SEC13_DROME
ID SEC13_DROME Reviewed; 356 AA.
AC Q9V3J4; Q7KLW8;
DT 12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Protein SEC13 homolog {ECO:0000305};
DE AltName: Full=GATOR complex protein SEC13 {ECO:0000305};
DE AltName: Full=Secretory protein 13 {ECO:0000312|FlyBase:FBgn0024509};
GN Name=Sec13 {ECO:0000312|FlyBase:FBgn0024509};
GN ORFNames=CG6773 {ECO:0000312|FlyBase:FBgn0024509};
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|EMBL:AEO27697.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Oregon-R {ECO:0000312|EMBL:AEO27697.1};
RC TISSUE=Larva {ECO:0000312|EMBL:AEO27697.1};
RX PubMed=21898761; DOI=10.1002/dvg.20791;
RA Verma A., Sengupta S., Lakhotia S.C.;
RT "DNApol-epsilon gene is indispensable for the survival and growth of
RT Drosophila melanogaster.";
RL Genesis 50:86-101(2012).
RN [2] {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 [3] {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 [4] {ECO:0000312|EMBL:AAD46849.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAD46849.2};
RC TISSUE=Embryo {ECO:0000312|EMBL:AAD46849.2};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=20144761; DOI=10.1016/j.cell.2009.12.054;
RA Capelson M., Liang Y., Schulte R., Mair W., Wagner U., Hetzer M.W.;
RT "Chromatin-bound nuclear pore components regulate gene expression in higher
RT eukaryotes.";
RL Cell 140:372-383(2010).
RN [6] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH MAD AND MSK.
RX PubMed=20547758; DOI=10.1128/mcb.00124-10;
RA Chen X., Xu L.;
RT "Specific nucleoporin requirement for Smad nuclear translocation.";
RL Mol. Cell. Biol. 30:4022-4034(2010).
RN [7] {ECO:0000305}
RP FUNCTION, IDENTIFICATION IN THE GATOR COMPLEX, INTERACTION WITH MSK AND
RP MAD, AND SUBCELLULAR LOCATION.
RX PubMed=27166823; DOI=10.1371/journal.pgen.1006036;
RA Cai W., Wei Y., Jarnik M., Reich J., Lilly M.A.;
RT "The GATOR2 component Wdr24 regulates TORC1 activity and lysosome
RT function.";
RL PLoS Genet. 12:E1006036-E1006036(2016).
CC -!- FUNCTION: Functions as a component of the nuclear pore complex (NPC)
CC and the COPII coat (By similarity). At the endoplasmic reticulum, SEC13
CC is involved in the biogenesis of COPII-coated vesicles (By similarity).
CC Recruited to transcriptionally active chromatin at the time of
CC transcription initiation by RNA polymerase II (PubMed:20144761).
CC Required for proper expression of ecdysone-responsive genes such as
CC Eip74EF and Eip75B during larval development (PubMed:20144761).
CC Required for reactivation of transcription after heat shock
CC (PubMed:20144761). Required for nuclear import of phosphorylated Mad
CC via importin msk (PubMed:20547758). Has no role in classical nuclear
CC localization signal (cNLS)-dependent nuclear import via importin-beta
CC (PubMed:20547758). {ECO:0000250|UniProtKB:P55735,
CC ECO:0000269|PubMed:20144761, ECO:0000269|PubMed:20547758}.
CC -!- FUNCTION: A component of the GATOR subcomplex GATOR2 which functions as
CC an activator of the amino acid-sensing branch of the TORC1 signaling
CC pathway (PubMed:27166823). The two GATOR subcomplexes, GATOR1 and
CC GATOR2, regulate the TORC1 pathway in order to mediate metabolic
CC homeostasis, female gametogenesis and the response to amino acid
CC limitation and complete starvation (PubMed:27166823). GATOR2 activates
CC the TORC1 signaling pathway through the inhibition of the GATOR1
CC subcomplex, controlling the switch to cell proliferation and growth
CC under nutrient replete conditions and during female oocyte development
CC (PubMed:27166823). {ECO:0000269|PubMed:27166823}.
CC -!- SUBUNIT: Probable component of the nuclear pore complex (NPC) (By
CC similarity). Component of the GATOR complex consisting of mio,
CC Nup44A/Seh1, Im11, Nplr3, Nplr2, Wdr24, Wdr59 and Sec13
CC (PubMed:27166823). Within the GATOR complex, probable component of the
CC GATOR2 subcomplex which is likely composed of mio, Nup44A/Seh1, Wdr24,
CC Wdr59 and Sec13 (PubMed:27166823). Interacts with msk
CC (PubMed:20547758). Interacts (preferentially when phosphorylated) with
CC Mad (PubMed:20547758). {ECO:0000250|UniProtKB:P55735,
CC ECO:0000269|PubMed:20547758, ECO:0000269|PubMed:27166823}.
CC -!- INTERACTION:
CC Q9V3J4; Q8MRL2: EG:9D2.4; NbExp=4; IntAct=EBI-169056, EBI-9964542;
CC -!- SUBCELLULAR LOCATION: Nucleus envelope {ECO:0000269|PubMed:20144761}.
CC Nucleus, nucleoplasm {ECO:0000269|PubMed:20144761}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000269|PubMed:20144761}. Nucleus, nuclear pore complex
CC {ECO:0000269|PubMed:20144761}. Cytoplasmic vesicle, COPII-coated
CC vesicle membrane; Peripheral membrane protein; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P55735}. Endoplasmic reticulum membrane;
CC Peripheral membrane protein; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P55735}. Lysosome membrane
CC {ECO:0000305|PubMed:27166823}. Note=Localizes to chromatin,
CC specifically to areas undergoing transcriptional activation. Chromatin
CC localization is independent of the nuclear pore complex
CC (PubMed:20144761).
CC -!- TISSUE SPECIFICITY: Salivary glands. {ECO:0000269|PubMed:20144761}.
CC -!- DEVELOPMENTAL STAGE: Expressed during larval development.
CC {ECO:0000269|PubMed:20144761}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in the larva results in
CC reduced transcription of developmental genes Eip74EF and Eip75B in the
CC salivary glands, compromised transcriptional recovery after heat shock
CC and defective recruitment of Nup98. {ECO:0000269|PubMed:20144761}.
CC -!- SIMILARITY: Belongs to the WD repeat SEC13 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD46849.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; JN600259; AEO27697.1; -; Genomic_DNA.
DR EMBL; AE014297; AAF56128.1; -; Genomic_DNA.
DR EMBL; AE014297; AHN57479.1; -; Genomic_DNA.
DR EMBL; AF160909; AAD46849.2; ALT_INIT; mRNA.
DR RefSeq; NP_001287480.1; NM_001300551.1.
DR RefSeq; NP_651977.1; NM_143720.4.
DR AlphaFoldDB; Q9V3J4; -.
DR SMR; Q9V3J4; -.
DR IntAct; Q9V3J4; 8.
DR STRING; 7227.FBpp0083801; -.
DR PaxDb; Q9V3J4; -.
DR PRIDE; Q9V3J4; -.
DR DNASU; 44437; -.
DR EnsemblMetazoa; FBtr0084409; FBpp0083801; FBgn0024509.
DR EnsemblMetazoa; FBtr0346160; FBpp0311988; FBgn0024509.
DR GeneID; 44437; -.
DR KEGG; dme:Dmel_CG6773; -.
DR UCSC; CG6773-RA; d. melanogaster.
DR CTD; 6396; -.
DR FlyBase; FBgn0024509; Sec13.
DR VEuPathDB; VectorBase:FBgn0024509; -.
DR eggNOG; KOG1332; Eukaryota.
DR GeneTree; ENSGT00940000153393; -.
DR HOGENOM; CLU_032441_0_1_1; -.
DR InParanoid; Q9V3J4; -.
DR OMA; TVDTGHE; -.
DR OrthoDB; 944756at2759; -.
DR PhylomeDB; Q9V3J4; -.
DR Reactome; R-DME-159227; Transport of the SLBP independent Mature mRNA.
DR Reactome; R-DME-159230; Transport of the SLBP Dependant Mature mRNA.
DR Reactome; R-DME-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR Reactome; R-DME-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-DME-204005; COPII-mediated vesicle transport.
DR Reactome; R-DME-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-DME-3301854; Nuclear Pore Complex (NPC) Disassembly.
DR Reactome; R-DME-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-DME-4085377; SUMOylation of SUMOylation proteins.
DR Reactome; R-DME-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-DME-5578749; Transcriptional regulation by small RNAs.
DR Reactome; R-DME-9615933; Postmitotic nuclear pore complex (NPC) reformation.
DR SignaLink; Q9V3J4; -.
DR BioGRID-ORCS; 44437; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 44437; -.
DR PRO; PR:Q9V3J4; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0024509; Expressed in eye disc (Drosophila) and 41 other tissues.
DR GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR GO; GO:0030127; C:COPII vesicle coat; ISS:FlyBase.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0061700; C:GATOR2 complex; TAS:FlyBase.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0031080; C:nuclear pore outer ring; ISS:FlyBase.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0005703; C:polytene chromosome puff; IDA:UniProtKB.
DR GO; GO:0035859; C:Seh1-associated complex; IDA:FlyBase.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0005198; F:structural molecule activity; ISS:FlyBase.
DR GO; GO:0034605; P:cellular response to heat; IMP:UniProtKB.
DR GO; GO:0035293; P:chitin-based larval cuticle pattern formation; IMP:FlyBase.
DR GO; GO:0090114; P:COPII-coated vesicle budding; ISS:FlyBase.
DR GO; GO:0035077; P:ecdysone-mediated polytene chromosome puffing; IDA:UniProtKB.
DR GO; GO:0008363; P:larval chitin-based cuticle development; IMP:FlyBase.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0032008; P:positive regulation of TOR signaling; IBA:GO_Central.
DR GO; GO:1904263; P:positive regulation of TORC1 signaling; IEA:InterPro.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; IMP:UniProtKB.
DR GO; GO:0032527; P:protein exit from endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0006606; P:protein import into nucleus; IMP:FlyBase.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR037596; Sec13.
DR InterPro; IPR037363; Sec13/Seh1_fam.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR11024; PTHR11024; 1.
DR PANTHER; PTHR11024:SF2; PTHR11024:SF2; 1.
DR Pfam; PF00400; WD40; 5.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Cytoplasmic vesicle; Cytoskeleton; Developmental protein;
KW Endoplasmic reticulum; Lysosome; Membrane; mRNA transport;
KW Nuclear pore complex; Nucleus; Protein transport; Reference proteome;
KW Repeat; Transcription; Transcription regulation; Translocation; Transport;
KW WD repeat.
FT CHAIN 1..356
FT /note="Protein SEC13 homolog"
FT /evidence="ECO:0000305"
FT /id="PRO_0000439657"
FT REPEAT 11..50
FT /note="WD 1"
FT /evidence="ECO:0000255"
FT REPEAT 54..95
FT /note="WD 2"
FT /evidence="ECO:0000255"
FT REPEAT 101..142
FT /note="WD 3"
FT /evidence="ECO:0000255"
FT REPEAT 149..205
FT /note="WD 4"
FT /evidence="ECO:0000255"
FT REPEAT 210..253
FT /note="WD 5"
FT /evidence="ECO:0000255"
FT REPEAT 259..298
FT /note="WD 6"
FT /evidence="ECO:0000255"
FT REGION 307..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 356 AA; 39528 MW; B4062B8BAD01A5BA CRC64;
MVSLLQEIDT EHEDMVHHAA LDFYGLLLAT CSSDGSVRIF HSRKNNKALA ELKGHQGPVW
QVAWAHPKFG NILASCSYDR KVIVWKSTTP RDWTKLYEYS NHDSSVNSVD FAPSEYGLVL
ACASSDGSVS VLTCNTEYGV WDAKKIPNAH TIGVNAISWC PAQAPDPAFD QRVTSRSAAV
KRLVSGGCDN LVKIWREDND RWVEEHRLEA HSDWVRDVAW APSIGLPRSQ IATASQDRHV
IVWSSNADLS EWTSTVLHTF DDAVWSISWS TTGNILAVTG GDNNVTLWKE NTEGQWIRIN
YESGTAIQSK QPSHLPHSHS QQQQALQQHQ QQAPSHPGPS SDSEHSSNLS NSQLSN