ID   SEC31_KLULA             Reviewed;        1231 AA.
AC   Q6CL75;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 122.
DE   RecName: Full=Protein transport protein SEC31;
GN   Name=SEC31; OrderedLocusNames=KLLA0F05159g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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}.
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DR   EMBL; CR382126; CAG98022.1; -; Genomic_DNA.
DR   RefSeq; XP_455314.1; XM_455314.1.
DR   AlphaFoldDB; Q6CL75; -.
DR   SMR; Q6CL75; -.
DR   STRING; 28985.XP_455314.1; -.
DR   EnsemblFungi; CAG98022; CAG98022; KLLA0_F05159g.
DR   GeneID; 2895754; -.
DR   KEGG; kla:KLLA0_F05159g; -.
DR   eggNOG; KOG0307; Eukaryota.
DR   HOGENOM; CLU_003033_2_0_1; -.
DR   InParanoid; Q6CL75; -.
DR   OMA; AQWAFGG; -.
DR   Proteomes; UP000000598; Chromosome F.
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; 1.
DR   Pfam; PF11549; Sec31; 1.
DR   Pfam; PF07304; SRA1; 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..1231
FT                   /note="Protein transport protein SEC31"
FT                   /id="PRO_0000295438"
FT   REPEAT          6..46
FT                   /note="WD 1"
FT   REPEAT          60..99
FT                   /note="WD 2"
FT   REPEAT          102..142
FT                   /note="WD 3"
FT   REPEAT          152..192
FT                   /note="WD 4"
FT   REPEAT          201..244
FT                   /note="WD 5"
FT   REPEAT          249..289
FT                   /note="WD 6"
FT   REPEAT          292..332
FT                   /note="WD 7"
FT   REPEAT          379..399
FT                   /note="WD 8; interaction with SEC13"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00221"
FT   REGION          725..802
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          941..1012
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        733..776
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        777..798
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        945..971
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        976..998
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1231 AA;  133054 MW;  154FAADB52239528 CRC64;
     MVKLAEYPRT ATFSWSHDRV PVLATGPASG AIDADFSSTS TLELWSLLSF DGSKPSGSVV
     ADGKFNDLDW SGDDKIIAGA LENGVVEFFD PKALKSVAKI HKHQGPVKTL KFNAKQNNVL
     VSGGTQGEIF VWDSNKIGSS DYSPFSAGIS NTPIDEVSSL SWNQSLAHVF ASASSSGYAS
     VWDLKAKKQV LHLNHSSSTT GIKVPLTVVD WHPTSSTIIA TASSSDTEPL VLTWDLRNAH
     VPLKVLSQGH SKGVLSLDWC KQDENLLLSS GRDNTSVLWN PQEGSILTQF APRGNWVFKS
     KFAPEAPDLF ASASFDSKIV VQTLQNLSNT LDAQANESKQ HASEDEFWNN VTSNSVDDKP
     NTVKIQAPKW YGNKSPAAQW AFGGKLVRIS DDGKGVSVVK PCISGLEKNQ LFDESLKSKD
     FVKLINKRLS QKINATNEDD WNLLENLSMD GTALYLKDAL SLDDAKEDII KKSEEDGADF
     FNQLNDKFVP EGAFKLDFSE SMKPLTNFLI KGDLKSALNQ ALEKDLLLEA LVIAITSNDA
     LLADKAKNAY FSKHSEQSGL ARTLFSVAQR DVEDIVTNID VSQWKDAVQF IFNYTKEDIS
     KKNSLLVKLG DRLLHEGNRK DAILLYLSGQ SLESIASIWL KEFPELENQL TSQKDTLYEA
     HLECLTEFVE RFTVLSDYLD KGTVKLTNQT LISKFLEFVN VTAANGDFEL SLRFLETLPD
     DNEEVKSEKQ RVLIASGKTS TTRSTERTAN STLQSRQGRY GSTSVPTANG APRLSNSGIP
     PPNPLAAPHQ PPASTAPNVV PRKPSFVPQT TSAIPTPNPY APAAVNQQIP LSVVGSRPSY
     TPPVNPYAQT ATSIPPNPYA PLPVAAPVPL GSPVAPPPIS GASGYSGQTP HLHDKPIDGW
     NDLPSVSKEK PTRAKAVNTA PIGMSTPSYG TPDLAAVPLS RASTNSTLPP PPPNVRRTPK
     LTSPPEVASP PLPLKKTNSY APTVSAVQSS QMPQQISNPL MPPASPNPAT NGRSFVPPVN
     PYSPAPSAVT PTGIVPPKAL VAAIPSPVPA PKAAAVPPPR KMNRKSTAVG DASAASNLLS
     SIQTKPTPPI HSPAMVDPVA VQYDQSAVSP TNVEIAAEQG AGITESDRPI VEFLTAELQR
     VTPLIPQEYT KQLKDCDKRI KILIKHLEHH DLLTQPTIDK LHQIVAFWKE GNYSEAMTIH
     QDLSANHSSE AGNWLTGIKR LMNIAEATSS Q