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Database: UniProt
Entry: A0A2K6SWA5_SAIBB
LinkDB: A0A2K6SWA5_SAIBB
Original site: A0A2K6SWA5_SAIBB 
ID   A0A2K6SWA5_SAIBB        Unreviewed;      1277 AA.
AC   A0A2K6SWA5;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Activating transcription factor 7 interacting protein {ECO:0000313|Ensembl:ENSSBOP00000011655.1};
GN   Name=ATF7IP {ECO:0000313|Ensembl:ENSSBOP00000011655.1};
OS   Saimiri boliviensis boliviensis (Bolivian squirrel monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC   Saimiriinae; Saimiri.
OX   NCBI_TaxID=39432 {ECO:0000313|Ensembl:ENSSBOP00000011655.1, ECO:0000313|Proteomes:UP000233220};
RN   [1] {ECO:0000313|Ensembl:ENSSBOP00000011655.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the MCAF family.
CC       {ECO:0000256|ARBA:ARBA00010344}.
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DR   AlphaFoldDB; A0A2K6SWA5; -.
DR   STRING; 39432.ENSSBOP00000011655; -.
DR   Ensembl; ENSSBOT00000028441.1; ENSSBOP00000011655.1; ENSSBOG00000022603.1.
DR   GeneTree; ENSGT00530000063707; -.
DR   OMA; QETIHEP; -.
DR   Proteomes; UP000233220; Unplaced.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0016604; C:nuclear body; IEA:Ensembl.
DR   GO; GO:0005667; C:transcription regulator complex; IEA:Ensembl.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:Ensembl.
DR   GO; GO:0003714; F:transcription corepressor activity; IEA:Ensembl.
DR   GO; GO:0006306; P:DNA methylation; IEA:Ensembl.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0090309; P:positive regulation of DNA methylation-dependent heterochromatin formation; IEA:Ensembl.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; IEA:Ensembl.
DR   GO; GO:0050821; P:protein stabilization; IEA:Ensembl.
DR   GO; GO:0045898; P:regulation of RNA polymerase II transcription preinitiation complex assembly; IEA:Ensembl.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 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; ACTIVATING TRANSCRIPTION FACTOR 7 INTERACTING PROTEIN; 1.
DR   PANTHER; PTHR23210:SF22; ACTIVATING TRANSCRIPTION FACTOR 7-INTERACTING PROTEIN 1; 1.
DR   Pfam; PF16788; ATF7IP_BD; 1.
DR   Pfam; PF16794; fn3_4; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 1.
DR   PROSITE; PS50853; FN3; 1.
PE   3: Inferred from homology;
KW   Activator {ECO:0000256|ARBA:ARBA00023159};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233220};
KW   Repressor {ECO:0000256|ARBA:ARBA00022491};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT   DOMAIN          1167..1277
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   REGION          108..234
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          255..381
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          401..436
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          465..576
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          665..728
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          829..869
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          893..1033
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1122..1167
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        108..130
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        157..185
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        196..214
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        315..354
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        363..381
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        419..433
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        548..576
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        682..728
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        829..843
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        893..973
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        989..1009
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1010..1024
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1139..1157
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1277 AA;  137349 MW;  60C43BF656673E45 CRC64;
     MHEDQRFKME SLEEPQKKVF KARKTMRVSD RQQLEAVYKV KEELLKTDVK LLNGNHENGD
     LDPTSPLENV DYIKDKEEVN GIEEICFDPE ESKTEWKETP CILSVNVKNK QDDDLNSEPL
     SPNNVTLEPE SKLTAEPVSG DPAPGDLDAG DPASGVLASG DSTSDDPASG DPTSSDPSSS
     DAASGDAPSD DVPSGDATSA DATSDLSSGA PTSSDPLPGE PVSVAPISGD CASDDIASSE
     ITSVDLASGA QASIDPASDD LASGELSSSE LASDDLATGE LASDELTSES AFDRTFEPSS
     VPVCEPVPEI DNIEPSSNKD GDFLEKNGDD EKLEQIQSKD SLDEKNKADS NIDTNEETLE
     TDDTTICSDR PPENEKKVEE DTITELALGE DAISSSMEID QVEKNEDENS ADLVGSISEN
     VTEDDKSENI LENTDSMETD EIIPILEKLA PSEDELTCFS KASLLPIDET NPDLEEKMES
     SFGSPSKQES SESLPKEAFL VLSDEEDISG EKDESEVISQ NETCSPAEVE SNEKDNKPEE
     EEQVTHEDDE RPSEKNEFSR RKRSKSEDMD NIQSKRRRYM EEEYEAEFQV KITAKGDINQ
     KLQKVIQWLL EEKLCALQCA VFDKTLAELK TRVEKIECNK RHKTVLTELQ AKIARLTKRF
     EAAKEDLKKR QEHPPNPPVS PGKTVNDVNS NNNMPYRNAG TVRQMLESKR NVSESAPPSF
     QTPVNTVSST NLVTPPTVVS SQPKLQTPVT SGSLTATSVL PAPNTAAVVA TTQVPSGNPQ
     PTISLQSLPV ILHVPVAVSS QPQLLQSHPG TLVTNQPSGN VEFISVQSPP TVSGLTKNPV
     SLPSLPNPTK PNNVPSVPSP SIQRNPTASA APLGTTLAVQ AVPTAHSIVQ ATRTSLPTVG
     PSGLYSPSNN RGPIQMKIPI SAFSTSSPAE QNSTTTARIE NQTNKTIDVS VNKKAADSTS
     QSGKATGSDS SGVIDLTMDD EESGASQDSK KLNHTPVSTM SSSQPVSRPL QPIQPAPPLQ
     PSGVPTSGPS QTTIHLLPTA PTTVNVTHRP VTQVTTRLPV PRAPANHQVV YTTLPAPPAQ
     APLRGTVMQA PAVRQVNPQN SVTVRVPQTT TYVVNNGLTL GSTGPQLTVH HRPPQVHTEP
     PRPVHPAPLP EAPQPQRLPP EAASTSLPQK PHLKLARVQS QNGIVLSWSV LEVDRSCATV
     DSYHLYAYHE EPSATVPSQW KKIGEVKALP LPMACTLTQF VSGSKYYFAV RAKDIYGRFG
     PFCDPQSTDV ISSTQSS
//
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