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MCAF1_CHICK
ID   MCAF1_CHICK             Reviewed;        1085 AA.
AC   Q5ZIE8;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 94.
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=RCJMB04_27g4;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
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; AJ720836; CAG32495.1; -; mRNA.
DR   RefSeq; NP_001012831.1; NM_001012813.1.
DR   AlphaFoldDB; Q5ZIE8; -.
DR   STRING; 9031.ENSGALP00000041710; -.
DR   PaxDb; Q5ZIE8; -.
DR   PRIDE; Q5ZIE8; -.
DR   GeneID; 417966; -.
DR   KEGG; gga:417966; -.
DR   CTD; 55729; -.
DR   VEuPathDB; HostDB:geneid_417966; -.
DR   eggNOG; ENOG502QSM2; Eukaryota.
DR   InParanoid; Q5ZIE8; -.
DR   OrthoDB; 88757at2759; -.
DR   PhylomeDB; Q5ZIE8; -.
DR   PRO; PR:Q5ZIE8; -.
DR   Proteomes; UP000000539; Unplaced.
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; 2.
DR   Pfam; PF16788; ATF7IP_BD; 1.
DR   Pfam; PF16794; fn3_4; 1.
DR   SUPFAM; SSF49265; SSF49265; 1.
DR   PROSITE; PS50853; FN3; 1.
PE   2: Evidence at transcript level;
KW   Activator; Coiled coil; Nucleus; Reference proteome; Repressor;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..1085
FT                   /note="Activating transcription factor 7-interacting
FT                   protein 1"
FT                   /id="PRO_0000281782"
FT   DOMAIN          976..1082
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          47..109
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          127..245
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          329..381
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          469..499
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          517..560
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          650..843
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          889..910
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          932..975
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          446..480
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        64..95
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        136..154
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        335..381
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        480..499
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        650..720
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        728..775
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        796..813
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        828..843
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        948..971
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1085 AA;  117377 MW;  14B3B5B1758AD3BF CRC64;
     MDNTDEPQKK VFKARKTMRA SDRQQLEAVY KAKEDLLKTT EVKLLNGKHE NGDSDLNSPL
     SNTDCTEDKR EVNGLVDSNE ISEIKRPESR AESVVSDLEP KPLSPVNVTR EQDTDVALVC
     EAENRVLGSN KVNFHEENNI KNRLDQRESD TPSGENKSNC DNSFSPEEKG KTNDITIISN
     SPVEEKKKAG EIIVEDTVGE EAISSSMETD QEPKNERDGT AGLSETVVEK AVDESSESIL
     ENTDSMEADE IIPILEKLAP AEDEMSCFSK SALLPVDDTA PDLEEKMDNC LSSPLKQESN
     ESLPKEAFLV LSDEEDPCDE REHAEVILPN KSGLPEEVEK SEEEDKEREV VHKEEEKHTE
     RGEVSRRKRS KSEDMDSVHS KRRRFVGEED YEAEFQVKIT ARRDVDQKLE KVIQRVLEEK
     LAALQCAVFD KTLADLKMRI EKVECNKRHK TVLTELQAKI TRLTKRFGAA KEDMKKKQEN
     TPNPSLSSGK AASSTANANN LTYRNITTVR QMLESKRNVG DSKPATLQAP VSAAPASSLA
     APQTPASGHP KPQTPVTSSP LTTTVISTAN TATVVGTSQV PSGSTQPMSV SLQSLPVILH
     VPVAVSSQPQ LLQGHAGTLV TNQQSGSVEF ISVQSSSTVG SLTKTAVSLA STNTTKPNNS
     PSVSSPGVQR NSPASAGSVR TTLAVQAVST THPVAQTTRT SLPTVGTSGL HNSTSSRGPI
     HMKIPLSAFN STAPTEPPTI TAPRVENQTS RPPTDSSANK RTAEGPTQSV KVTGSDSGGV
     IDLTLDDEDD VSSQAEAKKQ NQTASTAQSI PTQPLSRPLP PLQPNPLQQT GVPTSGPSQT
     TIHVLPTAPT TVNVTHRPVT QTAAKLPIPR TPTNHQVVYT TIPAPPAQNS VRGAVMPSPS
     LRPVNPQTGS MTVRMPQTTA YVVNNGLTLG SGAPQLTVHH RPPQVHAEPP RPVHPAPLPE
     APQPPRLPPE AANTSLPQKP QLKLARVQSQ NGIVLSWSVI EVDRSCASVD SYHLYAYHED
     PSATMPSQWK KIGEVKALPL PMACTLTQFV SGSKYYFAVR AKDIYGRFGP FCDPQSTDVI
     SSQSS
 
 
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