SEY1_SCHPO
ID SEY1_SCHPO Reviewed; 762 AA.
AC Q9UTE0;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 126.
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; ORFNames=SPAC222.14c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP INTERACTION WITH SAD1, AND SUBCELLULAR LOCATION.
RX PubMed=14655046; DOI=10.1007/s00438-003-0938-8;
RA Miki F., Kurabayashi A., Tange Y., Okazaki K., Shimanuki M., Niwa O.;
RT "Two-hybrid search for proteins that interact with Sad1 and Kms1, two
RT membrane-bound components of the spindle pole body in fission yeast.";
RL Mol. Genet. Genomics 270:449-461(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-746, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(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 -!- SUBUNIT: Interacts with sad1. {ECO:0000269|PubMed:14655046}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000255|HAMAP-Rule:MF_03109, ECO:0000269|PubMed:14655046}; Multi-
CC pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03109,
CC ECO:0000269|PubMed:14655046}. 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; CU329670; CAB60706.1; -; Genomic_DNA.
DR PIR; T50155; T50155.
DR RefSeq; NP_593153.1; NM_001018550.2.
DR AlphaFoldDB; Q9UTE0; -.
DR SMR; Q9UTE0; -.
DR BioGRID; 278414; 47.
DR IntAct; Q9UTE0; 1.
DR STRING; 4896.SPAC222.14c.1; -.
DR iPTMnet; Q9UTE0; -.
DR MaxQB; Q9UTE0; -.
DR PaxDb; Q9UTE0; -.
DR PRIDE; Q9UTE0; -.
DR EnsemblFungi; SPAC222.14c.1; SPAC222.14c.1:pep; SPAC222.14c.
DR GeneID; 2541926; -.
DR KEGG; spo:SPAC222.14c; -.
DR PomBase; SPAC222.14c; sey1.
DR VEuPathDB; FungiDB:SPAC222.14c; -.
DR eggNOG; KOG2203; Eukaryota.
DR HOGENOM; CLU_011270_0_0_1; -.
DR InParanoid; Q9UTE0; -.
DR OMA; TNFDVMD; -.
DR PhylomeDB; Q9UTE0; -.
DR PRO; PR:Q9UTE0; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
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; ISM:PomBase.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0016320; P:endoplasmic reticulum membrane fusion; ISO:PomBase.
DR GO; GO:0007029; P:endoplasmic reticulum organization; IMP:PomBase.
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 1: Evidence at protein level;
KW Endoplasmic reticulum; GTP-binding; Hydrolase; Membrane;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..762
FT /note="Protein sey1"
FT /id="PRO_0000155139"
FT TOPO_DOM 1..657
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 658..678
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 679..681
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 682..702
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 703..762
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT DOMAIN 36..251
FT /note="GB1/RHD3-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT REGION 736..762
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 46..53
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT MOD_RES 746
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 762 AA; 87510 MW; 3ADDA2FC8F8E813A CRC64;
MSTASNRVST QIVDEHKQFN NELPKFMQSV GLLDAGFNYH VVAVLGSQST GKSTLLNNLF
GTSFSVMDAS KRQQTTKGIW LSKANNSPIL VMDVEGTDGR ERGEDQDFER KSALFSISTS
EVIIVNMWEN QVGLYQGSNM ALLKTVLEVN LQLFHNKKER CLLQFVIRDF LGNTSMENLA
DTIMTDLNNI WASLSKPEGF ENSVINDFFD VGFTGLPHKI LCSDAFSEAV DSLRERFVDN
NNSDYIFNVS YHKKIPADGF SLYTREIWDT IENNKDLDLP TQQQLLAQYR CDEIITEVME
PFSTACTILQ KEFLPGNLCK DLPTKLLNMF ETVIEAYDRQ ASRYNVHIYQ KKKQELIASV
DSHLYVFFQA QLNALHKELI KSFFDASNEF PSDTPFKESS SIKINELVNK MREEGESLSL
PHVHWDVDPF ILKLSEELTQ NSETLCKEKL KEKLEELFTG FEFEVSEAVE VAFQKLSHNV
WDTLLNEFLA AQNTTIEKIK NIVPFYVDID DTKTTEEYII NFKKNSWLFF RKKIDSEMSE
VLLQQRLRVY FEELFRYDSD GMPKLWKKSG TIDRDYRESL TKTLDLINVL ASIKVSDGNY
PDLNVDIKTL EPEYTSPASF FTILNRRRVS DISVNFKRSA DLIFMDCKRS VINTTTRIPP
YFWVLLIVLG WNEFMAILRN PFVFMILMFG GTVVYGLYIS GLIWPAKMVL ERATNNLVDL
ATDRFSNTYQ EQVQQRAMQR TEKSGSPVAS ADDAEAEKTA LS
