SPN4_SCHPO
ID SPN4_SCHPO Reviewed; 380 AA.
AC P48009;
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 spn4;
GN Name=spn4; ORFNames=SPAC9G1.11c;
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].
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 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 [3]
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U29890; AAB53689.1; -; mRNA.
DR EMBL; CU329670; CAB11495.1; -; Genomic_DNA.
DR PIR; T39234; T39234.
DR RefSeq; NP_593566.1; NM_001018999.2.
DR AlphaFoldDB; P48009; -.
DR SMR; P48009; -.
DR BioGRID; 278668; 30.
DR STRING; 4896.SPAC9G1.11c.1; -.
DR MaxQB; P48009; -.
DR PaxDb; P48009; -.
DR PRIDE; P48009; -.
DR EnsemblFungi; SPAC9G1.11c.1; SPAC9G1.11c.1:pep; SPAC9G1.11c.
DR PomBase; SPAC9G1.11c; spn4.
DR VEuPathDB; FungiDB:SPAC9G1.11c; -.
DR eggNOG; KOG2655; Eukaryota.
DR HOGENOM; CLU_017718_0_0_1; -.
DR InParanoid; P48009; -.
DR OMA; EMKGSIP; -.
DR PhylomeDB; P48009; -.
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:P48009; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0032153; C:cell division site; HDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA: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:0031105; C:septin complex; IBA:GO_Central.
DR GO; GO:0005940; C:septin ring; IDA:PomBase.
DR GO; GO:0032176; C:split septin rings; IDA:PomBase.
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 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; Mitosis;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..380
FT /note="Septin homolog spn4"
FT /id="PRO_0000173506"
FT DOMAIN 25..298
FT /note="Septin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 35..42
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 93..96
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 174..177
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT BINDING 35..42
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 70
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 96
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 175..183
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 231
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 247
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 380 AA; 44773 MW; BFE92A3F784DE9B3 CRC64;
MNEEETNFVG IADLPNQRHK IVSRNGVAFT LMLCGESGLG KTTFCNTLFS TTIKSHMGPE
KVRAKHAEKT VEIEITKAEL EEKNFHLRLT VIDTPGFGDF INNSGCWESV VEFIEDQHES
YMRQDQQPDR RKIIDMRIHA CLYFLRPVRN GVRPMDLEAM KHISKRVNLI PVIAKADMYT
RRDLALYKTR ISQVLEYHQV NVYKPNMDEG DPVFHRQIQG IINCMPFAIV GSEDDIRTPD
GRVVKGREYP WGIVEIENEE HCDFKQLRNI LIRSCMLDLI QTTEEKLYEQ YRQEQMKVRQ
YGEPKLRTID NAKFKEEEEN LRKRFTEQVR VEETRFRQWE QRLIAERDSL NKDLEAQHVQ
IKQIELEIER LKAATSSRKR
