SEC31_EMENI
ID SEC31_EMENI Reviewed; 1282 AA.
AC Q5AZM3; C8V1I6;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 2.
DT 25-MAY-2022, entry version 119.
DE RecName: Full=Protein transport protein sec31;
GN Name=sec31; ORFNames=AN6257;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAA58641.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AACD01000107; EAA58641.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BN001301; CBF69840.1; -; Genomic_DNA.
DR RefSeq; XP_663861.1; XM_658769.1.
DR AlphaFoldDB; Q5AZM3; -.
DR SMR; Q5AZM3; -.
DR STRING; 162425.CADANIAP00006734; -.
DR EnsemblFungi; CBF69840; CBF69840; ANIA_06257.
DR EnsemblFungi; EAA58641; EAA58641; AN6257.2.
DR GeneID; 2871160; -.
DR KEGG; ani:AN6257.2; -.
DR VEuPathDB; FungiDB:AN6257; -.
DR eggNOG; KOG0307; Eukaryota.
DR HOGENOM; CLU_003033_2_0_1; -.
DR InParanoid; Q5AZM3; -.
DR OMA; NRYAPAP; -.
DR OrthoDB; 100998at2759; -.
DR Proteomes; UP000000560; Chromosome I.
DR Proteomes; UP000005890; Unassembled WGS sequence.
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 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; 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..1282
FT /note="Protein transport protein sec31"
FT /id="PRO_0000295437"
FT REPEAT 7..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..407
FT /note="WD 8; interaction with sec13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221"
FT REGION 491..511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 801..845
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 906..1176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 803..818
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 938..952
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 969..987
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 988..1047
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1066..1084
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1098..1145
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1146..1160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1282 AA; 137706 MW; EC6ACB04265978DE CRC64;
MVRLREIPRT ATFAWSPGAA SPLIATGTRA GAVDADFSNE TCLELWDLAL GNEDAGAELQ
PVAKIDTDSG FNDLAWTDSE DNSRGIIAGG LESGSLGLWD ADKLLSGASD AVLSKSSKHS
GAIKALQFNP RHSSLLATGG AKGELYISDL NDLENPYRLG SSTARADDIE CLDWNKKVAH
ILVTGSSAGF VTVWDVKTRK ESLTLNNMGR KAVSAVAWDP TKPTKLVTAT PHESDPIINL
WDLRNSHAPE RTLRGHEAGV LSLSWCNQDP DLLLSSGKDN RTICWNPQTG ISYGEFPVVT
NWTFQTRWNP RNPNFFATAS FDGRISIQTI QNTSTETAKA VADQNQALDG EDFFAKAQSQ
PQVSSFSLPK APKWLERPCS STFGFGGRVV SVNLLEKGGR ASKIKITPFE VDEAVGKSTE
TFESALKEGD LKSICENRIT SAATEEEKSD WRVIDALLSD SPRKGLVEYL GFNDQAEDVS
EGLAKLGLSK EDEVNGEAAP KESRRPGARK HKRLQSMFDA SPDDNFLSDL AASKGAKTNN
PFQIFNGEES EADKNITRAL LLGDFEKALD HALKEDRMSD AFMIAIVGGQ KCIEKAQEHY
FSKQTESPNY VRLLASVVGK NLWDVVYNAD LSNWKEIMVA LCTFADEKDF ADLCDALGDR
LEEQIRNTGD KAIRKDASLC YLAGSKLEKV VSIWIEEQRE NEQAAIETAA EDSSFSIHVR
ALQSLIEKVT IFRQVTKFED SERTKDCDWK LSVLYDKYIE YADVVATHGR LQVAQKYLDL
VPEKHPEAEI ARNRIKLAMR QPTTRAQPAT STARVVSNKP LPQPAAYQPP TTFSAGARAA
TPTSYAPPAP AANPYAPPAA ASNPYAPPVA ASNPYAPTAA AANPYAPSAA APSQSTNPYA
PAGGSYAPAA GYQPRQQSFG APPPSVGGVP PPPRASSQSP ATVTTYTTAK NLPAWNDLPE
GFAKQPVSRR GTPASSAPIS SPFPNQSPAV SQGPPPAGAG PQRTPSVPPP PKGVPPPPRM
TSPPSAGQAP PNPLSAVPPP PANPYAAVPQ SPSVGSMAPP ASIPRGSSPY NAPPTIPPPS
NRYAPSPAAQ AASPQLQARA PVPPPPQAAA SPYAPPPPAQ PLAANPYAPS TPPPMQPPLQ
QVPPPQSAGS RPSTASSVKK ASPAPPKYPP GDRSHIPAEA RPIFEILSED MQRVKSRAPS
SFKAQVDDAE RRLNFLFDHL NNEDLLKPNT VQDMVQLARA IQARDYETAR TIHIDIMTNR
TDECGNWMVG VKRLISMSKV TP
