ID   SEP10_PONAB             Reviewed;         467 AA.
AC   Q5REG8;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Septin-10;
GN   Name=SEPTIN10 {ECO:0000250|UniProtKB:Q9P0V9}; Synonyms=SEPT10;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Filament-forming cytoskeletal GTPase (By similarity). May
CC       play a role in cytokinesis (Potential). {ECO:0000250, ECO:0000305}.
CC   -!- SUBUNIT: Septins polymerize into heterooligomeric protein complexes
CC       that form filaments, and can associate with cellular membranes, actin
CC       filaments and microtubules. GTPase activity is required for filament
CC       formation (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton {ECO:0000250}.
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; CR857561; CAH89839.1; -; mRNA.
DR   AlphaFoldDB; Q5REG8; -.
DR   SMR; Q5REG8; -.
DR   STRING; 9601.ENSPPYP00000013540; -.
DR   eggNOG; KOG3859; Eukaryota.
DR   InParanoid; Q5REG8; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; 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   2: Evidence at transcript level;
KW   Cell cycle; Cell division; Cytoplasm; Cytoskeleton; GTP-binding;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..467
FT                   /note="Septin-10"
FT                   /id="PRO_0000173540"
FT   DOMAIN          63..329
FT                   /note="Septin-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT   REGION          73..80
FT                   /note="G1 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT   REGION          125..128
FT                   /note="G3 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT   REGION          208..211
FT                   /note="G4 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT   BINDING         73..80
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         128
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         209..217
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         263
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         278
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   467 AA;  54203 MW;  5B70FC4F2F69CDEF CRC64;
     MASSEVARHL LFQSHMATKT TCMSSQGSDD EQRKRENIRS LTMSDHVGFE SLPDQLVNRS
     IQQGFCFNIL CVGETGIGKS TLIDTLFNTN FEDYESSHFC PNVKLKAQTY ELQESNVQLK
     LTIVNTVGFG DQINKEESYQ PIVDYIDAQF EAYLQEELKI KRSLFTYHDS RIHVCLYFIS
     PTGHSLKTLD LLTMKNLDSK VNIIPVIAKA DTVSKTELQK FKIKLMSELV SNGVQIYQFP
     TDDDTIAKVN AAMNGQLPFA VVGSMDEVKV GNKMVKARQY PWGVVQVENE NHCDFVKLRE
     VLICTNMEDL REQTHTRHYE LYRRCKLEEM GFTDVGPENK PVSLQETYEA KRHEFHGERQ
     RKEEEMKQMF VQRVKEKEAI LKEAERELQA KFEHLKRLHQ EERMKLEEKR KLLEEEIIAF
     SKKKATSEIF HSQSFLATGS NLRKQPQLLI FMEKYFQVQG QYVSQSE