SEC31_DICDI
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 25-MAY-2022, entry version 119.
DE RecName: Full=Protein transport protein SEC31;
GN Name=sec31; ORFNames=DDB_G0270992;
OS Dictyostelium discoideum (Slime mold).
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.DDB0235185; -.
DR PaxDb; Q55CT5; -.
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; NRYAPAP; -.
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; 2.130.10.10; -; 1.
DR InterPro; IPR024298; ACE1_Sec16_Sec31.
DR InterPro; IPR040251; SEC31-like.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR13923; PTHR13923; 2.
DR Pfam; PF12931; Sec16_C; 1.
DR Pfam; PF00400; WD40; 2.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF50978; SSF50978; 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
