SPN5_SCHPO
ID SPN5_SCHPO Reviewed; 464 AA.
AC P48010; O13975; Q96WR7;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Septin homolog spn5;
DE AltName: Full=Mei4-dependent protein 9;
DE AltName: Full=Meiotic expression up-regulated protein 28;
GN Name=spn5; Synonyms=mde9, meu28; ORFNames=SPAC24C9.15c;
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 [GENOMIC DNA].
RA Al-Awar O.S., Pugh T.A., Kim H.B., Valencik M.L., Pringle J.R.;
RL Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases.
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 NUCLEOTIDE SEQUENCE [MRNA] OF 295-464.
RC STRAIN=CD16-1;
RX PubMed=11376151; DOI=10.1093/nar/29.11.2327;
RA Watanabe T., Miyashita K., Saito T.T., Yoneki T., Kakihara Y.,
RA Nabeshima K., Kishi Y.A., Shimoda C., Nojima H.;
RT "Comprehensive isolation of meiosis-specific genes identifies novel
RT proteins and unusual non-coding transcripts in Schizosaccharomyces pombe.";
RL Nucleic Acids Res. 29:2327-2337(2001).
RN [5]
RP INDUCTION.
RX PubMed=10747048; DOI=10.1093/genetics/154.4.1497;
RA Abe H., Shimoda C.;
RT "Autoregulated expression of Schizosaccharomyces pombe meiosis-specific
RT transcription factor Mei4 and a genome-wide search for its target genes.";
RL Genetics 154:1497-1508(2000).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION IN THE
RP SPORULATION-SPECIFIC SEPTIN COMPLEX.
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: Septin-like protein involved in the correct orientation of
CC forespore membrane extension during sporulation.
CC {ECO:0000269|PubMed:20123972}.
CC -!- SUBUNIT: Component of the sporulation-specific septin complex composed
CC of at least spn2, spn5, spn6 and spn7. {ECO:0000269|PubMed:20123972}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Forespore membrane; Peripheral membrane
CC protein. Note=The sporulation-specific septin complex associates to the
CC forespore membrane and forms partial or complete ring-like structures
CC that curl around each haploid nucleus.
CC -!- INDUCTION: Expressed during meiosis. Expression is under the control of
CC the meiosis-specific transcription factor mei4.
CC {ECO:0000269|PubMed:10747048}.
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; U29891; AAB53688.2; -; Genomic_DNA.
DR EMBL; CU329670; CAB11273.1; -; Genomic_DNA.
DR EMBL; AB054312; BAB60879.1; -; mRNA.
DR PIR; T38356; T38356.
DR RefSeq; NP_594040.1; NM_001019465.2.
DR AlphaFoldDB; P48010; -.
DR SMR; P48010; -.
DR BioGRID; 279095; 12.
DR STRING; 4896.SPAC24C9.15c.1; -.
DR PaxDb; P48010; -.
DR EnsemblFungi; SPAC24C9.15c.1; SPAC24C9.15c.1:pep; SPAC24C9.15c.
DR GeneID; 2542641; -.
DR KEGG; spo:SPAC24C9.15c; -.
DR PomBase; SPAC24C9.15c; spn5.
DR VEuPathDB; FungiDB:SPAC24C9.15c; -.
DR eggNOG; KOG2655; Eukaryota.
DR HOGENOM; CLU_017718_8_0_1; -.
DR InParanoid; P48010; -.
DR OMA; NPNGHRL; -.
DR PhylomeDB; P48010; -.
DR Reactome; R-SPO-111457; Release of apoptotic factors from the mitochondria.
DR Reactome; R-SPO-111469; SMAC, XIAP-regulated apoptotic response.
DR PRO; PR:P48010; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0032153; C:cell division site; IBA:GO_Central.
DR GO; GO:0032175; C:mating projection 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: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:0008104; P:protein localization; IBA:GO_Central.
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 Coiled coil; GTP-binding; Meiosis; Membrane; Nucleotide-binding; Nucleus;
KW Reference proteome; Sporulation.
FT CHAIN 1..464
FT /note="Septin homolog spn5"
FT /id="PRO_0000173507"
FT DOMAIN 115..370
FT /note="Septin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 28..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 125..132
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 174..177
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 256..259
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT COILED 396..453
FT /evidence="ECO:0000255"
FT COMPBIAS 34..57
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..81
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 125..132
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 151
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 177
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 257..265
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 304
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 319
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 464 AA; 53104 MW; F7BE83DE827ECE1B CRC64;
MDSSNLSSSM PQEGQLKLTE EAIITIKQVD ESSAKRSVSN ESRKSKDVTR KEQIASDQQG
DDQCPQSDTA KDKKTEFKQD EVPNSNGKSI PTFHPCNNIG INDFNHQHYS RVCRNGIDIN
LIVVGESSLG KTTFVNSFLQ SNDTNFRPKK TMDFVEHKAT LSDGDQKFNL TIVDTPGFGD
KSDNSNCWRP IATNLLHRLN AYFQNEVKMD RETSEIDSRI HGCLFFINPN GHRLQPLEIY
IMKKIDQFVN IIPVIGKADT MTSDELNHFK KRVIADMVRE KIRYFREPHN EKKAKIPIPF
AIVGAGAPIE HDGKCIRGRA YPWGLVDIDD PKQSDFCQLR NFLLYTHIEG LKHKTHKLIY
DTFRTEKLVA LNATPGSQFI SAEEMNQKYI SEQTQLVEEA LTKVMKEKYR EKENNLELLE
TNLKTHHKDY KHALKKRITA LEEEKNRLIK EIGPEKVKKA GILA
