CATIN_DROME
ID CATIN_DROME Reviewed; 720 AA.
AC Q9VR99; Q9NBV5;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 3.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Cactin;
DE AltName: Full=Cactus-interacting protein;
GN Name=cactin; ORFNames=CG1676;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH CACT, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Ovary;
RX PubMed=10842059; DOI=10.1016/s0925-4773(00)00314-2;
RA Lin P., Huang L.H., Steward R.;
RT "Cactin, a conserved protein that interacts with the Drosophila IkappaB
RT protein cactus and modulates its function.";
RL Mech. Dev. 94:57-65(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99 AND SER-104, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Plays a role during early embryonic development. Involved in
CC the dorsal-ventral embryonic patterning. Probably acts as a negative
CC regulator of the NF-kappa-B (Rel) signaling pathway.
CC {ECO:0000269|PubMed:10842059}.
CC -!- SUBUNIT: Interacts with cact. {ECO:0000269|PubMed:10842059}.
CC -!- TISSUE SPECIFICITY: Expressed in ovary (at protein level).
CC {ECO:0000269|PubMed:10842059}.
CC -!- DEVELOPMENTAL STAGE: Expressed during embryogenesis (at protein level).
CC {ECO:0000269|PubMed:10842059}.
CC -!- SIMILARITY: Belongs to the CACTIN family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF66981.1; Type=Frameshift; Evidence={ECO:0000305};
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; AF245116; AAF66981.1; ALT_FRAME; mRNA.
DR EMBL; AE014298; AAF50904.3; -; Genomic_DNA.
DR RefSeq; NP_523422.4; NM_078698.4.
DR AlphaFoldDB; Q9VR99; -.
DR SMR; Q9VR99; -.
DR BioGRID; 59332; 47.
DR IntAct; Q9VR99; 12.
DR STRING; 7227.FBpp0076997; -.
DR iPTMnet; Q9VR99; -.
DR PaxDb; Q9VR99; -.
DR PRIDE; Q9VR99; -.
DR DNASU; 33043; -.
DR EnsemblMetazoa; FBtr0340400; FBpp0309346; FBgn0031114.
DR GeneID; 33043; -.
DR KEGG; dme:Dmel_CG1676; -.
DR UCSC; CG1676-RA; d. melanogaster.
DR CTD; 58509; -.
DR FlyBase; FBgn0031114; cactin.
DR VEuPathDB; VectorBase:FBgn0031114; -.
DR eggNOG; KOG2370; Eukaryota.
DR GeneTree; ENSGT00950000183102; -.
DR HOGENOM; CLU_011759_0_0_1; -.
DR InParanoid; Q9VR99; -.
DR OMA; HEPYMLL; -.
DR OrthoDB; 1252926at2759; -.
DR PhylomeDB; Q9VR99; -.
DR SignaLink; Q9VR99; -.
DR BioGRID-ORCS; 33043; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 33043; -.
DR PRO; PR:Q9VR99; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0031114; Expressed in eye disc (Drosophila) and 23 other tissues.
DR ExpressionAtlas; Q9VR99; baseline and differential.
DR Genevisible; Q9VR99; DM.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; HDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005681; C:spliceosomal complex; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; ISS:FlyBase.
DR GO; GO:0009950; P:dorsal/ventral axis specification; IMP:UniProtKB.
DR GO; GO:0045292; P:mRNA cis splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IC:FlyBase.
DR GO; GO:0045752; P:positive regulation of Toll signaling pathway; IMP:FlyBase.
DR InterPro; IPR019134; Cactin_C.
DR InterPro; IPR018816; Cactin_central.
DR Pfam; PF10312; Cactin_mid; 1.
DR Pfam; PF09732; CactinC_cactus; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Developmental protein; Phosphoprotein; Reference proteome.
FT CHAIN 1..720
FT /note="Cactin"
FT /id="PRO_0000419266"
FT REGION 1..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 449..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 512..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 109..159
FT /evidence="ECO:0000255"
FT COILED 206..236
FT /evidence="ECO:0000255"
FT COILED 346..375
FT /evidence="ECO:0000255"
FT COMPBIAS 1..16
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..67
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..97
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..156
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..466
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..486
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 99
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 104
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 70..71
FT /note="EH -> DD (in Ref. 1; AAF66981)"
FT /evidence="ECO:0000305"
FT CONFLICT 93
FT /note="V -> M (in Ref. 1; AAF66981)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 720 AA; 86556 MW; D7C5175A3925FFDB CRC64;
MPKEKSKHRH RSRSRERRDH RSPDPRSSRN RDRDRERERE KDRDHRDHRD KERDQRRERE
KDKSRDKKRE HKSRRRRSSS SSSSPSSSTS SSVPGAPRSP LVKSPMKLLQ TLEARRLVEQ
KDRQRKKEEL KAHETPEEKR ARRLREKQAK EQRRRERMGW DNEYQTYSNE DNPFGDSNLT
STFHWGKKLE VEGLSNLSTK TVEVLSLQKQ LENRRELEKV KKRRQERELE RQVREDDLMM
QQRAKEAVQF REWQRQEDQF HLEQARLRSE IRIRDGRAKP IDLLAQYVAA GNEPLEECLE
MQMHEPYVLL NGLPVEELED LLVDIKVYEE LEQGKHIDFW NDMITIVQDE LQRQQKLEAE
NSSLNQRRDG IHQAVVKDVA DIFRGKNAQQ LEEMRHRIEA KISGRADGVD ISYWESLLSQ
LKAHMARARL RDRHQALLRE KLSLLKREND NETLQEKVAP QVKEEEMETQ DAEDPEVEEG
SPEDEEDPLN ELRKTVRLYQ AGNYSPRYIR EEDFTGRRAQ NEDVDEPEAE GLLYEEEDDE
RRTQRQRLLI LHPERVDNNQ LTPQELRMRN EAKQGMQGDE AEFSVETTLD AVPQLATDKY
RPRKPRYFNR VHTGFEWNKY NQTHYDMDNP PPKIVQGYKF NIFYPDLMDK SQTPQYFLTP
CADNGDFAVL RFHTGPPYED IAFKIVNREW EFSYKRGFRC QFHNNIFQLW FHFKRYRYRR
