SEC31_PICGU
ID SEC31_PICGU Reviewed; 1266 AA.
AC A5DB75;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 2.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Protein transport protein SEC31;
GN Name=SEC31; ORFNames=PGUG_00530;
OS Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX NCBI_TaxID=294746;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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; CH408155; EDK36432.2; -; Genomic_DNA.
DR RefSeq; XP_001487153.1; XM_001487103.1.
DR AlphaFoldDB; A5DB75; -.
DR SMR; A5DB75; -.
DR STRING; 4929.XP_001487153.1; -.
DR EnsemblFungi; EDK36432; EDK36432; PGUG_00530.
DR GeneID; 5129691; -.
DR KEGG; pgu:PGUG_00530; -.
DR VEuPathDB; FungiDB:PGUG_00530; -.
DR eggNOG; KOG0307; Eukaryota.
DR HOGENOM; CLU_003033_2_0_1; -.
DR InParanoid; A5DB75; -.
DR OMA; NRYAPAP; -.
DR OrthoDB; 100998at2759; -.
DR Proteomes; UP000001997; Unassembled WGS sequence.
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; 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; PF00400; WD40; 1.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 2.
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..1266
FT /note="Protein transport protein SEC31"
FT /id="PRO_0000295444"
FT REPEAT 5..45
FT /note="WD 1"
FT REPEAT 60..104
FT /note="WD 2"
FT REPEAT 115..155
FT /note="WD 3"
FT REPEAT 161..201
FT /note="WD 4"
FT REPEAT 203..246
FT /note="WD 5"
FT REPEAT 250..290
FT /note="WD 6"
FT REPEAT 293..333
FT /note="WD 7"
FT REPEAT 374..397
FT /note="WD 8; interaction with SEC13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221"
FT REGION 463..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 760..1157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 768..789
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 837..852
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 884..905
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 964..1018
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1028..1067
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1079..1094
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1107..1128
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1266 AA; 135234 MW; 43E70722E9C84F31 CRC64;
MKIEEISKTS TFAWNNDPLP LLASGTVAGA VDADFSTSSS LEIWDIFSAT NSKDPIFSAS
VDNRFYAIAW SKPSEGRSKG VLAGAFENGT IELWDVQELI TSKDLQKASI FKSSAHSGPV
KTLQFNPLQE HVLLSGGSNG QIFVWDTKKL SDPVAPGKAM TPMDEISCVS WNNSVSHIFA
TTGNSGYTSI WDLKSKREVL HLSYSANFSC VAWHPTQSTK LVTATGNDSD ALILTWDLKN
ANAPEKIMRG HKKGILSLDW CKQDPEILIS SGKDNATMLW NPIKGEKLGE YPTTANWAFH
TRFAPAAPEI FATASFDGKI VIQSLQDTSP PMTSKVTTKN DNDFWNEIST TETQQPVFTV
HQAPAWLKRT SSVSFGFGSK LVSISLDSDS HSVVKIQPFV KNGAVSETTS KFSQALKSND
FKDIIEARIS DARHSKTDKA DWEILSKLSG VGKEGFLKEI VSTEHEQANG KKPDVSSEDG
TEPSRKEEGD NDFFEQLGES PIKSIPNFVP EGKFSIDTSD QSEADKTIIK LLLSNKIEDA
ISACLDQKKL SAALVLALDA SPESKAKVRN AYFTNTKGDE IARLIYNASS KNITDIVANA
DVKSWKEIAA AIAAFSTDES DLSSKITELG DRIVQASENP STEDRNNAMI CYLAGNALEK
IASIWLRELP EYEKSLLESP DDDVSTPSDA HFKSLNNFME KLLAYRSITK ANDTLGGPSI
EPICNAILEY ANLVAGYGQF ELADSFLQLL PSDFAGLKTE KDRISRASGT KVQASNTRST
TSKATASRSY GKSPVPGASV PPTLPGNQTF APAASTPYGG LAGQPAASSV LTPATPSFPS
MPQPPQAPVS NRPPIASTPS IYGKPAPVGN PYAPQGATAF NPYKPPAPVA PEPVSAPPPA
VSGPPKPAYR QETEGWNDLP DAFKQKTSTR RAAPAAVVSP SLSPALPANN FAPPKRNSAV
AGPPPKGSRS SSRTAVPTIP TAASPSASTA QLHSRYAPPQ SFNAPTEVSN GSGSPTPSVH
APPKNPYAPA ATSSTNLPRN QYAPSVPTPS VQQPQTPKIG HASATPSGPS PNGPPKNPYA
PTAQQVSMSP SGMVPPRTGS YGAAPSGVTA PPPPKVGGVL PPPGPVLTQP RSRNASAAAP
VELTPPPTKP KYPAGDRSHI PEKSIQIYTS LDSLTQAVKP NVPERFIKHA EDMEKRLNFL
YDHLNNDDLL SDDAIAELKK VCSAVEAKDY ATATQLNVDF ATNHSEQTGK WYPGLKRLIS
MAEATL
