SEC13_DICDI
ID SEC13_DICDI Reviewed; 301 AA.
AC Q54DS8;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 116.
DE RecName: Full=Protein SEC13 homolog {ECO:0000305};
DE AltName: Full=GATOR complex protein SEC13 {ECO:0000305};
GN Name=sec13; ORFNames=DDB_G0292052;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Component of the coat protein complex II (COPII) which
CC promotes the formation of transport vesicles from the endoplasmic
CC reticulum (ER). The coat has two main functions, the physical
CC deformation of the endoplasmic reticulum membrane into vesicles and the
CC selection of cargo molecules. It also functions as a component of the
CC nuclear pore complex (NPC). NPC components, collectively referred to as
CC nucleoporins (NUPs), can play the role of both NPC structural
CC components and of docking or interaction partners for transiently
CC associated nuclear transport factors. SEC13 is required for efficient
CC mRNA export from the nucleus to the cytoplasm and for correct nuclear
CC pore biogenesis and distribution. {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 -!- SUBUNIT: Component of the COPII coat composed of at least 5 proteins:
CC the sec23/24 complex, the sec13/31 complex, and the protein sar1A or
CC sar1B. Component of the nuclear pore complex (NPC) which constitutes
CC the exclusive means of nucleocytoplasmic transport. Probably part of
CC the GATOR complex. {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 -!- MISCELLANEOUS: Present with 21400 molecules/cell in log phase SD
CC medium.
CC -!- SIMILARITY: Belongs to the WD repeat SEC13 family. {ECO:0000305}.
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DR EMBL; AAFI02000187; EAL61382.1; -; Genomic_DNA.
DR RefSeq; XP_629794.1; XM_629792.1.
DR AlphaFoldDB; Q54DS8; -.
DR SMR; Q54DS8; -.
DR STRING; 44689.DDB0235182; -.
DR PaxDb; Q54DS8; -.
DR EnsemblProtists; EAL61382; EAL61382; DDB_G0292052.
DR GeneID; 8628472; -.
DR KEGG; ddi:DDB_G0292052; -.
DR dictyBase; DDB_G0292052; sec13.
DR eggNOG; KOG1332; Eukaryota.
DR HOGENOM; CLU_032441_0_1_1; -.
DR InParanoid; Q54DS8; -.
DR OMA; TVDTGHE; -.
DR PhylomeDB; Q54DS8; -.
DR Reactome; R-DDI-204005; COPII-mediated vesicle transport.
DR Reactome; R-DDI-9639288; Amino acids regulate mTORC1.
DR PRO; PR:Q54DS8; -.
DR Proteomes; UP000002195; Chromosome 6.
DR GO; GO:0030127; C:COPII vesicle coat; ISS:dictyBase.
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:dictyBase.
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:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; ISS:dictyBase.
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: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; 4.
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 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..301
FT /note="Protein SEC13 homolog"
FT /id="PRO_0000328075"
FT REPEAT 9..48
FT /note="WD 1"
FT REPEAT 53..94
FT /note="WD 2"
FT REPEAT 100..141
FT /note="WD 3"
FT REPEAT 146..202
FT /note="WD 4"
FT REPEAT 207..250
FT /note="WD 5"
FT REPEAT 255..294
FT /note="WD 6"
SQ SEQUENCE 301 AA; 33602 MW; F680766A772598B3 CRC64;
MATQNVDSGH EDMVHDAQFD YYGKFLATCS SDKMIKIFDV GGENPQHLVD LRGHEGPVWQ
VAWAHPKFGK ILASASYDRK VIVWKEVGNN SWSIIHQYAG HELSVNSISW APHEFGLSLA
CASSDGSVTI HNYNNNVWEA PQKIQVSQIG VNSVSWSPAA IPTSLVNSAN TIIPAPIKRI
VTGSCDNLIK IFKNVEDKWI LDKQLEDHKD WVRDVAWAPN IGLPYSKIAS CSQDRSVIVW
TQDENGVWSG KPLPKFDDIV WRVSWSVIGN ILAVSCGDNQ VTLWKEGVDS EWKLISHVEN
N
