ID G3GYC9_CRIGR Unreviewed; 1234 AA.
AC G3GYC9;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Calmodulin-binding transcription activator 2 {ECO:0000313|EMBL:EGV93947.1};
GN ORFNames=I79_002806 {ECO:0000313|EMBL:EGV93947.1};
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029 {ECO:0000313|EMBL:EGV93947.1, ECO:0000313|Proteomes:UP000001075};
RN [1] {ECO:0000313|Proteomes:UP000001075}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CHO K1 cell line {ECO:0000313|Proteomes:UP000001075};
RX PubMed=21804562; DOI=10.1038/nbt.1932;
RA Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W., Xie M.,
RA Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B., Koh W.,
RA Fan H.C., Wang J., Gui Y., Lee K.H., Betenbaugh M.J., Quake S.R.,
RA Famili I., Palsson B.O., Wang J.;
RT "The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell line.";
RL Nat. Biotechnol. 29:735-741(2011).
CC -!- SUBUNIT: May interact with calmodulin. {ECO:0000256|ARBA:ARBA00029480}.
CC -!- SIMILARITY: Belongs to the CAMTA family.
CC {ECO:0000256|ARBA:ARBA00008267}.
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DR EMBL; JH000064; EGV93947.1; -; Genomic_DNA.
DR AlphaFoldDB; G3GYC9; -.
DR STRING; 10029.G3GYC9; -.
DR PaxDb; 10029-XP_007624514-1; -.
DR eggNOG; KOG0520; Eukaryota.
DR InParanoid; G3GYC9; -.
DR Proteomes; UP000001075; Unassembled WGS sequence.
DR GO; GO:0001772; C:immunological synapse; IEA:InterPro.
DR GO; GO:0097197; C:tetraspanin-enriched microdomain; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0060255; P:regulation of macromolecule metabolic process; IEA:UniProt.
DR GO; GO:0051171; P:regulation of nitrogen compound metabolic process; IEA:UniProt.
DR GO; GO:0080090; P:regulation of primary metabolic process; IEA:UniProt.
DR Gene3D; 1.20.5.190; -; 2.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR005559; CG-1_dom.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR026238; INCA1.
DR InterPro; IPR002909; IPT_dom.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR028181; SCIMP.
DR PANTHER; PTHR23335:SF9; CALMODULIN-BINDING TRANSCRIPTION ACTIVATOR 2; 1.
DR PANTHER; PTHR23335; CALMODULIN-BINDING TRANSCRIPTION ACTIVATOR CAMTA; 1.
DR Pfam; PF03859; CG-1; 1.
DR Pfam; PF15142; INCA1; 1.
DR Pfam; PF15050; SCIMP; 1.
DR Pfam; PF01833; TIG; 1.
DR PRINTS; PR02102; PROTEININCA1.
DR SMART; SM01076; CG-1; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR PROSITE; PS51437; CG_1; 1.
DR PROSITE; PS50096; IQ; 1.
PE 3: Inferred from homology;
KW Activator {ECO:0000256|ARBA:ARBA00023159};
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000001075};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..28
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 97..222
FT /note="CG-1"
FT /evidence="ECO:0000259|PROSITE:PS51437"
FT REGION 343..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 428..460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 516..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 747..780
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 895..924
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 981..1007
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1215..1234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..369
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..538
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 902..924
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1234 AA; 134945 MW; FC69B2CC8A2D750F CRC64;
MSWWRDNFWI ILAVAIVVVS LVLGLILYCV CRRQFRQGKK WAIAKPSKHN GRDEEKMYEL
KKAQWGSSES TSELPVLEDG CGFLGTTEYL DEEEERATYA QEENYFVTPR DQEIASYLIT
FEKHDEWLSC APKTRPQNGS IILYNRKKVK YRKDGYLWKK RKDGKTTRED HMKLKVQGME
CLYGCYVHSS IVPTFHRRCY WLLQNPDIVL VHYLNVPALE DCGKGCSPRE WLKWSREELL
GQLKPMFHGI KWSCGNGAEE FSVEQLVQQI LDTHPTKPAP RTHACLCSGG LGSWSLTHKC
SSTKHRIISP KVEPRALTLA SISHSQPPEP PPLITLILPE LPKAHTSPSS SSSSSSSSSS
SSSSSGFAEP LEIRPSPPTS RGGSSRGGTA ILLLTGLEQR AGGLTPTRHL APQAEPRPVS
LAVVVGSEPS ALPTPPSPAF DPDRFLNSPQ RGQTYGGGQG VNPDFPEAEG THTPCPALEP
AAALEPQAAA RGLPSQLGAS GRRGNQFFIQ DDDSGEELKG QETVPPVPSP PPSSPSSPAT
LQPSGRVTRG EALFGGSGGT SELEPFSLSS FPDLMGELIS DEAPSIPAPT PQLSPALNTI
TDFSPEWSYP EGGVKVLITG PWTEAAEHYS CVFDHIAVPA SLVQPGVLRC YCPAHEVGLV
SLQVAGREGP LSASVLFEYR ARRFLSLPST QLDWLSLDDS QFRMSILERL EQMEKRMAEI
AAAGQAPGQS PEAPPIQHDR LRTISDLKGG GEDEGGGGIR NVEPKSSVGS ESLKEKGWGL
REDDGSCGGK PYVDMTPVSA SMDTQHGHRC IRSVETGSLD LEQEVDPLNV DHFSCTPLMW
ACALGHLEAA VLLFCWNRQA LSIPDSLGRL PLSVAHSRGH VRLARCLEEL QRQEPSVEHP
LALSPPSSSP DTGLSSVSSP SELSDGTFSV TSAYSSAADG SPPPVPLLAS EITMEMIPGQ
LSPGATETPL LLMDYEATRS KESVPSLSGP PLAQKDGTPP EDAGSPPAVD VIPVDMISLA
KQIIEATPER IKREDFSGLP EAGASLREQT GTVGLSETMS WLASYLENVD HFPSSAPTSE
LPFERGRLAI PPTPSWAEFL SASTSGKMES DFALLTLSDH EQRELYEAAR VIQTAFRKYK
GRRLKEQQEV AAAVIQRCYR KYKQLTWIAL KFALYKKMTQ AAILIQSKFR SYYEQKRFQQ
SRRAAVLIQQ HYRSYRRRPG PAHRPSGPLP ARNK
//