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SYF1_DROME
ID   SYF1_DROME              Reviewed;         883 AA.
AC   A1Z9G2; C3KGI3;
DT   18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 141.
DE   RecName: Full=Pre-mRNA-splicing factor syf1 homolog {ECO:0000250|UniProtKB:Q9HCS7};
DE   AltName: Full=Pre-mRNA-splicing factor fandango {ECO:0000303|PubMed:24755291};
DE   AltName: Full=Protein faint sausage {ECO:0000303|PubMed:28087625};
GN   Name=fand {ECO:0000303|PubMed:24755291, ECO:0000312|FlyBase:FBgn0033859};
GN   Synonyms=fas {ECO:0000303|PubMed:28087625};
GN   ORFNames=CG6197 {ECO:0000312|FlyBase:FBgn0033859};
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 {ECO:0000312|Proteomes:UP000000803};
RN   [1] {ECO:0000312|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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   [2] {ECO:0000312|Proteomes:UP000000803}
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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   [3] {ECO:0000312|EMBL:ACO95726.1, ECO:0000312|EMBL:AEZ68806.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley {ECO:0000312|EMBL:ACO95726.1, ECO:0000312|EMBL:AEZ68806.1};
RC   TISSUE=Embryo {ECO:0000312|EMBL:ACO95726.1};
RA   Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL   Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000305}
RP   FUNCTION, AND MUTAGENESIS OF 69-TRP--GLU-883.
RX   PubMed=10502111; DOI=10.1007/s004270050287;
RA   Jack J., Myette G.;
RT   "Mutations that alter the morphology of the malpighian tubules in
RT   Drosophila.";
RL   Dev. Genes Evol. 209:546-554(1999).
RN   [5] {ECO:0000305}
RP   FUNCTION, INTERACTION WITH CG9667 AND PRP19, SUBCELLULAR LOCATION,
RP   DEVELOPMENTAL STAGE, AND MUTAGENESIS OF 355-ASN--HIS-360 AND ALA-401.
RX   PubMed=24755291; DOI=10.7554/elife.02181;
RA   Guilgur L.G., Prudencio P., Sobral D., Liszekova D., Rosa A.,
RA   Martinho R.G.;
RT   "Requirement for highly efficient pre-mRNA splicing during Drosophila early
RT   embryonic development.";
RL   Elife 3:E02181-E02181(2014).
RN   [6] {ECO:0000305}
RP   FUNCTION, AND MUTAGENESIS OF 69-TRP--GLU-883 AND 219-TRP--GLU-883.
RX   PubMed=28087625; DOI=10.1242/dev.144535;
RA   Sauerwald J., Soneson C., Robinson M.D., Luschnig S.;
RT   "Faithful mRNA splicing depends on the Prp19 complex subunit faint sausage
RT   and is required for tracheal branching morphogenesis in Drosophila.";
RL   Development 144:657-663(2017).
CC   -!- FUNCTION: Subunit of the NTC(Nineteen)/Prp19 complex, which is part of
CC       the spliceosome (PubMed:24755291, PubMed:28087625). The complex
CC       participates in spliceosome assembly, its remodeling and is required
CC       for efficient spliceosome activation (PubMed:24755291,
CC       PubMed:28087625). Essential for efficient pre-mRNA splicing
CC       (PubMed:24755291, PubMed:28087625). In embryos, efficient pre-mRNA
CC       splicing of zygotic transcripts is essential during dynamic cellular
CC       processes that require rapid division and/or dramatic changes in gene
CC       expression such as blastoderm cellularization, tracheal branching
CC       morphogenesis, Malpighian morphogenesis and epidermal development
CC       (PubMed:24755291, PubMed:28087625, PubMed:10502111). Part of its role
CC       in promoting embryo tracheal development is also due to specifically
CC       splicing bnl transcripts which results in the activation of the BNL-FGF
CC       pathway (PubMed:28087625). {ECO:0000269|PubMed:10502111,
CC       ECO:0000269|PubMed:24755291, ECO:0000269|PubMed:28087625}.
CC   -!- SUBUNIT: Component of the NTC(Nineteen)/Prp19 complex composed of at
CC       least fand, Prp19,CG9667/ISY1 and Cdc5/CDC5L. Within the complex,
CC       interacts with Prp19 and ISY1/CG9667. {ECO:0000269|PubMed:24755291}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24755291}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in adult ovaries and 0-3 hours embryos
CC       (at protein level). {ECO:0000269|PubMed:24755291}.
CC   -!- MISCELLANEOUS: Named 'fandango' after the Iberian folk dance to
CC       highlight the similarity of the blastoderm cellularization phenotype to
CC       the charleston/kuk phenotype (PubMed:24755291). The phenotype 'faint
CC       sausage (fas)', consisting of a poorly differentiated cuticle and head,
CC       was previously associated with the immunoglobulin domain protein
CC       CG17716 but is now known to be caused by mutations in the protein
CC       'fandango' (PubMed:24755291). {ECO:0000269|PubMed:24755291,
CC       ECO:0000303|PubMed:24755291}.
CC   -!- SIMILARITY: Belongs to the crooked-neck family. {ECO:0000305}.
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DR   EMBL; AE013599; AAF58348.1; -; Genomic_DNA.
DR   EMBL; BT082048; ACO95726.1; -; mRNA.
DR   EMBL; BT133178; AEZ68806.1; -; mRNA.
DR   RefSeq; NP_610891.1; NM_137047.3.
DR   AlphaFoldDB; A1Z9G2; -.
DR   SMR; A1Z9G2; -.
DR   IntAct; A1Z9G2; 5.
DR   STRING; 7227.FBpp0086749; -.
DR   PaxDb; A1Z9G2; -.
DR   PRIDE; A1Z9G2; -.
DR   DNASU; 36514; -.
DR   EnsemblMetazoa; FBtr0087623; FBpp0086749; FBgn0033859.
DR   GeneID; 36514; -.
DR   KEGG; dme:Dmel_CG6197; -.
DR   UCSC; CG6197-RA; d. melanogaster.
DR   CTD; 36514; -.
DR   FlyBase; FBgn0033859; fand.
DR   VEuPathDB; VectorBase:FBgn0033859; -.
DR   eggNOG; KOG2047; Eukaryota.
DR   GeneTree; ENSGT00550000075140; -.
DR   HOGENOM; CLU_007736_0_0_1; -.
DR   InParanoid; A1Z9G2; -.
DR   OMA; FLMQQPL; -.
DR   OrthoDB; 370051at2759; -.
DR   PhylomeDB; A1Z9G2; -.
DR   Reactome; R-DME-6781823; Formation of TC-NER Pre-Incision Complex.
DR   Reactome; R-DME-6782135; Dual incision in TC-NER.
DR   Reactome; R-DME-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR   Reactome; R-DME-72163; mRNA Splicing - Major Pathway.
DR   SignaLink; A1Z9G2; -.
DR   BioGRID-ORCS; 36514; 1 hit in 1 CRISPR screen.
DR   ChiTaRS; fas; fly.
DR   GenomeRNAi; 36514; -.
DR   PRO; PR:A1Z9G2; -.
DR   Proteomes; UP000000803; Chromosome 2R.
DR   Bgee; FBgn0033859; Expressed in embryonic/larval hemocyte (Drosophila) and 21 other tissues.
DR   GO; GO:0071013; C:catalytic step 2 spliceosome; HDA:FlyBase.
DR   GO; GO:0005634; C:nucleus; IC:FlyBase.
DR   GO; GO:0071014; C:post-mRNA release spliceosomal complex; IBA:GO_Central.
DR   GO; GO:0071011; C:precatalytic spliceosome; HDA:FlyBase.
DR   GO; GO:0000974; C:Prp19 complex; IDA:FlyBase.
DR   GO; GO:0071007; C:U2-type catalytic step 2 spliceosome; IBA:GO_Central.
DR   GO; GO:0007510; P:cardioblast cell fate determination; IMP:FlyBase.
DR   GO; GO:0000349; P:generation of catalytic spliceosome for first transesterification step; IBA:GO_Central.
DR   GO; GO:0007443; P:Malpighian tubule morphogenesis; IMP:FlyBase.
DR   GO; GO:0002009; P:morphogenesis of an epithelium; IMP:FlyBase.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR   GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; HMP:FlyBase.
DR   GO; GO:0008380; P:RNA splicing; IMP:FlyBase.
DR   Gene3D; 1.25.40.10; -; 3.
DR   InterPro; IPR003107; HAT.
DR   InterPro; IPR045075; Syf1-like.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   PANTHER; PTHR11246; PTHR11246; 1.
DR   SMART; SM00386; HAT; 13.
DR   SUPFAM; SSF48452; SSF48452; 5.
PE   1: Evidence at protein level;
KW   mRNA processing; mRNA splicing; Nucleus; Reference proteome; Repeat;
KW   Spliceosome.
FT   CHAIN           1..883
FT                   /note="Pre-mRNA-splicing factor syf1 homolog"
FT                   /id="PRO_0000447890"
FT   REPEAT          13..45
FT                   /note="HAT 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          46..78
FT                   /note="HAT 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          88..120
FT                   /note="HAT 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          122..156
FT                   /note="HAT 4"
FT                   /evidence="ECO:0000255"
FT   REPEAT          158..190
FT                   /note="HAT 5"
FT                   /evidence="ECO:0000255"
FT   REPEAT          268..303
FT                   /note="HAT 6"
FT                   /evidence="ECO:0000255"
FT   REPEAT          368..406
FT                   /note="HAT 7"
FT                   /evidence="ECO:0000255"
FT   REPEAT          463..495
FT                   /note="HAT 8"
FT                   /evidence="ECO:0000255"
FT   REPEAT          531..565
FT                   /note="HAT 9"
FT                   /evidence="ECO:0000255"
FT   REPEAT          570..604
FT                   /note="HAT 10"
FT                   /evidence="ECO:0000255"
FT   REPEAT          642..676
FT                   /note="HAT 11"
FT                   /evidence="ECO:0000255"
FT   REPEAT          678..712
FT                   /note="HAT 12"
FT                   /evidence="ECO:0000255"
FT   REGION          794..851
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          864..883
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        798..812
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        813..835
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         69..883
FT                   /note="Missing: Embryonic lethal and displays defects in
FT                   primary tracheal branching and Malpighian morphogenesis.
FT                   Displays abnormal splicing of zygotic transcripts resulting
FT                   in qualitative (intron retention) as well as quantitative
FT                   (transcript abundance) changes in gene expression. Tracheal
FT                   defects are likely due, at least in part, to the mis-
FT                   splicing of bnl transcripts. Embryonic Malpighian tubules
FT                   are shortened and round."
FT                   /evidence="ECO:0000269|PubMed:10502111,
FT                   ECO:0000269|PubMed:28087625"
FT   MUTAGEN         219..883
FT                   /note="Missing: H124; embryonic lethal and displays defects
FT                   in primary tracheal branching. Tracheal defects are likely
FT                   due at least in part, to the mis-splicing of bnl
FT                   transcripts. Earlier developmental processes, such as
FT                   gastrulation and germband retraction are unaffected."
FT                   /evidence="ECO:0000269|PubMed:28087625"
FT   MUTAGEN         355..360
FT                   /note="Missing: Fand2; embryos display significant splicing
FT                   defects in the small zygotic kuk transcript whereas there
FT                   is no effect on splicing of the large maternal kuk
FT                   transcript. Reduced protein levels of ISY1/CG9667 but no
FT                   effect on Prp19."
FT                   /evidence="ECO:0000269|PubMed:24755291"
FT   MUTAGEN         401
FT                   /note="A->V: Fand1; a large subset of zygotic but not
FT                   maternally encoded pre-mRNAs, including the kuk transcript,
FT                   display splicing defects. Consequently, maternally
FT                   controlled oogenesis, such as primordial germ-cell
FT                   formation and syncytial nuclear divisions, appear normal
FT                   but during zygotically controlled blastoderm
FT                   cellularization the cortical nuclei fail to elongate and
FT                   become mislocalized. Reduced protein levels of ISY1/CG9667
FT                   but no effect on Prp19."
FT                   /evidence="ECO:0000269|PubMed:24755291"
FT   CONFLICT        575
FT                   /note="A -> V (in Ref. 3; ACO95726)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   883 AA;  103327 MW;  35F5D93C849954FF CRC64;
     MVTKTIKSLN LEINFEVEDV PYEEEILRNA YSVKHWLRYI DHKAKAPNNG VNMVYERALK
     ELPGSYKIWH NYLRTRRKQV RGKIPTDPMY EEVNSAFERA LVFMHKMPRI WMDYGAFMTS
     QCKITRTRHV FDRALRALPI TQHGRIWPLY LQFVRRFEMP ETALRVYRRY LKLFPEDTEE
     YVDYLQEADR LDEAAQQLAH IVDNEHFVSK HGKSNHQLWN ELCDLISKNP HKVHSLNVDA
     IIRGGLRRYT DQLGHLWNSL ADYYVRSGLF DRARDIYEEA IQTVTTVRDF TQVFDEYAQF
     EELSLNRRME QVAANEAATE EDDIDVELRL SRFEYLMERR LLLLNSVLLR QNPHNVHEWH
     KRVTLYEDKP AEIISTYTEA VQTVQPKQAV GKLHTLWVEF AKFYEANGQV EDARVVFERG
     TEVEYVKVED LAAVWCEWAE MELRQQQFEA ALKLMQRATA MPKRKIAYYD DTETVQARLH
     RSLKVWSMYA DLEESFGTFK TCKAVYERII DLKICTPQII INYGMFLEEH NYFEEAYRAY
     EKGISLFKWP NVYDIWNSYL TKFLERYGGT KLERARDLFE QCLDQCPPEH AKYFYLLYAK
     LEEEHGLARH AMSVYDRATS AVKEDEMFDM YNIFIKKAAE IYGLPRTREI YEKAIESLPE
     QNMRHMCVKF AELETKLGEV DRARAIYAHC SQVCDPRITA DFWQTWKEFE VRHGNEDTMR
     EMLRIKRSVQ ATYNTQVNMM AAQFLSTNNG AAADAGAGAG PDAMRLLEEK ARQAAAESKQ
     KPIEKAASNI MFVRGETQGG AKDKKDTVVN PDEIDIGDSD EDDEEEDDDE ENEMTNENQA
     SAAVTKTDEE GLVMKKLRFE QKAIPAKVFG SLKPSNQGDS DGE
 
 
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