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SEC31_MAGO7
ID   SEC31_MAGO7             Reviewed;        1269 AA.
AC   A4RD35; G4NC93;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Protein transport protein SEC31;
GN   Name=SEC31; ORFNames=MGG_01108;
OS   Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS   fungus) (Pyricularia oryzae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX   NCBI_TaxID=242507;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX   PubMed=15846337; DOI=10.1038/nature03449;
RA   Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA   Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA   Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA   Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA   Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA   Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT   "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL   Nature 434:980-986(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 (By similarity). {ECO:0000250}.
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. SEC13 and
CC       SEC31 make a 2:2 tetramer that forms the edge element of the COPII
CC       outer coat. The tetramer self-assembles in multiple copies to form the
CC       complete polyhedral cage. Interacts (via WD 8) with SEC13 (By
CC       similarity). {ECO:0000250}.
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}.
CC   -!- SIMILARITY: Belongs to the WD repeat SEC31 family. {ECO:0000305}.
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DR   EMBL; CM001235; EHA48242.1; -; Genomic_DNA.
DR   RefSeq; XP_003717826.1; XM_003717778.1.
DR   AlphaFoldDB; A4RD35; -.
DR   SMR; A4RD35; -.
DR   STRING; 318829.MGG_01108T0; -.
DR   PRIDE; A4RD35; -.
DR   EnsemblFungi; MGG_01108T0; MGG_01108T0; MGG_01108.
DR   GeneID; 2674815; -.
DR   KEGG; mgr:MGG_01108; -.
DR   VEuPathDB; FungiDB:MGG_01108; -.
DR   eggNOG; KOG0307; Eukaryota.
DR   HOGENOM; CLU_003033_2_0_1; -.
DR   InParanoid; A4RD35; -.
DR   OMA; NRYAPAP; -.
DR   OrthoDB; 100998at2759; -.
DR   Proteomes; UP000009058; Chromosome 5.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0012507; C:ER to Golgi transport vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IEA:InterPro.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   Gene3D; 2.130.10.10; -; 1.
DR   InterPro; IPR024298; ACE1_Sec16_Sec31.
DR   InterPro; IPR040251; SEC31-like.
DR   InterPro; IPR009917; SRA1/Sec31.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   PANTHER; PTHR13923; PTHR13923; 2.
DR   Pfam; PF12931; Sec16_C; 1.
DR   Pfam; PF07304; SRA1; 1.
DR   Pfam; PF00400; WD40; 1.
DR   SMART; SM00320; WD40; 5.
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   Protein transport; Reference proteome; Repeat; Transport; WD repeat.
FT   CHAIN           1..1269
FT                   /note="Protein transport protein SEC31"
FT                   /id="PRO_0000295440"
FT   REPEAT          5..47
FT                   /note="WD 1"
FT   REPEAT          66..110
FT                   /note="WD 2"
FT   REPEAT          119..159
FT                   /note="WD 3"
FT   REPEAT          165..205
FT                   /note="WD 4"
FT   REPEAT          208..251
FT                   /note="WD 5"
FT   REPEAT          255..295
FT                   /note="WD 6"
FT   REPEAT          298..338
FT                   /note="WD 7"
FT   REPEAT          380..408
FT                   /note="WD 8; interaction with SEC13"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00221"
FT   REGION          474..503
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          792..1162
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        829..861
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        945..959
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        970..992
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1012..1027
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1068..1090
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1102..1150
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1269 AA;  135249 MW;  B46F371604A1D051 CRC64;
     MVRLREIPRT AAFAWSPDTS APIVVTGTRA GAVDADFSDE TKLELWDLKL DDEGQGLELQ
     PIASISADSR FFDIAWGPPN EDHPRGIIAG ALENGSLDLW DAEKLLSGAS DAHMSRTTKH
     TGAIKSLQFN PLKPQILATA GTKGELFIYD VNDISNPFRL GTAAARSDDL ECVAWNRKVP
     HILATGGSGG FVTVWDLKTR KASLTLNNSR KAVSAIAWDP NNSTKLLTAT PDDTMPVIFL
     WDLRNSNAPE RTLQGHEQGV LSVSWCQQDS DLLISCGKDN RTIVWNPQTG ERYGEFPEVT
     NWTFSARFNP TNPNLSATAS FDGKITIQTL QNTNPSATQA AAQNSLDGED FFTKAQTQPQ
     GASFTLTKAP LWYQRPVGAS FGFGGKVVVF KQTQTAPGQP RASEISISHF SVDSEIGSAT
     EKFEESIKAG DLKSICQSHL ENAKSEDETT AWKVMETLVA ENPRKQVVEY LGLSAEEAPA
     SPESTTEEGA EKEDAEVEPV KESFKKHKKN RLSTFFTEGG DGDDFLAGLA ATKGAKTDSP
     FHLLREGNTG LEDSVTRAIM LGNFAKAVEI CIKADRIADA FLIANCGGKE LVDQVQTAYI
     SAKKGSPSYL RLLGSVINDN LWDVVYNADI ADWKETMATL CTFAKPEEFP DLCEALGDRL
     FETGSRQDAS FCFLVGSKLE KVVGIWIDAL EEAEKNEIQE AEADNTFSVH ARSLQQLIEK
     VTVFRHVTKF QDAEASKTSD WKLASLYDKY IEYADIVAAH GQLSIAQKYL ELVPASYSGA
     EVARKRLQLA TTKSGAQPAA ARAQQAPAAA RLPTRQQPVG YQPPQQQPMS TPYGMPPAPQ
     AQTPAANPYG PPAPSPYAPA GATPYQPQQT SYAPPQPAGG AGAYGPTPGV GYGQPQQNFG
     APPPPRNATP SALPPSRTVD AGSWNDVPMV TKAPPPRRST PSVAPVPSPF ANQQAGMAPP
     PQSPYLGQRG TATPPPPPPK AGQGPPRMAS PLTSPPQAGY GGAAPPRPAS AASSTYAPPP
     PAPGQSFGMN APPARTASPY SVAPAAPPPS NRYAPSPAMQ QQQGGPGPAG SMPPPPAMSR
     PPPTNPYAAA PQQSPAPGGQ YAPSPYGAPP QAGQPPMAPP PSSQVGPPPG GRGPLSTPTP
     PPPRAAAAPP AKTKYPPGDR SHIPASAQQL VEILSRDMER VAAKAPASFA PHVKDTQKRL
     NYLFDHLNNE ELVKPDTIGQ LNTLAQAIEA KDYAGAQQLQ IKIQTEKTEE CGQWIVGVKR
     LISMSKATP
 
 
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