SEY1_COPC7
ID SEY1_COPC7 Reviewed; 784 AA.
AC A8N5E5;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 54.
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=CC1G_04523;
OS Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003)
OS (Inky cap fungus) (Hormographiella aspergillata).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Psathyrellaceae; Coprinopsis.
OX NCBI_TaxID=240176;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003;
RX PubMed=20547848; DOI=10.1073/pnas.1003391107;
RA Stajich J.E., Wilke S.K., Ahren D., Au C.H., Birren B.W., Borodovsky M.,
RA Burns C., Canbaeck B., Casselton L.A., Cheng C.K., Deng J., Dietrich F.S.,
RA Fargo D.C., Farman M.L., Gathman A.C., Goldberg J., Guigo R., Hoegger P.J.,
RA Hooker J.B., Huggins A., James T.Y., Kamada T., Kilaru S., Kodira C.,
RA Kuees U., Kupfer D., Kwan H.S., Lomsadze A., Li W., Lilly W.W., Ma L.-J.,
RA Mackey A.J., Manning G., Martin F., Muraguchi H., Natvig D.O.,
RA Palmerini H., Ramesh M.A., Rehmeyer C.J., Roe B.A., Shenoy N., Stanke M.,
RA Ter-Hovhannisyan V., Tunlid A., Velagapudi R., Vision T.J., Zeng Q.,
RA Zolan M.E., Pukkila P.J.;
RT "Insights into evolution of multicellular fungi from the assembled
RT chromosomes of the mushroom Coprinopsis cinerea (Coprinus cinereus).";
RL Proc. Natl. Acad. Sci. U.S.A. 107:11889-11894(2010).
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; AACS02000003; EAU91755.1; -; Genomic_DNA.
DR RefSeq; XP_001830090.1; XM_001830038.2.
DR AlphaFoldDB; A8N5E5; -.
DR SMR; A8N5E5; -.
DR STRING; 5346.XP_001830090.1; -.
DR PRIDE; A8N5E5; -.
DR EnsemblFungi; EAU91755; EAU91755; CC1G_04523.
DR GeneID; 6006528; -.
DR KEGG; cci:CC1G_04523; -.
DR VEuPathDB; FungiDB:CC1G_04523; -.
DR eggNOG; KOG2203; Eukaryota.
DR HOGENOM; CLU_011270_0_0_1; -.
DR InParanoid; A8N5E5; -.
DR OMA; TNFDVMD; -.
DR OrthoDB; 418635at2759; -.
DR Proteomes; UP000001861; 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..784
FT /note="Protein SEY1"
FT /id="PRO_0000384982"
FT TOPO_DOM 1..678
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 679..699
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 700..702
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 703..723
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 724..784
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT DOMAIN 47..267
FT /note="GB1/RHD3-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT REGION 764..784
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 447..487
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT BINDING 57..64
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
SQ SEQUENCE 784 AA; 89201 MW; 7852C31BE6246FE2 CRC64;
MASTANDRQQ LPNGDASTER IQIIDENKTF TPDLTQQIER WGLRDSGFNY NLVAVFGSQS
TGKSTLLNRL FGTTFDVMDE TRRQQTTKGI WMCRGKDMSV MVMDVEGTDG RERGEDQDFE
RKSALFSLAS SEVLIVNMWE HQVGLYQGAN MGLLKTVFEV NLGLFGKKAN DGTSGRTLLL
FVIRDHIGTT PLANLQATLI QDLNRIWDSL SKPDDLKDRL LSDYFDMAFT TLPHKVLVPD
KFEAEVANLR KRFTDKDNEG YLFKPVYHKR IPADGVAFYM ENIWEQVQNN KDLDLPTQQE
LLAQFRCDEI SAAALAEFNE QAKPQKRPIE AGRVVENLGN MMRNWRTQAL TRYDREASRY
HKGVYTRKRT DLIAVIDSTL SPLFLGQLKN LHKSCLVTFK KEILEGLKGD EYDFGTVVQK
ARTKCEKTFS EGAKEAVVEE GAAGWSWEEE MELLMEEVGA VADQCRKDET KKMINLIERN
VKKLISEPVE LHLTKPSTDM WDKVMKTFKD TLDKAESTYL AKAKSFNCTE EENTNALASL
KRRAWIVLRA KIEEQTSDQS LLGKLRGHFE ERFRYDEEGV PRVWKPDDDI DGAFKKAKEE
TLELVPLYSR IKPTDSSLEF ELPSDGSSDD LTNDEFDFAS SLTVLSDTKS LDLINKFRKD
ADAYYVEAKR STVSSIAQIP YWMYGVLVVL GWNEAMAVLF NPLYFTFLLF ALASAYMIIQ
LGLTGPLLQV TRAVASEVQK QATNKLREVV GQGQAEAVAL QPMRAQRQNE TEYENANGDD
LRQR
