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SEC31_ASPCL
ID   SEC31_ASPCL             Reviewed;        1276 AA.
AC   A1C6X5;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=Protein transport protein sec31;
GN   Name=sec31; ORFNames=ACLA_071790;
OS   Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS   NRRL 1 / QM 1276 / 107).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=344612;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027045; EAW14146.1; -; Genomic_DNA.
DR   RefSeq; XP_001275572.1; XM_001275571.1.
DR   AlphaFoldDB; A1C6X5; -.
DR   SMR; A1C6X5; -.
DR   STRING; 5057.CADACLAP00006389; -.
DR   PRIDE; A1C6X5; -.
DR   EnsemblFungi; EAW14146; EAW14146; ACLA_071790.
DR   GeneID; 4708309; -.
DR   KEGG; act:ACLA_071790; -.
DR   VEuPathDB; FungiDB:ACLA_071790; -.
DR   eggNOG; KOG0307; Eukaryota.
DR   HOGENOM; CLU_003033_2_0_1; -.
DR   OMA; NRYAPAP; -.
DR   OrthoDB; 100998at2759; -.
DR   Proteomes; UP000006701; Unassembled WGS sequence.
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; 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; PF07304; SRA1; 1.
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   Protein transport; Reference proteome; Repeat; Transport; WD repeat.
FT   CHAIN           1..1276
FT                   /note="Protein transport protein sec31"
FT                   /id="PRO_0000295428"
FT   REPEAT          5..47
FT                   /note="WD 1"
FT   REPEAT          66..109
FT                   /note="WD 2"
FT   REPEAT          118..158
FT                   /note="WD 3"
FT   REPEAT          164..204
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          382..407
FT                   /note="WD 8; interaction with sec13"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00221"
FT   REGION          820..885
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          906..1171
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        824..879
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        931..946
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        981..1018
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1057..1079
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1094..1114
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1121..1145
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1276 AA;  137178 MW;  A20D82BC4BAF3C9D CRC64;
     MVRLREIPRT ATFAWSPGAA SPLIATGTRA GAVDVDFSNE TCLELWDLGL SNDDASQELQ
     PIAKIGTDSG FNDLAWTDSQ DNSRGVIAGA LENGSLDLWD ADKLINGSSD AIISRMTKHS
     GAIKALQFNP KHSNLLATGG AKGELYISDL NNIANPYRLG STAARADDIE CLDWNKKVAH
     ILVTGSSAGF VTVWDVKTKK ESLTLNNMGR KAVSAVAWDP EKPTKLITST PLESDPLIYV
     WDLRNSHAPE RTLKGHESGV LSLSWCPQDP DLLLSSGKDN RTICWNPQSG QAYGEFPVVT
     NWTFQTRWNP HNPNFFATAS FDGRISIQTI QNTRTDTAQA IADQNQSLDG EDFFAKAQTQ
     PQVSNFSLPK APKWLERPSS ATFGFGGRVV SVGLIEKGKR ASRIKITPFE VDEAVAKSTE
     TFETALKEGD LRSICETRAS QAASEEEKAD WKVIEALISG NPRKGLIEYL GFQDQADEAA
     DKLAKLGLDK EDVNGDTLTE SRGSGAKKHK RLQSMFDANP EADSFLSDLA ASKGAKTNNP
     FHIFTGSESE AEQGITRALL LGNFEKALDV ALKEDRMSDA FVIAICGGQK CIEKAQEHYF
     SKQTGGPNYT RLLASIVGKN LWDVVYNADL SNWKEVMAAL CTFADDKEFA DLCEALGDRL
     GEQIRSTDDK ALRKDASFCF LAGSKLEKVV AMWIEELREN EQKGIETAAD DTSFSIHVRA
     LQGLIEKVTI FRQATNFQDT ERTKEADWKL AMLYDKYIEY ADVVATHGRL QVAQKYLDLV
     PEKHPEAEIA RNRIKLAMRQ AAPQRTQSTV PAARTTLNRP LPQINAYPPQ PTFSSPAPPA
     PQNPYAPPTA APSQPANPYA PPAAAPSQPS NPYAPPTAAA AIPQPQVNNP YAPIGGGGYT
     PAGYQPPQAP AYGVQSLGGG SVPPPPRASN QSPAVTTYTT ATNLPAWNDL PEGFTKPPTS
     RRGTPATAAA AISSPFPNQS PTFSQGPPPP GMPPTQRAPS VPPPPKGTVP PPRVTSPPTG
     FTPASNLSAP PPAANPYASL PQSPPIGSTM GIPAPASIPR GPSPYNAAPT MPPPSNRYAP
     SPAVQAASPQ LATRAAVPPP PPAAASPYAP QPAAQPPVAS SYAPSTPPPS QLPMQQGPPQ
     GPPSRPGTAS SQRKAAPAPP KYPPGDRSHI PADAMPIFEI LSADMQRVKT RAPSSFKAQV
     DDAERRLNIL FDHLNNEDLL RPNTIADMAE LARAIQARDY ETAKTIHIDI MTNRTDECGN
     WMVGVKRLIS MSRATP
 
 
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