ID   SEC31_CANGA             Reviewed;        1281 AA.
AC   Q6FNU4;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 126.
DE   RecName: Full=Protein transport protein SEC31;
GN   Name=SEC31; OrderedLocusNames=CAGL0J08998g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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; CR380956; CAG61051.1; -; Genomic_DNA.
DR   RefSeq; XP_448100.1; XM_448100.1.
DR   AlphaFoldDB; Q6FNU4; -.
DR   SMR; Q6FNU4; -.
DR   STRING; 5478.XP_448100.1; -.
DR   EnsemblFungi; CAG61051; CAG61051; CAGL0J08998g.
DR   GeneID; 2889475; -.
DR   KEGG; cgr:CAGL0J08998g; -.
DR   CGD; CAL0133638; CAGL0J08998g.
DR   VEuPathDB; FungiDB:CAGL0J08998g; -.
DR   eggNOG; KOG0307; Eukaryota.
DR   HOGENOM; CLU_003033_2_0_1; -.
DR   InParanoid; Q6FNU4; -.
DR   OMA; AQWAFGG; -.
DR   Proteomes; UP000002428; Chromosome J.
DR   GO; GO:0030127; C:COPII vesicle coat; IEA:EnsemblFungi.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005198; F:structural molecule activity; IEA:EnsemblFungi.
DR   GO; GO:0090114; P:COPII-coated vesicle budding; IEA:EnsemblFungi.
DR   GO; GO:1902953; P:positive regulation of ER to Golgi vesicle-mediated transport; IEA:EnsemblFungi.
DR   GO; GO:0070863; P:positive regulation of protein exit from endoplasmic reticulum; IEA:EnsemblFungi.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   Gene3D; 2.130.10.10; -; 1.
DR   InterPro; IPR021614; 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; PF11549; Sec31; 1.
DR   Pfam; PF07304; SRA1; 1.
DR   Pfam; PF00400; WD40; 1.
DR   SMART; SM00320; WD40; 5.
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..1281
FT                   /note="Protein transport protein SEC31"
FT                   /id="PRO_0000295433"
FT   REPEAT          5..46
FT                   /note="WD 1"
FT   REPEAT          60..99
FT                   /note="WD 2"
FT   REPEAT          106..146
FT                   /note="WD 3"
FT   REPEAT          158..198
FT                   /note="WD 4"
FT   REPEAT          207..250
FT                   /note="WD 5"
FT   REPEAT          261..301
FT                   /note="WD 6"
FT   REPEAT          329..371
FT                   /note="WD 7"
FT   REPEAT          392..412
FT                   /note="WD 8; interaction with SEC13"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00221"
FT   REGION          960..991
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1010..1157
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1034..1048
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1078..1092
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1114..1157
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1281 AA;  139375 MW;  CC08FF57DEBD236B CRC64;
     MVRIAEYSRT ATFAWSNDRI PYLVSGTASG TIDADFSNES KLELWSLLGT DADKPSHSVS
     TDAKFKDLDW SADNKYIAGA MDNGAVEIYE FNSSKQELKK QGSFKNHSTV VRTVKFNSKQ
     NNVLLSGGNS QEIFIWDLNK LLDSKANYQP LTPGVSMSPI DEIHSLSWNK SLAHVFASAS
     NSSFASIWDL KAKKEVIHLS YTSQNTGLKS DFSAVEWHPL NSTRVATATS NDNEPLILVW
     DLRNSNTPLQ TLSAANNQGH GHSKGILSLD WCQQDENLLL SSARDSSVML WNPQSGEALT
     EYNTTGNWCF KSKFAPQAPD LFAFATLDGK KIEVQTLQNY ETTLDEEVSK TKQQESETDF
     WNHVSEEKAE IKSTVVHLQA PSWYGNKSAS AQWAFGGKLV QVTKDGKGVE VNKPEITDLK
     SDDTLKNALA SKDFQPLINQ RLVKVVNETN EEDWNLLEKL SMDGKEEFLK EALELDEEED
     EEKDQEGKDG DEFFQKIESN FQPSGSFKID SNEESVINNI LSGNNSKAVS ELLKSGSILE
     AFVVAVTCND EKLKEDVKDA YFAAHGKESS LSRVLFSSSK KNSDDIVENL DISQWKYITK
     SIYNFHANDE VERTNKLLQL GDRLLANKNR QDALVIYIAA GSLDKIATVW LNEFSTLENK
     IKDQEKTIYE AHIECLTEFV ERFTILSNFV GKKQKITNES LISKFLEFIN ITSATGNFDL
     ALLFLDILPE DNEYVIAEKK RVMVASGKVV DQSQSRKGKY GSHANLASAG FSGHAKQPVN
     LPPTAAPFAA QTMGGYAPQA VGAVPTPAVP VPQTRNASVS IKSNPYGPAG TNVGTSDNKF
     NAYAPPTHTQ VPVATPVTSS FIPPANPYSN VAAQSLAMAA EQNAMSPNLA GSAPPVKSPS
     VYSGQTPHLN KKANDGWNDL ALPVKEKPQR AKPVTVAPSP ILAPATNGAA AAVPTKSIGT
     VFPPTGGNSR VPSSMVSPPP PQKRASRTPS LINIDDVVNA RPKAHTSIYA PQTTQAGPAP
     VAPQSDIPLA PTANPYAPNQ SVGSTPLQKP VNPYAPPAQQ AGIPSAANPY ASQIPSKAPV
     NAPPPMSSKK APVGPPPMSS RKKAHEGKTL SHEAASVLDS SKPVQTQPIA SELSREPAPV
     PTSASQTQVP PPVQETPARN TISPIDMAAP AVEQGISAAQ QPIRDFFSSE LARVTPLTPK
     EYNKQLKDCD KRLKILFTHL EKNLLSQPTV DKLLHIIELL KEKKYHEAME VHKDIATNHA
     EEGGNWLTGV KRLISISEAT A