SEC31_PHANO
ID SEC31_PHANO Reviewed; 1256 AA.
AC Q0ULF5;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 3.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=Protein transport protein SEC31;
GN Name=SEC31; ORFNames=SNOG_07409;
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(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 7) 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; CH445335; EAT84875.2; -; Genomic_DNA.
DR RefSeq; XP_001797743.1; XM_001797691.1.
DR AlphaFoldDB; Q0ULF5; -.
DR SMR; Q0ULF5; -.
DR STRING; 13684.SNOT_07409; -.
DR PRIDE; Q0ULF5; -.
DR EnsemblFungi; SNOT_07409; SNOT_07409; SNOG_07409.
DR GeneID; 5974521; -.
DR KEGG; pno:SNOG_07409; -.
DR eggNOG; KOG0307; Eukaryota.
DR HOGENOM; CLU_003033_2_0_1; -.
DR InParanoid; Q0ULF5; -.
DR OrthoDB; 100998at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
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; 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 SMART; SM00320; WD40; 4.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 2.
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..1256
FT /note="Protein transport protein SEC31"
FT /id="PRO_0000295443"
FT REPEAT 7..47
FT /note="WD 1"
FT REPEAT 66..110
FT /note="WD 2"
FT REPEAT 119..159
FT /note="WD 3"
FT REPEAT 165..205
FT /note="WD 4"
FT REPEAT 209..241
FT /note="WD 5"
FT REPEAT 242..281
FT /note="WD 6"
FT REPEAT 368..390
FT /note="WD 7; interaction with SEC13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221"
FT REGION 460..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 761..1139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 815..844
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 863..877
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 924..938
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 940..1004
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1042..1056
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1080..1112
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1256 AA; 134502 MW; B96B2C3D42CD1907 CRC64;
MVRLREIPRT ATFAWSPGPT QPLIATGTKA GAVDADFSND TQLELWELKL DDAEQGVELQ
PVATVSVDSR FNDIAWSQPS EQHPRGIIAG ALDSGALVLW DAEKLRTGAS DAQIDQIDKH
TGPIQAIQFN PFRPNILASA GAKGELFVHD LDDESKSFRL GKAGANPDEY TTLDWNKKVA
HILATGSSGG FVTVWDVKGK KENLTLNHFG RKTVSAVSWD PDVPTRLVTA IPTDQNPLVL
AHDQGVLSLS WCPQDSDILL SCGKDNRTIA WNPHSGEQLG RISGRDKLDL PDQIQPVEPE
PYSRPASFDG KIAVQTLQNT GANADQSKTA KQAPEGEDFF AQTHAEPQGA SFSLKSPPKW
LKRRAGVAFG FGGKLVRFGV VDAKSKITIS TFAVDSDISQ ASEDFDKALE TGDLTSILES
KISKAATDEE KADWTVIETL TSDNPRTKLV EYLGFADQSE EAPAEVKKEA QTNGDADEGS
SFFDNATDEG NFLSDLAARK GAKTNNPFQV YTGSESEADT KITRALMLGN FDAALDVCLK
ENRLSDAFMI AICGGEKCVA KAQAAYFKRQ SDAPNYLRLL ASVVGKNLWD FVYNADLKDW
KEVMATICTF ADQAEFPDLC EALGDRLEEA IAEGTTSYRK DASFCYLAGS KLEKVVVNWA
QELQENENAG LEQSETDNSF SIHARSLQDF IEKVTVFRKV TQFKDTEQSK ENDWKLEPLY
AKYVEYADIA SAHGQLAIAE KYLDLLPQKY PAADVARNRV KQATRKGAAP AAAGQRQSQP
AAAQRGQRVV PAYGAPAPQP TPAQRTASPY APANPLAPAQ TNSPYAPVNP LSQQAQQATQ
QPPARAGGAY TPAGYQPAPV QQGYGGYGQQ QQAPLAPPPQ NFSNPNGPSI VPAANRGHIP
AWNDTPDFGP PKTASRRGTP LNAVASPFPN QQQNYGPPGG ASPGFPPQSR PTPPPPPKGP
PQGPPRMTSP PSQAGGAPPN APNPYAPSPA ANNYAPPPSG FAPPQQAPVQ RGASPYQPPQ
SAAPPSNRYA PAPGSQPSAP SGMGGMPPPR NIAPPPGQFT PGASAYAPSP YAQSPAQQAP
AAVAPPPRGP PQGPPRAGPP PGGPPQGGPP RPESRPGTGQ SQPAAPAAAR YPPGDREHIP
MVSRPIYEIL GAEIQRVKAK APAQYKAHVT DTEKRLNILF DHLNNEDLLK PDTIQQMNEL
ASNIQAKQFD EAIAIFQDLM TNKNDEGSNW LVSDVITFDA DVGVKRLIQF SKSTPA
