SEY1_LACBS
ID SEY1_LACBS Reviewed; 785 AA.
AC B0D0N9;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 53.
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=LACBIDRAFT_189306;
OS Laccaria bicolor (strain S238N-H82 / ATCC MYA-4686) (Bicoloured deceiver)
OS (Laccaria laccata var. bicolor).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Tricholomataceae; Laccaria.
OX NCBI_TaxID=486041;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 / ATCC MYA-4686;
RX PubMed=18322534; DOI=10.1038/nature06556;
RA Martin F., Aerts A., Ahren D., Brun A., Danchin E.G.J., Duchaussoy F.,
RA Gibon J., Kohler A., Lindquist E., Pereda V., Salamov A., Shapiro H.J.,
RA Wuyts J., Blaudez D., Buee M., Brokstein P., Canbaeck B., Cohen D.,
RA Courty P.E., Coutinho P.M., Delaruelle C., Detter J.C., Deveau A.,
RA DiFazio S., Duplessis S., Fraissinet-Tachet L., Lucic E., Frey-Klett P.,
RA Fourrey C., Feussner I., Gay G., Grimwood J., Hoegger P.J., Jain P.,
RA Kilaru S., Labbe J., Lin Y.C., Legue V., Le Tacon F., Marmeisse R.,
RA Melayah D., Montanini B., Muratet M., Nehls U., Niculita-Hirzel H.,
RA Oudot-Le Secq M.P., Peter M., Quesneville H., Rajashekar B., Reich M.,
RA Rouhier N., Schmutz J., Yin T., Chalot M., Henrissat B., Kuees U.,
RA Lucas S., Van de Peer Y., Podila G.K., Polle A., Pukkila P.J.,
RA Richardson P.M., Rouze P., Sanders I.R., Stajich J.E., Tunlid A.,
RA Tuskan G., Grigoriev I.V.;
RT "The genome of Laccaria bicolor provides insights into mycorrhizal
RT symbiosis.";
RL Nature 452:88-92(2008).
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; DS547095; EDR11495.1; -; Genomic_DNA.
DR RefSeq; XP_001877392.1; XM_001877357.1.
DR AlphaFoldDB; B0D0N9; -.
DR SMR; B0D0N9; -.
DR STRING; 486041.B0D0N9; -.
DR EnsemblFungi; EDR11495; EDR11495; LACBIDRAFT_189306.
DR GeneID; 6073441; -.
DR KEGG; lbc:LACBIDRAFT_189306; -.
DR HOGENOM; CLU_011270_0_0_1; -.
DR InParanoid; B0D0N9; -.
DR OrthoDB; 418635at2759; -.
DR Proteomes; UP000001194; Unassembled WGS sequence.
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..785
FT /note="Protein SEY1"
FT /id="PRO_0000384983"
FT TOPO_DOM 1..689
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 690..710
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 711..713
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 714..734
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 735..785
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT DOMAIN 61..281
FT /note="GB1/RHD3-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 458..482
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT COMPBIAS 14..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 71..78
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
SQ SEQUENCE 785 AA; 89065 MW; FF06A75C792358B1 CRC64;
MASAAPINLR AQDTPYVPPT SLPTSSSQTG STARIQIIDD EKKFTPDLAT QIERWGLRDA
GFSYNIVAVF GSQSTGKSTL LNRLFGTTFD VMDETRRQQT TKGIWMCRGK DMGVMVMDVE
GTDGRERGED QDFERKSALF SLASSEILIV NLWEHQVGLY QGANMGLLKT VFEVNLGLFG
KKAQDGSNGR TLLLFVIRDH IGQTPLANLQ ATLTADLNRI WESLSKPTDL KDRLLSDYFD
LAFTALPHKI LSADKFESEV QELRTRFVDK ESSDYLFKPA YHKRIPADGV AFYMEGIWEQ
VQTNKDLDLP TQQELLAQFR CDEISAVALA EFNEQAKSQK RPVEGGRVVE GLGAMMNNWR
TQALTRYDRD ASRYHKGVYG RKRADLVAVL DSTLSPLFLG QLKNLHKSCL VTFKKEMLDG
LHGEDYDFAN VFKRAREKSE RTFSEGGKEA LVEGTDWSWE EELELLRDEI RAVADQCRKD
ETTKMINLIE RNLKKHISEP VELHLGKASP DMWDEILRVF RDTLDKAEKT YLTKAKSFNC
TEEENTAALD ALRKRGWVAL RAKIDEQTAD PIILGKLRNH FEERFRYDEQ GVPRVWKPDD
DIDSAFMKAK DQTLDLVPLY SKISPKDTSL EFNLPSESND SFSNDDFDLS TSPVIFTETK
CLDLTNKFRR DADAYYVEAK RSTVASIAQI PYWIYGVLVV LGWNEAMLVL FNPLYFAFLL
LAMATSYIIA QLGLVGPLFQ VTRTVGSEIQ RQATARLREH FSQPVLAEPV QVGPSRDREE
VGQIQ
