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Entry: N1QMY9_SPHMS
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Original site: N1QMY9_SPHMS 
ID   N1QMY9_SPHMS            Unreviewed;       305 AA.
AC   N1QMY9;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=Protein transport protein SEC13 {ECO:0000256|ARBA:ARBA00021281};
DE   AltName: Full=Protein transport protein sec13 {ECO:0000256|ARBA:ARBA00013473};
GN   ORFNames=SEPMUDRAFT_146066 {ECO:0000313|EMBL:EMF16939.1};
OS   Sphaerulina musiva (strain SO2202) (Poplar stem canker fungus) (Septoria
OS   musiva).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Sphaerulina.
OX   NCBI_TaxID=692275 {ECO:0000313|EMBL:EMF16939.1, ECO:0000313|Proteomes:UP000016931};
RN   [1] {ECO:0000313|EMBL:EMF16939.1, ECO:0000313|Proteomes:UP000016931}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SO2202 {ECO:0000313|EMBL:EMF16939.1,
RC   ECO:0000313|Proteomes:UP000016931};
RX   PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA   Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA   Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA   LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA   Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA   Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA   Grigoriev I.V.;
RT   "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT   genomes of eighteen Dothideomycetes fungi.";
RL   PLoS Pathog. 8:E1003037-E1003037(2012).
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:0000256|ARBA:ARBA00025261}.
CC   -!- SUBUNIT: The COPII coat is composed of at least 5 proteins: the
CC       SEC23/24 complex, the SEC13/31 complex, and the protein SAR1. Component
CC       of the nuclear pore complex (NPC). NPC constitutes the exclusive means
CC       of nucleocytoplasmic transport. NPCs allow the passive diffusion of
CC       ions and small molecules and the active, nuclear transport receptor-
CC       mediated bidirectional transport of macromolecules such as proteins,
CC       RNAs, ribonucleoparticles (RNPs), and ribosomal subunits across the
CC       nuclear envelope. Due to its 8-fold rotational symmetry, all subunits
CC       are present with 8 copies or multiples thereof.
CC       {ECO:0000256|ARBA:ARBA00011369}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex
CC       {ECO:0000256|ARBA:ARBA00004567}.
CC   -!- SIMILARITY: Belongs to the WD repeat SEC13 family.
CC       {ECO:0000256|ARBA:ARBA00010102}.
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DR   EMBL; KB456260; EMF16939.1; -; Genomic_DNA.
DR   RefSeq; XP_016765060.1; XM_016903434.1.
DR   AlphaFoldDB; N1QMY9; -.
DR   STRING; 692275.N1QMY9; -.
DR   GeneID; 27900571; -.
DR   eggNOG; KOG1332; Eukaryota.
DR   HOGENOM; CLU_032441_0_1_1; -.
DR   OMA; TVDTGHE; -.
DR   OrthoDB; 177928at2759; -.
DR   Proteomes; UP000016931; Unassembled WGS sequence.
DR   GO; GO:0005643; C:nuclear pore; IEA:UniProtKB-SubCell.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR   InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR   InterPro; IPR037363; Sec13/Seh1_fam.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   InterPro; IPR001680; WD40_rpt.
DR   PANTHER; PTHR11024; NUCLEAR PORE COMPLEX PROTEIN SEC13 / SEH1 FAMILY MEMBER; 1.
DR   PANTHER; PTHR11024:SF2; PROTEIN SEC13 HOMOLOG; 1.
DR   Pfam; PF00400; WD40; 4.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00320; WD40; 6.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 3.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE   3: Inferred from homology;
KW   mRNA transport {ECO:0000256|ARBA:ARBA00022816};
KW   Nuclear pore complex {ECO:0000256|ARBA:ARBA00023132};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023132};
KW   Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016931};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Translocation {ECO:0000256|ARBA:ARBA00023010};
KW   Transport {ECO:0000256|ARBA:ARBA00022816};
KW   WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW   ProRule:PRU00221}.
FT   REPEAT          51..84
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REPEAT          179..201
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REPEAT          206..250
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
SQ   SEQUENCE   305 AA;  33635 MW;  B1DF5F9435C19D6D CRC64;
     MTQVISNSGH DDMIHDAVLD YYGRRLATCS SDKTIKIFEI DGDQHRLTET LKGHEGAVWA
     VAWAHPKFGT ILASCSYDGR ILIWREQNSQ WQRIYDFTHH TASVNLVAWS PPETGCHLAA
     ASSDGHVSVL TFENNAFTHA MFEAHGLGVN SISWSPAILP AQLTSAQPPG QNPAPVKRFV
     SGGSDNLVKI WSFNTNSQAY ENIAELQGHQ DWVRDVAWSP TPLSKSYIAS ASQDHTVRIW
     TLPAGADIGD ANAWKSEVLN LDVVVWRVSW SMAGNVLAVS CGNNQVSLWK EKLKGGWEVV
     KTIED
//
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