MCAF1_DANRE
ID MCAF1_DANRE Reviewed; 815 AA.
AC A0JME2; A2BH15;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 2.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Activating transcription factor 7-interacting protein 1;
DE AltName: Full=MBD1-containing chromatin-associated factor 1;
GN Name=atf7ip; Synonyms=mcaf1; ORFNames=si:dkey-48a12.2, zgc:152981;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=SJD;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125; SER-127; THR-344 AND
RP SER-628, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18307296; DOI=10.1021/pr700667w;
RA Lemeer S., Pinkse M.W.H., Mohammed S., van Breukelen B., den Hertog J.,
RA Slijper M., Heck A.J.R.;
RT "Online automated in vivo zebrafish phosphoproteomics: from large-scale
RT analysis down to a single embryo.";
RL J. Proteome Res. 7:1555-1564(2008).
CC -!- FUNCTION: Recruiter that couples transcriptional factors to general
CC transcription apparatus and thereby modulates transcription regulation
CC and chromatin formation. Can both act as an activator or a repressor
CC depending on the context. Mediates MBD1-dependent transcriptional
CC repression, probably by recruiting complexes containing histone
CC methyltransferase activity. May belong to a complex that represses
CC transcription and couples DNA methylation and histone H3 'Lys-9'
CC trimethylation (H3K9me3) (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the MCAF family. {ECO:0000305}.
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DR EMBL; BX537268; CAM16111.1; -; Genomic_DNA.
DR EMBL; BC125844; AAI25845.1; -; mRNA.
DR AlphaFoldDB; A0JME2; -.
DR STRING; 7955.ENSDARP00000125013; -.
DR iPTMnet; A0JME2; -.
DR PaxDb; A0JME2; -.
DR PeptideAtlas; A0JME2; -.
DR PRIDE; A0JME2; -.
DR Ensembl; ENSDART00000135089; ENSDARP00000122892; ENSDARG00000069619.
DR ZFIN; ZDB-GENE-061103-178; atf7ip.
DR eggNOG; ENOG502QSM2; Eukaryota.
DR GeneTree; ENSGT00530000063707; -.
DR HOGENOM; CLU_018446_0_0_1; -.
DR InParanoid; A0JME2; -.
DR PhylomeDB; A0JME2; -.
DR Reactome; R-DRE-3214841; PKMTs methylate histone lysines.
DR PRO; PR:A0JME2; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 1.
DR Bgee; ENSDARG00000069619; Expressed in early embryo and 27 other tissues.
DR ExpressionAtlas; A0JME2; baseline and differential.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0090309; P:positive regulation of DNA methylation-dependent heterochromatin assembly; ISS:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
DR GO; GO:0031647; P:regulation of protein stability; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR026085; ATF7-int.
DR InterPro; IPR031870; ATF7IP_BD.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR23210; PTHR23210; 1.
DR Pfam; PF16788; ATF7IP_BD; 1.
DR Pfam; PF16794; fn3_4; 1.
DR SUPFAM; SSF49265; SSF49265; 1.
DR PROSITE; PS50853; FN3; 1.
PE 1: Evidence at protein level;
KW Activator; Coiled coil; Nucleus; Phosphoprotein; Reference proteome;
KW Repressor; Transcription; Transcription regulation.
FT CHAIN 1..815
FT /note="Activating transcription factor 7-interacting
FT protein 1"
FT /id="PRO_0000281783"
FT DOMAIN 698..811
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 1..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 315..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 400..438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 579..704
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 164..311
FT /evidence="ECO:0000255"
FT COMPBIAS 1..25
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..191
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..228
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..385
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..600
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 621..677
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 678..697
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 125
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18307296"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18307296"
FT MOD_RES 344
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18307296"
FT MOD_RES 628
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18307296"
FT CONFLICT 69
FT /note="D -> E (in Ref. 2; AAI25845)"
FT /evidence="ECO:0000305"
FT CONFLICT 88
FT /note="V -> A (in Ref. 2; AAI25845)"
FT /evidence="ECO:0000305"
FT CONFLICT 193
FT /note="E -> EA (in Ref. 2; AAI25845)"
FT /evidence="ECO:0000305"
FT CONFLICT 597..598
FT /note="AS -> PA (in Ref. 2; AAI25845)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 815 AA; 85267 MW; DD710EF2E72D867A CRC64;
MEVAVPEEPQ KKIFRARKTM KMSDRQQLEV LHNTLATTNS SLSSSPPQTP LMNGTHTETE
KDLNNKEGDL MAPATDSARC SPSPSFPVSR SPSPPNTQTT SPAMDLEDPL VATEEKKETS
NKSSSSSPSA SPAGLNCDPE VKEGFLCLSE EDETQADKDE KDSSEEKMNV DAETEDQKEE
KDEKDTDTPE NAEDNSAPVG LKRTLSEEKD EDDKEIEEER DGKRARLEGE ELEAQLELKI
TANGGNRDKI EKMVQQLVEE RLRVLQLTVF DRSLKELKDR VEKIDNVTKQ QNALQHINTL
QAKISRLAKK FGAANQASEN AKRTQDAQAA AAAAQANNAT NATTPQRTVK TTVDSKLSSS
PTVSNSTAVP AQPKPLSTPA TPTSSALATT APILQIISTT TSSTPSSTSL PGQSQTGTLL
LKTGPNPTVM TNAPATSGGQ PVAMQQLLIQ LPLAMANGQS GALVNAAGGV GLIPVSSLST
VSNINKAKTT TPATTFMLQK TAGNVSSATS SAPAVSLARA VYPGGTGTVS SPNTGISVTT
ARTPTQCAAV VGVSTAAASP GTTGPAATGS AAAAAGSPSA SALASKTDNQ ASTPKTASQP
GRPKGSVIDL TEDDDDVQVT GVQKATVSPV TTQRSSGPPP LVSSTPNTGT GVRSAQRSTV
DSPSQSRPSS SSSTSLPPLP LAPSPPARLP PEANHTSPPQ QPQLKLARVQ SQNGIVLSWC
VAETDRNCAA VDTYHLYAYH QDHQSSVSGA SAQMLWKKIG EVKALPLPMA CTLTQFVSGS
TYYFAVRAKD VYGRFGPFCE PQCTDVITPA SSAST
