SEP14_BOVIN
ID SEP14_BOVIN Reviewed; 432 AA.
AC A6QQL3;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Septin-14;
GN Name=SEPTIN14 {ECO:0000250|UniProtKB:Q6ZU15};
GN Synonyms=SEPT14 {ECO:0000250|UniProtKB:Q6ZU15};
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=Hereford; TISSUE=Testis;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Filament-forming cytoskeletal GTPase (Probable). Involved in
CC the migration of cortical neurons and the formation of neuron leading
CC processes during embryonic development (By similarity). Plays a role in
CC sperm head formation during spermiogenesis, potentially via
CC facilitating localization of ACTN4 to cell filaments (By similarity).
CC {ECO:0000250|UniProtKB:Q6ZU15, ECO:0000250|UniProtKB:Q9DA97,
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 ACTN4 (By similarity). Interacts with SEPTIN9
CC (By similarity). Interacts (via C-terminus) with SEPTIN4 (By
CC similarity). {ECO:0000250|UniProtKB:Q6ZU15,
CC ECO:0000250|UniProtKB:Q9DA97}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6ZU15}.
CC Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q6ZU15}. Cell
CC projection, axon {ECO:0000250|UniProtKB:Q9DA97}. Cell projection,
CC dendrite {ECO:0000250|UniProtKB:Q9DA97}. Perikaryon
CC {ECO:0000250|UniProtKB:Q9DA97}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:Q9DA97}. Cytoplasmic vesicle, secretory vesicle,
CC acrosome {ECO:0000250|UniProtKB:Q6ZU15}. Note=Colocalizes with actin
CC stress fibers (By similarity). Expressed in the perinuclear rim and
CC manchette structure in early elongating spermatids during
CC spermiogenesis (By similarity). {ECO:0000250|UniProtKB:Q6ZU15,
CC ECO:0000250|UniProtKB:Q9DA97}.
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; BC149885; AAI49886.1; -; mRNA.
DR RefSeq; NP_001095557.1; NM_001102087.2.
DR AlphaFoldDB; A6QQL3; -.
DR SMR; A6QQL3; -.
DR STRING; 9913.ENSBTAP00000012280; -.
DR PaxDb; A6QQL3; -.
DR GeneID; 524980; -.
DR KEGG; bta:524980; -.
DR CTD; 346288; -.
DR eggNOG; KOG3859; Eukaryota.
DR InParanoid; A6QQL3; -.
DR OrthoDB; 845354at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0001669; C:acrosomal vesicle; ISS:UniProtKB.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0032153; C:cell division site; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; ISS:UniProtKB.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR GO; GO:0043204; C:perikaryon; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0031105; C:septin complex; IBA:GO_Central.
DR GO; GO:0005940; C:septin ring; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0060090; F:molecular adaptor activity; IBA:GO_Central.
DR GO; GO:0061640; P:cytoskeleton-dependent cytokinesis; IBA:GO_Central.
DR GO; GO:0001764; P:neuron migration; ISS:UniProtKB.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:1905719; P:protein localization to perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0007286; P:spermatid development; ISS:UniProtKB.
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 Pfam; PF00735; Septin; 1.
DR PIRSF; PIRSF006698; Septin; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51719; G_SEPTIN; 1.
PE 2: Evidence at transcript level;
KW Cell cycle; Cell division; Cell projection; Coiled coil; Cytoplasm;
KW Cytoplasmic vesicle; Cytoskeleton; GTP-binding; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..432
FT /note="Septin-14"
FT /id="PRO_0000363234"
FT DOMAIN 49..315
FT /note="Septin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 59..66
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 194..197
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 369..432
FT /note="Required for interaction with SEPTIN4. Required for
FT migration of cortical neurons during corticogenesis"
FT /evidence="ECO:0000250|UniProtKB:Q9DA97"
FT REGION 412..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 331..413
FT /evidence="ECO:0000255"
FT BINDING 59..66
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 195..203
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 249
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 264
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 432 AA; 50146 MW; 935CF546A560B22D CRC64;
MAEKPMCPST QIPDDEDTQK EDNIRCLNML GHFGFDCLAH QLVDKSVQQG FFFNILCVGE
TGIGKSTLID TLFNTSLKDK KSSHFYASVG LKIQTYELQE NNVQLKLTVV KTVGYGDQIN
KEASYQPIVD YLDAQFESYL QEELKIKRSL GNYRDSRVHV CLYFISPTGH SLKSLDILTM
KNIDSKVNII PVIAKADAIS KSDLQTFKCA IMNELISNGI QMYQFPTDNE TSTHMNSSMN
GLLPFAVVGS TEEVKVGKRT VRGRQYPWGI LQVENENHCD FVKLRDMLLC TNREDLKEQT
HTRHYERYRR NRLHMMGFTD MGPNNQPVSF QEIYEAKRQE LLEQCQREEE ELKHKFMQRV
KEKETAFKEA EKELQDKFEH LKKVQQEETM RLEEERRQLE EEILELCKMK ASSGTLQSQV
CTSVKKDKER KK
