SPN1_SCHPO
ID SPN1_SCHPO Reviewed; 469 AA.
AC O36023; Q09126;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2000, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Septin homolog spn1;
GN Name=spn1; ORFNames=SPAC4F10.11;
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].
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).
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 {ECO:0000269|PubMed:15385632}.
CC -!- SUBUNIT: Component of the septin complex composed of two copies of each
CC spn1, spn2, spn3 and spn4. {ECO:0000269|PubMed:15385632}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex
CC {ECO:0000269|PubMed:15385632}. Note=Localizes to the medial ring at the
CC cell cortex of dividing cells.
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; U31742; AAB53692.2; -; Genomic_DNA.
DR EMBL; CU329670; CAB11714.2; -; Genomic_DNA.
DR PIR; T38815; T38815.
DR PIR; T52562; T52562.
DR RefSeq; NP_594754.1; NM_001020181.2.
DR AlphaFoldDB; O36023; -.
DR SMR; O36023; -.
DR BioGRID; 279934; 74.
DR STRING; 4896.SPAC4F10.11.1; -.
DR iPTMnet; O36023; -.
DR MaxQB; O36023; -.
DR PaxDb; O36023; -.
DR PRIDE; O36023; -.
DR EnsemblFungi; SPAC4F10.11.1; SPAC4F10.11.1:pep; SPAC4F10.11.
DR GeneID; 2543516; -.
DR KEGG; spo:SPAC4F10.11; -.
DR PomBase; SPAC4F10.11; spn1.
DR VEuPathDB; FungiDB:SPAC4F10.11; -.
DR eggNOG; KOG2655; Eukaryota.
DR HOGENOM; CLU_017718_8_0_1; -.
DR InParanoid; O36023; -.
DR OMA; HTNNFLY; -.
DR PhylomeDB; O36023; -.
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:O36023; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0032153; C:cell division site; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0031097; C:medial cortex; IDA:PomBase.
DR GO; GO:0036391; C:medial cortex septin ring; IDA:PomBase.
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: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:0000281; P:mitotic cytokinesis; IMP:PomBase.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
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 InterPro; IPR025662; Sigma_54_int_dom_ATP-bd_1.
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; Coiled coil; Cytoplasm; GTP-binding; Mitosis;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..469
FT /note="Septin homolog spn1"
FT /id="PRO_0000173503"
FT DOMAIN 92..367
FT /note="Septin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 102..109
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 162..165
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 243..246
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT COILED 383..469
FT /evidence="ECO:0000255"
FT COMPBIAS 23..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 102..109
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 139
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 165
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 244..252
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 317
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 469 AA; 53738 MW; 3CCC9AD0052897A4 CRC64;
MASMVLADGM PTVKDDSTRS RGSDVDSFTS TDNVTQINVE AAISENKNEE KPIQDNSEQE
FNPHVSIIQR QLNGYVGFAS LPNQWHRRCV RQGFNFNVLV LGESGSGKST LVNTLLNRDV
YPPTQKSLTG DFGVNPEPTV MINSSAVEIV ENGISLQLNV IDTPGFGDFI DNTDCWQPVL
TDIEGRYDQY LELEKHNPRS TIQDPRVHAC IFFIQPTGHA ISAMELRVML ALHEKVNIIP
IIAKADTLTD DELNFTKEMI LRDIQYHNIR IFFPPTYETD DPESVAENAD IMSRIPFAII
ASNTFVVNNE GKRVRGRRYP WGVVEVDNEE HSDFPKLREM LIRTHLEELK EQTNKLYEAY
RTERLLSSGI SQDHSVFREV NPSAKLEEER ALHEEKLMKM EAEMKTIFSQ KVQEKEDRLK
QSENELRTRH REMKAALEKQ KADLIDHKNR LMQAKAAAEN EKSKRKFFK
