVP VTSTGGPSSG GAYSNLPRLS TSSTHQPPDL
SQIGRGFSIV NNLFPQQQQL QNQHRQQQQQ QQQQSHQQPP FKTPSFSTGL TGSSSQYQFL
PRNDNTSQPP SKRNSVYLGP NDGPDFEFFS MQQSQQPQFQ PSSRRESNSM RPPLLIPAAT
TKSQSNGTNN SGNMNTNADY ESFFNTGTNN SNSNQNPYFL SSRNNSLKFN PEDFDFQFKR
RNSFVRGTLD HSSQNAFIPE SRLNSLSVNN KANGDPVADN VTNNMKGKSN EVDNDDGNDS
SNNNNNNNNN NNNENNNDNN NDNNDNSINS ATSTNIPNQE DHSLASTDTT SNSRKDLKEI
EQRLRKHLND EDNYSSAISR PLDKNDVIEG SEGLNKHIDE SGMQPNIIKK RKKDDSTVYV
KNEMPRTDPP MSKDNSTSAE GAAMANFSGK EPPIPDISSV SDDATNLIGA TKVDQLMLII
QARKKGFTEK VNTTQDGDLL FNQTMDILPP KSELVGGVEK PKGTQNTRAV KKHECPYCHR
LFSQATHLEV HVRSHIGYKP FVCDYCGKRF TQGGNLRTHE RLHTGEKPYS CDICDKKFSR
KGNLAAHLVT HQKLKPFVCK LENCNKTFTQ LGNMKAHQNR FHKETLNALT AKLAEMNPSE
NIPLEERQLL EYFASIYKNS NRGIKGRGKG VGTKKSTISS PENHPASTIL NPNTNANNAI
ANDSENNGNP EGNIDSSSNS NPGSHSMISP TQKDMGTLQS QFIQNNFNNS VNSSNPSNQP
IINYNYTTLP HSRLGSSSSS NTNNNNSNFS VGAAPGVLMA PTTNNDFSFN LDQSNDNERS
QQEQVRFKNI NYKS
