SPN7_SCHPO
ID SPN7_SCHPO Reviewed; 428 AA.
AC O60165; O94648; Q7Z994; Q96US7;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 14-AUG-2001, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Septin homolog spn7;
GN Name=spn7; ORFNames=SPBC19F8.01c, SPBC21.08c;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 298-428.
RA Wu J.-Q., Pringle J.R.;
RT "Roles of septins in the fission yeast S. pombe.";
RL Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP CHARACTERIZATION.
RA Wu J.-Q., Pringle J.R.;
RL Submitted (MAR-2001) to UniProtKB.
RN [4]
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 [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: Septin-like protein involved in the correct orientation of
CC forespore membrane extension during sporulation. Binds
CC phosphatidylinositol 4-phosphate. {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. Nucleus. Forespore membrane;
CC Peripheral membrane protein. Note=The sporulation-specific septin
CC complex associates to the forespore membrane and forms partial or
CC complete 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; CU329671; CAD99124.1; -; Genomic_DNA.
DR EMBL; AF417166; AAL13302.1; -; mRNA.
DR PIR; T39824; T39824.
DR RefSeq; XP_001713143.1; XM_001713091.2.
DR AlphaFoldDB; O60165; -.
DR SMR; O60165; -.
DR BioGRID; 276941; 6.
DR STRING; 4896.SPBC19F8.01c.1; -.
DR iPTMnet; O60165; -.
DR MaxQB; O60165; -.
DR PaxDb; O60165; -.
DR PRIDE; O60165; -.
DR EnsemblFungi; SPBC19F8.01c.1; SPBC19F8.01c.1:pep; SPBC19F8.01c.
DR PomBase; SPBC19F8.01c; spn7.
DR VEuPathDB; FungiDB:SPBC19F8.01c; -.
DR eggNOG; KOG2655; Eukaryota.
DR HOGENOM; CLU_017718_7_4_1; -.
DR InParanoid; O60165; -.
DR OMA; AHGRFEN; -.
DR PhylomeDB; O60165; -.
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:O60165; -.
DR Proteomes; UP000002485; Chromosome II.
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: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:0008289; F:lipid binding; IEA:UniProtKB-KW.
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 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 PROSITE; PS51719; G_SEPTIN; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; GTP-binding; Lipid-binding; Meiosis; Membrane;
KW Nucleotide-binding; Nucleus; Reference proteome; Sporulation.
FT CHAIN 1..428
FT /note="Septin homolog spn7"
FT /id="PRO_0000173509"
FT DOMAIN 15..290
FT /note="Septin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 25..32
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 83..86
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 165..168
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 287..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 387..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..312
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..327
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 389..406
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 25..32
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 86
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 166..174
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 224
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 428 AA; 49298 MW; CD0B4E1D82DF41A4 CRC64;
MNKGPRHRPK FLSKKGKKLR IMVAGSSYTS YQACINSLCS KQILEAETEI DPLKAHIDRI
LEIREFNADI LEDEFHVDLT VIEVNGFGDK IDNSASFEVV THYLESQFDQ ALIEESKIKR
NSKFTDTRVD ALLYFIAPRG HCLSEFDLEA MKRFSKRVNV IPVIGNSNAF TEEELKNFKD
VIMKDLKQCN IKVFDFPWDP EEDEDEVIED NKRLWESVPF AVSGGVSEED EEGYQRIVKK
FQWGTFVIDD PAHSDFLNLK TVLFISHLDI LKSITKQTYY ENYRTEKLSN DSPSNTSLSL
QKQNSIVANE DKRSVNGSER TETRSSIDQS EMRTNVSDST KSEELKKINS IKVDNTSSLK
CDSYGNTKTK TNQLNCEQIG LEVISPKEFP HRTTSSRNSL PNNTTKELEM KKMDDLSHER
YENLPFYR
