ID   SEC31_ASPTN             Reviewed;        1247 AA.
AC   Q0CYG9;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=Protein transport protein sec31;
GN   Name=sec31; ORFNames=ATEG_01265;
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CH476595; EAU38022.1; -; Genomic_DNA.
DR   RefSeq; XP_001208630.1; XM_001208630.1.
DR   AlphaFoldDB; Q0CYG9; -.
DR   SMR; Q0CYG9; -.
DR   STRING; 341663.Q0CYG9; -.
DR   EnsemblFungi; EAU38022; EAU38022; ATEG_01265.
DR   GeneID; 4315901; -.
DR   VEuPathDB; FungiDB:ATEG_01265; -.
DR   eggNOG; KOG0307; Eukaryota.
DR   HOGENOM; CLU_003033_2_0_1; -.
DR   OMA; NRYAPAP; -.
DR   OrthoDB; 100998at2759; -.
DR   Proteomes; UP000007963; 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   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..1247
FT                   /note="Protein transport protein sec31"
FT                   /id="PRO_0000295431"
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          163..203
FT                   /note="WD 4"
FT   REPEAT          207..250
FT                   /note="WD 5"
FT   REPEAT          254..294
FT                   /note="WD 6"
FT   REPEAT          297..337
FT                   /note="WD 7"
FT   REPEAT          381..406
FT                   /note="WD 8; interaction with sec13"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00221"
FT   REGION          487..509
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          798..854
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          908..1141
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        487..503
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        801..815
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        939..1048
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1062..1114
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1247 AA;  134483 MW;  0C41684187F684A8 CRC64;
     MVRLREIPRT ATFAWSPGAD SPLIATGTRA GAVDVDFSNE TCLELWDLGL SREDVSGELQ
     PAAKIDTDSG FNDIAWTESD DNKRGVIAGA LENGSLDLWD ADKLLNGSSD SVISRSTKHS
     GAIKALQFNP KHSNLLATGG AKGELYISDL NNVANPYRLG TAARADDIEC LDWNKKVAHI
     LVTGSNAGFV TVWDVKSKKE SLTLNNVGRK AVSAVAWDPE KPTRLVTATP LESDPMICVW
     DLRNSHAPER TLRGHESGVL SLSWCTQDPD LLLSSGKDNR TLCWNPQTGY AYGEFPVVTN
     WTFQTRWNPH NPNFFATASF DGRISIQTIQ NTSTDTAKAI ADQNQALDGE DFFAKAQSQP
     QVSSFSLPKA PKWLERPCGA TFGFGGRVVS VGLTEKGSRT STIKITPFEV DEAVGKSTET
     FENALKEGDL RSICETRATN AATEEEKADW KVIEALISEN PRKSLVDYLG FQDKADEAAD
     SLAKLGLGKD EDVNGEPAKE SRGPGAKKHK RLQSMFDANP EGDSFLSDLA ASKGAKTNNP
     FQIFNGSESE AEKGITRALL VGDFEKALDV ALKEDRMSDA FMIAICGGQK CIEKAQEHYF
     SKQTDSPNYV RLLASIVGKN LWDVVHNADL SNWKEVMAAL CTFAEEKEFA DLCEALGDRL
     EEQVRSSDEK SARKDASFCF LAGSKLEKVV AIWIEELAEN EQKAIETGAN DTTFSIHVHA
     LQSLIEKVTI FRQVSKFQDT EHTKDSDWKL GMLYDKYIEY ADVVATHGRL QVAQKYLDLV
     PEKHPEAEIA RNRIKLAMRQ AAPQRTQTTA PATRATRTPM GRPMPQPSAY QPQSTFAPAA
     PAAPNTYAPP TAAPNPYAPA APAAAAPAPP QPVNPLLPHR RMAVFLLLLR ANNQSPATVT
     TYTTATNLPA WNDLPEGFMK PPTSRRATPA TAAAPITSPF PNQSPPIGHG PPPPGAPPTQ
     RTPSVPPPPK GTAPPPRMSS PLAGAPPMAS MAPPPAAAPA PAPPANPYAT LPQSPPMASS
     MAPPASIPRG PSPYNAPPTA PPPSNRYAPS PAAQAASPQL QTRAPVPPPP QAAASPYAPQ
     PMAQPPAANP YAPSTPPMVA PPMQQGPPPP QAGGSRPSTA NSQRKAAPPP PKYPPGDRSH
     IPAEAMPVFE ILSADMQRVK SRAPSSFKAQ VDDAERRLNI LFDHLNNEDL LKPNTIADMA
     ELARAIQARD YDTARAIHVD IMTNRMDECG QWMVGVKRLI SMSRATP