SEP10_SCHMA
ID SEP10_SCHMA Reviewed; 412 AA.
AC A0A3Q0KDV9; G4VFI8;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 13-FEB-2019, sequence version 1.
DT 03-AUG-2022, entry version 15.
DE RecName: Full=Septin-10 {ECO:0000305, ECO:0000312|EMBL:AGT02087.1};
DE AltName: Full=SmSEPT10 {ECO:0000303|PubMed:24367716, ECO:0000303|PubMed:24464615, ECO:0000303|PubMed:24768753, ECO:0000303|PubMed:27687162};
GN Name=SEPT10 {ECO:0000305};
GN ORFNames=Smp_029890 {ECO:0000312|EMBL:CCD78697.1};
OS Schistosoma mansoni (Blood fluke).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=6183 {ECO:0000312|Proteomes:UP000008854, ECO:0000312|WBParaSite:Smp_029890.1};
RN [1] {ECO:0000312|EMBL:AGT02087.1}
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND
RP PHYLOGENETIC ANALYSIS.
RX PubMed=24367716; DOI=10.1371/journal.pntd.0002602;
RA Zeraik A.E., Rinaldi G., Mann V.H., Popratiloff A., Araujo A.P.,
RA Demarco R., Brindley P.J.;
RT "Septins of Platyhelminths: identification, phylogeny, expression and
RT localization among developmental stages of Schistosoma mansoni.";
RL PLoS Negl. Trop. Dis. 7:e2602-e2602(2013).
RN [2] {ECO:0000312|Proteomes:UP000008854}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Puerto Rican {ECO:0000312|Proteomes:UP000008854};
RX PubMed=22253936; DOI=10.1371/journal.pntd.0001455;
RA Protasio A.V., Tsai I.J., Babbage A., Nichol S., Hunt M., Aslett M.A.,
RA De Silva N., Velarde G.S., Anderson T.J., Clark R.C., Davidson C.,
RA Dillon G.P., Holroyd N.E., LoVerde P.T., Lloyd C., McQuillan J.,
RA Oliveira G., Otto T.D., Parker-Manuel S.J., Quail M.A., Wilson R.A.,
RA Zerlotini A., Dunne D.W., Berriman M.;
RT "A systematically improved high quality genome and transcriptome of the
RT human blood fluke Schistosoma mansoni.";
RL PLoS Negl. Trop. Dis. 6:E1455-E1455(2012).
RN [3]
RP PROTEIN SEQUENCE OF 176-184 AND 383-393, AND SUBUNIT.
RX PubMed=24768753; DOI=10.1016/j.ijpara.2014.03.010;
RA Zeraik A.E., Galkin V.E., Rinaldi G., Garratt R.C., Smout M.J., Loukas A.,
RA Mann V.H., Araujo A.P., DeMarco R., Brindley P.J.;
RT "Reversible paralysis of Schistosoma mansoni by forchlorfenuron, a
RT phenylurea cytokinin that affects septins.";
RL Int. J. Parasitol. 44:523-531(2014).
RN [4]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, DOMAIN, MUTAGENESIS OF
RP THR-157; TRP-257 AND HIS-267, AND CIRCULAR DICHROISM ANALYSIS.
RX PubMed=27687162; DOI=10.1016/j.biochi.2016.09.014;
RA Zeraik A.E., Staykova M., Fontes M.G., Nemuraite I., Quinlan R.,
RA Araujo A.P., DeMarco R.;
RT "Biophysical dissection of schistosome septins: Insights into
RT oligomerization and membrane binding.";
RL Biochimie 131:96-105(2016).
RN [5] {ECO:0007744|PDB:4KV9, ECO:0007744|PDB:4KVA}
RP X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) IN COMPLEXES WITH GDP; GTP AND
RP MAGNESIUM, FUNCTION, COFACTOR, AND SUBUNIT.
RX PubMed=24464615; DOI=10.1074/jbc.m113.525352;
RA Zeraik A.E., Pereira H.M., Santos Y.V., Brandao-Neto J., Spoerner M.,
RA Santos M.S., Colnago L.A., Garratt R.C., Araujo A.P., DeMarco R.;
RT "Crystal structure of a Schistosoma mansoni septin reveals the phenomenon
RT of strand slippage in septins dependent on the nature of the bound
RT nucleotide.";
RL J. Biol. Chem. 289:7799-7811(2014).
CC -!- FUNCTION: Filament-forming GTP-binding protein. Lacks GTPase activity,
CC which is likely due to absence of an essential threonine residue
CC important for hydrolytic activity in septins. May be involved in
CC membrane remodeling, potentially by its nucleotide-dependent cellular
CC membrane association/dissociation ability (PubMed:24464615). Able to
CC bind to phosphatidylinositol-4,5-bisphosphate (PIP2)-containing giant
CC unilamellar vesicles (GUVs), which serve as a model of biological
CC membranes. Self-assembles into ordered cage-like structures on the
CC vesicle membrane. Binds also to 1,2-dioleoyl-sn-glycero-3-phospho-L-
CC serine (DOPS)-containing vesicles suggesting the requirement for
CC negatively charged membranes. Is also able to promote deformation of
CC the GUVs (PubMed:27687162). {ECO:0000269|PubMed:24464615,
CC ECO:0000269|PubMed:27687162}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:24464615};
CC Note=Mg(2+) is essential for the GTP-binding, but GDP-binding does not
CC require a metal cofactor. {ECO:0000269|PubMed:24464615};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Stable at wide pH range from 4 to 9. {ECO:0000269|PubMed:27687162};
CC Temperature dependence:
CC Temperature-sensitive. Stable at 15 degrees Celsius. Starts to
CC aggregate at 37 degrees Celsius. {ECO:0000269|PubMed:27687162};
CC -!- SUBUNIT: Septins polymerize into heterooligomeric protein complexes
CC that form filaments, and can associate with cellular membranes, actin
CC filaments and microtubules (By similarity). Homodimer (PubMed:27687162,
CC PubMed:24464615). Homooligomerizes (PubMed:27687162). Forms (via GTP-
CC binding domain) heterodimers with SEPT5 (via GTP-binding domain) in a
CC nucleotide-dependent manner with GTP promoting heterodimerization most
CC efficiently (PubMed:27687162). Component of the filamentous forming
CC heterocomplex composed of SEPT10, SEPT5 and SEPT7.2 (PubMed:24768753,
CC PubMed:27687162). Heterocomplex formation and the filamentous
CC polymerization of the complexes is enhanced by forchlorfenuron (FCF), a
CC synthetic phenylurea cytokinin (PubMed:24768753). The heterocomplex is
CC able to bind on the membranes of the phosphatidylinositol-4,5-
CC bisphosphate (PIP2)-containing giant unilamellar vesicles (GUVs), which
CC serve as a model of biological membranes (PubMed:27687162).
CC {ECO:0000250|UniProtKB:Q9NVA2, ECO:0000269|PubMed:24464615,
CC ECO:0000269|PubMed:24768753, ECO:0000269|PubMed:27687162}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q8C1B7}. Note=Colocalizes with actin in the
CC longitudinal and circular muscles of the sporocyst.
CC {ECO:0000269|PubMed:24367716}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout the developmental cycle of
CC the schistosome, with the highest expression in 14-day old
CC schistosomula. Expressed in superficial structures of the miracidia and
CC sporocysts, with high expression in ciliated epidermal plates of the
CC miracidium, and in the longitudinal and circular muscles of the
CC sporocyst. High expression also in the optical sections of germ cells
CC in miracidia and 2-day old sporocysts. Expressed along the
CC protonephridial ducts of the cercaria, extending laterally nearly the
CC whole length on both sides of the larva. More specifically expressed at
CC the collecting tubules of this osmoregulatory system. Expressed
CC ubiquitously in the schistosomulum. In adults, expression is higher in
CC males than in females. {ECO:0000269|PubMed:24367716}.
CC -!- DOMAIN: C-terminus (307-412) is necessary for binding to liposomal
CC membranes as assessed by phosphatidylinositol-4,5-bisphosphate (PIP2)-
CC containing giant unilamellar vesicles (GUVs), models of biological
CC membranes. {ECO:0000269|PubMed:27687162}.
CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC GTPase superfamily. Septin GTPase family.
CC {ECO:0000255|PIRNR:PIRNR006698, ECO:0000255|PROSITE-ProRule:PRU01056,
CC ECO:0000255|RuleBase:RU004560}.
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; KC916726; AGT02087.1; -; mRNA.
DR EMBL; HE601626; CCD78697.1; -; Genomic_DNA.
DR RefSeq; XP_018651305.1; XM_018799525.1.
DR PDB; 4KV9; X-ray; 1.93 A; A/B=1-412.
DR PDB; 4KVA; X-ray; 2.14 A; A/B=1-412.
DR PDBsum; 4KV9; -.
DR PDBsum; 4KVA; -.
DR AlphaFoldDB; A0A3Q0KDV9; -.
DR STRING; 6183.Smp_029890.1; -.
DR EnsemblMetazoa; Smp_029890.1; Smp_029890.1; Smp_029890.
DR GeneID; 8347800; -.
DR KEGG; smm:Smp_029890; -.
DR WBParaSite; Smp_029890.1; Smp_029890.1; Smp_029890.
DR CTD; 8347800; -.
DR eggNOG; KOG3859; Eukaryota.
DR HOGENOM; CLU_017718_8_1_1; -.
DR InParanoid; A0A3Q0KDV9; -.
DR OMA; NGFIFNI; -.
DR OrthoDB; 845354at2759; -.
DR PhylomeDB; A0A3Q0KDV9; -.
DR Proteomes; UP000008854; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 3D-structure; Coiled coil; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Glycoprotein; GTP-binding; Magnesium;
KW Metal-binding; Nucleotide-binding; Reference proteome.
FT CHAIN 1..412
FT /note="Septin-10"
FT /id="PRO_0000455606"
FT DOMAIN 38..304
FT /note="Septin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 48..55
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 100..103
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 183..186
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT COILED 308..401
FT /evidence="ECO:0000255"
FT BINDING 51..56
FT /ligand="GDP"
FT /ligand_id="ChEBI:CHEBI:58189"
FT /evidence="ECO:0000269|PubMed:24464615,
FT ECO:0007744|PDB:4KV9"
FT BINDING 51..56
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:24464615,
FT ECO:0007744|PDB:4KVA"
FT BINDING 55
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:24464615,
FT ECO:0007744|PDB:4KVA"
FT BINDING 100
FT /ligand="GDP"
FT /ligand_id="ChEBI:CHEBI:58189"
FT /evidence="ECO:0000269|PubMed:24464615,
FT ECO:0007744|PDB:4KV9"
FT BINDING 100
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:24464615,
FT ECO:0007744|PDB:4KVA"
FT BINDING 100
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:24464615,
FT ECO:0007744|PDB:4KVA"
FT BINDING 184..187
FT /ligand="GDP"
FT /ligand_id="ChEBI:CHEBI:58189"
FT /evidence="ECO:0000269|PubMed:24464615,
FT ECO:0007744|PDB:4KV9"
FT BINDING 184..187
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:24464615,
FT ECO:0007744|PDB:4KVA"
FT BINDING 192
FT /ligand="GDP"
FT /ligand_id="ChEBI:CHEBI:58189"
FT /evidence="ECO:0000269|PubMed:24464615,
FT ECO:0007744|PDB:4KV9"
FT BINDING 192
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:24464615,
FT ECO:0007744|PDB:4KVA"
FT BINDING 238
FT /ligand="GDP"
FT /ligand_id="ChEBI:CHEBI:58189"
FT /evidence="ECO:0000269|PubMed:24464615,
FT ECO:0007744|PDB:4KV9"
FT BINDING 238
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:24464615,
FT ECO:0007744|PDB:4KVA"
FT BINDING 253..255
FT /ligand="GDP"
FT /ligand_id="ChEBI:CHEBI:58189"
FT /evidence="ECO:0000269|PubMed:24464615,
FT ECO:0007744|PDB:4KV9"
FT BINDING 253..255
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:24464615,
FT ECO:0007744|PDB:4KVA"
FT BINDING 253
FT /ligand="GDP"
FT /ligand_id="ChEBI:CHEBI:58189"
FT /evidence="ECO:0000269|PubMed:24464615,
FT ECO:0007744|PDB:4KV9"
FT BINDING 253
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:24464615,
FT ECO:0007744|PDB:4KVA"
FT CARBOHYD 405
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 157
FT /note="T->D: No effect on homooligomerization."
FT /evidence="ECO:0000269|PubMed:27687162"
FT MUTAGEN 257
FT /note="W->A: No effect on homooligomerization."
FT /evidence="ECO:0000269|PubMed:27687162"
FT MUTAGEN 267
FT /note="H->D: No effect on homooligomerization."
FT /evidence="ECO:0000269|PubMed:27687162"
FT CONFLICT 72
FT /note="N -> T (in Ref. 1; AGT02087)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 412 AA; 48090 MW; 2D31E24CF0BD69C4 CRC64;
MTADVLKALP PDVRTLKLSG HVGFDSLPDQ LVNKAISQGF VFNILCVGET GIGKSTLLET
LFNQKFDFSP SNHDLTDPKL KAVTYDLKEA NVKLKLTVVE TCGYGDQINK ENNIKPVVDY
IDNQFENYLQ EELKMKRSMQ AFHDTRVHVC LYFIAPTGHS LKSIDLVAMK KLENKVNVIP
VIAKSDTITK SELQKFKARI LSEIQSNEIG IYQFPTDDEA VSETNSVMNQ HIPFAVVGSS
EEVKINGKTV RVRQYPWGSV QVENENHCDF VRLREMLLRV NMEDLRERTH GVHYETYRRQ
RLIEMGFRDD EKMSLQETYE KRRELQRKEL QQKEEEMRQM FVQRVKEKEQ VLKEAERELQ
TKFESLKKTH AEEKKKLEEK KRFLEEEIAA FERRKQLAEQ ARQGNLTMKK RK
