SEC31_ASPOR
ID SEC31_ASPOR Reviewed; 1273 AA.
AC Q2UF60;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 2.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=Protein transport protein sec31;
GN Name=sec31; ORFNames=AO090026000337;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE59805.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP007159; BAE59805.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001821807.2; XM_001821755.2.
DR AlphaFoldDB; Q2UF60; -.
DR SMR; Q2UF60; -.
DR STRING; 510516.Q2UF60; -.
DR PRIDE; Q2UF60; -.
DR VEuPathDB; FungiDB:AO090026000337; -.
DR Proteomes; UP000006564; Chromosome 3.
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..1273
FT /note="Protein transport protein sec31"
FT /id="PRO_0000295430"
FT REPEAT 5..47
FT /note="WD 1"
FT REPEAT 66..109
FT /note="WD 2"
FT REPEAT 119..159
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..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 796..829
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 881..1168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 798..829
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 881..901
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 940..956
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 991..1084
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1098..1136
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1137..1153
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1273 AA; 136703 MW; DF22F0F1E1F655F4 CRC64;
MVRLREIPRT ATFAWSPGAA SPLIATGTRA GAVDVDFSNE TCLELWDLGL DRQSTGEELQ
PIAKFDTDSG FNDLAWTPSE DNTRGIIAGA LESGSLDLWD ADKLINGSSD DAVISRTSKH
SGAIKALQFN PRHSNLLATG GAKGELYISD LNNVANPYRL GTAARADDIE CLDWNKKVAH
ILVTGSSAGF VTVWDVKTKK ESLTLNNMGR KAVSAVAWDP EKPTKLVTAT PLESDPMIYV
WDLRNSHAPE RVLKGHESGV LSLSWCSHDP DLLLSSGKDN RTLCWNPQTG HAYGEFPVVT
NWTFQTRWNP HNPNFFATAS FDGKIAVQTV QNTSTDTAQA IADQNQALDG EDFFAKAQTQ
PQVSSFSLPK APKWLERPCG ATFGFGGRVV SVNLVEKGQR ASKIKITPFE VDEAVGQSTE
TFENALKEGD LRSICETRAA NAATEEEKAD WKVIQALISE NPRKGLAEYL GFQDQSADEA
ADKLANLGLG KEETNGESPK ESRGPGAKKH KRLQSMFDAS PEADNFLSDL AASKGAKTNN
PFHIFNGSET EADKGITRAL LLGDFEKALD VSLKEDRLSD AFMIAICGGQ KCIAKAQEHY
FSKQTESPNY VRLLASIVGK NLWDVVYNAD LSNWKEVMAA LCTFAEEKEF ADLCDALGDR
LEEQIRASDD KSLRKDASFC FLAGSKLEKV VAIWIEELRE NEQKALETAA NDTSFSIHVR
ALQGLIEKVT IFRQVTKFQD TERTKESDWK LSNLYDKYIE YADVVATHGR LQVAQKYLDL
VPEKHPEAEV ARNRIKLATR QPTAQKTQQT TTGRGTPLNK PLPTTNAYQP QRTFSPVATA
AAPSPYAPPA PTTNAYAPPA AATNPYAPPA AATNPYAPPA PASNPYAPPG AAAPPQPTNP
YAPASGGSYA PTGYQPTPAP SYGAKPLGGS VPPPPRASNQ SPATVTTYTT ATNLPAWNDL
PEGFAKAPTP RRGTPAGAAA PISSPFPNQS PSIAQGPPPP GAPPTQRTPS VPPPPKGTAP
PPRVTSPPSA IPPGPTPPPN PYASLPQSPP QLNPGTMGVP APIPRGPSPY NAPPSMPPPT
NRYAPSPAAQ AANPQLQARG PVPPPPQAAA SPYAPQPPAA SQYAPSTPPL QQGPPPASTS
RPGTASSQKV TPAPATPKYP PGDRSHIPED AMPIYEILSA DMQRIKGRAP TSFKQQVEDA
DRRLNLLFDH LNNGDLLKPN TVSDMADLAR AIQARDYEAA RAIHVDILTN RTDECGQWMV
GVKRLISMSK ATP
