SEC13_CAEBR
ID SEC13_CAEBR Reviewed; 306 AA.
AC A8XJ40;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=Protein SEC13 homolog {ECO:0000250|UniProtKB:Q9N4A7};
DE Short=CeSEH13R {ECO:0000250|UniProtKB:Q9N4A7};
DE AltName: Full=GATOR complex protein SEC13 {ECO:0000305};
DE AltName: Full=Nuclear pore complex protein 20 {ECO:0000250|UniProtKB:Q9N4A7};
GN Name=npp-20 {ECO:0000312|WormBase:CBG13889}; ORFNames=CBG13889;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1] {ECO:0000312|EMBL:CAP32667.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
CC -!- FUNCTION: Functions as a component of the nuclear pore complex (NPC)
CC and the COPII coat. {ECO:0000250|UniProtKB:P55735}.
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: Probably part of the GATOR complex.
CC {ECO:0000250|UniProtKB:P55735}.
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:0000250|UniProtKB:P55735}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P55735}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P55735}. Nucleus, nuclear pore complex
CC {ECO:0000250|UniProtKB:P55735}. Lysosome membrane
CC {ECO:0000250|UniProtKB:P55735}.
CC -!- SIMILARITY: Belongs to the WD repeat SEC13 family. {ECO:0000255}.
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DR EMBL; HE601467; CAP32667.2; -; Genomic_DNA.
DR AlphaFoldDB; A8XJ40; -.
DR SMR; A8XJ40; -.
DR STRING; 6238.CBG13889; -.
DR EnsemblMetazoa; CBG13889.1; CBG13889.1; WBGene00034572.
DR WormBase; CBG13889; CBP30374; WBGene00034572; Cbr-npp-20.
DR eggNOG; KOG1332; Eukaryota.
DR HOGENOM; CLU_032441_0_1_1; -.
DR InParanoid; A8XJ40; -.
DR OMA; TVDTGHE; -.
DR OrthoDB; 944756at2759; -.
DR Proteomes; UP000008549; Chromosome IV.
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; ISS: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:0090114; P:COPII-coated vesicle budding; IBA:GO_Central.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0010973; P:positive regulation of division septum assembly; ISS: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; IBA:GO_Central.
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; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 3: Inferred from homology;
KW Cytoplasmic vesicle; Endoplasmic reticulum; ER-Golgi transport; Lysosome;
KW Membrane; mRNA transport; Nuclear pore complex; Nucleus; Protein transport;
KW Reference proteome; Repeat; Translocation; Transport; WD repeat.
FT CHAIN 1..306
FT /note="Protein SEC13 homolog"
FT /id="PRO_0000405803"
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"
SQ SEQUENCE 306 AA; 34521 MW; 250CEF488480F10C CRC64;
MTTIRQRIDT QHRDAIHDAQ LNIYGNRLAT CGSDRLVKIF EVRPNGQSYP LIELSGHNGP
VWKVSWAHPK YGGLLASASY DKKVIIWQEV NGRWQKTYEW ETHEASVTSV AFAPHQFGLM
LASSSADGTI GILRFDAQTQ QWQSSRIQNC HDQGVNSVSW APGTADPAGK KRFVSAGNDK
LVKIWLLNEE LNEWTCEKAI HCHKDFVREA AWCPVTNKGQ HSIVSCGLDG NLVLYRIADI
ETAEWKSKLL EQAPCALYHA SFSPCGSFLS VSGDDNMITL WRENLQGQWI KIPRENKERE
GMGQQR
