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   24-JAN-2024, entry version 138.
DE   RecName: Full=Splicing factor Cactin {ECO:0000305};
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 in pre-mRNA splicing by facilitating excision of
CC       a subset of introns (By similarity). Plays a role during early
CC       embryonic development (PubMed:10842059). Involved in the dorsal-ventral
CC       embryonic patterning (PubMed:10842059). Probably acts as a negative
CC       regulator of the NF-kappa-B (Rel) signaling pathway (PubMed:10842059).
CC       {ECO:0000250|UniProtKB:Q8WUQ7, ECO:0000269|PubMed:10842059}.
CC   -!- SUBUNIT: Interacts with cact. {ECO:0000269|PubMed:10842059}.
CC   -!- INTERACTION:
CC       Q9VR99; Q03017: cact; NbExp=5; IntAct=EBI-175417, EBI-200600;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8WUQ7}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q8WUQ7}.
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};
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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; 13.
DR   STRING; 7227.FBpp0309346; -.
DR   iPTMnet; Q9VR99; -.
DR   PaxDb; 7227-FBpp0076997; -.
DR   DNASU; 33043; -.
DR   EnsemblMetazoa; FBtr0340400; FBpp0309346; FBgn0031114.
DR   GeneID; 33043; -.
DR   KEGG; dme:Dmel_CG1676; -.
DR   UCSC; CG1676-RA; d. melanogaster.
DR   AGR; FB:FBgn0031114; -.
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; HIDFWND; -.
DR   OrthoDB; 558574at2759; -.
DR   PhylomeDB; Q9VR99; -.
DR   Reactome; R-DME-72163; mRNA Splicing - Major Pathway.
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 cell types or tissues.
DR   ExpressionAtlas; Q9VR99; baseline and differential.
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; IMP: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   PANTHER; PTHR21737:SF4; CACTIN; 1.
DR   PANTHER; PTHR21737; POLYGLUTAMINE BINDING PROTEIN 1/MARVEL MEMBRANE-ASSOCIATING DOMAIN CONTAINING 3; 1.
DR   Pfam; PF10312; Cactin_mid; 1.
DR   Pfam; PF09732; CactinC_cactus; 1.
DR   SMART; SM01050; CactinC_cactus; 1.
DR   Genevisible; Q9VR99; DM.
PE   1: Evidence at protein level;
KW   Coiled coil; Cytoplasm; Developmental protein; Nucleus; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..720
FT                   /note="Splicing factor 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
//