SEC31_ASPNC
ID SEC31_ASPNC Reviewed; 1259 AA.
AC A2QBZ0;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=Protein transport protein sec31;
GN Name=sec31; ORFNames=An02g01690;
OS Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AM269996; CAK96387.1; -; Genomic_DNA.
DR RefSeq; XP_001399310.1; XM_001399273.2.
DR AlphaFoldDB; A2QBZ0; -.
DR SMR; A2QBZ0; -.
DR PaxDb; A2QBZ0; -.
DR EnsemblFungi; CAK96387; CAK96387; An02g01690.
DR GeneID; 4978655; -.
DR KEGG; ang:ANI_1_226024; -.
DR VEuPathDB; FungiDB:An02g01690; -.
DR HOGENOM; CLU_003033_2_0_1; -.
DR Proteomes; UP000006706; Chromosome 4R.
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; 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..1259
FT /note="Protein transport protein sec31"
FT /id="PRO_5000219541"
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 822..845
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 868..1154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 923..939
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 972..1026
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1045..1064
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1077..1126
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1259 AA; 135577 MW; CAC4C58F9C9D00F3 CRC64;
MVRLREIPRT ATFAWSPGAA SPLIATGTRA GAVDVDFSNQ TCLELWDLAL SRHETGGELQ
PVAKIDTDSG FNDLAWTESE DNSRGVIAGA LENGSLDLWD ADKLLNGSDD AVISRTSKHS
GAVKALQFNP KHSNLLATGG AKGELYISDL DNIANPYRLG GTAARADDIE CLDWNKKVAH
ILVTGSSAGF VTVWDVKTKK ESLTLNNMGR KAVSAVAWDP EKPTKLVTAT PLESDPLICV
WDLRNSHAPE RTLRGHESGV LSLSWCAQDP DLLLSSGKDN RTMCWNPQTG HAYGEFPVVT
NWTFQTRWNP HNPNFFATAS FDGKISIQTI QNTSTETAQA IADQNQALDG EDFFAKAQTQ
PQVSSFSLPK PPKWLERPCS ATFGFGGRVV SVNLVEKGQR ASKIKITPFE VDEAVGKSTE
TFETALKEGD LRSICESRAA NAGSDEEKAD WKVIEALISK DPRKGLVEYL GFADQADEAA
DSLSKLGLDK EEEVNGEVAK ESRGSGAKKH RRLQSMFDAN PEADSFLSDL AASKGAKTNN
PFHIFNGSEN EADTGITRAL LLGDFEKALD VALKEDRLSD AFMIAICGGP KCIEKAQEHY
FQKQTNSPNY VRLLASIVGK NLWDVVYNAD LSNWKEVMAA LCTFADEKDF ADLCEALGDR
LEEELRNNED KGMRKDASFC FLAGSKLEKV VAIWIEELRE HEQKAIETAA DDSAFSIHVR
ALQGLIEKVT IFRQVTKFED TERTKESDWK LSTLYDKYIE YADVVATHGR LQVAQKYLDL
VPEKHPEAEI ARNRIKLATR QATPQRTQPA AATVTRAALN KPLPQPNAFQ PQRAYSPATP
AAVPSPYAPA AAAANAYAPP TTATNPYAPS TASAPAQPVN PYAPPAGGSS YTPAGYQPPK
APAYGAQPLG GGVPPPPRAS NQSPAPTVTT YTTATNLPAW NDLPEGFAKA PTPRRSTPAA
ATVASPFPNQ SPTLTQGPPP PAGQRAPSVP PPPKGTAPPP RMTSPPAAQP ASTTMPPPPA
NPYASLPQSP PMASTMGVPA SIPRGPSPYN APPTMPPPPN RYAPSPAAQA ASPQLQTRAP
VPPPPQAAAS PYAPQPPAAG HYVPSTPPPH VQPPPQQAPP PQAAPGSRPS TASSQKKPAP
APPKYPPGDR SHIPADAMPV YEILSADMQR VKSRAPSSFK AQVDDAERRL NILFDHLNNE
DLLKPNTIAD MAELARAIQA RDYETARTIH VDIMTNRLDE CGNWMVGVKR LISMSRATP
