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