SEC31_PICST
ID SEC31_PICST Reviewed; 1244 AA.
AC A3GFK8;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2010, sequence version 2.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=Protein transport protein SEC31;
GN Name=SEC31; ORFNames=PICST_80311;
OS Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS Y-11545) (Yeast) (Pichia stipitis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX NCBI_TaxID=322104;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX PubMed=17334359; DOI=10.1038/nbt1290;
RA Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA Passoth V., Richardson P.M.;
RT "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT yeast Pichia stipitis.";
RL Nat. Biotechnol. 25:319-326(2007).
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; AAVQ01000001; EAZ63772.2; -; Genomic_DNA.
DR RefSeq; XP_001387795.2; XM_001387758.1.
DR AlphaFoldDB; A3GFK8; -.
DR SMR; A3GFK8; -.
DR STRING; 4924.XP_001387795.2; -.
DR EnsemblFungi; EAZ63772; EAZ63772; PICST_80311.
DR GeneID; 4851057; -.
DR KEGG; pic:PICST_80311; -.
DR eggNOG; KOG0307; Eukaryota.
DR HOGENOM; CLU_003033_2_0_1; -.
DR InParanoid; A3GFK8; -.
DR OMA; AQWAFGG; -.
DR OrthoDB; 100998at2759; -.
DR Proteomes; UP000002258; Chromosome 1.
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; 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; 2.
DR Pfam; PF07304; SRA1; 1.
DR Pfam; PF00400; WD40; 1.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 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..1244
FT /note="Protein transport protein SEC31"
FT /id="PRO_0000295445"
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 460..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 794..820
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 868..1007
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1066..1136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..490
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 794..815
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 868..886
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 923..937
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 960..974
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 988..1005
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1094..1124
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1244 AA; 132788 MW; 9D39ECDB9EBEA5C6 CRC64;
MVKISEIART STFAWSSDTL PILATGTVAG AVDASFNSSS SLELWDIFSA TNTNEPIFSA
AVEHRFYALA WSKPFEGRPR GLIAAAFENG VIEFWDAEVL IISKDLAKAS VHKSSKHSGP
VRSLQFNPLQ SHVLVSGGSH GQIFIWDTKK FTEPFSPGSA MTPMDEISSV AWNNSVSHIL
ASTGNSGYTS IWDLKSKREV LHLSYTGASG RANFSHVAWH PTKSTELITA SDNDACPLIL
TWDLRNSNAP EKILEGHKKG VLSLDWCQQD PELLISSGKD NTTFLWNPTT GQKLGEYPTT
ANWAFQTAFA PKVPDIFATA SFDGKIVVQS LQDTSPPVSE KVTSNDDNVF WNQLSTTDTQ
QPVFDIKQAP QWLKTPSAVS FGFGSKLVQV SKDSNGKSII NIQKFVAKGQ SSSSELYTAL
KNNNFKSIID EKISSNVASD LDKSDWKLLQ KLAESGKDEI LTEVTTEEEE KKPETEIESE
DKKNGDSEDV PASADDSFFD NLGNGKVVLE NEAPFVPSGS FKIFSAKVSE EDKSLIKLVL
GNKIEDAVHD CIERGKLLEA LVLALDASDD IKEKVKNAYF KKNVKKEVSR VLYSVSSQNI
TDIVSNANVA NWKEIAAGIT SFTNDPDDFN SKITELGDRI LESKTVADSR DTAIRCYLAG
NALDKIASIW LKELPALEAH LLESDNAENV SSPSEARLIA LTNFVSKIAA YRSISNISGE
ISGPSAEPIS KAIVEYTNLV AGNGEFELAN IFLQLLPSDL AGTEKDRINK ATGAVAAVTA
SKTVKSGTSA VANSVTAKTS KVSREVSSTP KPSYQATMPP IGAPLAPSAI PSASVPSSNP
YVRASNPYAP HVSSTNIYKP AAPVVQAPPP AQATAVSPPP TGPPKPVYKQ ETDGWNDLPD
TFKSKAPARR AAAVVTATPS PTPLPQTTVP PMSIPPGPKR SMSSGSAAPP PPKGSRANSK
VAVPTIQSSP RPAPVHVNNR YAPPPSADVN APSNTHSSPV GVSPSTKKNP YAVAPEVAPR
VAYAPPPASL SGLGFSGGAA APPAPPKNPY APSASSVISP RVSNAGIVPP PMGRGIVSPP
TSFGSMHAAP IQPAFSGVPP PPPAIGHQPA ASAPPPPPAA KTPVPTKSKY PKGDRSHIPE
KSVLIYQYLT KVLEAVKPNI PEKYTAHGED LEKRLNILFD HLNNEDLLTD DAIEDLKEVC
TALESKDIES ASSLNTSFAA NHIDQLGNWH RGITRLITMA EAMY
