SEC13_CAEEL
ID SEC13_CAEEL Reviewed; 313 AA.
AC Q9N4A7; Q9N4A6;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Protein SEC13 homolog {ECO:0000250|UniProtKB:P55735};
DE Short=CeSEH13R {ECO:0000303|PubMed:12937276};
DE AltName: Full=GATOR complex protein SEC13 {ECO:0000305};
DE AltName: Full=Nuclear pore complex protein 20 {ECO:0000303|PubMed:12937276};
GN Name=npp-20 {ECO:0000312|WormBase:Y77E11A.13a};
GN Synonyms=CeSec13R {ECO:0000312|WormBase:Y77E11A.13a},
GN sec-13 {ECO:0000312|WormBase:Y77E11A.13a};
GN ORFNames=Y77E11A.13 {ECO:0000312|WormBase:Y77E11A.13a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP DISRUPTION PHENOTYPE.
RX PubMed=12937276; DOI=10.1091/mbc.e03-04-0237;
RA Galy V., Mattaj I.W., Askjaer P.;
RT "Caenorhabditis elegans nucleoporins Nup93 and Nup205 determine the limit
RT of nuclear pore complex size exclusion in vivo.";
RL Mol. Biol. Cell 14:5104-5115(2003).
RN [3]
RP IDENTIFICATION IN COPII COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=21478858; DOI=10.1038/ncb2225;
RA Witte K., Schuh A.L., Hegermann J., Sarkeshik A., Mayers J.R., Schwarze K.,
RA Yates J.R. III, Eimer S., Audhya A.;
RT "TFG-1 function in protein secretion and oncogenesis.";
RL Nat. Cell Biol. 13:550-558(2011).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=28122936; DOI=10.1242/jcs.196709;
RA Ferreira J., Stear J.H., Saumweber H.;
RT "Nucleoporins NPP-10, NPP-13 and NPP-20 are required for HCP-4 nuclear
RT import to establish correct centromere assembly.";
RL J. Cell Sci. 130:963-974(2017).
CC -!- FUNCTION: Functions as a component of the nuclear pore complex (NPC)
CC and the COPII coat (By similarity). Required for the nuclear import of
CC hcp-4 during mitotic prophase, this step is essential for centrosome
CC assembly and resolution (PubMed:28122936).
CC {ECO:0000250|UniProtKB:P55735, ECO:0000269|PubMed:28122936}.
CC -!- FUNCTION: As a component of the GATOR complex may function in the amino
CC acid-sensing branch of the TORC1 signaling pathway.
CC {ECO:0000250|UniProtKB:P55735}.
CC -!- SUBUNIT: Component of a heterotertrameric COPII coat complex composed
CC of npp-20 and sec-31 (Probable). Probably part of the GATOR complex.
CC {ECO:0000250|UniProtKB:P55735, ECO:0000305|PubMed:21478858}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPII-coated vesicle
CC membrane {ECO:0000250|UniProtKB:P55735}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P55735}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P55735}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:21478858}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P55735}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P55735}. Nucleus, nuclear pore complex
CC {ECO:0000269|PubMed:21478858}. Lysosome membrane
CC {ECO:0000250|UniProtKB:P55735}. Note=Localizes close to endoplasmic
CC reticulum exit sites (ERES) and the nuclear envelopes of proliferating
CC germ nuclei. {ECO:0000269|PubMed:21478858}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000312|WormBase:Y77E11A.13a};
CC IsoId=Q9N4A7-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:Y77E11A.13b};
CC IsoId=Q9N4A7-2; Sequence=VSP_040693, VSP_040694;
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in embryonic
CC lethality (PubMed:12937276, PubMed:28122936). Causes severe defects in
CC mitosis (PubMed:28122936). Cytokinesis is blocked and nucleus formation
CC is impaired after the first embryonic mitosis (PubMed:12937276).
CC Centrosome assembly during prophase and prometaphase and their
CC subsequent resolution are impaired which results from impaired nuclear
CC import of hcp-4 (PubMed:28122936). Impaired sister chromatin
CC segregation (PubMed:28122936). {ECO:0000269|PubMed:12937276,
CC ECO:0000269|PubMed:28122936}.
CC -!- SIMILARITY: Belongs to the WD repeat SEC13 family. {ECO:0000255}.
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DR EMBL; BX284604; CCD72599.1; -; Genomic_DNA.
DR EMBL; BX284604; CCD72600.1; -; Genomic_DNA.
DR RefSeq; NP_500086.1; NM_067685.3. [Q9N4A7-1]
DR RefSeq; NP_500087.1; NM_067686.4. [Q9N4A7-2]
DR AlphaFoldDB; Q9N4A7; -.
DR SMR; Q9N4A7; -.
DR BioGRID; 42113; 29.
DR DIP; DIP-25859N; -.
DR IntAct; Q9N4A7; 6.
DR STRING; 6239.Y77E11A.13a; -.
DR EPD; Q9N4A7; -.
DR PaxDb; Q9N4A7; -.
DR PeptideAtlas; Q9N4A7; -.
DR EnsemblMetazoa; Y77E11A.13a.1; Y77E11A.13a.1; WBGene00003806. [Q9N4A7-1]
DR EnsemblMetazoa; Y77E11A.13b.1; Y77E11A.13b.1; WBGene00003806. [Q9N4A7-2]
DR GeneID; 176957; -.
DR KEGG; cel:CELE_Y77E11A.13; -.
DR UCSC; Y77E11A.13b; c. elegans.
DR CTD; 176957; -.
DR WormBase; Y77E11A.13a; CE25614; WBGene00003806; npp-20. [Q9N4A7-1]
DR WormBase; Y77E11A.13b; CE25615; WBGene00003806; npp-20. [Q9N4A7-2]
DR eggNOG; KOG1332; Eukaryota.
DR GeneTree; ENSGT00940000153393; -.
DR HOGENOM; CLU_032441_0_1_1; -.
DR InParanoid; Q9N4A7; -.
DR OMA; TVDTGHE; -.
DR OrthoDB; 944756at2759; -.
DR PhylomeDB; Q9N4A7; -.
DR Reactome; R-CEL-159227; Transport of the SLBP independent Mature mRNA.
DR Reactome; R-CEL-159230; Transport of the SLBP Dependant Mature mRNA.
DR Reactome; R-CEL-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR Reactome; R-CEL-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-CEL-191859; snRNP Assembly.
DR Reactome; R-CEL-204005; COPII-mediated vesicle transport.
DR Reactome; R-CEL-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-CEL-3301854; Nuclear Pore Complex (NPC) Disassembly.
DR Reactome; R-CEL-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-CEL-4085377; SUMOylation of SUMOylation proteins.
DR Reactome; R-CEL-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-CEL-9615933; Postmitotic nuclear pore complex (NPC) reformation.
DR PRO; PR:Q9N4A7; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00003806; Expressed in embryo and 4 other tissues.
DR GO; GO:0030127; C:COPII vesicle coat; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005643; C:nuclear pore; IDA:UniProtKB.
DR GO; GO:0031080; C:nuclear pore outer ring; IBA:GO_Central.
DR GO; GO:0005198; F:structural molecule activity; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0090114; P:COPII-coated vesicle budding; IBA:GO_Central.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:UniProtKB.
DR GO; GO:1990893; P:mitotic chromosome centromere condensation; IMP:UniProtKB.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0051169; P:nuclear transport; IC:UniProtKB.
DR GO; GO:0006997; P:nucleus organization; IMP:UniProtKB.
DR GO; GO:0010973; P:positive regulation of division septum assembly; IMP:UniProtKB.
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:0032527; P:protein exit from endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0006606; P:protein import into nucleus; IMP:UniProtKB.
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; 2.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cell division; Cytoplasmic vesicle;
KW Endoplasmic reticulum; ER-Golgi transport; Lysosome; Membrane; Mitosis;
KW mRNA transport; Nuclear pore complex; Nucleus; Protein transport;
KW Reference proteome; Repeat; Translocation; Transport; WD repeat.
FT CHAIN 1..313
FT /note="Protein SEC13 homolog"
FT /id="PRO_0000405542"
FT REPEAT 11..50
FT /note="WD 1"
FT /evidence="ECO:0000255"
FT REPEAT 56..97
FT /note="WD 2"
FT /evidence="ECO:0000255"
FT REPEAT 102..143
FT /note="WD 3"
FT /evidence="ECO:0000255"
FT REPEAT 150..195
FT /note="WD 4"
FT /evidence="ECO:0000255"
FT REPEAT 202..245
FT /note="WD 5"
FT /evidence="ECO:0000255"
FT REPEAT 252..291
FT /note="WD 6"
FT /evidence="ECO:0000255"
FT REGION 294..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 187..211
FT /note="FDDATNEWILEKTLAGHTDFVREAA -> LSQFGAKIFRDNGSKCHVTIRNA
FT RE (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_040693"
FT VAR_SEQ 212..313
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_040694"
SQ SEQUENCE 313 AA; 34692 MW; F161D1635B3DDA80 CRC64;
MTTVRQRIDT QHRDAIHDAQ LNIYGSRLAT CGSDRLVKIF EVRPNGQSYP MAELVGHSGP
VWKVSWAHPK YGGLLASASY DKKVIIWNEQ QGRWQKAYEW AAHEASTTCV AFAPHQYGLM
LASASADGDI GILRYDNSSN EWISSKIQKC HEQGVNSVCW APGSADPAAK KRLVSAGNDK
NVKIWAFDDA TNEWILEKTL AGHTDFVREA AWCPVTNNGQ HTIVSCGMEG NLVLFRTSNI
ETEEWKAKLL ETAPCALYHS SFSPCGSFLS VAGDDNVITI WRENLQGQWI KVPRDNKERE
GMSQAVGAPG AQR
