SEC31_ASPFU
ID SEC31_ASPFU Reviewed; 1263 AA.
AC Q4X0M4;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 120.
DE RecName: Full=Protein transport protein sec31;
GN Name=sec31; ORFNames=AFUA_2G12980;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(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; AAHF01000001; EAL93591.1; -; Genomic_DNA.
DR RefSeq; XP_755629.1; XM_750536.1.
DR AlphaFoldDB; Q4X0M4; -.
DR SMR; Q4X0M4; -.
DR STRING; 746128.CADAFUBP00002799; -.
DR EnsemblFungi; EAL93591; EAL93591; AFUA_2G12980.
DR GeneID; 3512865; -.
DR KEGG; afm:AFUA_2G12980; -.
DR VEuPathDB; FungiDB:Afu2g12980; -.
DR eggNOG; KOG0307; Eukaryota.
DR HOGENOM; CLU_003033_2_0_1; -.
DR InParanoid; Q4X0M4; -.
DR OMA; NRYAPAP; -.
DR OrthoDB; 100998at2759; -.
DR PHI-base; PHI:2527; -.
DR Proteomes; UP000002530; Chromosome 2.
DR GO; GO:0030127; C:COPII vesicle coat; IBA:GO_Central.
DR GO; GO:0070971; C:endoplasmic reticulum exit site; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005198; F:structural molecule activity; IBA:GO_Central.
DR GO; GO:0090110; P:COPII-coated vesicle cargo loading; IBA:GO_Central.
DR GO; GO:0007029; P:endoplasmic reticulum organization; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
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 Pfam; PF00400; WD40; 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..1263
FT /note="Protein transport protein sec31"
FT /id="PRO_0000295429"
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 487..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 801..1158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 487..504
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 803..822
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 853..886
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 895..921
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 922..938
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 950..972
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 973..1017
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1018..1032
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1033..1065
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1079..1122
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1123..1141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1263 AA; 136772 MW; AA3975CB8E4D61AC CRC64;
MVRLREIPRT ATFAWSPGAA SPLIATGTRA GAVDVDFSNE TCLELWDLGL SSQDASQELQ
PIAKIGTDSG FNDLAWTDYE DNSRGVIAGA LENGSLDLWD ADKLINGSSD AVISRMTKHS
GAIKALQFNP KHSNLLATGG AKGELYISDL NNITNPYRLG SAAARADDIE CLDWNKKVAH
ILVTGSSAGF VTVWDVKTRK ESLTLNNMGR KAVSAVAWDP EKPTKLITST PLESDPLIYV
WDLRNSHAPE RTLKGHESGV LSLSWCPQDP DLLLSSGKDN RTLCWNPQTG QAYGEFPVVT
NWTFQTRWNP HNPNFFATAS FDGRISIQTV QNTRTDTARA IADQNQALDG ADFFAKAQTQ
PQVSNFSLPK APKWLERPCG ASFGFGGRVI SVSLIEKGKR ASKIKITPFE VDETVAKSTE
TFENALKEGD LRSICETRAS QAASDEEKAD WKVIEALISE NPRKSLIEYL GFQDQDDETA
DKLAQLGLNK EEDEVNGKSA KESRGSGAKK HKRLQSMFDA NPEADNFLSD LAASKGAKTN
NPFQIFNGSE TEADKGITRA LLLGNFEKAL DVALKEDRMS DAFMIAICGG QKCIEKAQEH
YFSKQTDGPN YIRLLASIVG KNLWDVVHNA DLSNWREVMA ALCTFADDNE FADLCEALGD
RLEEQIRNTK DKSLRKDASF CFLAGSKLEK VVAIWIEELR ENEQRSIETA TDDTSFSIHV
RALQSLIEKV TIFRQVTNFQ DTERTKDADW KLSMLYDKYI EYADVVATHG RLQVAQKYLD
LVPEKHPEAE IARNRIKLAM RHATPQRSQQ TVPTTRTPVN KPLPQASMYP AQPAFSAPAA
APAAATTAPR NPYAPPTAAT TQPVNPYTPP SAAATQPQTS NSYAPIGGGG YTPAGYQPPQ
PPTYGTQPLG GSVPPPPRAS NQSPATVTTY TTATNLPAWN DLPEGFTKPP TSRRGTSATA
AATISSPFPN QSPTLSQGPP PPGAPPTQRA PSVPPPPKGT APPPRVTSPP TNPPGPSSAA
NPYASLPQSP PMGSTMGVPP PPSIPRGPSP YNAPPSMPPP SNRYAPSPAT QAASPQLSTR
APVPPPPHAA ASPYTSQPGS HPPPANPYAP STPPPSQLPM QQAPPPQATS SRPSTASSQR
KAAPAPPKYP PGDRSHIPAD AMPIYEILSA DMQRVKSRAP SSFKAQVEDA ERRLNILFDH
LNNEDLLKPN TVADMAELAR AIQARDYETA KTIHIDIMTN RTEECGNWMV GVKRLISMSR
ATP
