SEY1_YEAST
ID SEY1_YEAST Reviewed; 776 AA.
AC Q99287; D6W2M3;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Protein SEY1 {ECO:0000255|HAMAP-Rule:MF_03109};
DE EC=3.6.5.- {ECO:0000255|HAMAP-Rule:MF_03109};
DE AltName: Full=Synthetic enhancer of YOP1 protein {ECO:0000255|HAMAP-Rule:MF_03109};
GN Name=SEY1 {ECO:0000255|HAMAP-Rule:MF_03109}; OrderedLocusNames=YOR165W;
GN ORFNames=O3590;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=S288c / FY1678;
RX PubMed=8972579;
RX DOI=10.1002/(sici)1097-0061(199612)12:15<1563::aid-yea44>3.0.co;2-m;
RA Madania A., Poch O., Tarassov I.A., Winsor B., Martin R.P.;
RT "Analysis of a 22,956 bp region on the right arm of Saccharomyces
RT cerevisiae chromosome XV.";
RL Yeast 12:1563-1573(1996).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [4]
RP INDUCTION.
RX PubMed=11292078; DOI=10.1023/a:1006460231978;
RA Shen Q., Chen C.-N., Brands A., Pan S.-M., Ho T.-H.D.;
RT "The stress- and abscisic acid-induced barley gene HVA22: developmental
RT regulation and homologues in diverse organisms.";
RL Plant Mol. Biol. 45:327-340(2001).
RN [5]
RP FUNCTION.
RX PubMed=12427979; DOI=10.1104/pp.007716;
RA Brands A., Ho T.-H.D.;
RT "Function of a plant stress-induced gene, HVA22. Synthetic enhancement
RT screen with its yeast homolog reveals its role in vesicular traffic.";
RL Plant Physiol. 130:1121-1131(2002).
RN [6]
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 [7]
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 [8]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RTN1 AND YOP1, AND
RP MUTAGENESIS OF LYS-50.
RX PubMed=19665976; DOI=10.1016/j.cell.2009.05.025;
RA Hu J., Shibata Y., Zhu P.-P., Voss C., Rismanchi N., Prinz W.A.,
RA Rapoport T.A., Blackstone C.;
RT "A class of dynamin-like GTPases involved in the generation of the tubular
RT ER network.";
RL Cell 138:549-561(2009).
CC -!- FUNCTION: Cooperates with the reticulon proteins RTN1 and RTN2 and the
CC tubule-shaping DP1 family protein YOP1 to generate and maintain the
CC structure of the tubular endoplasmic reticulum network. Has GTPase
CC activity, which is required for its function in ER organization.
CC {ECO:0000255|HAMAP-Rule:MF_03109, ECO:0000269|PubMed:12427979,
CC ECO:0000269|PubMed:19665976}.
CC -!- SUBUNIT: Interacts with RTN1 and YOP1; GTP binding is not required for
CC these interactions. {ECO:0000255|HAMAP-Rule:MF_03109,
CC ECO:0000269|PubMed:19665976}.
CC -!- INTERACTION:
CC Q99287; Q04947: RTN1; NbExp=3; IntAct=EBI-37523, EBI-38020;
CC Q99287; Q12402: YOP1; NbExp=2; IntAct=EBI-37523, EBI-37092;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000255|HAMAP-Rule:MF_03109, ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:19665976}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_03109, ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:19665976}. Note=Enriched in the cortical ER.
CC Concentrated in punctae along the ER tubules.
CC -!- INDUCTION: By salt stress. {ECO:0000269|PubMed:11292078}.
CC -!- MISCELLANEOUS: Present with 2265 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
CC superfamily. GB1/RHD3 GTPase family. RHD3 subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU01052}.
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DR EMBL; U55021; AAB47412.1; -; Genomic_DNA.
DR EMBL; Z75073; CAA99371.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10939.1; -; Genomic_DNA.
DR PIR; S67053; S67053.
DR RefSeq; NP_014808.1; NM_001183584.1.
DR AlphaFoldDB; Q99287; -.
DR SMR; Q99287; -.
DR BioGRID; 34561; 120.
DR DIP; DIP-49373N; -.
DR IntAct; Q99287; 12.
DR MINT; Q99287; -.
DR STRING; 4932.YOR165W; -.
DR TCDB; 1.N.5.1.6; the endoplasmic reticulum fusion gtpase, atlastin (atlastin) family.
DR iPTMnet; Q99287; -.
DR MaxQB; Q99287; -.
DR PaxDb; Q99287; -.
DR PRIDE; Q99287; -.
DR EnsemblFungi; YOR165W_mRNA; YOR165W; YOR165W.
DR GeneID; 854336; -.
DR KEGG; sce:YOR165W; -.
DR SGD; S000005691; SEY1.
DR VEuPathDB; FungiDB:YOR165W; -.
DR eggNOG; KOG2203; Eukaryota.
DR HOGENOM; CLU_011270_0_0_1; -.
DR InParanoid; Q99287; -.
DR OMA; TNFDVMD; -.
DR BioCyc; YEAST:G3O-33681-MON; -.
DR PRO; PR:Q99287; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q99287; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0005933; C:cellular bud; HDA:SGD.
DR GO; GO:0032541; C:cortical endoplasmic reticulum; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; NAS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; IMP:SGD.
DR GO; GO:0048309; P:endoplasmic reticulum inheritance; IGI:UniProtKB.
DR GO; GO:0016320; P:endoplasmic reticulum membrane fusion; IDA:SGD.
DR GO; GO:0007029; P:endoplasmic reticulum organization; IGI:UniProtKB.
DR GO; GO:0061024; P:membrane organization; IGI:SGD.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_03109; Sey1; 1.
DR InterPro; IPR030386; G_GB1_RHD3_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR008803; RHD3/Sey1.
DR PANTHER; PTHR45923; PTHR45923; 1.
DR Pfam; PF05879; RHD3; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51715; G_GB1_RHD3; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; GTP-binding; Hydrolase; Membrane;
KW Nucleotide-binding; Reference proteome; Stress response; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..776
FT /note="Protein SEY1"
FT /id="PRO_0000155140"
FT TOPO_DOM 1..681
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 682..702
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 703..705
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 706..726
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 727..776
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT DOMAIN 34..263
FT /note="GB1/RHD3-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT BINDING 44..51
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT MUTAGEN 50
FT /note="K->A: Abolishes GTP binding."
FT /evidence="ECO:0000269|PubMed:19665976"
SQ SEQUENCE 776 AA; 89432 MW; DEC0C9EC3AB172DF CRC64;
MADRPAIQLI DEEKEFHQSA LQYFQQCIGN RDVGLDYHVI SVFGSQSSGK STLLNVLFNT
NFDTMDAQVK RQQTTKGIWL AHTKQVNTTI EIDNDRPDIF VLDVEGSDGS ERGEDQDFER
KAALFAIAVS EVLIVNMWEQ QIGLYQGNNM ALLKTVFEVN LSLFGKNDND HKVLLLFVIR
DHVGVTPLSS LSDSVTRELE KIWTELSKPA GCEGSSLYDY FDLKFVGLAH KLLQEDKFTQ
DVKKLGDSFV MKGTENYYFK PQYHHRLPLD GWTMYAENCW DQIERNKDLD LPTQQILVAR
FKTEEISNEA LEEFISKYDE SIAPLKGNLG SLTSQLVKLK EECLTKYDEQ ASRYARNVYM
EKREALNTKL NSHISGTINE FLESLMEKLW DDLKLEVSSR DKATTSFVES VAAGKSKIEK
EFNESMETFK KLGLLISNEE ITCKFSDDIE ERIKQLRDAE LKAKIGRIKK NLVPELKDHV
IHLLSHPSKK VWDDIMNDFE STIKDNISAY QVEKDKYDFK IGLSESENAK IYKNIRILAW
RTLDTTVHDY LKIDTIVSIL RDRFEDVFRY DAEGSPRLWK TEEEIDGAFR VAKEHALEVF
EVLSLAVTSD NVEIIPDVPM AEEESGEDNE IYRDNEGVFH SRRFAHILTE LQKENVLDQF
RRQINITVLD SKRSIITTRT HIPPWIYVLL AVLGWNEFVA VIRNPLFVTL TLILGATFFV
IHKFGLWGPV VNVVQSAVGE TRTAIKDKLR QFVVEDHEVK ESFEMKDFSK NEQKEK
