SEC31_NEOFI
ID SEC31_NEOFI Reviewed; 1263 AA.
AC A1DHK2;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=Protein transport protein sec31;
GN Name=sec31; ORFNames=NFIA_088150;
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC / WB 181;
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; DS027696; EAW18859.1; -; Genomic_DNA.
DR RefSeq; XP_001260756.1; XM_001260755.1.
DR AlphaFoldDB; A1DHK2; -.
DR SMR; A1DHK2; -.
DR STRING; 36630.CADNFIAP00008199; -.
DR EnsemblFungi; EAW18859; EAW18859; NFIA_088150.
DR GeneID; 4587314; -.
DR KEGG; nfi:NFIA_088150; -.
DR VEuPathDB; FungiDB:NFIA_088150; -.
DR eggNOG; KOG0307; Eukaryota.
DR HOGENOM; CLU_003033_2_0_1; -.
DR OMA; NRYAPAP; -.
DR OrthoDB; 100998at2759; -.
DR Proteomes; UP000006702; 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; 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; 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_0000295441"
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 488..511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 801..828
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 840..1159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..505
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 869..886
FT /note="Polar 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 973..1025
FT /note="Pro 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..1132
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1263 AA; 136326 MW; 5D1515D8ABD2EE2A CRC64;
MVRLREIPRT ATFAWSPGAA SPLIATGTRA GAVDVDFSNE TCLELWDLGL SSQDASQELQ
PIAKIGTDSG FNDLAWTDSE DNSRGVIAGA LENGSLDLWD ADKLINGSSD AVISRMTKHS
GAIKALQFNP KHSNLLATGG AKGELYISDL NNIANPYRLG SAAARADDIE CLDWNKKVAH
ILVTGSSAGF VTVWDVKTKK ESLTLNNMGR KAVSAVAWDP EKPTKLITST PLESDPLIYV
WDLRNSHAPE RTLKGHESGV LSLSWCPQDP DLLLSSGKDN RTLCWNPQTG QAYGEFPVVT
NWTFQTRWNP HNPNFFATAS FDGRISIQTV QNTRTDTARA IADQNQALDG ADFFAKAQTQ
PQVSNFSLPK APKWLERPCG ASFGFGGRVI SVGLIEKGKR ASKIKITPFE VDEAVAKSTE
TFENALKEGD LRSICENRAS QAASDEEKAD WKVIEALISE NPRKGLIEYL GFQDQADETA
DKLAQLGLDK EDDEVNGESA KESRGSGAKK HKRLQSMFDA NPEADNFLSD LAASKGAKTN
NPFQIFNGSE TEADKGITRA LLLGNFEKAL DVALKEDRMS DAFMIAICGG QKCIEKAQEH
YFSKQTDGPN YIRLLASIVG KNLWDVVHNA DLSNWKEVMA ALCTFADDNE FADLCEALGD
RLEEQIRSTE DKSLRKDASF CFLAGSKLEK VIAIWIEELR EYEQKSIETA ADDTSFSIHV
RALQSLIEKV TIFRQVTKFQ DTERTKDADW KLSMLYDKYI EYADVVATHG RLQVAQKYLD
LVPEKHPEAE IARNRIKLAM RHATPQRSQQ TVPTTRTPVN KPLPQASMYP AQPAFSATAA
APAAATTAPR NPYAPPTAAT AQPVNPYAPP SAAATQPQTS NSYAPIGGGG YTPAGYQPLQ
PPTYGAQPLG GSVPPPPRAS NQSPATVTTY TTATNLPAWN DLPEGFTKPP TSRRGTPAAA
AATISSPFPN QSPTLSQGPP PPGAPPTQRA PSVPPPPKGT APPPRVTSPP TNLPGPSPAA
NPYASLPQSP PMGSAMGVPP PASIPRGPSP YNAPPSMPPP SNRYAPSPAA QAASPQLSTR
APVPPPPHAA ASPYASQPAS HPPPANPYAP STPPPSQLPM QQAPPPQAPP SRPSTASSQR
KAAPAPPKYP PGDRSHIPSD AMPIYEILSA DMQRVKSRAP SSFKAQVEDA ERRLNILFDH
LNNEDLLKPN TVADMAELAR AIQARDYETA KTIHIDIMTN RTEECGNWMV GVKRLISMSR
ATP