SEY1_PICST
ID SEY1_PICST Reviewed; 827 AA.
AC A3LWM9;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 73.
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}; ORFNames=PICST_84922;
OS Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS Y-11545) (Yeast) (Pichia stipitis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX NCBI_TaxID=322104;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX PubMed=17334359; DOI=10.1038/nbt1290;
RA Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA Passoth V., Richardson P.M.;
RT "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT yeast Pichia stipitis.";
RL Nat. Biotechnol. 25:319-326(2007).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000500; ABN67661.2; -; Genomic_DNA.
DR RefSeq; XP_001385690.2; XM_001385653.1.
DR AlphaFoldDB; A3LWM9; -.
DR SMR; A3LWM9; -.
DR STRING; 4924.XP_001385690.2; -.
DR EnsemblFungi; ABN67661; ABN67661; PICST_84922.
DR GeneID; 4839766; -.
DR KEGG; pic:PICST_84922; -.
DR eggNOG; KOG2203; Eukaryota.
DR HOGENOM; CLU_011270_0_0_1; -.
DR InParanoid; A3LWM9; -.
DR OMA; TNFDVMD; -.
DR OrthoDB; 418635at2759; -.
DR Proteomes; UP000002258; Chromosome 6.
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:0007029; P:endoplasmic reticulum organization; IEA:UniProtKB-UniRule.
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..827
FT /note="Protein SEY1"
FT /id="PRO_0000384997"
FT TOPO_DOM 1..719
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 720..740
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 741..743
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 744..764
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 765..827
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT DOMAIN 63..291
FT /note="GB1/RHD3-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 389..409
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT COILED 472..492
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT COILED 803..823
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT BINDING 73..80
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
SQ SEQUENCE 827 AA; 95440 MW; CBC0A52C6FF73D62 CRC64;
MSQSSPSNAE TDEDLSTTSS SSSFVPIEQH QIQDAIQVID ENKEFNKNIL PYVVKTTPIS
SVGNNYHIIS VFGSQSTGKS TLLNRLFNTN FDVMDESRRQ QTTKGIWMAH SPQVSTTKQM
DTHQENIFVM DVEGTDGRER GEDQDFERKA ALFALATSEI LIVNIWETQI GLYQGANMGL
LKTVFEVNLT LFGKSKLEKN DHKVLLLIVI RDHVGLTPKE NLSSTITQDL LKIWESLNKP
AELAHLQFED FFDTDFHTLR HKVLQPKEFL EDVNELGDRL VVKKDLFRPN YHHNIPIDGW
TMYAENCWQQ IDSNKDLDLP TQQILVAKFK CDEISASVYE EFHQKFKAIS SANTPGISTL
DYQDLGLLLV DLRSDTLENY DLSASRYTKS VYEQRKDLLK EKLNEKFREF FDAHIKHLSE
KSVKEFETNI VGLKGKNFDK EATRLTRETT DYFINSAILL SLENELDYDV HVSNLQDQLT
KLIQQQQLVE LKNIVNKSIK KLSSGLTKAV SFELADPTET SWNNILSKFK EFVLDFLSKN
ELEEEAGTYD FGLGTNRAQN KEAVETFKFK SWNAFYEIIH KIISKDNLLT LLKDRFDDKF
RYDENGLPRM YQNTVELETN FGISKSFALR IVPLLTIAKL NDNSEILPDY DIFDSKLRAK
YLGLVENEHD SEDEEDEEDR CFAEIISESE KAEVLNKFKK ETDARFIETK RSIVQHVTQI
PYYIYLVIMV LGWNEFMAIV RNPLFFSLVL VFGAGLYILY SMNLLKPAMV VVQRLIDEII
AMAKEKMREF LIDDHPTQAH NLQKISASNR EKVEEEKVVE TIEMQDL