SEC31_AJECA
ID SEC31_AJECA Reviewed; 1273 AA.
AC Q5S580;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=Protein transport protein SEC31;
GN Name=SEC31;
OS Ajellomyces capsulatus (Darling's disease fungus) (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=5037;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 255-270; 335-346 AND
RP 405-412.
RC STRAIN=ATCC 26032 / G217B;
RX PubMed=16479524; DOI=10.1086/500244;
RA Scheckelhoff M.R., Deepe G.S. Jr.;
RT "Pulmonary V beta 4+ T cells from Histoplasma capsulatum-infected mice
RT respond to a homologue of Sec31 that confers a protective response.";
RL J. Infect. Dis. 193:888-897(2006).
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; AY772719; AAV59730.1; -; mRNA.
DR AlphaFoldDB; Q5S580; -.
DR SMR; Q5S580; -.
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; 1.
DR Pfam; PF07304; SRA1; 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 1: Evidence at protein level;
KW Cytoplasmic vesicle; Direct protein sequencing; Endoplasmic reticulum;
KW ER-Golgi transport; Membrane; Protein transport; Repeat; Transport;
KW WD repeat.
FT CHAIN 1..1273
FT /note="Protein transport protein SEC31"
FT /id="PRO_0000295426"
FT REPEAT 5..47
FT /note="WD 1"
FT REPEAT 66..109
FT /note="WD 2"
FT REPEAT 118..158
FT /note="WD 3"
FT REPEAT 164..204
FT /note="WD 4"
FT REPEAT 208..251
FT /note="WD 5"
FT REPEAT 255..295
FT /note="WD 6"
FT REPEAT 298..338
FT /note="WD 7"
FT REPEAT 383..411
FT /note="WD 8; interaction with SEC13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221"
FT REGION 489..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 808..921
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 940..1168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 812..856
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 863..889
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 896..921
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 961..1007
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1015..1040
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1043..1115
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1127..1141
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1273 AA; 137698 MW; 63E51FE924029789 CRC64;
MVRLREIPRT AALAWSPGSA SPYIATGTRA GAVDADFSNE TDLELWDLAL EQEGGSAELQ
PAAKLSTESG FHDLAWTESE DSSRGIIAGA LENGSLDLWN ADKLLSGASD PLVSRASQHS
GPVKTLQFNP RHSNLLATGG SKGELFISDL NNIDHPFRLG NVNARLDDIE CLDWNKKVPH
ILVTGSSAGF VTVWDVKTKK ESLTLNNLGR KAVSAVAWDP EKPTKLITSI PLETDPLILV
WDLRNSNAPE RVLRGHESGV LSLSWCAQDP DLLLSSGKDN RTICWNPQTG VQYGEFPVVT
NWTFLTRWNP HNPNMFATAS FDGRISIQTI QNTKSDAIAQ AGASQVQPVD DEDFFAKAQS
QPQASTFSLP TAPKWLQRPS SVSFGFGGRV ISVGLTDPSK PASRTSKVRI TRFEVDSILS
STTQTFEEAL KAGDLRRICE TRIENAQNDS DRVDWKIIET LISDNPKMQL INYLGFSSEV
DETADSLSKL GLGKSEDGGA NGVPESDSRG PGVKKHKRLS SIFDTHADSD NFLTDLSASK
GAKTNNPFQI YTGSESEADR GITRALLLGD FEKALDICLQ EDRMSDAFMV AICGGQKCID
KAQEAYFQKQ LEGPNYLRLM AAIVGKNLWD IVHNAGLANW KEAIATICTF ATDAEFPDLC
ETLGDRLEEQ AKAEGDKESR KNAAFCFLAS SKLEKVVGIW IDELQENENK AIQEATNGET
SFSIHVRALQ NLIEKVTVFR HVTKFEDAET QKPSDWKLTL LYDKYIEYAD VAAAHGQLGV
AERYLDLLPQ AHPAAVVARN RIKLATEKTT ARSAPAHISA ASHLTTKPPQ QPNVPRGMYN
PSAPMTQANN LFKPPAPMQV SNPYAPTGAS SAYSPAGYQP SQQHQPTVPL GGPPQAFGTA
QQSNIAPPPR AANQSPSTVT SYTQATNLPA WNDLPEGFAK ALTPRRGTPS AAAATISSPF
PHQQPPQPSQ SPQTISPHQP PPPRQRTSMA VPPPPRGPAP PRMTSPPAVG QPHGFPSTRK
TSLNFKCIYP TTQHTPTGPG MNVPQIPRGP SPYNAPPTGP PPSNRYAPSP AAQPSAPQPP
RAAVAAPPPT GPPAPAPAQS PYSYQHPPPA HGSYAPPSAP TGARPDHQPQ HQPPPPGSSP
VSRPGTAQSQ RKPAPAAKYP PGDRSHIPAN AQPIFEILSA DMQRVKARAP TSFKAQVNDA
ERRLNILFDH LNNEDLLKPA TVESMAELAR ALQARDYETA QSIHLDIFTN RNDECGNWMV
GVKRLIGMSR ATP
