SEC31_CANAL
ID SEC31_CANAL Reviewed; 1265 AA.
AC Q5AAU3; A0A1D8PDX6;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2017, sequence version 2.
DT 25-MAY-2022, entry version 107.
DE RecName: Full=Protein transport protein SEC31;
GN Name=PGA63; Synonyms=SEC31; OrderedLocusNames=CAALFM_C106930WA;
GN ORFNames=CaO19.13598, CaO19.6217;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
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; CP017623; AOW26347.1; -; Genomic_DNA.
DR RefSeq; XP_718807.2; XM_713714.2.
DR AlphaFoldDB; Q5AAU3; -.
DR SMR; Q5AAU3; -.
DR STRING; 237561.Q5AAU3; -.
DR PRIDE; Q5AAU3; -.
DR GeneID; 3639524; -.
DR KEGG; cal:CAALFM_C106930WA; -.
DR CGD; CAL0000193385; PGA63.
DR VEuPathDB; FungiDB:C1_06930W_A; -.
DR eggNOG; KOG0307; Eukaryota.
DR HOGENOM; CLU_003033_2_0_1; -.
DR InParanoid; Q5AAU3; -.
DR OMA; NRYAPAP; -.
DR OrthoDB; 100998at2759; -.
DR PRO; PR:Q5AAU3; -.
DR Proteomes; UP000000559; Chromosome 1.
DR GO; GO:0015629; C:actin cytoskeleton; IEA:InterPro.
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:0007155; P:cell adhesion; IEA:InterPro.
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 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 Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR040251; SEC31-like.
DR InterPro; IPR009917; SRA1/Sec31.
DR InterPro; IPR000633; Vinculin_CS.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR13923; PTHR13923; 2.
DR Pfam; PF07304; SRA1; 1.
DR Pfam; PF00400; WD40; 2.
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..1265
FT /note="Protein transport protein SEC31"
FT /id="PRO_0000295432"
FT REPEAT 6..46
FT /note="WD 1"
FT REPEAT 61..105
FT /note="WD 2"
FT REPEAT 116..156
FT /note="WD 3"
FT REPEAT 162..202
FT /note="WD 4"
FT REPEAT 209..252
FT /note="WD 5"
FT REPEAT 256..296
FT /note="WD 6"
FT REPEAT 299..339
FT /note="WD 7"
FT REPEAT 380..403
FT /note="WD 8; interaction with SEC13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221"
FT REGION 457..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 765..784
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 793..1163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 795..809
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 810..829
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 846..872
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 919..938
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 939..1028
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1079..1105
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1113..1127
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1265 AA; 136310 MW; 0D161CCF26861CD6 CRC64;
MVKISEIART STFAWSSKNL PLLAAGTVAG AVDINFSSSA TLELWDIFSP TNKTEPIFSA
TVDNRFYALA WSKPFEGRPQ GLLAGAFENG TVEFWDADVL IKTKDLAKAS VHKSNKHTGA
VKSLQFNPIQ NHVLVTGGSN GQIFIWDTKT FSEPFAPGQA MTPMDEITSV SWNNSVSHIL
ASTGNGGYTS IWDLKTKREV LHLSYTGAGG RANFSYVSWH PSQSTKLITA SDNDSCPLIL
TWDLRNSNAP EKILEGHKKG VLSLDWCKQD PTLLLSSGKD NSTFLWNPIE GIKLGEYPTT
ANWAFETKFA PAAPDIFATA SFDGKVVVQT IQDTSPSVST KVASTDDNEF WSELSTTETQ
QPVFEVKQAP NWLKNPSNVS FGFGSKLVII NTDSSGKSTV KVDKFVAKGQ EKTEKLFKDL
KNDNYSSLIQ DKLEGETVNE NNKSDWEVLK RLSETGKESL FEDANNDEKE ATSPETKKEN
GEDDFFEHLG NGETAKKEEV FVPEGNFKIF TNNENEDSKK LINLILRNKT EEAVSSCLEQ
KKLVEALVLA LDGSDDVKQQ VKNAYFKKNK ENNLSRVIYN ASTKNVTDLV AHANVENWKE
VAVGISSFTT DSSEYNSKMS ELGDRILKAK DGKRNDAVVC YLAGGALDKI SNLWLQELPD
YESELLSLKS EEITSPSDAR LQALTNFVEK VATYRYITKS TGEFSGPMVE PLAKAILEFV
NLVAGSGDFD LANKFLQLLP SEFSGTEKER ILKATSKAVE PASAVKSSAN AKIAKPASSS
GQTRASINAV PAPAYAPPVQ APPVQAPQPP LVQQQQQQQQ QQQPNRYGYA QPTYAGAAPK
TNPYARTNPY APSNNIYKPA SPVATPSSLS GTTSGVPPPP PKASYKHETE GWNDLPDTFK
AKTAAPRRAA AAATPPVSTP TPVSAPAFGS PGQPPSAPSQ PGSVGSVSSA GYPKKTFSAT
NVLPPPPKSI SRSTSRTTVP TSSTVPASPK PTPVSNKYAP AVTSDASQPP SSGFASPTLN
SSPRLAKNPY APSVTEQLPP KISYATPPAH HLANNGPSTP SYAPPKNPYA VPPSTSVSHA
GIAPPPPAPK LGSAAPPPPQ PFGSSMSMPV QPAFNGVPPP PPPVGRAVST PAAAKIEQPP
AREPELPVQS KHPKGDRTHI PENSLPIYNS LTNVLEAIKP NIPEKYAKHG TDMEQRLNIL
FDHLNNEEIS NGVIELLLKV ATSLESKDFA NATAVNLQIA TEHSDEIGNW HTGLKRLITM
AEAMY
