SPN6_SCHPO
ID SPN6_SCHPO Reviewed; 380 AA.
AC Q09883;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Septin homolog spn6;
GN Name=spn6; ORFNames=SPCC188.12, SPCC584.09;
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 CHARACTERIZATION.
RA Wu J.-Q., Pringle J.R.;
RL Submitted (MAR-2001) to UniProtKB.
RN [3]
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 [4]
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: Cytoplasm. Forespore membrane; Peripheral
CC membrane protein. Note=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; CU329672; CAB37422.1; -; Genomic_DNA.
DR PIR; T41191; S62523.
DR RefSeq; XP_001713168.1; XM_001713116.2.
DR AlphaFoldDB; Q09883; -.
DR SMR; Q09883; -.
DR BioGRID; 275524; 4.
DR STRING; 4896.SPCC188.12.1; -.
DR PaxDb; Q09883; -.
DR EnsemblFungi; SPCC188.12.1; SPCC188.12.1:pep; SPCC188.12.
DR PomBase; SPCC188.12; spn6.
DR VEuPathDB; FungiDB:SPCC188.12; -.
DR eggNOG; KOG2655; Eukaryota.
DR HOGENOM; CLU_017718_8_0_1; -.
DR InParanoid; Q09883; -.
DR OMA; MDLVCMK; -.
DR PhylomeDB; Q09883; -.
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:Q09883; -.
DR Proteomes; UP000002485; Chromosome III.
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: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: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: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; Cytoplasm; GTP-binding; Meiosis; Membrane; Nucleotide-binding;
KW Reference proteome; Sporulation.
FT CHAIN 1..380
FT /note="Septin homolog spn6"
FT /id="PRO_0000173508"
FT DOMAIN 27..297
FT /note="Septin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 37..44
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 95..98
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 176..179
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT COILED 304..380
FT /evidence="ECO:0000255"
FT BINDING 37..44
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 72
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 98
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 177..185
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 246
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 380 AA; 44011 MW; 450D86AEBEC2BC8F CRC64;
MSLTENLQLL LNLDSLPSKR ENLIKRKECG LTIMLCGASG TGKTTFFNTL FATSLQPEKS
YETAKETIAK KTLEVKKNKA VIEEDGFHIN LTVLDTPGFG DFIDNTSCWN TVAEYLDEQH
ERYLIHDQNS LRVPRKDTRV HVCLYFITPV SFGMLPLDVL AMKELSTHVN LVPVIAKADT
FTTPELTQIK QKIRRILEAQ SIDVFHPSTE YSDYETAELL DSSLPYAIIS SVNEVCKDDG
EKSQGRRYPW GTSEIYEETH CDFLKLKKLL INRHMLELIN TTETNIYERY RREQLTNRKS
GIPKLKKEHY ERLNNEKRAI QQKITQMTNE TESFFQAKEE KMIETRDALN SELSEYHERI
RALETQIESL KSYKGRGHKK
