ID A0A2U4CI21_TURTR Unreviewed; 399 AA.
AC A0A2U4CI21;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Septin {ECO:0000256|PIRNR:PIRNR006698};
GN Name=SEPTIN6 {ECO:0000313|RefSeq:XP_019805082.1,
GN ECO:0000313|RefSeq:XP_019805091.1};
OS Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Delphinidae; Tursiops.
OX NCBI_TaxID=9739 {ECO:0000313|Proteomes:UP000245320, ECO:0000313|RefSeq:XP_019805091.1};
RN [1] {ECO:0000313|RefSeq:XP_019805082.1, ECO:0000313|RefSeq:XP_019805091.1}
RP IDENTIFICATION.
RC TISSUE=Spleen {ECO:0000313|RefSeq:XP_019805082.1,
RC ECO:0000313|RefSeq:XP_019805091.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 RefSeq; XP_019805082.1; XM_019949523.2.
DR RefSeq; XP_019805091.1; XM_019949532.2.
DR GeneID; 101332228; -.
DR OrthoDB; 5396944at2759; -.
DR Proteomes; UP000245320; Chromosome X.
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 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00023212, ECO:0000256|PIRNR:PIRNR006698};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212,
KW 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000245320}.
FT DOMAIN 1..247
FT /note="Septin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51719"
FT REGION 342..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 263..341
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 343..359
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..380
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 399 AA; 45914 MW; D704E8130ACB8C7B CRC64;
MDTLFNTKFE GEPATHTQPG VQLQSNTYDL QESNVGLKLT IVSTVGFGDQ INKEDSYRPI
VEFIDAQFEA YLQEELKIRR LLHNYHDSRI HACLYFIAPT GHSLKSLDLV TMKKLDSKVN
VIPIIAKSDA ISKSELTKFK IKITSELVSN GVQIYQFPTD DEAVAEINGT MNAHLPFAVI
GSTEELKIGN KMVKARQYPW GTVQVENEAH CDFVKLREML IRVNMEDLRE QTHSRHYELY
RRCKLEEMGF KDTDPDSKPF SLQETYEAKR NEFLGELQKK EEEMRQMFVQ RVKEKEAELK
EAEKELHEKF DRLKKLHQDE KKKLEDKKKS LDDEVNAFKQ RKTAAELLQS QGSQAGGSQT
LKRDKEKKKT REEKSISDRT CTTPGKHPVV PCALVVCAV
//
