ID A0A2Y9RXT1_PHYMC Unreviewed; 429 AA.
AC A0A2Y9RXT1;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Septin {ECO:0000256|PIRNR:PIRNR006698};
GN Name=SEPTIN11 {ECO:0000313|RefSeq:XP_023971118.1};
OS Physeter macrocephalus (Sperm whale) (Physeter catodon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Physeteridae; Physeter.
OX NCBI_TaxID=9755 {ECO:0000313|Proteomes:UP000248484, ECO:0000313|RefSeq:XP_023971118.1};
RN [1] {ECO:0000313|RefSeq:XP_023971118.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_023971118.1};
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 -!- SUBCELLULAR LOCATION: Cell projection, axon
CC {ECO:0000256|ARBA:ARBA00004489}. Cell projection, dendritic spine
CC {ECO:0000256|ARBA:ARBA00004552}.
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_007125105.1; XM_007125043.1.
DR RefSeq; XP_023971118.1; XM_024115350.3.
DR AlphaFoldDB; A0A2Y9RXT1; -.
DR SMR; A0A2Y9RXT1; -.
DR Ensembl; ENSPCTT00005008898; ENSPCTP00005008077; ENSPCTG00005005661.
DR KEGG; pcad:102978169; -.
DR Proteomes; UP000248484; Chromosome 7.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
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:SF48; SEPTIN-11; 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 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 Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000248484}.
FT DOMAIN 38..304
FT /note="Septin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51719"
FT REGION 403..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 429 AA; 49565 MW; C357ED8705FFD028 CRC64;
MAVAVGRPSN EELRNLSLSG HVGFDSLPDQ LVNKSTSQGF CFNILCVGET GIGKSTLMDT
LFNTKFESDP ATHNEPGVRL KARSYELQES NVRLKLTIVD TVGFGDQINK DDSYKPIVEY
IDAQFEAYLQ EELKIKRSLF NYHDTRIHAC LYFIAPTGHS LKSLDLVTMK KLDSKVNIIP
IIAKADTIAK NELHKFKSKI MSELVSNGVQ IYQFPTDEET VAEINATMSV HLPFAVVGST
EEVKIGNKMA KARQYPWGVV QVENENHCDF VKLREMLIRV NMEDLREQTH TRHYELYRRC
KLEEMGFKDT DPDSKPFSLQ ETYEAKRNEF LGELQKKEEE MRQMFVMRVK EKEAELKEAE
KELHEKFDLL KRTHQEEKKK VEDKKKELEE EVNNFQKKKA AAQLLQSQAQ QSGAQQTKKD
KDKKNFFFM
//
