ID   SEP10_RAT               Reviewed;         456 AA.
AC   Q5PQK1;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Septin-10;
GN   Name=Septin10 {ECO:0000250|UniProtKB:Q9P0V9};
GN   Synonyms=Sept10 {ECO:0000312|RGD:1359307};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PROTEIN SEQUENCE OF 37-56, AND IDENTIFICATION BY MASS SPECTROMETRY.
RA   Lubec G., Chen W.-Q.;
RL   Submitted (SEP-2006) to UniProtKB.
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}.
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DR   EMBL; BC087157; AAH87157.1; -; mRNA.
DR   RefSeq; NP_001014055.1; NM_001014033.1.
DR   AlphaFoldDB; Q5PQK1; -.
DR   SMR; Q5PQK1; -.
DR   STRING; 10116.ENSRNOP00000064265; -.
DR   jPOST; Q5PQK1; -.
DR   PaxDb; Q5PQK1; -.
DR   PRIDE; Q5PQK1; -.
DR   Ensembl; ENSRNOT00000071663; ENSRNOP00000064265; ENSRNOG00000049507.
DR   GeneID; 309891; -.
DR   KEGG; rno:309891; -.
DR   CTD; 151011; -.
DR   RGD; 1359307; Sept10.
DR   eggNOG; KOG3859; Eukaryota.
DR   GeneTree; ENSGT00940000155238; -.
DR   HOGENOM; CLU_017718_8_1_1; -.
DR   InParanoid; Q5PQK1; -.
DR   OrthoDB; 845354at2759; -.
DR   PhylomeDB; Q5PQK1; -.
DR   PRO; PR:Q5PQK1; -.
DR   Proteomes; UP000002494; Chromosome 20.
DR   GO; GO:0032153; C:cell division site; IBA:GO_Central.
DR   GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
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; IEA:UniProtKB-KW.
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: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; Cytoskeleton;
KW   Direct protein sequencing; GTP-binding; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..456
FT                   /note="Septin-10"
FT                   /id="PRO_0000173541"
FT   DOMAIN          40..306
FT                   /note="Septin-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT   REGION          50..57
FT                   /note="G1 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT   REGION          102..105
FT                   /note="G3 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT   REGION          185..188
FT                   /note="G4 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT   BINDING         50..57
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         105
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         186..194
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         240
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         255
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         418
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8C650"
FT   CONFLICT        38..39
FT                   /note="IE -> TS (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   456 AA;  53039 MW;  C4EB9C1793BE75E9 CRC64;
     MASCDEVRQL KKEHTRSLTM CGHVGFESLP DQLVDRSIEQ GFCFNILCVG ETGIGKSTLI
     NTLFNTNFEE LESSHFCPCV RLRAQTYELQ ESNVRLKLTI VNTVGFGDQI NKEESYQPIV
     DYIDNQFEAY LQEELKIKRA LFNYHDSRIH VCLYFIAPTG HSLRTLDLLT MKSLDNKVNI
     IPLIAKADTI SKSELQKFKM KLMSELVING VQIYQFPTDD DTTAKINGAM NGHLPFAVVG
     SMDEIKVGNK MVKARQYPWG IVQVENENHC DFVKLREMLI CTNMEDLREQ THMRHYELYR
     RCKLQEMGFI DIGPENKPLS LQETYEAKRH EFCGERQRKE EQMKQMFVQR VKEKEAILKE
     AERELQAKFE HLKRIHQEER MKLEEKRRML EEESVAFAKK KATCELFPHQ SFLASGSSIR
     RDKDRKKTDG ASAFCDCITA QENVRLCISS QRKEMD