SEC13_NEUCR
ID SEC13_NEUCR Reviewed; 304 AA.
AC Q7RZF5;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Protein transport protein sec13;
DE AltName: Full=Nucleoporin 20;
GN Name=nup-20; Synonyms=sec13; ORFNames=NCU04063;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
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. Nup-20/sec13 is required for
CC efficient mRNA export from the nucleus to the cytoplasm and for correct
CC nuclear pore biogenesis and distribution (By similarity).
CC {ECO:0000250|UniProtKB:Q04491}.
CC -!- SUBUNIT: The COPII coat is composed of at least 5 proteins: the
CC sec23/24 complex, the sec13/31 complex, and the protein vtr-7/sar1.
CC Component of the nuclear pore complex (NPC). NPC constitutes the
CC exclusive means of nucleocytoplasmic transport. NPCs allow the passive
CC diffusion of ions and small molecules and the active, nuclear transport
CC receptor-mediated bidirectional transport of macromolecules such as
CC proteins, RNAs, ribonucleoparticles (RNPs), and ribosomal subunits
CC across the nuclear envelope. Due to its 8-fold rotational symmetry, all
CC subunits are present with 8 copies or multiples thereof.
CC {ECO:0000250|UniProtKB:Q04491}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPII-coated vesicle
CC membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250};
CC Cytoplasmic side {ECO:0000250}. Endoplasmic reticulum membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC side {ECO:0000250}. Nucleus, nuclear pore complex {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the WD repeat SEC13 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM002241; EAA28442.2; -; Genomic_DNA.
DR RefSeq; XP_957678.2; XM_952585.3.
DR AlphaFoldDB; Q7RZF5; -.
DR SMR; Q7RZF5; -.
DR STRING; 5141.EFNCRP00000003685; -.
DR PRIDE; Q7RZF5; -.
DR EnsemblFungi; EAA28442; EAA28442; NCU04063.
DR GeneID; 3873801; -.
DR KEGG; ncr:NCU04063; -.
DR VEuPathDB; FungiDB:NCU04063; -.
DR HOGENOM; CLU_032441_0_1_1; -.
DR InParanoid; Q7RZF5; -.
DR OMA; TVDTGHE; -.
DR Proteomes; UP000001805; Chromosome 5, Linkage Group VI.
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:0061700; C:GATOR2 complex; IEA:EnsemblFungi.
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:0051664; P:nuclear pore localization; IEA:EnsemblFungi.
DR GO; GO:1902953; P:positive regulation of ER to Golgi vesicle-mediated transport; IEA:EnsemblFungi.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IEA:EnsemblFungi.
DR GO; GO:0070863; P:positive regulation of protein exit from endoplasmic reticulum; IEA:EnsemblFungi.
DR GO; GO:0032008; P:positive regulation of TOR signaling; IBA:GO_Central.
DR GO; GO:1904263; P:positive regulation of TORC1 signaling; IEA:EnsemblFungi.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:EnsemblFungi.
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 GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IEA:EnsemblFungi.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR024977; Apc4_WD40_dom.
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; PF12894; ANAPC4_WD40; 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 3: Inferred from homology;
KW Cytoplasmic vesicle; Endoplasmic reticulum; ER-Golgi transport; Membrane;
KW mRNA transport; Nuclear pore complex; Nucleus; Protein transport;
KW Reference proteome; Repeat; Translocation; Transport; WD repeat.
FT CHAIN 1..304
FT /note="Protein transport protein sec13"
FT /id="PRO_0000295419"
FT REPEAT 12..51
FT /note="WD 1"
FT REPEAT 56..97
FT /note="WD 2"
FT REPEAT 102..143
FT /note="WD 3"
FT REPEAT 147..203
FT /note="WD 4"
FT REPEAT 211..253
FT /note="WD 5"
FT REPEAT 259..298
FT /note="WD 6"
SQ SEQUENCE 304 AA; 33385 MW; BEA93F7353C0C2FC CRC64;
MTAGAQVIAN SGHDDMIHDA VLDYYGRRLA TCSSDRTIKI FEIEGESQRL VETLKGHDGA
VWSVAWAHPK YGNILASAGY DGKVLIWREQ AGSWQRIFDF ALHKASVNIV SWSPHEAGCL
LACASSDGNV SVLEFKDNSW EHNIFHAHGL GVNSVSWAPA TTPGSIVSSN PGPGSTGNRR
FVTGGSDNLL KIWTFDPATN GYKLEREPLA GHTDWVRDVA WSPTVLQKSY IASASQDKTV
RIWTSDAANP GEWKCKVLNF DAAVWRVSWS LSGNVLAASS DNNKVTLWKE NLKGEWENVK
TIEE