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Database: UniProt
Entry: A0A2K5NDH5_CERAT
LinkDB: A0A2K5NDH5_CERAT
Original site: A0A2K5NDH5_CERAT 
ID   A0A2K5NDH5_CERAT        Unreviewed;       378 AA.
AC   A0A2K5NDH5;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Septin {ECO:0000256|PIRNR:PIRNR006698};
GN   Name=SEPTIN5 {ECO:0000313|Ensembl:ENSCATP00000035476.1};
OS   Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Cercocebus.
OX   NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000035476.1, ECO:0000313|Proteomes:UP000233060};
RN   [1] {ECO:0000313|Ensembl:ENSCATP00000035476.1}
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: Cytoplasm, cytoskeleton
CC       {ECO:0000256|ARBA:ARBA00004245}.
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_011948782.1; XM_012093392.1.
DR   AlphaFoldDB; A0A2K5NDH5; -.
DR   SMR; A0A2K5NDH5; -.
DR   STRING; 9531.ENSCATP00000035476; -.
DR   Ensembl; ENSCATT00000059758.1; ENSCATP00000035476.1; ENSCATG00000040593.1.
DR   GeneID; 105601287; -.
DR   CTD; 5413; -.
DR   GeneTree; ENSGT00940000159913; -.
DR   OrthoDB; 5396944at2759; -.
DR   Proteomes; UP000233060; Unplaced.
DR   Bgee; ENSCATG00000040593; Expressed in frontal cortex and 10 other cell types or tissues.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR   GO; GO:0008021; C:synaptic vesicle; 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:0017157; P:regulation of exocytosis; 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:SF68; SEPTIN-5; 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:ARBA00022490};
KW   Cytoskeleton {ECO:0000256|PIRNR:PIRNR006698};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|PIRSR:PIRSR006698-
KW   2}; Methylation {ECO:0000256|ARBA:ARBA00022481};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRSR:PIRSR006698-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233060}.
FT   DOMAIN          50..323
FT                   /note="Septin-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51719"
FT   SITE            172
FT                   /note="Important for dimerization"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006698-2"
SQ   SEQUENCE   378 AA;  43845 MW;  0FD53C9F47E7BB0D CRC64;
     MDSLAAPQDR LVEQLLSPRT QAQRRLKDID KQYVGFATLP NQVHRKSVKK GFDFTLMVAG
     ESGLGKSTLV HSLFLTDLYK DRKLLSAEER ISQTVEILKH TVDIEEKGVK LKLTIVDTPG
     FGDAVNNTEC WKPITDYVDQ QFEQYFRDES GLNRKNIQDN RVHCCLYFIS PFGHGLRPVD
     VGFMKALHEK VNIVPLIAKA DCLVPSEIRK LKERIREEID KFGIHVYQFP ECDSDEDEDF
     KQQDRELKES APFAVIGSNT VVEAKGQRVR GRLYPWGIVE VENQAHCDFV KLRNMLIRTH
     MHDLKDVTCD VHYENYRAHC IQQMTSKLTQ DSRMESPIPI LPLPTPDAET EKLIRMKDEE
     LRRMQEMLQR MKQQMQDQ
//
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