SEC12_YEAST
ID SEC12_YEAST Reviewed; 471 AA.
AC P11655; D6W1K0;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Guanine nucleotide-exchange factor SEC12;
DE AltName: Full=Protein transport protein SEC12;
GN Name=SEC12; Synonyms=SED2; OrderedLocusNames=YNR026C; ORFNames=N3244;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=3047151; DOI=10.1083/jcb.107.3.851;
RA Nakano A., Brada D., Schekman R.W.;
RT "A membrane glycoprotein, Sec12p, required for protein transport from the
RT endoplasmic reticulum to the Golgi apparatus in yeast.";
RL J. Cell Biol. 107:851-863(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP FUNCTION.
RX PubMed=6996832; DOI=10.1016/0092-8674(80)90128-2;
RA Novick P., Field C., Schekman R.W.;
RT "Identification of 23 complementation groups required for post-
RT translational events in the yeast secretory pathway.";
RL Cell 21:205-215(1980).
RN [5]
RP FUNCTION.
RX PubMed=2512296; DOI=10.1083/jcb.109.6.2677;
RA Nakano A., Muramatsu M.-A.;
RT "A novel GTP-binding protein, Sar1p, is involved in transport from the
RT endoplasmic reticulum to the Golgi apparatus.";
RL J. Cell Biol. 109:2677-2691(1989).
RN [6]
RP FUNCTION.
RX PubMed=1649197; DOI=10.1083/jcb.114.2.219;
RA Rexach M.F., Schekman R.W.;
RT "Distinct biochemical requirements for the budding, targeting, and fusion
RT of ER-derived transport vesicles.";
RL J. Cell Biol. 114:219-229(1991).
RN [7]
RP FUNCTION.
RX PubMed=1907973; DOI=10.1083/jcb.114.4.663;
RA d'Enfert C., Wuestehube L.J., Lila T., Schekman R.W.;
RT "Sec12p-dependent membrane binding of the small GTP-binding protein Sar1p
RT promotes formation of transport vesicles from the ER.";
RL J. Cell Biol. 114:663-670(1991).
RN [8]
RP FUNCTION.
RX PubMed=1907974; DOI=10.1083/jcb.114.4.671;
RA Oka T., Nishikawa S., Nakano A.;
RT "Reconstitution of GTP-binding Sar1 protein function in ER to Golgi
RT transport.";
RL J. Cell Biol. 114:671-679(1991).
RN [9]
RP FUNCTION, TOPOLOGY, AND GLYCOSYLATION.
RX PubMed=1922074; DOI=10.1128/mcb.11.11.5727-5734.1991;
RA d'Enfert C., Barlowe C., Nishikawa S., Nakano A., Schekman R.W.;
RT "Structural and functional dissection of a membrane glycoprotein required
RT for vesicle budding from the endoplasmic reticulum.";
RL Mol. Cell. Biol. 11:5727-5734(1991).
RN [10]
RP FUNCTION.
RX PubMed=1327759; DOI=10.1002/j.1460-2075.1992.tb05512.x;
RA Hardwick K.G., Boothroyd J.C., Rudner A.D., Pelham H.R.B.;
RT "Genes that allow yeast cells to grow in the absence of the HDEL
RT receptor.";
RL EMBO J. 11:4187-4195(1992).
RN [11]
RP FUNCTION.
RX PubMed=8377826; DOI=10.1038/365347a0;
RA Barlowe C., Schekman R.W.;
RT "SEC12 encodes a guanine-nucleotide-exchange factor essential for transport
RT vesicle budding from the ER.";
RL Nature 365:347-349(1993).
RN [12]
RP SUBCELLULAR LOCATION.
RX PubMed=8367481; DOI=10.1073/pnas.90.17.8179;
RA Nishikawa S., Nakano A.;
RT "Identification of a gene required for membrane protein retention in the
RT early secretory pathway.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:8179-8183(1993).
RN [13]
RP FUNCTION.
RX PubMed=8106544; DOI=10.1083/jcb.124.4.425;
RA Oka T., Nakano A.;
RT "Inhibition of GTP hydrolysis by Sar1p causes accumulation of vesicles that
RT are a functional intermediate of the ER-to-Golgi transport in yeast.";
RL J. Cell Biol. 124:425-434(1994).
RN [14]
RP FUNCTION.
RX PubMed=7865879; DOI=10.1091/mbc.5.10.1129;
RA Nishikawa S., Hirata A., Nakano A.;
RT "Inhibition of endoplasmic reticulum (ER)-to-Golgi transport induces
RT relocalization of binding protein (BiP) within the ER to form the BiP
RT bodies.";
RL Mol. Biol. Cell 5:1129-1143(1994).
RN [15]
RP FUNCTION.
RX PubMed=8583945; DOI=10.1016/s0076-6879(95)57015-2;
RA Barlowe C., Schekman R.W.;
RT "Expression, purification, and assay of Sec12p: a Sar1p-specific GDP
RT dissociation stimulator.";
RL Methods Enzymol. 257:98-106(1995).
RN [16]
RP SUBCELLULAR LOCATION.
RX PubMed=8589449; DOI=10.1091/mbc.6.11.1459;
RA Sato K., Nishikawa S., Nakano A.;
RT "Membrane protein retrieval from the Golgi apparatus to the endoplasmic
RT reticulum (ER): characterization of the RER1 gene product as a component
RT involved in ER localization of Sec12p.";
RL Mol. Biol. Cell 6:1459-1477(1995).
RN [17]
RP SUBCELLULAR LOCATION.
RX PubMed=8707815; DOI=10.1083/jcb.134.2.279;
RA Sato M., Sato K., Nakano A.;
RT "Endoplasmic reticulum localization of Sec12p is achieved by two
RT mechanisms: Rer1p-dependent retrieval that requires the transmembrane
RT domain and Rer1p-independent retention that involves the cytoplasmic
RT domain.";
RL J. Cell Biol. 134:279-293(1996).
RN [18]
RP SUBCELLULAR LOCATION.
RX PubMed=9152025; DOI=10.1242/jcs.110.8.991;
RA Boehm J., Letourneur F., Ballensiefen W., Ossipov D., Demolliere C.,
RA Schmitt H.D.;
RT "Sec12p requires Rer1p for sorting to coatomer (COPI)-coated vesicles and
RT retrieval to the ER.";
RL J. Cell Sci. 110:991-1003(1997).
RN [19]
RP FUNCTION.
RX PubMed=9023343; DOI=10.1073/pnas.94.3.837;
RA Campbell J.L., Schekman R.W.;
RT "Selective packaging of cargo molecules into endoplasmic reticulum-derived
RT COPII vesicles.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:837-842(1997).
RN [20]
RP SUBCELLULAR LOCATION.
RX PubMed=9275186; DOI=10.1073/pnas.94.18.9693;
RA Sato K., Sato M., Nakano A.;
RT "Rer1p as common machinery for the endoplasmic reticulum localization of
RT membrane proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:9693-9698(1997).
RN [21]
RP SUBCELLULAR LOCATION.
RX PubMed=10189369; DOI=10.1083/jcb.145.1.69;
RA Rossanese O.W., Soderholm J., Bevis B.J., Sears I.B., O'Connor J.,
RA Williamson E.K., Glick B.S.;
RT "Golgi structure correlates with transitional endoplasmic reticulum
RT organization in Pichia pastoris and Saccharomyces cerevisiae.";
RL J. Cell Biol. 145:69-81(1999).
RN [22]
RP FUNCTION.
RX PubMed=11694599; DOI=10.1091/mbc.12.11.3690;
RA Ishihara N., Hamasaki M., Yokota S., Suzuki K., Kamada Y., Kihara A.,
RA Yoshimori T., Noda T., Ohsumi Y.;
RT "Autophagosome requires specific early Sec proteins for its formation and
RT NSF/SNARE for vacuolar fusion.";
RL Mol. Biol. Cell 12:3690-3702(2001).
RN [23]
RP DOMAIN.
RX PubMed=12163183; DOI=10.1016/s0014-5793(02)03068-5;
RA Chardin P., Callebaut I.;
RT "The yeast Sar exchange factor Sec12, and its higher organism orthologs,
RT fold as beta-propellers.";
RL FEBS Lett. 525:171-173(2002).
RN [24]
RP FUNCTION.
RX PubMed=12655150; DOI=10.1247/csf.28.49;
RA Hamasaki M., Noda T., Ohsumi Y.;
RT "The early secretory pathway contributes to autophagy in yeast.";
RL Cell Struct. Funct. 28:49-54(2003).
RN [25]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [26]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [27]
RP FUNCTION.
RX PubMed=16413259; DOI=10.1016/s0076-6879(05)04008-5;
RA Futai E., Schekman R.W.;
RT "Purification and functional properties of yeast Sec12 GEF.";
RL Methods Enzymol. 404:74-82(2005).
CC -!- FUNCTION: Guanine nucleotide-exchange factor (GEF) required for the
CC formation or budding of transport vesicles from the ER. This function
CC involves the cytoplasmic domain of the protein, which is thought to
CC interact with the small GTP-binding protein SAR1. Required for
CC autophagy. {ECO:0000269|PubMed:11694599, ECO:0000269|PubMed:12655150,
CC ECO:0000269|PubMed:1327759, ECO:0000269|PubMed:16413259,
CC ECO:0000269|PubMed:1649197, ECO:0000269|PubMed:1907973,
CC ECO:0000269|PubMed:1907974, ECO:0000269|PubMed:1922074,
CC ECO:0000269|PubMed:2512296, ECO:0000269|PubMed:3047151,
CC ECO:0000269|PubMed:6996832, ECO:0000269|PubMed:7865879,
CC ECO:0000269|PubMed:8106544, ECO:0000269|PubMed:8377826,
CC ECO:0000269|PubMed:8583945, ECO:0000269|PubMed:9023343}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type
CC II membrane protein. Golgi apparatus, cis-Golgi network membrane;
CC Single-pass type II membrane protein. Note=Cycling between endoplasmic
CC reticulum and the early Golgi.
CC -!- MISCELLANEOUS: In the process of transport, SEC12 itself may migrate to
CC the Golgi apparatus and function in subsequent transport events.
CC -!- MISCELLANEOUS: Present with 6160 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the WD repeat SEC12 family. {ECO:0000305}.
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DR EMBL; X13161; CAA31559.1; -; Genomic_DNA.
DR EMBL; Z71641; CAA96306.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10566.1; -; Genomic_DNA.
DR PIR; A31103; A31103.
DR RefSeq; NP_014423.1; NM_001183203.1.
DR PDB; 4H5I; X-ray; 1.36 A; A/B=1-354.
DR PDB; 4H5J; X-ray; 2.60 A; A/B=1-354.
DR PDB; 6X90; X-ray; 2.26 A; B=1-354.
DR PDBsum; 4H5I; -.
DR PDBsum; 4H5J; -.
DR PDBsum; 6X90; -.
DR AlphaFoldDB; P11655; -.
DR SMR; P11655; -.
DR BioGRID; 35850; 744.
DR DIP; DIP-7541N; -.
DR IntAct; P11655; 2.
DR MINT; P11655; -.
DR STRING; 4932.YNR026C; -.
DR MaxQB; P11655; -.
DR PaxDb; P11655; -.
DR PRIDE; P11655; -.
DR EnsemblFungi; YNR026C_mRNA; YNR026C; YNR026C.
DR GeneID; 855760; -.
DR KEGG; sce:YNR026C; -.
DR SGD; S000005309; SEC12.
DR VEuPathDB; FungiDB:YNR026C; -.
DR eggNOG; KOG0771; Eukaryota.
DR GeneTree; ENSGT00390000000916; -.
DR HOGENOM; CLU_033006_0_0_1; -.
DR InParanoid; P11655; -.
DR OMA; KAHEFPP; -.
DR BioCyc; YEAST:G3O-33339-MON; -.
DR Reactome; R-SCE-204005; COPII-mediated vesicle transport.
DR PRO; PR:P11655; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P11655; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR GO; GO:0005794; C:Golgi apparatus; IDA:SGD.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:SGD.
DR GO; GO:0009306; P:protein secretion; IBA:GO_Central.
DR GO; GO:0003400; P:regulation of COPII vesicle coating; IDA:SGD.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR045260; Sec12-like.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR PANTHER; PTHR23284; PTHR23284; 1.
DR SMART; SM00320; WD40; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Endoplasmic reticulum; ER-Golgi transport; Glycoprotein;
KW Golgi apparatus; GTPase activation; Membrane; Protein transport;
KW Reference proteome; Repeat; Signal-anchor; Transmembrane;
KW Transmembrane helix; Transport; WD repeat.
FT CHAIN 1..471
FT /note="Guanine nucleotide-exchange factor SEC12"
FT /id="PRO_0000097657"
FT TOPO_DOM 1..354
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:1922074"
FT TRANSMEM 355..373
FT /note="Helical; Signal-anchor for type II membrane protein"
FT TOPO_DOM 374..471
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:1922074"
FT REPEAT 259..300
FT /note="WD 1"
FT REPEAT 302..341
FT /note="WD 2"
FT CARBOHYD 439
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 462
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT STRAND 5..9
FT /evidence="ECO:0007829|PDB:4H5I"
FT STRAND 14..21
FT /evidence="ECO:0007829|PDB:4H5I"
FT STRAND 24..30
FT /evidence="ECO:0007829|PDB:4H5I"
FT STRAND 33..37
FT /evidence="ECO:0007829|PDB:4H5I"
FT STRAND 40..47
FT /evidence="ECO:0007829|PDB:4H5I"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:4H5I"
FT HELIX 54..57
FT /evidence="ECO:0007829|PDB:4H5I"
FT STRAND 58..65
FT /evidence="ECO:0007829|PDB:4H5I"
FT STRAND 75..79
FT /evidence="ECO:0007829|PDB:4H5I"
FT STRAND 82..86
FT /evidence="ECO:0007829|PDB:4H5I"
FT HELIX 91..96
FT /evidence="ECO:0007829|PDB:4H5I"
FT STRAND 103..109
FT /evidence="ECO:0007829|PDB:4H5I"
FT TURN 110..113
FT /evidence="ECO:0007829|PDB:4H5I"
FT STRAND 114..121
FT /evidence="ECO:0007829|PDB:4H5I"
FT STRAND 133..138
FT /evidence="ECO:0007829|PDB:4H5I"
FT STRAND 145..150
FT /evidence="ECO:0007829|PDB:4H5I"
FT STRAND 155..160
FT /evidence="ECO:0007829|PDB:4H5I"
FT TURN 161..164
FT /evidence="ECO:0007829|PDB:4H5I"
FT STRAND 165..171
FT /evidence="ECO:0007829|PDB:4H5I"
FT STRAND 178..181
FT /evidence="ECO:0007829|PDB:4H5I"
FT STRAND 185..191
FT /evidence="ECO:0007829|PDB:4H5I"
FT STRAND 196..200
FT /evidence="ECO:0007829|PDB:4H5I"
FT TURN 201..203
FT /evidence="ECO:0007829|PDB:4H5I"
FT STRAND 206..210
FT /evidence="ECO:0007829|PDB:4H5I"
FT STRAND 217..226
FT /evidence="ECO:0007829|PDB:4H5I"
FT STRAND 229..239
FT /evidence="ECO:0007829|PDB:4H5I"
FT STRAND 242..250
FT /evidence="ECO:0007829|PDB:4H5I"
FT STRAND 253..265
FT /evidence="ECO:0007829|PDB:4H5I"
FT STRAND 269..274
FT /evidence="ECO:0007829|PDB:4H5I"
FT STRAND 280..285
FT /evidence="ECO:0007829|PDB:4H5I"
FT STRAND 290..294
FT /evidence="ECO:0007829|PDB:4H5I"
FT TURN 295..298
FT /evidence="ECO:0007829|PDB:4H5I"
FT STRAND 299..304
FT /evidence="ECO:0007829|PDB:4H5I"
FT STRAND 307..310
FT /evidence="ECO:0007829|PDB:4H5I"
FT STRAND 312..317
FT /evidence="ECO:0007829|PDB:4H5I"
FT STRAND 323..328
FT /evidence="ECO:0007829|PDB:4H5I"
FT STRAND 331..337
FT /evidence="ECO:0007829|PDB:4H5I"
FT TURN 340..343
FT /evidence="ECO:0007829|PDB:4H5I"
SQ SEQUENCE 471 AA; 51608 MW; DD4CEED041E776C3 CRC64;
MKFVTASYNV GYPAYGAKFL NNDTLLVAGG GGEGNNGIPN KLTVLRVDPT KDTEKEQFHI
LSEFALEDND DSPTAIDASK GIILVGCNEN STKITQGKGN KHLRKFKYDK VNDQLEFLTS
VDFDASTNAD DYTKLVYISR EGTVAAIASS KVPAIMRIID PSDLTEKFEI ETRGEVKDLH
FSTDGKVVAY ITGSSLEVIS TVTGSCIARK TDFDKNWSLS KINFIADDTV LIAASLKKGK
GIVLTKISIK SGNTSVLRSK QVTNRFKGIT SMDVDMKGEL AVLASNDNSI ALVKLKDLSM
SKIFKQAHSF AITEVTISPD STYVASVSAA NTIHIIKLPL NYANYTSMKQ KISKFFTNFI
LIVLLSYILQ FSYKHNLHSM LFNYAKDNFL TKRDTISSPY VVDEDLHQTT LFGNHGTKTS
VPSVDSIKVH GVHETSSVNG TEVLCTESNI INTGGAEFEI TNATFREIDD A
