STC_DROME
ID STC_DROME Reviewed; 1106 AA.
AC P40798; Q8IP49; Q9VJQ1; Q9Y0Z5;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 02-FEB-2004, sequence version 2.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Protein shuttle craft;
GN Name=stc; ORFNames=CG3647;
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] (ISOFORMS A AND B).
RC TISSUE=Ovary;
RX PubMed=8524296; DOI=10.1128/mcb.16.1.192;
RA Stroumbakis N.D., Li Z., Tolias P.P.;
RT "A homolog of human transcription factor NF-X1 encoded by the Drosophila
RT shuttle craft gene is required in the embryonic central nervous system.";
RL Mol. Cell. Biol. 16:192-201(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10471707; DOI=10.1093/genetics/153.1.179;
RA Ashburner M., Misra S., Roote J., Lewis S.E., Blazej R.G., Davis T.,
RA Doyle C., Galle R.F., George R.A., Harris N.L., Hartzell G., Harvey D.A.,
RA Hong L., Houston K.A., Hoskins R.A., Johnson G., Martin C., Moshrefi A.R.,
RA Palazzolo M., Reese M.G., Spradling A.C., Tsang G., Wan K.H., Whitelaw K.,
RA Celniker S.E., Rubin G.M.;
RT "An exploration of the sequence of a 2.9-Mb region of the genome of
RT Drosophila melanogaster: the Adh region.";
RL Genetics 153:179-219(1999).
RN [3]
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 [4]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=10731138; DOI=10.1126/science.287.5461.2222;
RA Rubin G.M., Hong L., Brokstein P., Evans-Holm M., Frise E., Stapleton M.,
RA Harvey D.A.;
RT "A Drosophila complementary DNA resource.";
RL Science 287:2222-2224(2000).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-335; SER-336; SER-339;
RP SER-343 AND SER-354, AND 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 an essential role during the late stages of embryonic
CC neurogenesis. May either fine-tune the guidance or the spatial
CC maintenance of the migrating SNB and in nerve roots, which are composed
CC of axons originating from distinct groups of motor neurons and may be
CC required to either guide or maintain the position of these nerves along
CC a direct and straight path to their ultimate targets in particular
CC muscle fields. May play a role in egg chamber development and/or may
CC confer essential maternal contributions to the early embryo.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A;
CC IsoId=P40798-1; Sequence=Displayed;
CC Name=B;
CC IsoId=P40798-2; Sequence=VSP_005757;
CC -!- TISSUE SPECIFICITY: Ovaries and embryonic central nervous system.
CC -!- DEVELOPMENTAL STAGE: Major expression is seen in the ovaries while
CC moderate levels of expression are observed during embryogenesis and
CC throughout subsequent stages of fly development.
CC -!- SIMILARITY: Belongs to the NFX1 family. {ECO:0000305}.
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DR EMBL; U09306; AAB60255.1; -; mRNA.
DR EMBL; AE014134; AAF53441.2; -; Genomic_DNA.
DR EMBL; AE014134; AAN10891.1; -; Genomic_DNA.
DR EMBL; AF145679; AAD38654.1; -; mRNA.
DR PIR; T13938; T13938.
DR PIR; T44598; T44598.
DR RefSeq; NP_476598.1; NM_057250.4. [P40798-2]
DR RefSeq; NP_476599.1; NM_057251.4. [P40798-1]
DR AlphaFoldDB; P40798; -.
DR SMR; P40798; -.
DR BioGRID; 60906; 24.
DR IntAct; P40798; 3.
DR STRING; 7227.FBpp0080265; -.
DR iPTMnet; P40798; -.
DR PaxDb; P40798; -.
DR PRIDE; P40798; -.
DR DNASU; 34888; -.
DR EnsemblMetazoa; FBtr0080705; FBpp0080265; FBgn0001978. [P40798-1]
DR EnsemblMetazoa; FBtr0080706; FBpp0080266; FBgn0001978. [P40798-2]
DR GeneID; 34888; -.
DR KEGG; dme:Dmel_CG3647; -.
DR CTD; 34888; -.
DR FlyBase; FBgn0001978; stc.
DR VEuPathDB; VectorBase:FBgn0001978; -.
DR eggNOG; KOG1952; Eukaryota.
DR GeneTree; ENSGT00940000156325; -.
DR InParanoid; P40798; -.
DR PhylomeDB; P40798; -.
DR SignaLink; P40798; -.
DR BioGRID-ORCS; 34888; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 34888; -.
DR PRO; PR:P40798; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0001978; Expressed in egg chamber and 27 other tissues.
DR ExpressionAtlas; P40798; baseline and differential.
DR Genevisible; P40798; DM.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:FlyBase.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISS:FlyBase.
DR GO; GO:0008270; F:zinc ion binding; ISM:FlyBase.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0051865; P:protein autoubiquitination; ISS:FlyBase.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR CDD; cd02643; R3H_NF-X1; 1.
DR Gene3D; 3.30.1370.50; -; 1.
DR InterPro; IPR034078; NFX1_fam.
DR InterPro; IPR001374; R3H_dom.
DR InterPro; IPR036867; R3H_dom_sf.
DR InterPro; IPR034076; R3H_NF-X1.
DR InterPro; IPR000967; Znf_NFX1.
DR InterPro; IPR001841; Znf_RING.
DR PANTHER; PTHR12360; PTHR12360; 1.
DR Pfam; PF01424; R3H; 1.
DR Pfam; PF01422; zf-NF-X1; 7.
DR SMART; SM00393; R3H; 1.
DR SMART; SM00438; ZnF_NFX; 9.
DR SUPFAM; SSF82708; SSF82708; 1.
DR PROSITE; PS51061; R3H; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; RNA-binding; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..1106
FT /note="Protein shuttle craft"
FT /id="PRO_0000056190"
FT DOMAIN 1006..1071
FT /note="R3H"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00382"
FT ZN_FING 386..433
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 474..492
FT /note="NF-X1-type 1"
FT ZN_FING 527..546
FT /note="NF-X1-type 2"
FT ZN_FING 585..604
FT /note="NF-X1-type 3"
FT ZN_FING 644..667
FT /note="NF-X1-type 4"
FT ZN_FING 706..725
FT /note="NF-X1-type 5"
FT ZN_FING 733..752
FT /note="NF-X1-type 6"
FT ZN_FING 844..867
FT /note="NF-X1-type 7"
FT ZN_FING 876..896
FT /note="NF-X1-type 8"
FT REGION 7..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 189..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..211
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..339
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..355
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 335
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 336
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 339
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 354
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 109..115
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|PubMed:8524296"
FT /id="VSP_005757"
FT CONFLICT 12
FT /note="A -> P (in Ref. 1; AAB60255)"
FT /evidence="ECO:0000305"
FT CONFLICT 25
FT /note="A -> V (in Ref. 1; AAB60255)"
FT /evidence="ECO:0000305"
FT CONFLICT 617
FT /note="M -> I (in Ref. 1; AAB60255)"
FT /evidence="ECO:0000305"
FT CONFLICT 784
FT /note="C -> S (in Ref. 1; AAB60255)"
FT /evidence="ECO:0000305"
FT CONFLICT 820..821
FT /note="EL -> DW (in Ref. 1; AAB60255)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1106 AA; 123183 MW; 9502C6185994700D CRC64;
MAEYWQQLTN GAGEAGPGNE SSAMADCNGG HESAAVGGSC NRHSNNNYVN FNQFIMQHNL
GGGAPSNATS TMQHPVGSSY TNFSLGGGGG AFGLNPPVAS ASTSHFANVS HQSPNFYSQA
MIPTYQNGDG IARVTVTSSY GSVNPSNSNF SSFYTPFGNN PFDFSASKLQ ASAPEFVPNF
AKLSLEETPA AATTNGNSTA SLETAINETR PRTLRAQEPA ERGANNQCSN HNYERERERE
RDRDRDRERD RDRDRDRDRD RDRDRDRDSR PGNTRQQRRS DYRDDREDRY ERSDRRRPQK
QQRYDNHRSN KRRDDWNRNR DRINGFPRAV DDLDTSNESA HPSPEKQSQL QQISPRRGPP
LPPADNEKLS QREKLVRDIE QRRLECLVCV EAIKSHQPTW SCRNCYHMLH LKCTITWASS
SKSEVGWRCP ACQNVLQDLP RDYLCFCGKL KNPPVSRTEL AHSCGEVCCR IEGCSHACTL
LCHPGPCPPC QANVVRSCGC GRSTKTMQCA MKEEVLCGEI CDKLLNCGEH RCQAECHSGK
CAACSEQVVQ QCHCGKQERK VPCTRESQDK RTYSCKDSCG QPLPCGHHKC KDSCHAGSCR
PCKLSPEQIT SCPCGKMPVP AGQRSSCLDP IPTCEGICSR TLRCGKPAHP HQCGSKCHLG
QCPPCPKQTG VKCRCGHMDQ MIKCRQLCNR ADDARCKRRC TKKRSCGKHK CNVECCIDID
HDCPLPCNRT LSCGKHKCDQ PCHRGNCPPC YRSSFEELYC ECGAEVIYPP VPCGTKKPIC
KLPCSRIHPC DHPPQHNCHS GPTCPPCMIF TTKLCHGNHE LRKTIPCSQP NFSCGMACGK
PLPCGGHKCI KPCHEGPCQS AGEICRQSCT KPRPTCGHKC AAACHEGACP ETPCKELVEV
QCECGNRKQN RSCQELAREH SRIATIQLAS SMAEMSRGNY MELSEILAPA KKSNKTLDCN
DECRLLERNR RLAAALSSGN SDTKQKCLTK YSEFVRGFAK KNPALTKSVY ETLTDLVKLA
KESKQRSRSH SFPTMNREKR QLVHELCEVF GIESVSYDKE PNRNVVATAH KDRCWFPATS
IMEVLARESG QRRVPVPSNN AWGLKK
