ID   SEC31_DICDI             Reviewed;        1355 AA.
AC   Q55CT5;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   27-MAR-2024, entry version 125.
DE   RecName: Full=Protein transport protein SEC31;
GN   Name=sec31; ORFNames=DDB_G0270992;
OS   Dictyostelium discoideum (Social amoeba).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
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 sar1A or sar1B.
CC       sec13 and sec31 make a 2:2 tetramer that forms the edge element of the
CC       COPII outer coat. The tetramer self-assembles in multiple copies to
CC       form the 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; AAFI02000005; EAL72846.1; -; Genomic_DNA.
DR   RefSeq; XP_646396.1; XM_641304.1.
DR   AlphaFoldDB; Q55CT5; -.
DR   SMR; Q55CT5; -.
DR   STRING; 44689.Q55CT5; -.
DR   PaxDb; 44689-DDB0235185; -.
DR   EnsemblProtists; EAL72846; EAL72846; DDB_G0270992.
DR   GeneID; 8617351; -.
DR   KEGG; ddi:DDB_G0270992; -.
DR   dictyBase; DDB_G0270992; sec31.
DR   eggNOG; KOG0307; Eukaryota.
DR   HOGENOM; CLU_254825_0_0_1; -.
DR   InParanoid; Q55CT5; -.
DR   OMA; WLERPCG; -.
DR   PhylomeDB; Q55CT5; -.
DR   Reactome; R-DDI-204005; COPII-mediated vesicle transport.
DR   PRO; PR:Q55CT5; -.
DR   Proteomes; UP000002195; Chromosome 1.
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:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; ISS:dictyBase.
DR   GO; GO:0006886; P:intracellular protein transport; ISS:dictyBase.
DR   Gene3D; 1.25.40.1030; -; 1.
DR   Gene3D; 1.20.940.10; Functional domain of the splicing factor Prp18; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR   InterPro; IPR024298; ACE1_Sec16_Sec31.
DR   InterPro; IPR040251; SEC31-like.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   InterPro; IPR001680; WD40_rpt.
DR   PANTHER; PTHR13923; SEC31-RELATED PROTEIN; 1.
DR   PANTHER; PTHR13923:SF11; SECRETORY 31, ISOFORM D; 1.
DR   Pfam; PF12931; Sec16_C; 1.
DR   Pfam; PF00400; WD40; 3.
DR   SMART; SM00320; WD40; 5.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 2.
DR   PROSITE; PS50082; WD_REPEATS_2; 3.
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..1355
FT                   /note="Protein transport protein SEC31"
FT                   /id="PRO_0000328076"
FT   REPEAT          5..48
FT                   /note="WD 1"
FT   REPEAT          65..109
FT                   /note="WD 2"
FT   REPEAT          127..167
FT                   /note="WD 3"
FT   REPEAT          175..215
FT                   /note="WD 4"
FT   REPEAT          220..263
FT                   /note="WD 5"
FT   REPEAT          267..307
FT                   /note="WD 6"
FT   REPEAT          334..374
FT                   /note="WD 7"
FT   REPEAT          412..463
FT                   /note="WD 8; interaction with sec13"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00221"
FT   REGION          108..127
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          311..338
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          558..585
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          602..632
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          898..1035
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1190..1255
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        112..127
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        564..582
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        602..630
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        898..921
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        922..936
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        937..1003
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1004..1035
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1190..1252
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1355 AA;  150127 MW;  885303FDEEB8959F CRC64;
     MSKLKEISRQ STTSWSPIAQ YPDYMAVGTV TGTIGADFDT SSKLEIYSLD ITNESKQMTL
     KGSTSSSTRF NKVVWGQASS NFQNGIIAGA MDNGTINLWD PTKILASDAT DGGGSDDQSS
     LIGVGQRHSG PVQSIDFNVQ NPNLLASGGS DSEVFIWDLS DPTQPSALNP GSKSQQSSDI
     TCVAWNKKVA HILGSASYNG YIVIWDLKSK KTLMTINDRN RKCKYRSIVW HPSEATQIVA
     ASEDDDHPVI QAWDLRNTTS PVKSMEGHKK GVWGLSWCPS DNALLLSTGK DNKTFCWNFD
     RQEILCEIND NNSRNNINNN SNNSNSDNNN GNTDPNAWNF EVQWSPRVPA LLSTSSYVGK
     VNVYSLQDVN EKSTSGSSAG QLNALGIQEQ TSQITPTIKH TPNWLLRPCG AAFGFGGKIA
     VFGRNKKVTA AANGATSPSS SSSPASSVQQ SQLQQQQRVI HISHVTTEVD IVKSSEQLEN
     VIHTGQYEQY CQEKIDQSTS DEEKSIWGFL KVKFAKDDRL KILDYLGYDI ETIKKELKQF
     LGTLPELPIE SGFNELPIEN VDDQSKPEPT TTTTNETVHL EPVVDENNNV VDADSFFDTA
     ASDANKEQQD DSSSSPSTKS PTTTTTPIEF PGDEKEQMIT KALLVGDHNS AVECCLRLGR
     YSDALILAHA AGQELWKKTQ EAYFEIVRSP FGRVVSCIVK RDFQLLVKSA DLKDWKASLA
     ILCTYAPPTD FKILSGILGD RLDKEASDLK SAILCYICAG DIDKTVDIWS RVSQQHQQQQ
     RQSLTSSGNS ITVLEQESNK DLQNLIEKVS IFRSACNGNS NNNTLNQVLS MKYAKYAEIL
     ASQGNLSASL RYLAPITNSQ CKQEYGVLFD RVYRATSNHQ GIPQPPFPFQ LVDVYSSNQP
     IQQQQQQQQN KAQQVGHQHQ HQHQHQNQHQ HQHQHQHQHQ PPQQQQQQQQ QQQMGRQNTF
     NQPPQPMGQH QHQQQQQQQQ PPIMMNQSPM QNNNNNRIPM MNQPPMMNQP PMMNQPPMMN
     QPPQMMNQPP QMMNQPPPQM MNQPPPQMMN NNQPPIMMRP MQPSGPSPMN PPPTMNNTQP
     PPMMNTMGGP SSVNNSQPPI IPMNGNPLPM NPMSPMMSDK SNQPPMNPMM NPMNPMNPMM
     NPIQPTAPPP MNPMIPQGGS PMINHPPPPM NPMINNGPVS TPPMNPMMNQ VVPQNISPPQ
     MPTRSPVLEN KSSSPSSESF TSPAPKPNVH NKTPSIITGQ LGVTTPSEGP SNEDTERFVE
     KLQRSIQELN GRTDSKVWED ANKRCQGLIN KVSKKDISAE AFKALDAILA SIVEKDFKKA
     SDTYIQITST PLWGEVGSQS MVGLKRLIDL GLKSH
//