SEY1_YARLI
ID SEY1_YARLI Reviewed; 938 AA.
AC Q6C3B0;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=YALI0F01166g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
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; CR382132; CAG77654.1; -; Genomic_DNA.
DR RefSeq; XP_504852.1; XM_504852.1.
DR AlphaFoldDB; Q6C3B0; -.
DR SMR; Q6C3B0; -.
DR STRING; 4952.CAG77654; -.
DR EnsemblFungi; CAG77654; CAG77654; YALI0_F01166g.
DR GeneID; 2908213; -.
DR KEGG; yli:YALI0F01166g; -.
DR VEuPathDB; FungiDB:YALI0_F01166g; -.
DR HOGENOM; CLU_011270_0_0_1; -.
DR InParanoid; Q6C3B0; -.
DR OMA; TNFDVMD; -.
DR Proteomes; UP000001300; Chromosome F.
DR GO; GO:0032541; C:cortical endoplasmic reticulum; IEA:EnsemblFungi.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0048309; P:endoplasmic reticulum inheritance; IEA:EnsemblFungi.
DR GO; GO:0016320; P:endoplasmic reticulum membrane fusion; IBA:GO_Central.
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..938
FT /note="Protein SEY1"
FT /id="PRO_0000155138"
FT TOPO_DOM 1..839
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 840..860
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 861..863
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 864..884
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 885..938
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT DOMAIN 192..423
FT /note="GB1/RHD3-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT REGION 1..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 911..938
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 603..630
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT COMPBIAS 26..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..94
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..119
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..159
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 915..938
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 202..209
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
SQ SEQUENCE 938 AA; 103133 MW; 9928611CAA0746D7 CRC64;
MTSQSHGAPP VPSSRPPASR VPVSGYDSHD SHSVSSSHSS HSPVTTHHHP APPPPASRPV
RESGVAPVTA PEPIAAPEPI AAPEPIPAPE PIAAPVPEGL KSEHKPVERE HKPVERKPVS
SPAEKSIPAS SPVHKAAPTP AASHAVPTSQ KSAKSTPGSY AGIPSLQLID GNKEFNPDVS
SYFKKVHLDR AGLDYHVVAV FGSQSTGKST LLNALFGTQF DVMNETARQQ TTKGIWMARA
QLEAPHSANS AHSQDCSDSG VLVMDVEGTD GRERGEDQDF ERKSALFALA TSEVLIVNIW
EHQIGLYQGA NMGLLKTVFE VNLNLFATSQ NRSLIMFVIR DHIGATPLAN LSTTLKTDMG
KLWDSINKPE GLEHAKLEDF FDLQFTALPH KLLQPNEFYA DVEQLACRFT VPKDPNYVFK
PVYHRNVPLD GWSFYAEQVW DQIEQNKDLD LPTQQILVAR FRCDEIAAGA LDIFLSLLVK
IRDQLSGGAV ASAVLGGLMG EARKQTVDEY DSQASRYTPS VYSATLEKLE DRVDNDLGKV
YQSYLAQLKR ESLEQFNAAL ESSSALTFGE NLSRASKAAH AHFIDNAKQV TAAIGQPNSS
HFSYDDTLAA LEQELDTLRD HKSKVEIDRL ISRSAKRFKS SFHEEFDENL NKPDETVWDR
ILESFETLLN ASIKKIDPNY SPSAPSAFSF GFGSPKTSAE GLKQIQQEAW AVFGAELKEL
SKEEQVLSRL KNKFKESFRY DANGVPIVWR PGDDIDGAFA KSREQALEIM PLLSTAKLSS
GKSIEPTVAL EDDEDDDDET AFAVILTPKR QASLIEKFKK QAEGLYLEAK RSTIQSTTQI
PLYMYGLLLL LGWNEIMAVL RSPVYFMFLL VAAGAAYVIH TLHLWGPLTH MTNTMIAEAT
DMAKAKLKQV LNEAPTGETR EREAPVGSSR DDVELKDL
