ID A0A2K6AFR3_MANLE Unreviewed; 396 AA.
AC A0A2K6AFR3;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Septin {ECO:0000256|PIRNR:PIRNR006698};
GN Name=SEPTIN2 {ECO:0000313|Ensembl:ENSMLEP00000038870.1};
OS Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Mandrillus.
OX NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000038870.1, ECO:0000313|Proteomes:UP000233140};
RN [1] {ECO:0000313|Ensembl:ENSMLEP00000038870.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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, cilium membrane
CC {ECO:0000256|ARBA:ARBA00004309}. Cell projection, cilium, flagellum
CC {ECO:0000256|ARBA:ARBA00004230}. Cleavage furrow
CC {ECO:0000256|ARBA:ARBA00004626}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000256|ARBA:ARBA00004186}. Membrane
CC {ECO:0000256|ARBA:ARBA00004370}. Midbody
CC {ECO:0000256|ARBA:ARBA00004214}.
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_011851766.1; XM_011996376.1.
DR RefSeq; XP_011851767.1; XM_011996377.1.
DR AlphaFoldDB; A0A2K6AFR3; -.
DR STRING; 9568.ENSMLEP00000038870; -.
DR Ensembl; ENSMLET00000062484.1; ENSMLEP00000038870.1; ENSMLEG00000043469.1.
DR GeneID; 105551219; -.
DR KEGG; mleu:105551219; -.
DR CTD; 4735; -.
DR GeneTree; ENSGT00940000155098; -.
DR OrthoDB; 5396944at2759; -.
DR Proteomes; UP000233140; Unplaced.
DR GO; GO:0015629; C:actin cytoskeleton; IEA:Ensembl.
DR GO; GO:0005930; C:axoneme; IEA:Ensembl.
DR GO; GO:0060170; C:ciliary membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR GO; GO:0045171; C:intercellular bridge; IEA:Ensembl.
DR GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0032391; C:photoreceptor connecting cilium; IEA:Ensembl.
DR GO; GO:0031105; C:septin complex; IEA:Ensembl.
DR GO; GO:0097227; C:sperm annulus; IEA:Ensembl.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:InterPro.
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 InterPro; IPR008113; Septin2.
DR PANTHER; PTHR18884; SEPTIN; 1.
DR PANTHER; PTHR18884:SF67; SEPTIN-2; 1.
DR Pfam; PF00735; Septin; 1.
DR PIRSF; PIRSF006698; Septin; 1.
DR PRINTS; PR01740; SEPTIN2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51719; G_SEPTIN; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW Cell division {ECO:0000256|ARBA:ARBA00022776};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Cytoplasm {ECO:0000256|PIRNR:PIRNR006698};
KW Cytoskeleton {ECO:0000256|PIRNR:PIRNR006698};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|PIRSR:PIRSR006698-
KW 2}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Mitosis {ECO:0000256|ARBA:ARBA00022776};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR006698-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000233140}.
FT DOMAIN 69..341
FT /note="Septin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51719"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 191
FT /note="Important for dimerization"
FT /evidence="ECO:0000256|PIRSR:PIRSR006698-2"
SQ SEQUENCE 396 AA; 45450 MW; 8A58BF1F2E4DB907 CRC64;
MRRISGERAT RPCLRVPSAR RGDEGLPQRD EASQKMSKQQ PTQFINPETP GYVGFANLPN
QVHRKSVKKG FEFTLMVVGE SGLGKSTLIN SLFLTDLYPE RVIPGAAEKI ERTVQIEAST
VEIEERGVKL RLTVVDTPGY GDAINCRDCF KTIISYIDEQ FERYLHDESG LNRRHIIDNR
VHCCFYFISP FGHGLKPLDV AFMKAIHNKV NIVPVIAKAD TLTLKERERL KKRILDEIEE
HNIKIYHLPD AESDEDEDFK EQTRLLKASI PFSVVGSNQL IEAKGKKVRG RLYPWGVVEV
ENPEHNDFLK LRTMLITHMQ DLQEVTQDLH YENFRSERLK RGGRKVENED MNKDQILLEK
EAELRRMQEM IARMQAQMQM QMQGGDGDGG ALGHHV
//
