ID A0A7J8GXC6_ROUAE Unreviewed; 1282 AA.
AC A0A7J8GXC6;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 02-APR-2025, entry version 13.
DE SubName: Full=Calcineurin binding protein 1 {ECO:0000313|EMBL:KAF6464239.1};
GN ORFNames=HJG63_001969 {ECO:0000313|EMBL:KAF6464239.1};
OS Rousettus aegyptiacus (Egyptian fruit bat) (Pteropus aegyptiacus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Yinpterochiroptera; Pteropodoidea;
OC Pteropodidae; Rousettinae; Rousettus.
OX NCBI_TaxID=9407 {ECO:0000313|EMBL:KAF6464239.1, ECO:0000313|Proteomes:UP000593571};
RN [1] {ECO:0000313|EMBL:KAF6464239.1, ECO:0000313|Proteomes:UP000593571}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRouAeg1 {ECO:0000313|EMBL:KAF6464239.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:KAF6464239.1};
RX PubMed=32699395;
RA Jebb D., Huang Z., Pippel M., Hughes G.M., Lavrichenko K., Devanna P.,
RA Winkler S., Jermiin L.S., Skirmuntt E.C., Katzourakis A., Burkitt-Gray L.,
RA Ray D.A., Sullivan K.A.M., Roscito J.G., Kirilenko B.M., Davalos L.M.,
RA Corthals A.P., Power M.L., Jones G., Ransome R.D., Dechmann D.K.N.,
RA Locatelli A.G., Puechmaille S.J., Fedrigo O., Jarvis E.D., Hiller M.,
RA Vernes S.C., Myers E.W., Teeling E.C.;
RT "Six reference-quality genomes reveal evolution of bat adaptations.";
RL Nature 583:578-584(2020).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAF6464239.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JACASE010000005; KAF6464239.1; -; Genomic_DNA.
DR Proteomes; UP000593571; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0031491; F:nucleosome binding; IEA:TreeGrafter.
DR GO; GO:0006325; P:chromatin organization; IEA:InterPro.
DR CDD; cd13839; MEF2_binding; 1.
DR FunFam; 1.25.40.10:FF:000076; calcineurin-binding protein cabin-1 isoform X1; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR033053; Hir3/CABIN1.
DR InterPro; IPR015134; MEF2-bd.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR15502; CALCINEURIN-BINDING PROTEIN CABIN 1-RELATED; 1.
DR PANTHER; PTHR15502:SF7; CALCINEURIN-BINDING PROTEIN CABIN-1; 1.
DR Pfam; PF09047; MEF2_binding; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
PE 4: Predicted;
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000593571}.
FT DOMAIN 1218..1252
FT /note="Calcineurin-binding protein cabin-1 MEF2-binding"
FT /evidence="ECO:0000259|Pfam:PF09047"
FT REGION 421..589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 761..888
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 906..945
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1008..1192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1206..1227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1258..1282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..446
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..465
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 470..494
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..505
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 875..885
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 906..922
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1061..1080
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1081..1092
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1158..1172
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1258..1268
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1269..1282
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1282 AA; 140665 MW; 0663D3A0DB2CCB91 CRC64;
MSETPMLPSS LMLLNTAHEY LGRRSWCCNS DGALLRFYVR VLQKELTAST SEDTHPYKEE
LETALEQCFY CLYSFPSKKS KARYLEEHSA QQVDLIWEDA LFMFEYFKPK TLPEFDSYKT
STVSADLANL LKRIATIVPR TERPALSLDK VSAYIEGTSA EVPCLPEGAD PSPPVVNELY
YLLADYHFKN KEQSKAIKFY MHDICICPDR FDSWAGMALA RASRIQDKLN SNELKSDGPI
WKHATPVLNC FRRALEIDSS NLSLWIEYGT MSYALHSFAS RQLKQWKGEL PSELVQQMES
RRDSMLETAR HCFTSAARCE GDGDEEEWLI HYMLGKVAEK QQQPPAIYLL HYRQAGHYLH
EEAARYPKKI HYHNPPELAM EALEVYFRLH ASILKLLGKP DSGVGAEVLV NFMKEAAEGP
FARGEEKNTP KASEKEKACL VDEDSHSSAG TLPGPGASLP SSSGPERSQD STAVALSDSS
STQDFFNEPP SSLEGSRKPY AEKRLPMPSS QPGPSGKDLP GATEERGKTE ESLESTEGFR
ATEQGSQKPA ADSLASACIP VKPPASAPAL WDGRKRGDPP GESAAFPQGL PAGAEEQRQF
LTEQCIASFR LCLSRFPQHY KSLYRLAFLY TYSKTHRNLQ WARDVLLGSS IPWQQLQHMP
AQGLFCERNK TNFFNGIWRI PVDEIDRPGS FAWHMNRSIV LLLKVLAQLR DHSTLLKVSS
MLQRTPDQGK KYLRDADRQV LAQRAFILTV KVLEDTLSEL AEGSEHPGPK ACGLPGARMT
TDVSHKASPE DGQESLPHPK KPPLADGSEP GAEPGGKACC LNHRPMDAGD SADQGEEQKD
KESPRAGPTE PMDTGEAAAR RLDPERALPL PPGRSPRDRA PESRPAELSL EELSISARQQ
PSLLALAQPA PTTSAPTTTT ARVGSHPEEP PPRPSRKRKL LEDTESGKTL LLDAYRVWQQ
GQKGMAYDLG RIERIMSETY MLIKQVDEEA ALEQAVKFCQ VHLGAAAQRQ AAGDTPTTPK
HPKDSRENFF PAAVAPTPPD SVPADALQRP SDTHTKPRPA PAATTAGITC PSSASASTPD
PSKDPESPRP HGPEATPSMA SLGPEREELA GGAEGAGYPP EEPPCSEPVK TAPEDPQAEL
HRWPAEGAPH IGTEPTCSQV ASSKVSSSGS AQPPECHLGK AEPSRAKSRL LPNMPKLVIP
SAATKFPPEI TVTPPTPTLL SPKGSISEET KQKLKSAILS AQSAANVRKE SLCQPALEVL
ETSSQESSLE SDTDEDDDYM DI
//
