SPN2_SCHPO
ID SPN2_SCHPO Reviewed; 331 AA.
AC Q09116; Q9UT47;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Septin homolog spn2;
GN Name=spn2; ORFNames=SPAC821.06;
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 [MRNA].
RX PubMed=8791410; DOI=10.1016/s0955-0674(96)80054-8;
RA Longtine M.S., DeMarini D.J., Valencik M.L., Al-Awar O.S., Fares H.,
RA De Virgilio C., Pringle J.R.;
RT "The septins: roles in cytokinesis and other processes.";
RL Curr. Opin. Cell Biol. 8:106-119(1996).
RN [2]
RP SEQUENCE REVISION.
RA Al-Awar O.S.;
RL Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN THE SEPTIN COMPLEX, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15385632; DOI=10.1091/mbc.e04-07-0640;
RA An H., Morrell J.L., Jennings J.L., Link A.J., Gould K.L.;
RT "Requirements of fission yeast septins for complex formation, localization,
RT and function.";
RL Mol. Biol. Cell 15:5551-5564(2004).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN THE SPORULATION-SPECIFIC
RP SEPTIN COMPLEX, AND PHOSPHATIDYLINOSITOL 4-PHOSPHATE-BINDING.
RX PubMed=20123972; DOI=10.1128/mcb.01529-09;
RA Onishi M., Koga T., Hirata A., Nakamura T., Asakawa H., Shimoda C.,
RA Bahler J., Wu J.Q., Takegawa K., Tachikawa H., Pringle J.R., Fukui Y.;
RT "Role of septins in the orientation of forespore membrane extension during
RT sporulation in fission yeast.";
RL Mol. Cell. Biol. 30:2057-2074(2010).
CC -!- FUNCTION: Plays a role in the cell cycle. Involved in a late stage of
CC septum formation leading to the separation of the daughter cells.
CC Involved in the correct orientation of forespore membrane extension
CC during sporulation. Binds phosphatidylinositol 4-phosphate.
CC {ECO:0000269|PubMed:15385632, ECO:0000269|PubMed:20123972}.
CC -!- SUBUNIT: Component of the septin complex composed of two copies of each
CC spn1, spn2, spn3 and spn4. Component of the sporulation-specific septin
CC complex composed of at least spn2, spn5, spn6 and spn7.
CC {ECO:0000269|PubMed:15385632, ECO:0000269|PubMed:20123972}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex. Forespore membrane;
CC Peripheral membrane protein. Note=Localizes to the medial ring at the
CC cell cortex of dividing cells. The sporulation-specific septin complex
CC associates to the forespore membrane and forms partial or complete
CC ring-like structures that curl around each haploid nucleus.
CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC GTPase superfamily. Septin GTPase family. {ECO:0000255|PROSITE-
CC ProRule:PRU01056}.
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DR EMBL; U29888; AAB53690.2; -; mRNA.
DR EMBL; CU329670; CAB57440.1; -; Genomic_DNA.
DR PIR; T41717; T41717.
DR PIR; T52560; T52560.
DR RefSeq; NP_593159.1; NM_001018557.2.
DR AlphaFoldDB; Q09116; -.
DR SMR; Q09116; -.
DR BioGRID; 279931; 32.
DR STRING; 4896.SPAC821.06.1; -.
DR iPTMnet; Q09116; -.
DR MaxQB; Q09116; -.
DR PaxDb; Q09116; -.
DR PRIDE; Q09116; -.
DR EnsemblFungi; SPAC821.06.1; SPAC821.06.1:pep; SPAC821.06.
DR GeneID; 2543513; -.
DR KEGG; spo:SPAC821.06; -.
DR PomBase; SPAC821.06; spn2.
DR VEuPathDB; FungiDB:SPAC821.06; -.
DR eggNOG; KOG1547; Eukaryota.
DR HOGENOM; CLU_017718_7_1_1; -.
DR InParanoid; Q09116; -.
DR OMA; QCEFVYL; -.
DR PhylomeDB; Q09116; -.
DR PRO; PR:Q09116; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0032153; C:cell division site; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0032175; C:mating projection septin ring; IDA:PomBase.
DR GO; GO:0036391; C:medial cortex septin ring; IDA:PomBase.
DR GO; GO:0032152; C:meiotic septin complex; IDA:PomBase.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR GO; GO:0120104; C:mitotic actomyosin contractile ring, proximal layer; IDA:PomBase.
DR GO; GO:0032151; C:mitotic septin complex; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0032169; C:prospore septin ring; IDA:PomBase.
DR GO; GO:0031105; C:septin complex; IBA:GO_Central.
DR GO; GO:0005940; C:septin ring; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; ISM:PomBase.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0060090; F:molecular adaptor activity; IBA:GO_Central.
DR GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; IDA:PomBase.
DR GO; GO:0061640; P:cytoskeleton-dependent cytokinesis; IBA:GO_Central.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:PomBase.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:0000921; P:septin ring assembly; IMP:PomBase.
DR GO; GO:0070583; P:spore membrane bending pathway; IMP:PomBase.
DR CDD; cd01850; CDC_Septin; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR030379; G_SEPTIN_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR016491; Septin.
DR Pfam; PF00735; Septin; 1.
DR PIRSF; PIRSF006698; Septin; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51719; G_SEPTIN; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cytoplasm; GTP-binding; Lipid-binding; Membrane;
KW Mitosis; Nucleotide-binding; Reference proteome.
FT CHAIN 1..331
FT /note="Septin homolog spn2"
FT /id="PRO_0000173504"
FT DOMAIN 29..301
FT /note="Septin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 39..46
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 96..99
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 178..181
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 311..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 39..46
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 73
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 99
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 179..187
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 235
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 250
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 331 AA; 38129 MW; AAE06F4037D4ACE8 CRC64;
MEVPSAVTLN NYVGFDSITS QINRKLIRRG FQFNVMVVGP SGSGKSTLIN TLFSAHLMDS
KGRLDYQAPY RQTTEIHVTS QVVRENRVQL QLNLIDTPGY GDQINNDKCW EPIIKYIRDQ
HSSYLRRELN SHREKRLQDT RVHCCLFFIR PTGHSLRPID IAVLKRLTEV VNVVPVIAKS
DSLTLEERAA FKQQIREEFV KHDINLYPYD SDDADEEEIN LNAAVRNLIP FAVVGSEKAI
IVDGRPIRGR QNRWGVVNVD DENHCEFVFL RNFLMRTHLQ DLIETTSYYH YEKFRFKQLS
SLKEQSSLAT RMGSPAPVYP SEPHLHTATA Q
