ID   B4E049_HUMAN            Unreviewed;       369 AA.
AC   B4E049;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   24-JAN-2024, entry version 93.
DE   RecName: Full=Septin {ECO:0000256|PIRNR:PIRNR006698};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|EMBL:BAG64311.1};
RN   [1] {ECO:0000313|EMBL:BAG64311.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Thymus {ECO:0000313|EMBL:BAG64311.1};
RA   Wakamatsu A., Yamamoto J., Kimura K., Ishii S., Watanabe K., Sugiyama A.,
RA   Murakawa K., Kaida T., Tsuchiya K., Fukuzumi Y., Kumagai A., Oishi Y.,
RA   Yamamoto S., Ono Y., Komori Y., Yamazaki M., Kisu Y., Nishikawa T.,
RA   Sugano S., Nomura N., Isogai T.;
RT   "NEDO human cDNA sequencing project focused on splicing variants.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Filament-forming cytoskeletal GTPase.
CC       {ECO:0000256|PIRNR:PIRNR006698}.
CC   -!- SUBUNIT: Septins polymerize into heterooligomeric protein complexes
CC       that form filaments. {ECO:0000256|PIRNR:PIRNR006698}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC       GTPase superfamily. Septin GTPase family.
CC       {ECO:0000256|PIRNR:PIRNR006698, ECO:0000256|RuleBase:RU004560}.
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DR   EMBL; AK303224; BAG64311.1; -; mRNA.
DR   AlphaFoldDB; B4E049; -.
DR   MaxQB; B4E049; -.
DR   PeptideAtlas; B4E049; -.
DR   ProteomicsDB; 5649; -.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   CDD; cd01850; CDC_Septin; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR030379; G_SEPTIN_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR016491; Septin.
DR   PANTHER; PTHR18884; SEPTIN; 1.
DR   PANTHER; PTHR18884:SF55; SEPTIN-6; 1.
DR   Pfam; PF00735; Septin; 1.
DR   PIRSF; PIRSF006698; Septin; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51719; G_SEPTIN; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|PIRNR:PIRNR006698};
KW   Cytoskeleton {ECO:0000256|PIRNR:PIRNR006698};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|RuleBase:RU004560};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004560}.
FT   DOMAIN          1..247
FT                   /note="Septin-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51719"
FT   REGION          347..369
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          263..341
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   369 AA;  42895 MW;  D5C7D2E73016D172 CRC64;
     MDTLFNTKFE GEPATHTQPG VQLQSNTYDL QESNVRLKLT IVSTVGFGDQ INKEDSYKPI
     VEFIDAQFEA YLQEELKIRR VLHTYHDSRI HVCLYFIAPT GHSLKSLDLV TMKKLDSKVN
     IIPIIAKADA ISKSELTKFK IKITSELVSN GVQIYQFPTD DESVAEINGT MNAHLPFAVI
     GSTEELKIGN KMMRARQYPW GTVQVENEAH CDFVKLREML IRVNMEDLRE QTHTRHYELY
     RRCKLEEMGF KDTDPDSKPF SLQETYEAKR NEFLGELQKK EEEMRQMFVQ RVKEKEAELK
     EAEKELHEKF DRLKKLHQDE KKKLEDKKKS LDDEVNAFKQ RKTAAELLQS QGSQAGGSQT
     LKRDKEKKK
//