SEC31_COCIM
ID SEC31_COCIM Reviewed; 1261 AA.
AC Q1DX43; A0A0D8JUX1; I9NNL8;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Protein transport protein SEC31;
GN Name=SEC31; ORFNames=CIMG_05120;
OS Coccidioides immitis (strain RS) (Valley fever fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=246410;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RS;
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=RS;
RX PubMed=20516208; DOI=10.1101/gr.103911.109;
RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA Taylor J.W., Rounsley S.D.;
RT "Population genomic sequencing of Coccidioides fungi reveals recent
RT hybridization and transposon control.";
RL Genome Res. 20:938-946(2010).
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; GG704914; KJF61105.1; -; Genomic_DNA.
DR RefSeq; XP_004446159.1; XM_004446102.1.
DR AlphaFoldDB; Q1DX43; -.
DR SMR; Q1DX43; -.
DR STRING; 246410.Q1DX43; -.
DR PRIDE; Q1DX43; -.
DR EnsemblFungi; KJF61105; KJF61105; CIMG_05120.
DR GeneID; 4563783; -.
DR KEGG; cim:CIMG_05120; -.
DR VEuPathDB; FungiDB:CIMG_05120; -.
DR InParanoid; Q1DX43; -.
DR OrthoDB; 100998at2759; -.
DR Proteomes; UP000001261; 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; 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 SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
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..1261
FT /note="Protein transport protein SEC31"
FT /id="PRO_0000295435"
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 382..406
FT /note="WD 8; interaction with SEC13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221"
FT REGION 797..1156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 846..883
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 884..906
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 947..970
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 971..1000
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1035..1062
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1063..1077
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1078..1128
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1261 AA; 136350 MW; 858D478D1629DCDA CRC64;
MVRLREIPRT ATFTWSPGSA APFIATGTRA GAVDADFSNE TFLELWNLDL DNDKLGQELE
PVAKISTESG FHDIAWAESE DHTRGVIAGA LENGSLDLWD ADKLLNGASD ALISSASKHT
GPIKALQFNP RHSNLLATGG GKGELFISDL NNVDQAFRLG SGAARVDDIE CLDWNKKVPH
ILVTGSSAGF VTVWDVKTKK ESLTLNNLGR KAVSAVAWDP EKPTKLITSI PLETDPLILV
WDLRNSNAPE RVLRGHESGV LSLSWCAQDP DLLLSCGKDN RTICWNPQTG NAYGEFPVVT
NWTFQTRWNP HNPNMFATAS FDGKIVVQTI QNTRQDASQA GNNQEQAVND EDFFAKAQTR
PQISTFSLPK APKWLERPVT ASFGFGGRVV SAGLSSGSRS SKITISHFDV DPNVGSATEN
FESSVKTGDF RGICESRIAS SQCEEEKTDW KVIETLLSDN PRKQLVNYLG FSNEVDEAAD
SLSKLGLDKK EANGEGQLSP KSEGVKKHKR ITSIFETNVE GESFLDEIAS SKGAKTNNPF
QIYTGSESEA DRAITRALLL GQFEKALDVC LQEDRMSDAF MVAVCGGQKC IEKAQEAYFS
KQSEGPSFVR LLASVVGKNL WDVVHNAGLA NWKEAIAAIC TFADDKEFPD LCEALGDRLE
ESYRSKKAKQ ARKDASFCYL ASSKLEKVVS IWIQELKENE AYSIQNATDD TSFSIHVRAL
QSFIEKVTVF RHVSKFQDPE RQKSSDWKLS SLYEKYLEYA DVVASHGRLD VAEKYLDLLP
ASYPEAEVAR SRIQFATKKP ASKAATGRAP APRHPPTAPT LTGTFQPAQI PTHKGPAPGS
VNQFAPPALS KPTNPYAPTT TTSYTSAGGT TYTPTTGYQP PQPRQSNVIP PPQPLAPPPQ
SGPAGLAPPP RASSQSPSVA APYTRATNIP AWNDLPEGFG RAATPRRSTP VTGSSVISSP
FPNTPSLTQP GSHTSPPPST MPAPRDSVPP PPPKGPAPPR MASPSTAGIP HGLQPAERPP
SRTHVYSPPL AQQTSPGMAV PPPIPRGPSP YNAPPTVPPP TNRYAPAQVS QPTGQLHGQP
PIAPPPHSSM PPPPGPYAPQ PFQQAPAQSP YAPPPTGPQA PPPPVSQQGS RPSTAQSQKK
APPAQKYPPG DRSHIPANAQ PIYEILSSDM QRVKARAPAA FKAQVNDTER RLNILFDHLN
NEDLLQPSTI ESMAELAHAI QVKDYETAQA IHLDILTNKT DECGNWMVGV KRLIGMSRAT
P