SEC31_YARLI
ID SEC31_YARLI Reviewed; 1184 AA.
AC Q6C414; Q8J0E5;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=Protein transport protein SEC31;
GN Name=SEC31; OrderedLocusNames=YALI0E30635g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=E 122;
RX PubMed=12456001; DOI=10.1128/ec.1.4.526-537.2002;
RA Hurtado C.A., Rachubinski R.A.;
RT "Isolation and characterization of YlBEM1, a gene required for cell
RT polarization and differentiation in the dimorphic yeast Yarrowia
RT lipolytica.";
RL Eukaryot. Cell 1:526-537(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
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 -!- SEQUENCE CAUTION:
CC Sequence=AAM09808.1; Type=Erroneous gene model prediction; Evidence={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; AY084034; AAM09808.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CR382131; CAG80202.1; -; Genomic_DNA.
DR RefSeq; XP_504598.1; XM_504598.1.
DR AlphaFoldDB; Q6C414; -.
DR SMR; Q6C414; -.
DR STRING; 4952.CAG80202; -.
DR EnsemblFungi; CAG80202; CAG80202; YALI0_E30635g.
DR GeneID; 2911749; -.
DR KEGG; yli:YALI0E30635g; -.
DR VEuPathDB; FungiDB:YALI0_E30635g; -.
DR HOGENOM; CLU_003033_2_0_1; -.
DR InParanoid; Q6C414; -.
DR OMA; NRYAPAP; -.
DR Proteomes; UP000001300; Chromosome E.
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: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 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; 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..1184
FT /note="Protein transport protein SEC31"
FT /id="PRO_0000295448"
FT REPEAT 4..44
FT /note="WD 1"
FT REPEAT 65..106
FT /note="WD 2"
FT REPEAT 112..152
FT /note="WD 3"
FT REPEAT 159..199
FT /note="WD 4"
FT REPEAT 201..244
FT /note="WD 5"
FT REPEAT 248..288
FT /note="WD 6"
FT REPEAT 291..331
FT /note="WD 7"
FT REPEAT 366..388
FT /note="WD 8; interaction with SEC13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221"
FT REGION 692..723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 751..1079
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 698..723
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 751..779
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 784..828
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 853..887
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 929..944
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 963..1006
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1028..1067
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1184 AA; 125002 MW; 176E3F51A589ADB3 CRC64;
MKLKEIDRTA TFAWSPNNLR IATGTVAGTV DADFSSSSQL EIWDVDLMDR SSEGFRLTKP
AVSISADTRF HDLVWHNTGK HSLIVGATES GSLEVWEADN IKDSSTSVSV KEHSGPIKTL
QFDPHNPTRL VSGGTKGEIF VWDLSDPKKP IAKKLGTDNK AGDIESLAFN NITRNILATS
SSNGITTIWN VDQNKELTRV KHDKPVSHVV WHPSKPTKLI TAVADDAEPV MLIWDLKNAN
APEGVLQGHS KGILSVDWCQ LDPRFLLSCG KDNRTLLWNP DTHECLGEYG AAQNWTFKTK
LNERTPDLFA TASFEGKIVI QTLQDVNGGD APAQEGDFFQ NLGTQSQAKI SLKQAPSWLQ
RPVSNSFGFG GKIVTVTTTD GKSTVQVGKF VGDKVDTESI EVVLKGDLTS AFDEVKGAEW
KVLEALSKGT DEVRSFLDIP VMKEEPAVED DSEDVFSKMS PSGAFSLESS DPINQAIING
NLSTAVDLCL KEDRLLDAFA LAEKASDAVK TKVQNAYFAK QTSSTARLLN AVNTNKLDDV
VENANLKDWK EILALLYTYG GAQFGDLAAA LGDRLRESDR DNAATCYLVS GKLDKVSGLW
ESEITTREKE LTKDNVAPYT AHFSALKEFI EKISVFRKAT NAVDSGTVDG LYNKYREFAN
IVASQGNLEL AQQFLALLPA SFEGVGLERE RLNKAAKPSV ATTATSKASA YGKPSYGSAT
PQASAYTPTA SAYGSMYAPA VPAAAAPAAA APPPTAAAVP PSPAKNMYAP QPPAPVTGFA
PAAQSPGAPQ QNTHNPYNPT PQTNAYAPQG NAYSAAPQQN TYGRSTPGGG PVRTTAPRHD
TAGYNDLPAG SVPPPKKSAP SPGPISSAYA PPTPAAPSAP PAGGPRPPSV NRVTSPGVPS
GGVNAYGFPI GGAPSPYGAQ AAYGARPPVP AVVSPPPPNP YAPAHSPAQN NVQPAVNPYA
PAPGAVVSPP PVHAGIVPPP AQRSAPSNPY APAPGAGAPP ASNPYAPPTG GFTGAPAPHA
GGGYTAPPPA QVAPPPAGPP RNSVAPPPGG PARNPVPSSP APPPAAAKHP AGDRTHIPAT
SRPIFDTLST QWAGLKPHIP EQYSKHVRDA EKRLNILYDH LNNDDAQPEM VEDLLKLSNA
IAQRDFPTAQ ALQLQIATAR PDECGKWMVG LKRFVEMAAA VRTW
