SEC31_DEBHA
ID SEC31_DEBHA Reviewed; 1265 AA.
AC Q6BRR2;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=Protein transport protein SEC31;
GN Name=SEC31; OrderedLocusNames=DEHA2D14476g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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; CR382136; CAG87276.2; -; Genomic_DNA.
DR RefSeq; XP_459108.2; XM_459108.1.
DR AlphaFoldDB; Q6BRR2; -.
DR SMR; Q6BRR2; -.
DR STRING; 4959.XP_459108.2; -.
DR EnsemblFungi; CAG87276; CAG87276; DEHA2D14476g.
DR GeneID; 2901269; -.
DR KEGG; dha:DEHA2D14476g; -.
DR VEuPathDB; FungiDB:DEHA2D14476g; -.
DR eggNOG; KOG0307; Eukaryota.
DR HOGENOM; CLU_003033_2_0_1; -.
DR InParanoid; Q6BRR2; -.
DR OMA; NRYAPAP; -.
DR OrthoDB; 100998at2759; -.
DR Proteomes; UP000000599; Chromosome D.
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; 2.
DR SMART; SM00320; WD40; 5.
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_0000295436"
FT REPEAT 5..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 462..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 786..1163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 786..827
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 857..890
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 935..951
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 967..1014
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1017..1031
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1041..1055
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1056..1072
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1107..1134
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1265 AA; 135966 MW; C34072D28DA8601E CRC64;
MVKIDEISRT STFAWSQDCL PLLATGTVAG AVDVNFDSTS TLDLWDIFSP TNGGKPVFSA
SVDNRFYALA WSKPFEGRPK GLLAGAFENG VVEFWDAEVL IKSKDLNKAS VHKGTKHSGP
VKTLSFNPNQ DHVLVTGGSN GEIFIWDTKK FTEPSVPGQA MTPMDEVTSV AWNNSVSHIF
ASAGNGGYTS IWDLKSKREV LHLSYNGPSG RANFSCVAWH PTQSTKLITA SDNDGCPLIL
TWDLRNANAP EKIMEGHKKG VLSLDWCKHD PELLISSGKD NSTMLWNPIK GEKLGEYPTT
ANWAFHTKFA PAAPEIFATS SFDGKIIIQS LQDTSPPVST KVASNDDNEF WNEISTTETQ
QPVFDVKQAP NWLKVPSSVS FGFGSKLVSV KKDSNGKSIV SIEKFVTNTG FQGSSNRLTD
AFKSNDFNSI IDSKLEGKFV NKIDQSDWEL LKKLHDTGKD KLFDEEVNGS EQPKVDGEKS
EQKDEGANEA ISSTEDSFFD KLGSNSGNGT SNTVSYIPQG DFKIFDSKQS EGDKKLIKLI
LNKNIDEAVS SCLEQDKLVE ALILALDSSD AIKEKVRNSF FKKNDNELAR VLYSASSNNV
TDLVCHADVA NWKEIAMSIS SFCTDVNEYN SKMTELGDRI IDSKGTSDEK RNNAILCYLS
GNALGKIASI WLRELPELEE ELLQSKDTKI STPSDARYEA LSNFVEKITT YRSISNISGE
FEGPSIEPIC KAILEYANLV AGYGQFDLAE KFLELLPSDF AGLKSERDRI LKASGTTTIK
QGTVHSRTAS QRPTAINAGN AYGKPTNFAP STGLGGFQST PSNVVPPINP ASMRLPQGHT
QPPINQPHIS AAPAANPYVK TASTNPYMPA HPSNSFSNPY KPATPSATHA TNPLSPPPPG
PPKASFKNQT EGWNDLPDTF KPKAAPRRAA ASAVSPSPVP SSPQLATSAP KRTSVAPPLA
PPPPKGVSRN QSKTSISTSN ANSPRQSQAQ MSSRYAPPPG VSTAPSTPGV NEAPPTVTSA
PIPPPKNPYA PAMQAASPSL PKNPYAPPPS YGQPGILQPT IPTPNIASPS LGRATTAAPP
KNPYAPPPGS AVSPKPHAAG IPAPRMGGVV APPPPVASST SSLPPPPGIS QQPPAANAPP
MATTVDQEPP KYPPGDRSHI PEQSLPIFNS LSSILDDIKP KIPERYAKHG VDMDKRINLL
FDHLNNSDLL SDESIASLKE VCTALEARDF PTANALNIQI ATNHSEETGN WHTGVKRLIQ
MSEAL
