ID A0A2Y9MAG7_DELLE Unreviewed; 427 AA.
AC A0A2Y9MAG7;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Septin {ECO:0000256|PIRNR:PIRNR006698};
GN Name=SEPTIN6 {ECO:0000313|RefSeq:XP_022418719.1,
GN ECO:0000313|RefSeq:XP_022418720.1, ECO:0000313|RefSeq:XP_022418721.1};
OS Delphinapterus leucas (Beluga whale).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Monodontidae; Delphinapterus.
OX NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022418720.1};
RN [1] {ECO:0000313|RefSeq:XP_022418719.1, ECO:0000313|RefSeq:XP_022418720.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022418719.1,
RC ECO:0000313|RefSeq:XP_022418720.1};
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_022418719.1; XM_022563011.1.
DR RefSeq; XP_022418720.1; XM_022563012.1.
DR RefSeq; XP_022418721.1; XM_022563013.1.
DR Ensembl; ENSDLET00000029331; ENSDLEP00000026669; ENSDLEG00000019290.
DR Proteomes; UP000248483; Unplaced.
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:UP000248483}.
FT DOMAIN 39..305
FT /note="Septin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51719"
FT REGION 400..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 321..399
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 401..417
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 427 AA; 48742 MW; 66398C08E4793E25 CRC64;
MAATDIARQA GEGCRTVPLA GHVGFDSLPD QLVNQSISQG FCFNILCVGE TGLGKSTLMD
TLFNTKFEGE PATHTQPGVQ LQSNTYDLQE SNVGLKLTIV STVGFGDQIN KEDSYRPIVE
FIDAQFEAYL QEELKIRRLL HNYHDSRIHA CLYFIAPTGH SLKSLDLVTM KKLDSKVNVI
PIIAKSDAIS KSELTKFKIK ITSELVSNGV QIYQFPMDDE AVAEVNGTMN AHLPFAVIGS
TEELKIGNKM VKVRQYPWGT VQVENEAHCD FVKLREMLIR VNMEDLREQT HSRHYELYRR
CKLEEMGFKD TDPDSKPFSL QETYEAKRNE FLGELQKKEE EMRQMFVQRV KEKEAELKEA
EKELHEKFDR LKKLHQDEKK KLEDKKKSLD DEVNAFKQRK TAAELLQSQG SQAGGSQTLK
RDKEKKN
//
