ID   SEP10_BOVIN             Reviewed;         453 AA.
AC   Q2KJB1;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Septin-10;
GN   Name=SEPTIN10 {ECO:0000250|UniProtKB:Q9P0V9}; Synonyms=SEPT10;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Hypothalamus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (SEP-2005) 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}.
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DR   EMBL; BC105431; AAI05432.1; -; mRNA.
DR   RefSeq; NP_001039641.1; NM_001046176.1.
DR   AlphaFoldDB; Q2KJB1; -.
DR   SMR; Q2KJB1; -.
DR   STRING; 9913.ENSBTAP00000048430; -.
DR   PaxDb; Q2KJB1; -.
DR   PRIDE; Q2KJB1; -.
DR   Ensembl; ENSBTAT00000081710; ENSBTAP00000074087; ENSBTAG00000022461.
DR   GeneID; 514603; -.
DR   KEGG; bta:514603; -.
DR   CTD; 151011; -.
DR   VEuPathDB; HostDB:ENSBTAG00000022461; -.
DR   VGNC; VGNC:34450; SEPTIN10.
DR   eggNOG; KOG3859; Eukaryota.
DR   GeneTree; ENSGT00940000155238; -.
DR   InParanoid; Q2KJB1; -.
DR   OrthoDB; 845354at2759; -.
DR   Proteomes; UP000009136; Chromosome 11.
DR   Bgee; ENSBTAG00000022461; Expressed in spermatid and 105 other tissues.
DR   ExpressionAtlas; Q2KJB1; baseline and differential.
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   2: Evidence at transcript level;
KW   Cell cycle; Cell division; Cytoplasm; Cytoskeleton; GTP-binding;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..453
FT                   /note="Septin-10"
FT                   /id="PRO_0000270224"
FT   DOMAIN          62..328
FT                   /note="Septin-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT   REGION          18..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          72..79
FT                   /note="G1 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT   REGION          124..127
FT                   /note="G3 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT   REGION          207..210
FT                   /note="G4 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT   REGION          433..453
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         72..79
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         127
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         208..216
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         262
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         277
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   453 AA;  52809 MW;  A5FB39ABF2100353 CRC64;
     MASEVARHLL FQSHITTKTA HTSSQVSDHE QKQKDSPRSL TMSGHVGFES LPDQLVNRSI
     QQGFCFNILC VGETGIGKST LIDTLFNTNF EDHESSHFYP HVRLKAQTYE LQESNVRLKL
     TIVNTVGFGD QINKEESYQP IVDYIDAQFE AYLQEELKIK RSLFNYHDSR VHVCLYFISP
     TGHSLKTLDL LTMKSLDSKV NIIPVIAKAD AISKTELQKF KIKLMSELVS NGVQIYQFPT
     DDETIAKINA SMNGHLPFAV VGSMDEVKVG NKMVKARQYP WGVVQVENEN HCDFVKLREM
     LICTNMEDLR DQTHTRHYEL YRRRKLEEMG FMDVGPENQP LSLQETYEAK RHEFYGERQR
     KEEEMKQLFV QRVKEKEAIL KEAERELQAK FEHLKRVHQE EKLRLEEKRR LLEEEIMAFS
     KKKATSEIYQ NQTFMTPGSN LRKDKDRKNS NFM