EAF_SCHPO
ID EAF_SCHPO Reviewed; 994 AA.
AC O59773;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2012, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Chromatin modification-related protein vid21;
DE AltName: Full=Esa1-associated factor vid21;
DE AltName: Full=Vacuolar import and degradation protein 21;
GN Name=vid21; ORFNames=SPCC1795.08c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP REVISION OF GENE MODEL.
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [4]
RP IDENTIFICATION IN NUA4 COMPLEX, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=19040720; DOI=10.1186/gb-2008-9-11-r167;
RA Shevchenko A., Roguev A., Schaft D., Buchanan L., Habermann B., Sakalar C.,
RA Thomas H., Krogan N.J., Shevchenko A., Stewart A.F.;
RT "Chromatin Central: towards the comparative proteome by accurate mapping of
RT the yeast proteomic environment.";
RL Genome Biol. 9:R167.1-R167.22(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-298 AND SER-378, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Component of the NuA4 histone acetyltransferase complex which
CC is involved in transcriptional activation of selected genes principally
CC by acetylation of nucleosomal histone H4 and H2A. The NuA4 complex is
CC also involved in DNA repair (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the NuA4 histone acetyltransferase complex.
CC {ECO:0000269|PubMed:19040720}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00549,
CC ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the EAF1 family. {ECO:0000305}.
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DR EMBL; CU329672; CAA18643.2; -; Genomic_DNA.
DR PIR; T41135; T41135.
DR RefSeq; NP_588036.2; NM_001023028.2.
DR AlphaFoldDB; O59773; -.
DR BioGRID; 275686; 5.
DR IntAct; O59773; 1.
DR MINT; O59773; -.
DR STRING; 4896.SPCC1795.08c.1; -.
DR iPTMnet; O59773; -.
DR MaxQB; O59773; -.
DR PaxDb; O59773; -.
DR PRIDE; O59773; -.
DR EnsemblFungi; SPCC1795.08c.1; SPCC1795.08c.1:pep; SPCC1795.08c.
DR GeneID; 2539114; -.
DR KEGG; spo:SPCC1795.08c; -.
DR PomBase; SPCC1795.08c; vid21.
DR VEuPathDB; FungiDB:SPCC1795.08c; -.
DR eggNOG; ENOG502QSEY; Eukaryota.
DR HOGENOM; CLU_305264_0_0_1; -.
DR InParanoid; O59773; -.
DR OMA; WLLRTEM; -.
DR PRO; PR:O59773; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0000785; C:chromatin; NAS:PomBase.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0000812; C:Swr1 complex; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; ISM:PomBase.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; ISO:PomBase.
DR GO; GO:0043967; P:histone H4 acetylation; IBA:GO_Central.
DR GO; GO:0007127; P:meiosis I; IEP:PomBase.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR014012; HSA_dom.
DR InterPro; IPR001005; SANT/Myb.
DR Pfam; PF07529; HSA; 1.
DR SMART; SM00573; HSA; 1.
DR SMART; SM00717; SANT; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR PROSITE; PS51204; HSA; 1.
DR PROSITE; PS50090; MYB_LIKE; 1.
PE 1: Evidence at protein level;
KW Activator; Chromatin regulator; Coiled coil; DNA damage; DNA repair;
KW Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..994
FT /note="Chromatin modification-related protein vid21"
FT /id="PRO_0000065822"
FT DOMAIN 475..548
FT /note="HSA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00549"
FT DOMAIN 713..773
FT /note="Myb-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00133"
FT REGION 122..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 288..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 671..693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 857..880
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 975..994
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 880..912
FT /evidence="ECO:0000255"
FT COMPBIAS 160..195
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..241
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..267
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..304
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 671..692
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 298
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 378
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 994 AA; 113498 MW; 0BBAA79E7CA8BD21 CRC64;
MKQKETKTSQ IALVDGEKLS ITDSFASLFT LDEEEENDSV DNEEIKLTKE KHEKLLLLFW
LHCKFPNGLE WLHSSSDLLP EQVSEWFNFY QKYRFKRGRN FNLSARESVT PIVEEPIVPE
EPDNLEGVSE ETPLKETSLE LSEEEIITSK SPIPSPETIH KNIDVEEKET IEPTTPVKEV
ETTAHAEEEK GPLTPDSEYA ARQLTEELAN KSSQEEGVDK QLRVVEATEK EHEEDGNEEN
VTVTKPVEVA TDQVESKEVK KKEVSETTEP TAPPVTVAEV LEIEDKVPKV DEVEEVHSPE
AKVTENDVEN VQSGIDIEKT IQLLNNQEIP SEQQIISVDK ATESPVQEVA VDVNEKPVDE
IVEPSKLQME NKLPSEKSPT IDRTGVEAPL FELSVSMPLT LIPPSKFSEP VKPELSSEAW
LLRTEMSPLH LRLKNAHKYV LSDNWSHAYR EEIVRQSLHH LTVAKEKGIW SFRQPKRQNE
MPRLKTHRDY VLDEMQWMSI DFSQERKWKI ILAHRMANWV MDYHQASDKC TVCTPASLSK
NKKPYMQENE HQKDSHEETF NEQIVSHFNL NDNNNNKVLS IPRDSLQFYN AVFSDDIFVT
TNSEQIQNCV LNVPMYGPPT ENNEYCEEIS EKYPITPVSR FAYAKTKLKS TCAKASRKRL
FNQLELSPPE SFMEKKARSD ENQLDGNKIK DDNQKLSSVG TFSVRPPYPP SSKDIRPEAP
WLPEEDELLL LLLRRYSFNW EFVASRLTPP GLYIPLAEKR TAWDCFERWI QVDPRAANVQ
LTGSHARLAQ QKLDESLRHS DKVSQHLSLR DEGTPNHLIK HNSYFLLPTV SRHYRPITIF
EAIRKILKKR EFAKKPTMTK RAIAPSAAST EKLPPVPSPL ELSRLKSERE AQIQQIQAQR
NFAQLQSQNR ALRPQNAAVA AGAQQHNQQL AAFQAVAASQ NSSNNSSAGV SPIAGRMVPR
LQPYAVSSSL KLTPEQIHQL QQRKQTVPTT ERTQ
