ID   A0A3Q1ML00_BOVIN        Unreviewed;       534 AA.
AC   A0A3Q1ML00;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Septin 9 {ECO:0000313|Ensembl:ENSBTAP00000072279.1};
GN   Name=SEPTIN9 {ECO:0000313|Ensembl:ENSBTAP00000072279.1,
GN   ECO:0000313|VGNC:VGNC:34459};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000072279.1, ECO:0000313|Proteomes:UP000009136};
RN   [1] {ECO:0000313|Ensembl:ENSBTAP00000072279.1, ECO:0000313|Proteomes:UP000009136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000072279.1,
RC   ECO:0000313|Proteomes:UP000009136};
RA   Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA   Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA   Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT   "ARS-UCD1.2.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSBTAP00000072279.1}
RP   IDENTIFICATION.
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000072279.1};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC       GTPase superfamily. Septin GTPase family.
CC       {ECO:0000256|RuleBase:RU004560}.
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DR   AlphaFoldDB; A0A3Q1ML00; -.
DR   Ensembl; ENSBTAT00000074531.1; ENSBTAP00000072279.1; ENSBTAG00000002633.6.
DR   VEuPathDB; HostDB:ENSBTAG00000002633; -.
DR   VGNC; VGNC:34459; SEPTIN9.
DR   GeneTree; ENSGT00940000157195; -.
DR   Proteomes; UP000009136; Chromosome 19.
DR   Bgee; ENSBTAG00000002633; Expressed in thymus and 106 other cell types or tissues.
DR   ExpressionAtlas; A0A3Q1ML00; baseline and differential.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
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:SF47; SEPTIN-9; 1.
DR   Pfam; PF00735; Septin; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51719; G_SEPTIN; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00023212};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|RuleBase:RU004560};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004560};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:A0A3Q1ML00};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009136}.
FT   DOMAIN          287..534
FT                   /note="Septin-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51719"
FT   REGION          50..266
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        101..115
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        147..161
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        196..216
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   534 AA;  59594 MW;  605E08887DB8D479 CRC64;
     MSDPAVNAQL DGIISDFEAL KRSFEVEEVE TPNSTPPRRV QTPLLRSSVA SSTQKFQDLG
     VKNSEPAARH VDSLSQRSPK AALRRVELSG PKAEPVSRRT EISIDISSKQ VENAGTAGPS
     RFGLKRAEAL GHKTPEPAPR RTEITIVKPQ ESAHRRMETP ASKMPEVPAA PAADAAPKRV
     EIQVPKPAEG PASPIPPQSL ENSELAPMSQ LQSRLEPKPQ PPVAEIPPKS QEATEAAPSS
     AGDMADTPRD AALKQPPAPR NEKAPVDFGY VGIDSILEQM RRKAMKQGFE FNIMVVGQSG
     LGKSTLINTL FKSKISRKSV QPTSEERIPK TIEIKSITHD IEEKGVRMKL TVIDTPGFGD
     HINNENCWQP IMQFINDQYE KYLQEEVNIN RKKRIPDTRV HCCLYFIPAT GHSLRPLDIE
     FMKRLSKVVN IVPVIAKADT LTLEERVYFK QRITADLLSN GIDVYPQKEF DEDSEDRLVN
     EKFREMIPFA VVGSDHEYQV NGKRILGRKT KWGTIEVENT THCEFAYLRD LLIR
//