SEY1_CANGA
ID SEY1_CANGA Reviewed; 783 AA.
AC Q6FLC5;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Protein SEY1 {ECO:0000255|HAMAP-Rule:MF_03109};
DE EC=3.6.5.- {ECO:0000255|HAMAP-Rule:MF_03109};
GN Name=SEY1 {ECO:0000255|HAMAP-Rule:MF_03109};
GN OrderedLocusNames=CAGL0L04466g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Cooperates with the reticulon proteins and tubule-shaping DP1
CC family proteins to generate and maintain the structure of the tubular
CC endoplasmic reticulum network. Has GTPase activity, which is required
CC for its function in ER organization. {ECO:0000255|HAMAP-Rule:MF_03109}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000255|HAMAP-Rule:MF_03109}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_03109}. Note=Enriched in the cortical ER.
CC Concentrated in punctae along the ER tubules. {ECO:0000255|HAMAP-
CC Rule:MF_03109}.
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; CR380958; CAG61939.1; -; Genomic_DNA.
DR RefSeq; XP_448969.1; XM_448969.1.
DR AlphaFoldDB; Q6FLC5; -.
DR SMR; Q6FLC5; -.
DR STRING; 5478.XP_448969.1; -.
DR EnsemblFungi; CAG61939; CAG61939; CAGL0L04466g.
DR GeneID; 2890639; -.
DR KEGG; cgr:CAGL0L04466g; -.
DR CGD; CAL0135064; CAGL0L04466g.
DR VEuPathDB; FungiDB:CAGL0L04466g; -.
DR eggNOG; KOG2203; Eukaryota.
DR HOGENOM; CLU_011270_0_0_1; -.
DR InParanoid; Q6FLC5; -.
DR OMA; TNFDVMD; -.
DR Proteomes; UP000002428; Chromosome L.
DR GO; GO:0032541; C:cortical endoplasmic reticulum; IEA:EnsemblFungi.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-UniRule.
DR GO; GO:0048309; P:endoplasmic reticulum inheritance; IEA:EnsemblFungi.
DR GO; GO:0016320; P:endoplasmic reticulum membrane fusion; IEA:EnsemblFungi.
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 3: Inferred from homology;
KW Coiled coil; Endoplasmic reticulum; GTP-binding; Hydrolase; Membrane;
KW Nucleotide-binding; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..783
FT /note="Protein SEY1"
FT /id="PRO_0000155130"
FT TOPO_DOM 1..677
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 678..698
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 699..701
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 702..722
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 723..783
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT DOMAIN 33..265
FT /note="GB1/RHD3-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT COILED 449..472
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT BINDING 43..50
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
SQ SEQUENCE 783 AA; 90959 MW; 7007F040DDF69D5C CRC64;
MTSQAIQLID VNKEYNKESL EYFKQCVGTR DVGFNYHVIS VFGSQSSGKS TLLNILFNTQ
FDTMDAQVKR QQTTKGIWLA HTQNVNNHKS TTDTDSDYFI LDVEGSDGAE RGEDQDFERK
AALFAISVSE VLIVNMWEQQ IGLYQGNNMG LLKTVFEVNL SLFGKRGNDH KVLLLFVIRD
HVGVTPLKSL QESLITELEQ IWSELNKPTG CEETTLYDFF DLEFKGLGHK LLQEEQFYDD
VKSLGDSFID SESNEYLLKP NYHHKLPIDG WNMYAEQCWE QIENNRDLDL PTQQILVARF
KTEDIANEAY AKFTEEYETE TEKRINDKTE LVSYLKKIKD ECLGEYDEHA SRYAKAVYEE
KRIELVDKVN ERLFTTASKY LDMLTAVLLT KLENGMKEKE NIKLPFEDRY LKLFKDIEAE
FDAAITEFFS KDLLTKIKDF ELKFAADVHE KKLQLRESEL NALLSKIKKQ LTLRIKDEEI
ELLSKPTPDL WDKVTDTFEN IMKKTLSRFA TGEGEYEFKM GLSEDENKKQ YHAIRAFAWT
LLETVVHDYL KEDTIVSLLR DRFESKFRYD SNDVPRLWKN EDEIDQSFRV AKEHALEILD
ILTLAVKTDG TEVIPDAFED EPNEGLIYDD SHDVYHSNRF AHILNETQKE KVQQQFRRQI
NVTVLDCKRS IVTSSTHIPI WIYAVIVVLG WNEFMIVIRN PLFVTLALLS IVSFYFIQKF
GLWGPVMNVV NTALGESRTT IKEKLRQFVL EEHELKKTAK VEEEIELQDL SKNSSSSGNE
DSD
