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Database: UniProt
Entry: G1NY11_MYOLU
LinkDB: G1NY11_MYOLU
Original site: G1NY11_MYOLU 
ID   G1NY11_MYOLU            Unreviewed;       394 AA.
AC   G1NY11;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   RecName: Full=Septin {ECO:0000256|PIRNR:PIRNR006698};
GN   Name=SEPTIN5 {ECO:0000313|Ensembl:ENSMLUP00000002283.2};
OS   Myotis lucifugus (Little brown bat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC   Myotis.
OX   NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000002283.2, ECO:0000313|Proteomes:UP000001074};
RN   [1] {ECO:0000313|Ensembl:ENSMLUP00000002283.2, ECO:0000313|Proteomes:UP000001074}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21993624; DOI=10.1038/nature10530;
RA   Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA   Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA   Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA   Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA   Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA   Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA   Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA   Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA   Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA   Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA   Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA   Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA   Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA   Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA   Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT   "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL   Nature 478:476-482(2011).
RN   [2] {ECO:0000313|Ensembl:ENSMLUP00000002283.2}
RP   IDENTIFICATION.
RG   Ensembl;
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: 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   EMBL; AAPE02038859; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; G1NY11; -.
DR   STRING; 59463.ENSMLUP00000002283; -.
DR   Ensembl; ENSMLUT00000002513.2; ENSMLUP00000002283.2; ENSMLUG00000002506.2.
DR   eggNOG; KOG2655; Eukaryota.
DR   GeneTree; ENSGT00940000159913; -.
DR   HOGENOM; CLU_017718_0_0_1; -.
DR   InParanoid; G1NY11; -.
DR   OMA; TNMYLRS; -.
DR   TreeFam; TF101079; -.
DR   Proteomes; UP000001074; Unassembled WGS sequence.
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|ARBA:ARBA00023212,
KW   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:UP000001074}.
FT   DOMAIN          66..339
FT                   /note="Septin-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51719"
FT   SITE            188
FT                   /note="Important for dimerization"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006698-2"
SQ   SEQUENCE   394 AA;  45472 MW;  2358C297A6612447 CRC64;
     PGLGVRRRPR GPGVAVMDSL AAPQDRLVEQ LLSPRTQAQR RLKDIDKQYV GFATLPNQVH
     RKSVKKGFDF TLMVAGESGL GKSTLVHSLF LTDLYKDRKL LSAEERISQT VEILKHTVDI
     EEKGVKLKLT IVDTPGFGDA VNNSECWKPI TDYVDQQFEQ YFRDESGLNR KNIQDNRVHC
     CLYFISPFGH GLRPVDVGFM KALHEKVNIV PLIAKADCLV PCEIRKLKER IREEIDKFGI
     HVYQFPECDS DEDEDFKQQD RELKESAPFA VIGSNTVVEA KGQRVRGRLY PWGIVEVENQ
     AHCDFVKLRN MLIRTHMHDL KDVTCDVHYE NYRAHCIQQM TSKLTQDNRM ESPIPILPLP
     TPDAETEKLI RMKDEELRRM QEMLQKMKQQ MQDQ
//
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