SEC31_ASHGO
ID SEC31_ASHGO Reviewed; 1234 AA.
AC Q75A30;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 2.
DT 25-MAY-2022, entry version 134.
DE RecName: Full=Protein transport protein SEC31;
GN Name=SEC31; OrderedLocusNames=ADR090W;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 591; 600; 608; 617 AND
RP 624-640.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(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; AE016817; AAS52010.2; -; Genomic_DNA.
DR RefSeq; NP_984186.2; NM_209539.2.
DR AlphaFoldDB; Q75A30; -.
DR SMR; Q75A30; -.
DR STRING; 33169.AAS52010; -.
DR PRIDE; Q75A30; -.
DR EnsemblFungi; AAS52010; AAS52010; AGOS_ADR090W.
DR GeneID; 4620335; -.
DR KEGG; ago:AGOS_ADR090W; -.
DR eggNOG; KOG0307; Eukaryota.
DR HOGENOM; CLU_003033_2_0_1; -.
DR InParanoid; Q75A30; -.
DR OMA; AQWAFGG; -.
DR Proteomes; UP000000591; Chromosome IV.
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 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; IPR024298; ACE1_Sec16_Sec31.
DR InterPro; IPR021614; Sec31.
DR InterPro; IPR040251; SEC31-like.
DR InterPro; IPR009917; SRA1/Sec31.
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; 1.
DR Pfam; PF12931; Sec16_C; 1.
DR Pfam; PF11549; Sec31; 1.
DR Pfam; PF07304; SRA1; 1.
DR Pfam; PF00400; WD40; 1.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 1.
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..1234
FT /note="Protein transport protein SEC31"
FT /id="PRO_0000295427"
FT REPEAT 5..46
FT /note="WD 1"
FT REPEAT 59..98
FT /note="WD 2"
FT REPEAT 101..141
FT /note="WD 3"
FT REPEAT 151..191
FT /note="WD 4"
FT REPEAT 200..243
FT /note="WD 5"
FT REPEAT 248..288
FT /note="WD 6"
FT REPEAT 291..331
FT /note="WD 7"
FT REPEAT 378..398
FT /note="WD 8; interaction with SEC13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221"
FT REGION 822..870
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1053..1115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 826..870
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1234 AA; 133191 MW; 70EB6690AF8970C9 CRC64;
MVKLAEYPRT ATFAWSPDKV PVLATGTASG TVDADFSSTA TLEFWEVGSA ESGPQGSVTA
DAKFNDLDWS RDGAMLAGAL ENGVVEFFCA RERRSVARVA RHTTGVRAVR FNAKQANVAV
SGGSQGEIFV WDTNKISAAG YSPFGPGTAM TPIDEVQSLA WNQSLAHVFA SAGSSGFASI
WDLKAKKEVI HLSYTSPHSG LKNQLAVVEW HPSNSTRVAT ATGNDNEPVI LVWDLRNANM
PLQVMSQGHS KGILSLDWCK HDEKLMLSSG RDNTCILWNP EEAQKLTQYP TRGNWCFKTK
FAPEAPDLFA SASFDNKIQV QTLQNLANKL DLDETAFKQQ ESEADFWNNV SQSESKEKPV
VTKIQAPAWH SKKSPAAHWA FGGKIVRITS DGLGVSVSKP HIEGFEKNVM LDEALQSKNF
VPIINKRLAQ TVTPTNEEDW SLLESLSMDG KDTYLQEALS FDDNEAVDSQ PDTKDEDFFL
NLTGQYEPSG EFELDAANPG ITLNLLKGEL SKAVNLALEK DLLLESLVIA LNSDDDQIKQ
KVKNAYYTKY ASNSQLARSL YAISERKIED LVDNLNVSQW KHIVMAIKTY ATEQSKNSLL
IRLGDRLLQA GQRQNAVTLY LAGQSLDKVA SVWLRELPAL ESEMRSHKNT LNEAHLEALT
EFVERFTVLS AYINEDGGAK LTNEELVSKF LEFVSMASSS GDFELALKFL ENLPGDNEQV
KTEKQRVLIA SGKCATTSAT STRRGKYGST TVAPGVPGMP AAPMPVVGMQ PPANPLADRT
ASYGAPGYNV AAPMPPPNGR PNPYAAPAPA YQMANPAAHG KYVNSASASP GHNTPRGSVS
MPHNPYAPST NGAGAVSHNS YAPQHVQPAG QPQNMYGVPP QRNFMNQTQD KPPVNPAATN
VLSGQSPHLN RKANNGWNDL PEIVKEKKSR AKPVSTAPVA VASMTGMQAS PNVTGGTIPP
PPITRVTSNT SIAGSPMTPQ KLSRKSSVVQ TTALNAPVPV NPYAPPVTGR NAVQSPPLNP
YAPSGAHAAA PPTGTYSPHL AGQAIDHTHR ATPLSNMAAP PQKAMPGPPP KSMARKSTTS
EKDIDSANQL LSSIQKAPNG GPPPRKQVVA PQPSVHAASP VAEPVAIPPQ QQLIIEFFKE
ELARVTPLVP PEYNKQLKDC SKRLNILFTH IEKQDLLSAP TIEKLHTIVA LLREHKYSDA
LAVHVDIATN HVQEAGNWLT GVKRLIGLAE ATSS
