ID H9YUU3_MACMU Unreviewed; 431 AA.
AC H9YUU3;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Septin {ECO:0000256|PIRNR:PIRNR006698};
GN Name=SEPT10 {ECO:0000313|EMBL:AFH27459.1};
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544 {ECO:0000313|EMBL:AFH27459.1};
RN [1] {ECO:0000313|EMBL:AFH27459.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Thymus {ECO:0000313|EMBL:AFH27459.1};
RX PubMed=25319552; DOI=10.1186/1745-6150-9-20;
RA Zimin A.V., Cornish A.S., Maudhoo M.D., Gibbs R.M., Zhang X., Pandey S.,
RA Meehan D.T., Wipfler K., Bosinger S.E., Johnson Z.P., Tharp G.K.,
RA Marcais G., Roberts M., Ferguson B., Fox H.S., Treangen T., Salzberg S.L.,
RA Yorke J.A., Norgren R.B.Jr.;
RT "A new rhesus macaque assembly and annotation for next-generation
RT sequencing analyses.";
RL Biol. Direct 9:20-20(2014).
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 {ECO:0000256|ARBA:ARBA00004496}.
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 EMBL; JU470655; AFH27459.1; -; mRNA.
DR RefSeq; XP_014968600.1; XM_015113114.1.
DR AlphaFoldDB; H9YUU3; -.
DR GeneID; 695515; -.
DR CTD; 151011; -.
DR OrthoDB; 5396944at2759; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 CDD; cd22249; UDM1_RNF168_RNF169-like; 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:SF50; SEPTIN-10; 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 2: Evidence at transcript level;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|PIRNR:PIRNR006698};
KW Cytoskeleton {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}.
FT DOMAIN 40..306
FT /note="Septin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51719"
FT COILED 344..400
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 431 AA; 50063 MW; AAA279E72E773941 CRC64;
MASSEVARHL KRENVRSLTM SGHVGFESLP DQLVNRSIQQ GFCFNILCVG ETGIGKSTLI
DTLFNTNFED YESSHFCPNV KLKAQTYELQ ESNVRLKLTI VNTVGFGDQI NKEESYQPIV
DYIDAQFEAY LQEELKIKRS LFTYHDSRIH VCLYFISPTG HSLKTLDLLT MKNLDSKVNI
IPVIAKADTV SKTELQKFKI KLMSELVSNG VQIYQFPTDD DTIAKVNAAM NGQLPFAVVG
SMDEVKVGNK MVKARQYPWG VVQVENENHC DFVKLREMLI CTNMEDLREQ THTRHYELYR
RCKLEEMGFT DVGPENKPVS LQETYEAKRH EFHGERQRKE EEMKQMFVQR VKEKEAILKE
AERELQAKFE HLKRLHQEER MKLEEKRRLL EEEIIAFSKK KATSEIFHGQ SFLATGSNLR
KDKDRKNSNF L
//
