SEP12_BOVIN
ID SEP12_BOVIN Reviewed; 361 AA.
AC A5D7Q3;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Septin-12;
GN Name=SEPTIN12 {ECO:0000250|UniProtKB:Q8IYM1}; Synonyms=SEPT12;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Filament-forming cytoskeletal GTPase (By similarity). May
CC play a role in cytokinesis (Potential). Involved in spermatogenesis.
CC Involved in the morphogenesis of sperm heads and the elongation of
CC sperm tails probably implicating the association with alpha- and beta-
CC tubulins. Forms a filamentous structure with SEPTIN7, SEPTIN6, SEPTIN2
CC and probably SEPTIN4 at the sperm annulus which is required for the
CC structural integrity and motility of the sperm tail during postmeiotic
CC differentiation (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:Q8IYM1, ECO:0000250|UniProtKB:Q9D451,
CC ECO:0000305}.
CC -!- SUBUNIT: Septins polymerize into heterooligomeric protein complexes
CC that form filaments, and can associate with cellular membranes, actin
CC filaments and microtubules. GTPase activity is required for filament
CC formation. Interacts with SEPTIN6 and SEPTIN11. Component of a
CC octomeric complex consisting of SEPTIN12, SEPTIN7, SEPTIN6 and SEPTIN2
CC or SEPTIN4 in the order 12-7-6-2-2-6-7-12 or 12-7-6-4-4-6-7-12 and
CC located in the sperm annulus; the octomer polymerizes into filaments
CC via the SEPTIN12 N- and C-termini; the SEPTIN12:SEPTIN7 association is
CC mediated by the GTP-binding domains. Interacts with SPAG4 and LMNB1.
CC Associates with alpha- and beta-tubulins (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton
CC {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Cell
CC projection, cilium, flagellum {ECO:0000250|UniProtKB:Q4V8G5,
CC ECO:0000250|UniProtKB:Q8IYM1, ECO:0000250|UniProtKB:Q9D451}. Note=At
CC interphase, forms a filamentous structure in the cytoplasm. During
CC anaphase, translocates to the central spindle region and to the midbody
CC during cytokinesis (By similarity). Found in the sperm annulus (By
CC similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q4V8G5,
CC ECO:0000250|UniProtKB:Q8IYM1}.
CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC GTPase superfamily. Septin GTPase family. {ECO:0000255|PROSITE-
CC ProRule:PRU01056}.
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DR EMBL; BC140643; AAI40644.1; -; mRNA.
DR RefSeq; NP_001091612.1; NM_001098143.2.
DR AlphaFoldDB; A5D7Q3; -.
DR SMR; A5D7Q3; -.
DR STRING; 9913.ENSBTAP00000021722; -.
DR PaxDb; A5D7Q3; -.
DR PRIDE; A5D7Q3; -.
DR GeneID; 618676; -.
DR KEGG; bta:618676; -.
DR CTD; 124404; -.
DR eggNOG; KOG1547; Eukaryota.
DR InParanoid; A5D7Q3; -.
DR OrthoDB; 845354at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0032153; C:cell division site; IBA:GO_Central.
DR GO; GO:0032154; C:cleavage furrow; ISS:UniProtKB.
DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0031105; C:septin complex; ISS:UniProtKB.
DR GO; GO:0005940; C:septin ring; IBA:GO_Central.
DR GO; GO:0097227; C:sperm annulus; ISS:UniProtKB.
DR GO; GO:0005819; C:spindle; ISS:UniProtKB.
DR GO; GO:0001725; C:stress fiber; ISS:UniProtKB.
DR GO; GO:0019003; F:GDP binding; ISS:UniProtKB.
DR GO; GO:0005525; F:GTP binding; ISS:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0060090; F:molecular adaptor activity; IBA:GO_Central.
DR GO; GO:0035091; F:phosphatidylinositol binding; ISS:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0061640; P:cytoskeleton-dependent cytokinesis; IBA:GO_Central.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR CDD; cd01850; CDC_Septin; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR030379; G_SEPTIN_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR016491; Septin.
DR InterPro; IPR008114; Septin3.
DR Pfam; PF00735; Septin; 1.
DR PIRSF; PIRSF006698; Septin; 1.
DR PRINTS; PR01741; SEPTIN3.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51719; G_SEPTIN; 1.
PE 2: Evidence at transcript level;
KW Cell cycle; Cell division; Cell projection; Cilium; Cytoplasm;
KW Cytoskeleton; Differentiation; Flagellum; GTP-binding; Nucleotide-binding;
KW Reference proteome; Spermatogenesis.
FT CHAIN 1..361
FT /note="Septin-12"
FT /id="PRO_0000312859"
FT DOMAIN 45..316
FT /note="Septin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 45..318
FT /note="Interaction with SEPTIN7"
FT /evidence="ECO:0000250|UniProtKB:Q8IYM1"
FT REGION 55..62
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 111..114
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 193..196
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 257..361
FT /note="Self-association (via N-terminus) to polymerize
FT octomeric septin 12-7-6-2/4-2/4-6-7-12 filaments"
FT /evidence="ECO:0000250|UniProtKB:Q8IYM1"
FT REGION 333..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 55..62
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 88
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 114
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 194..202
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 250
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 265
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 361 AA; 41210 MW; 8BA2FEF6038144A1 CRC64;
MDPLRQSPSP SSSRASSPRT LSCERLGYVG IEAVLDQLKI KAMKMGFEFN IMVVGQSGLG
KSTMVNTLFK SKIWKSTMPG LRVPMPQTLQ LHYVTHVIEE NGVKLKLTVT DTPGFGDQIN
NDKCWDPILG YINEQYERYL QEEILITRQR HIPDTRVHCC IYFVPPTGHC LRPLDLEFLQ
RLCRAVNVVP VIARADSLTI EEREAFRHRI QDDLKTHSIE VYPQKSFDED VNDKILNSKI
RERIPFAVVG ADREHMVNGR CVLGRKTKWG IIEVENMAHC EFPLLRDLLI RSHLQDLKDI
THNVHYENYR IIRLKESHAL PQGPGWVNLA PAPPPAPTGT RASPGPAKMC RWAEDNSDED
F
