SEC31_LODEL
ID SEC31_LODEL Reviewed; 953 AA.
AC A5DTX3;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Protein transport protein SEC31;
GN Name=SEC31; ORFNames=LELG_00809;
OS Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC Lodderomyces.
OX NCBI_TaxID=379508;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL
RC YB-4239;
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; CH981524; EDK42631.1; -; Genomic_DNA.
DR RefSeq; XP_001528289.1; XM_001528239.1.
DR AlphaFoldDB; A5DTX3; -.
DR SMR; A5DTX3; -.
DR STRING; 379508.A5DTX3; -.
DR PRIDE; A5DTX3; -.
DR EnsemblFungi; EDK42631; EDK42631; LELG_00809.
DR GeneID; 5235378; -.
DR KEGG; lel:LELG_00809; -.
DR VEuPathDB; FungiDB:LELG_00809; -.
DR eggNOG; KOG0307; Eukaryota.
DR HOGENOM; CLU_003033_2_0_1; -.
DR InParanoid; A5DTX3; -.
DR OMA; AQWAFGG; -.
DR OrthoDB; 100998at2759; -.
DR Proteomes; UP000001996; 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; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR13923; PTHR13923; 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..953
FT /note="Protein transport protein SEC31"
FT /id="PRO_0000295439"
FT REPEAT 6..46
FT /note="WD 1"
FT REPEAT 61..105
FT /note="WD 2"
FT REPEAT 117..157
FT /note="WD 3"
FT REPEAT 163..203
FT /note="WD 4"
FT REPEAT 210..253
FT /note="WD 5"
FT REPEAT 257..297
FT /note="WD 6"
FT REPEAT 300..340
FT /note="WD 7"
FT REPEAT 382..405
FT /note="WD 8; interaction with SEC13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221"
FT REGION 459..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 860..953
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..519
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 860..891
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 900..926
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 953 AA; 103410 MW; 8D64F462938AC8D5 CRC64;
MVKIGEINRT STFAWSLDAL PLLATGTVAG AVDINFTSSA TLEIWEIFSP TKKNEPIFTA
SVEHKFYALA WSKPFENRPK GLIAGAFEDG TVEFWDADVL IKSKNLKKAS VHKSTKHSGG
AVKSLQFNPI QHHVLVTGGS NGQIFVWDTK TFGEPFSPGQ AMTPMDEISC VAWNNSVSHI
LASTGNSGYT SIWDLKSKKE VLHLSYTGAT GKANFSHVAW HPTKSTKLVT ASDSESCPVI
LTWDLRNSNA PEKVMEGHKK GVLSLDWCKQ DPELLISSGK DNATILWNPI EGKKLGEYPT
TANWAFKTRF APSAPDIFAT ASFDGKIIVQ TIQDTSPPVS TKVSASHDDN EFWSELSVTE
TQQPVFEVKQ APIWLKNPVS VSFGFGSKLV VVGKDANGKS TLKVTKFLVK GHERAENLLK
HLKSENYDAI VDYHLQGPAI NEQDKSDWEV LKSLSKNGKQ GLFDDEEDGS DTTEEKKNSA
NKEDADADAT TKDKDIENGK DGKDDTANAA NDGDGDDDFF AHLGNGSTRQ TVETYSPSGD
FDIYNSQTSK SDKKLTKLIL KNKIDDAVDS CLEQDNLLEA LVLALDSSAQ VKEKVKNAYF
SKHKESSLAR VIYNATEKNV TDLVAHANVK NWKDIALGIS AFATDSEEYS SKISELGDRI
LHHDKSARDE AITCYIAGGA LDKIANLWLQ ELPQYEADLL KTDDKNISSP SEARLQALTS
FVEKIETFKY YAKLGSVLSG PLVEPISKTI LEFVNLISGA GEFELANKLL MLLPGDIAGV
EKERISKATG KDTKPIVSEG SAARASVSSS KYSKIPRKSL TSANANANAN ANVNSNASST
GALPTPATNI LPPLANHHIQ GQTPSFVQPQ PQTAFGQLPT PSTSSAYPTA PVAKSNPYAK
PNPYTPNNIY KTSPVPQPSV APQASFSGTA PPPPPAVQKA NSKERMERLA RNI
