SEC31_USTMA
ID SEC31_USTMA Reviewed; 1416 AA.
AC Q4P2B6; A0A0D1BYS2;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Protein transport protein SEC31;
GN Name=SEC31; ORFNames=UMAG_05747;
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021;
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT maydis.";
RL Nature 444:97-101(2006).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021;
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-2014) 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; CM003155; KIS66967.1; -; Genomic_DNA.
DR RefSeq; XP_011391488.1; XM_011393186.1.
DR AlphaFoldDB; Q4P2B6; -.
DR SMR; Q4P2B6; -.
DR STRING; 5270.UM05747P0; -.
DR EnsemblFungi; KIS66967; KIS66967; UMAG_05747.
DR GeneID; 23565550; -.
DR KEGG; uma:UMAG_05747; -.
DR VEuPathDB; FungiDB:UMAG_05747; -.
DR eggNOG; KOG0307; Eukaryota.
DR HOGENOM; CLU_003033_2_0_1; -.
DR InParanoid; Q4P2B6; -.
DR OMA; NRYAPAP; -.
DR OrthoDB; 100998at2759; -.
DR Proteomes; UP000000561; Chromosome 16.
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; 1.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
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..1416
FT /note="Protein transport protein SEC31"
FT /id="PRO_0000295447"
FT REPEAT 8..48
FT /note="WD 1"
FT REPEAT 70..114
FT /note="WD 2"
FT REPEAT 125..165
FT /note="WD 3"
FT REPEAT 171..211
FT /note="WD 4"
FT REPEAT 236..279
FT /note="WD 5"
FT REPEAT 283..323
FT /note="WD 6"
FT REPEAT 326..366
FT /note="WD 7"
FT REPEAT 410..435
FT /note="WD 8; interaction with SEC13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221"
FT REGION 1015..1040
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1078..1317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1021..1040
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1122..1139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1140..1180
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1190..1231
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1416 AA; 149059 MW; 5931861C588C6B99 CRC64;
MKAYINRTAT FAWSPATYES DSPLIATGTV AGALDESFSN ESLLELWKPF YAASADANID
ADAKPLASIS TSARFNRLAW GYANPSRPKG LLAAGLENGE LGIWDADKVL AAAAESDAQV
IKNTTHTGPV RGLDFNPLQP NLLSSGAVAG EIFIWDLNSP AKPYSPGARS SKLDEITSLA
WNCQVPHVLA TSSSSGYTVV WDLRGKREVV ALQYGGGAGT AVGSLGINAG SALAAGGRRG
MSAVAWHPDT PTRLVTASED DSSPVIMLWD LRNSRAPEKI MTGHDKGILS LSWCKQDADL
LLSCGKDNRS ICWNPQTCDI VGELPSSSNW SFEVQWSPRN PGMLATASFD GKIGVHSLQS
TNAPEPDAPA TQQLNEDSDF FNQATAPQTT SKGLSLKQPP KWLRRPVSAV FGFGGQLVSS
GGPSSKPFTP TVHLRDFVSE PSIVERATKL QHALDGQSLA EFCAQRSQDP STRPDDIANW
KALQTLFRAD SRDELVALLG FSKEDIAQKV SQSIAAFKTN GTAAVEPEVT PVTNPIDEPE
LTKPVTSADD GADAVEAANE IVEPAAIATE PAPEVEANDI DEPGLFGDDA AGAANNDASD
FFNQISAGQT PAVRSALPSH LLSESQPHIH SSAATIGSPA PSSVASESIR PSTFKIYPSE
ESEADKLITR ALVLGEFESA VSLCINSDRF ADAFLLAVRG GEELLAKTQK AYFEKRTAQL
PYLRLFQSIV SDDLTDVVQN ADLGEWQEIF VVLCTFSKQD EFSNLTEQLG QRLEFQYSLA
RNSDITQAKE HRKNAVLCYL AAGKLEKVAG MWIDEMKEEE LALRSNTKNA DESHKGTLYS
ARAEALQTFM EKITVFQSAV GYVDVDLQQP TQDSIVAETG ARSYKLAPLY DRIHEYVELL
ADQGLISPAL RFANQTPADY RPHGPADQSA TATALKQRLL KAEIARPKTD TAASSSTNNV
VAAASASASS YAAAPASNGY APYDPYGQST SSSVPTVPSV PAVPAVNTYQ DPYAAAAPSP
SVAAPQPPTQ SRYAPAVPAP VPTAMQPEPV QTNAYGAYGA QSYQSAYQPA QPMIPAAPAF
GASSYGQQQH QQQLPPPPPL KRDQSGWNDV PEGLAAPKRT PSAMSQHKSA NAITSPFPNA
PAQAPSPYGG APGAPPTGPP RGATPSRGMM SPPPQGPPSG PGLAQQRVGP PGVRPPPMGP
AQGQPRPGQQ QPGPPSQAAP SAGPYARPPA GPGAPSANGM QQQQQPGAPP VGPGAGALRP
PGQALPGAPG LAGPPGVPQR SATPGGGAGA PSRSATPGAR GASQMKYPPG DRSHIPENQR
PIQHALQREV ARLKATAPPA QKRMIDDTER RINLLLDHLN CGTIDAKTVG GLMQIVAAIE
ARNKQAALNI HLQLVTSSSG DVAAGLVGVK MIISRL
