SED4_YEAST
ID SED4_YEAST Reviewed; 1065 AA.
AC P25365; D6VR70;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Putative guanine nucleotide-exchange factor SED4;
GN Name=SED4; OrderedLocusNames=YCR067C; ORFNames=YCR67C, YCR901;
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 CHARACTERIZATION.
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1574125; DOI=10.1038/357038a0;
RA Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
RA Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
RA Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
RA Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
RA Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
RA Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
RA Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F.,
RA Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C.,
RA Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E.,
RA Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P.,
RA Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J.,
RA Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P.,
RA Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
RA Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
RA Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
RA Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
RA Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
RA Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
RA Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
RA Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M.,
RA Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A.,
RA Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
RA Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J.,
RA Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I.,
RA Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M.,
RA Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M.,
RA Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D.,
RA Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K.,
RA Sgouros J.G.;
RT "The complete DNA sequence of yeast chromosome III.";
RL Nature 357:38-46(1992).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 446-1065.
RX PubMed=1561837; DOI=10.1002/yea.320080209;
RA Benit P., Chanet R., Fabre F., Faye G., Fukuhara H., Sor F.;
RT "Sequence of the sup61-RAD18 region on chromosome III of Saccharomyces
RT cerevisiae.";
RL Yeast 8:147-153(1992).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, GLYCOSYLATION, AND INTERACTION WITH SEC16.
RX PubMed=7593162; DOI=10.1083/jcb.131.2.325;
RA Gimeno R.E., Espenshade P.J., Kaiser C.A.;
RT "SED4 encodes a yeast endoplasmic reticulum protein that binds Sec16p and
RT participates in vesicle formation.";
RL J. Cell Biol. 131:325-338(1995).
RN [7]
RP FUNCTION.
RX PubMed=9880808; DOI=10.1093/oxfordjournals.jbchem.a022249;
RA Saito Y., Yamanushi T., Oka T., Nakano A.;
RT "Identification of SEC12, SED4, truncated SEC16, and EKS1/HRD3 as multicopy
RT suppressors of ts mutants of Sar1 GTPase.";
RL J. Biochem. 125:130-137(1999).
RN [8]
RP FUNCTION.
RX PubMed=11168590; DOI=10.1046/j.1365-2443.2000.00391.x;
RA Saito-Nakano Y., Nakano A.;
RT "Sed4p functions as a positive regulator of Sar1p probably through
RT inhibition of the GTPase activation by Sec23p.";
RL Genes Cells 5:1039-1048(2000).
RN [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
CC -!- FUNCTION: Putative guanine nucleotide-exchange factor (GEF) involved in
CC the formation or budding of transport vesicles from the ER. Positive
CC regulator of SAR1 probably through inhibition of the GTPase activation
CC by SEC23. {ECO:0000269|PubMed:11168590, ECO:0000269|PubMed:7593162,
CC ECO:0000269|PubMed:9880808}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type
CC II membrane protein. Golgi apparatus membrane {ECO:0000305}; Single-
CC pass type II membrane protein {ECO:0000305}. Note=In the process of
CC transport, SED4 itself may migrate to the Golgi apparatus and function
CC in subsequent transport events.
CC -!- SIMILARITY: Belongs to the WD repeat SEC12 family. {ECO:0000305}.
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DR EMBL; X59720; CAA42273.1; -; Genomic_DNA.
DR EMBL; AY693176; AAT93195.1; -; Genomic_DNA.
DR EMBL; BK006937; DAA07539.1; -; Genomic_DNA.
DR PIR; S19482; S19482.
DR RefSeq; NP_009993.1; NM_001178778.1.
DR AlphaFoldDB; P25365; -.
DR SMR; P25365; -.
DR BioGRID; 31043; 107.
DR DIP; DIP-1173N; -.
DR IntAct; P25365; 2.
DR MINT; P25365; -.
DR STRING; 4932.YCR067C; -.
DR iPTMnet; P25365; -.
DR MaxQB; P25365; -.
DR PaxDb; P25365; -.
DR PRIDE; P25365; -.
DR EnsemblFungi; YCR067C_mRNA; YCR067C; YCR067C.
DR GeneID; 850431; -.
DR KEGG; sce:YCR067C; -.
DR SGD; S000000663; SED4.
DR VEuPathDB; FungiDB:YCR067C; -.
DR eggNOG; KOG0771; Eukaryota.
DR GeneTree; ENSGT00390000000916; -.
DR HOGENOM; CLU_301307_0_0_1; -.
DR InParanoid; P25365; -.
DR OMA; NETSTRD; -.
DR BioCyc; YEAST:G3O-29370-MON; -.
DR PRO; PR:P25365; -.
DR Proteomes; UP000002311; Chromosome III.
DR RNAct; P25365; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:SGD.
DR GO; GO:0005096; F:GTPase activator activity; IDA:SGD.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0043547; P:positive regulation of GTPase 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 InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR23284; PTHR23284; 1.
DR Pfam; PF00400; WD40; 1.
DR SMART; SM00320; WD40; 2.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00014; ER_TARGET; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; ER-Golgi transport; Glycoprotein; Golgi apparatus;
KW GTPase activation; Membrane; Phosphoprotein; Protein transport;
KW Reference proteome; Repeat; Signal-anchor; Transmembrane;
KW Transmembrane helix; Transport; WD repeat.
FT CHAIN 1..1065
FT /note="Putative guanine nucleotide-exchange factor SED4"
FT /id="PRO_0000051211"
FT TOPO_DOM 1..346
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 347..365
FT /note="Helical; Signal-anchor for type II membrane protein"
FT TOPO_DOM 366..1065
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REPEAT 259..298
FT /note="WD 1"
FT REPEAT 302..341
FT /note="WD 2"
FT REPEAT 824..833
FT /note="1"
FT REPEAT 834..843
FT /note="2"
FT REPEAT 844..853
FT /note="3"
FT REPEAT 854..863
FT /note="4"
FT REGION 458..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 482..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 551..625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 824..863
FT /note="4 X 10 AA tandem repeats"
FT MOTIF 1062..1065
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT COMPBIAS 482..500
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 561..625
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CARBOHYD 388
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 620
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1039
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1065 AA; 114079 MW; 0F1DAE0D428085A8 CRC64;
MSGNSANYDV GYPIYGAKFI NEGTLLVAGG GGQFNSSFPN KITALKVNFQ KKKHIRRFRE
ITLDSIDDAP TSLDCNNNLI LVGCNELFND SSMENVNHHL RKFVFEQEHL KFVASIDFNR
TTDPSVFTKF VYINQRATVA AIASSEVPTV IRIIDPRNLT ENYEIETGRE VNDLHFAPNG
ILLSYITSNS LEVASVRDGN FVARKTDFDK NLVLSNIRFL NDNTLLVAAS LSNSDGVSLL
KLGVSSKGVK ILKTASFMFD LNGITSMDVS PNKKFVALSS NDNLVAIVSV EKLKLVQLVP
RVHESTITKV TFSPDSRYLA STSMGNTINV LKLSGTSSSI LRNIWKFFLN FVLLVVLAGA
IQLGYKHNVH GFIYKHAHDI YKSKFKENTT IDQGSSSYFT INDDYRGITE SADIISATDV
ASDIETEFSS FDTSTMRTTT EDEQKFVWIS SSADSQFTSA DIPTSASSSS SSSSSSFYEE
SVTNEPIVSS PTSEITKPLA SPTEPNIVEK PSLPLNSESI DLLSSSSNSI TEYPEPTPDL
EEKLSSLIVE QSESEITTDR ESVSKLLSTE SPSLSHMPSS SSSSLSLSSS LTTSPTTALS
TSTATAVTTT QTNPTNDAAN TSFLDNSKPA STREIYKTKI ITEVITKIEY RNIPASDSNA
EAEQYVTTSS SMLLTPTDTM VSSPVSEIDP IASELERMVE TPTHSISIAS EFDSVASNLI
PNEEILSTSA SQDSISSHPS TFSDSSITSG FQSIEVSTVT SSVLASESIP SISDSTFSKF
HSISEPVSSA IVETATSSFS KTETKTSRVI AFSTEDSERS SALIDNSEYT SVLADNLEPT
SVLADNSEPT SVLADSSEPT SVFTDAVQSP KTSVGQSSLS ESTNIEGTSM ASMIFSSSGA
SIGALSDIGK GTLSVESASS TVAQPMPGVT TTAPSFVSSP HKISASSIDA SGFVQKEIMI
EVQSSKDSSE AFGVRHKISE NVNTPVSRML TTEMQASGTV DVTEDVSLSS EVISALNVEI
TSLPNPVAPP QTIAAPLNNN SNTNIVNDDN AVAGTVNYAG LHDEL
