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Database: UniProt
Entry: A0A2K5ZRZ9_MANLE
LinkDB: A0A2K5ZRZ9_MANLE
Original site: A0A2K5ZRZ9_MANLE 
ID   A0A2K5ZRZ9_MANLE        Unreviewed;       380 AA.
AC   A0A2K5ZRZ9;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=Septin {ECO:0000256|PIRNR:PIRNR006698};
GN   Name=SEPTIN1 {ECO:0000313|Ensembl:ENSMLEP00000030566.1};
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:ENSMLEP00000030566.1, ECO:0000313|Proteomes:UP000233140};
RN   [1] {ECO:0000313|Ensembl:ENSMLEP00000030566.1}
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   -!- 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   AlphaFoldDB; A0A2K5ZRZ9; -.
DR   STRING; 9568.ENSMLEP00000030566; -.
DR   Ensembl; ENSMLET00000054132.1; ENSMLEP00000030566.1; ENSMLEG00000039481.1.
DR   GeneTree; ENSGT00940000161794; -.
DR   OMA; EMKGSIP; -.
DR   Proteomes; UP000233140; Unplaced.
DR   GO; GO:0072687; C:meiotic spindle; IEA:Ensembl.
DR   GO; GO:0030496; C:midbody; IEA:Ensembl.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0051311; P:meiotic metaphase chromosome alignment; IEA:Ensembl.
DR   GO; GO:0007056; P:spindle assembly involved in female meiosis; IEA:Ensembl.
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:SF6; SEPTIN-1; 1.
DR   Pfam; PF00735; Septin; 1.
DR   PIRSF; PIRSF006698; Septin; 2.
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|PIRNR:PIRNR006698};
KW   Cytoskeleton {ECO:0000256|PIRNR:PIRNR006698};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|PIRSR:PIRSR006698-
KW   2};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRSR:PIRSR006698-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233140}.
FT   DOMAIN          69..309
FT                   /note="Septin-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51719"
FT   REGION          313..333
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          360..380
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        362..380
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   380 AA;  42876 MW;  3E1332CC6140609E CRC64;
     MSHHDNGVTV GLGIQMCERW RVEAALSFLP HQRKWGETAG AVMAGGVMDK EYVGFAALPN
     QLHRKSVKKG FDFTLMVAGE SGLGKSTLIN SLFLTNLYED RQVPEASARL TQTLAIERRG
     VEIEEGGVKV KLTLVDTPGF GDSVDCSDCW LPVVKFIEEQ FEQYLRDESG LNRKNIQDSR
     VHCCLYFISP FGRGLRPLDV AFLRAVHEKV NIIPVIGKAD ALMPQETQAL KQKESIPFAV
     VGSCEVVRDG GKRPVRGRRY SWGTVEVENP HHCDFLNLRR MLVQTHLQDL KEVTHDLLYE
     GYRARCLQSL ARPGARDRAS RSKLSRQSAT EIPLPMLPLA DTEKLIREKD EELRRMQEML
     EKMQAQMQQS QAQGEQSDTL
//
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