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Protein SEY1 (EC 3.6.5.-) (Synthetic enhancer of YOP1 protein)

 SEY1_YEAST              Reviewed;         776 AA.
Q99287; D6W2M3;
30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
25-OCT-2017, entry version 130.
RecName: Full=Protein SEY1 {ECO:0000255|HAMAP-Rule:MF_03109};
EC=3.6.5.- {ECO:0000255|HAMAP-Rule:MF_03109};
AltName: Full=Synthetic enhancer of YOP1 protein {ECO:0000255|HAMAP-Rule:MF_03109};
Name=SEY1 {ECO:0000255|HAMAP-Rule:MF_03109};
OrderedLocusNames=YOR165W; ORFNames=O3590;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=S288c / FY1678;
PubMed=8972579;
DOI=10.1002/(SICI)1097-0061(199612)12:15<1563::AID-YEA44>3.0.CO;2-M;
Madania A., Poch O., Tarassov I.A., Winsor B., Martin R.P.;
"Analysis of a 22,956 bp region on the right arm of Saccharomyces
cerevisiae chromosome XV.";
Yeast 12:1563-1573(1996).
[2]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169874;
Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W.,
Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R.,
Boyer J., Camasses A., Casamayor A., Casas C., Cheret G.,
Cziepluch C., Daignan-Fornier B., Dang V.-D., de Haan M., Delius H.,
Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F.,
Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A.,
Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J.,
Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P.,
Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M.,
Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R.,
Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S.,
Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A.,
Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M.,
Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C.,
Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S.,
Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
Nature 387:98-102(1997).
[4]
INDUCTION.
PubMed=11292078; DOI=10.1023/A:1006460231978;
Shen Q., Chen C.-N., Brands A., Pan S.-M., Ho T.-H.D.;
"The stress- and abscisic acid-induced barley gene HVA22:
developmental regulation and homologues in diverse organisms.";
Plant Mol. Biol. 45:327-340(2001).
[5]
FUNCTION.
PubMed=12427979; DOI=10.1104/pp.007716;
Brands A., Ho T.-H.D.;
"Function of a plant stress-induced gene, HVA22. Synthetic enhancement
screen with its yeast homolog reveals its role in vesicular traffic.";
Plant Physiol. 130:1121-1131(2002).
[6]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[7]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[8]
TOPOLOGY [LARGE SCALE ANALYSIS].
STRAIN=ATCC 208353 / W303-1A;
PubMed=16847258; DOI=10.1073/pnas.0604075103;
Kim H., Melen K., Oesterberg M., von Heijne G.;
"A global topology map of the Saccharomyces cerevisiae membrane
proteome.";
Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
[9]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RTN1 AND YOP1, AND
MUTAGENESIS OF LYS-50.
PubMed=19665976; DOI=10.1016/j.cell.2009.05.025;
Hu J., Shibata Y., Zhu P.-P., Voss C., Rismanchi N., Prinz W.A.,
Rapoport T.A., Blackstone C.;
"A class of dynamin-like GTPases involved in the generation of the
tubular ER network.";
Cell 138:549-561(2009).
-!- FUNCTION: Cooperates with the reticulon proteins RTN1 and RTN2 and
the tubule-shaping DP1 family protein YOP1 to generate and
maintain the structure of the tubular endoplasmic reticulum
network. Has GTPase activity, which is required for its function
in ER organization. {ECO:0000255|HAMAP-Rule:MF_03109,
ECO:0000269|PubMed:12427979, ECO:0000269|PubMed:19665976}.
-!- SUBUNIT: Interacts with RTN1 and YOP1; GTP binding is not required
for these interactions. {ECO:0000255|HAMAP-Rule:MF_03109,
ECO:0000269|PubMed:19665976}.
-!- INTERACTION:
Q04947:RTN1; NbExp=3; IntAct=EBI-37523, EBI-38020;
Q12402:YOP1; NbExp=2; IntAct=EBI-37523, EBI-37092;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000255|HAMAP-Rule:MF_03109, ECO:0000269|PubMed:14562095,
ECO:0000269|PubMed:19665976}; Multi-pass membrane protein
{ECO:0000255|HAMAP-Rule:MF_03109, ECO:0000269|PubMed:14562095,
ECO:0000269|PubMed:19665976}. Note=Enriched in the cortical ER.
Concentrated in punctae along the ER tubules.
-!- INDUCTION: By salt stress. {ECO:0000269|PubMed:11292078}.
-!- MISCELLANEOUS: Present with 2265 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
superfamily. GB1/RHD3-type GTPase family. RHD3 subfamily.
{ECO:0000255|HAMAP-Rule:MF_03109}.
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EMBL; U55021; AAB47412.1; -; Genomic_DNA.
EMBL; Z75073; CAA99371.1; -; Genomic_DNA.
EMBL; BK006948; DAA10939.1; -; Genomic_DNA.
PIR; S67053; S67053.
RefSeq; NP_014808.1; NM_001183584.1.
ProteinModelPortal; Q99287; -.
SMR; Q99287; -.
BioGrid; 34561; 98.
DIP; DIP-49373N; -.
IntAct; Q99287; 11.
MINT; MINT-2493571; -.
STRING; 4932.YOR165W; -.
iPTMnet; Q99287; -.
MaxQB; Q99287; -.
PRIDE; Q99287; -.
EnsemblFungi; YOR165W; YOR165W; YOR165W.
GeneID; 854336; -.
KEGG; sce:YOR165W; -.
EuPathDB; FungiDB:YOR165W; -.
SGD; S000005691; SEY1.
HOGENOM; HOG000206561; -.
InParanoid; Q99287; -.
OMA; QASRYHK; -.
OrthoDB; EOG092C0ULX; -.
BioCyc; YEAST:G3O-33681-MONOMER; -.
PRO; PR:Q99287; -.
Proteomes; UP000002311; Chromosome XV.
GO; GO:0032541; C:cortical endoplasmic reticulum; IDA:SGD.
GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
GO; GO:0005789; C:endoplasmic reticulum membrane; NAS:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0003924; F:GTPase activity; IMP:SGD.
GO; GO:0048309; P:endoplasmic reticulum inheritance; IGI:UniProtKB.
GO; GO:0016320; P:endoplasmic reticulum membrane fusion; IDA:SGD.
GO; GO:0007029; P:endoplasmic reticulum organization; IGI:UniProtKB.
GO; GO:0061024; P:membrane organization; IGI:SGD.
HAMAP; MF_03109; Sey1; 1.
InterPro; IPR030386; G_GB1_RHD3_dom.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR008803; RHD3/Sey1.
Pfam; PF05879; RHD3; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS51715; G_GB1_RHD3; 1.
1: Evidence at protein level;
Complete proteome; Endoplasmic reticulum; GTP-binding; Hydrolase;
Membrane; Nucleotide-binding; Reference proteome; Stress response;
Transmembrane; Transmembrane helix.
CHAIN 1 776 Protein SEY1.
/FTId=PRO_0000155140.
TOPO_DOM 1 681 Cytoplasmic. {ECO:0000255|HAMAP-
Rule:MF_03109}.
TRANSMEM 682 702 Helical. {ECO:0000255|HAMAP-
Rule:MF_03109}.
TOPO_DOM 703 705 Lumenal. {ECO:0000255|HAMAP-
Rule:MF_03109}.
TRANSMEM 706 726 Helical. {ECO:0000255|HAMAP-
Rule:MF_03109}.
TOPO_DOM 727 776 Cytoplasmic. {ECO:0000255|HAMAP-
Rule:MF_03109}.
DOMAIN 34 263 GB1/RHD3-type G.
NP_BIND 44 51 GTP. {ECO:0000255|HAMAP-Rule:MF_03109}.
MUTAGEN 50 50 K->A: Abolishes GTP binding.
{ECO:0000269|PubMed:19665976}.
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


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