SEPT7_BOVIN
ID SEPT7_BOVIN Reviewed; 437 AA.
AC Q6Q137;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Septin-7;
DE AltName: Full=CDC10 protein homolog;
GN Name=SEPTIN7 {ECO:0000250|UniProtKB:Q16181}; Synonyms=CDC10, SEPT7;
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 [MRNA].
RC STRAIN=Brown Swiss;
RA Oberg E.A., Medrano J.F., DeNise S.K.;
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Filament-forming cytoskeletal GTPase. Required for normal
CC organization of the actin cytoskeleton. Required for normal progress
CC through mitosis. Involved in cytokinesis. Required for normal
CC association of CENPE with the kinetochore. Plays a role in ciliogenesis
CC and collective cell movements. Forms a filamentous structure with
CC SEPTIN12, SEPTIN6, SEPTIN2 and probably SEPTIN4 at the sperm annulus
CC which is required for the structural integrity and motility of the
CC sperm tail during postmeiotic differentiation (By similarity).
CC {ECO:0000250, ECO:0000250|UniProtKB:Q16181}.
CC -!- SUBUNIT: Septins polymerize into heterooligomeric protein complexes
CC that form filaments, and associate with cellular membranes, actin
CC filaments and microtubules. GTPase activity is required for filament
CC formation. Filaments are assembled from asymmetrical heterotrimers,
CC composed of SEPTIN2, SEPTIN6 and SEPTIN7 that associate head-to-head to
CC form a hexameric unit. Within the trimer, directly interacts with
CC SEPTIN6, while interaction with SEPTIN2 seems indirect. In the absence
CC of SEPTIN6, forms homodimers. Interacts directly with CENPE and links
CC CENPE to septin filaments composed of SEPTIN2, SEPTIN6 and SEPTIN7.
CC Interacts with SEPTIN5, SEPTIN8, SEPTIN9 and SEPTIN11. Component of a
CC septin core octomeric complex consisting of SEPTIN12, SEPTIN7, SEPTIN6
CC and SEPTIN2 or SEPTIN4 in the order 12-7-6-2-2-6-7-12 or 12-7-6-4-4-6-
CC 7-12 and located in the sperm annulus; the SEPTIN12:SEPTIN7 association
CC is mediated by the respective GTP-binding domains (By similarity).
CC {ECO:0000250, ECO:0000250|UniProtKB:Q16181}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Chromosome, centromere, kinetochore
CC {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Cleavage
CC furrow {ECO:0000250}. Midbody {ECO:0000250}. Cytoplasm, cytoskeleton,
CC cilium axoneme {ECO:0000250}. Cell projection, cilium, flagellum
CC {ECO:0000250|UniProtKB:Q16181}. Note=Distributed throughout the
CC cytoplasm in prometaphase cells. Associated with the spindle during
CC metaphase. Associated with the central spindle and at the cleavage
CC furrow in anaphase cells. Detected at the midbody in telophase.
CC Associated with actin stress fibers. Found in the sperm annulus (By
CC similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q16181}.
CC -!- MISCELLANEOUS: Coordinated expression with SEPTIN2 and SEPTIN6.
CC {ECO:0000250}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAS73247.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY568576; AAS73247.1; ALT_INIT; mRNA.
DR RefSeq; NP_001001168.1; NM_001001168.1.
DR AlphaFoldDB; Q6Q137; -.
DR SMR; Q6Q137; -.
DR STRING; 9913.ENSBTAP00000001568; -.
DR PaxDb; Q6Q137; -.
DR PeptideAtlas; Q6Q137; -.
DR PRIDE; Q6Q137; -.
DR GeneID; 408000; -.
DR KEGG; bta:408000; -.
DR CTD; 989; -.
DR eggNOG; KOG2655; Eukaryota.
DR InParanoid; Q6Q137; -.
DR OrthoDB; 845354at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005930; C:axoneme; ISS:UniProtKB.
DR GO; GO:0032153; C:cell division site; IBA:GO_Central.
DR GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR GO; GO:0031514; C:motile cilium; IEA:UniProtKB-SubCell.
DR GO; GO:0031105; C:septin complex; ISS:UniProtKB.
DR GO; GO:0005940; C:septin ring; IBA:GO_Central.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
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:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR GO; GO:0061640; P:cytoskeleton-dependent cytokinesis; IBA:GO_Central.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:0016476; P:regulation of embryonic cell shape; ISS:UniProtKB.
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; IPR008115; Septin7.
DR Pfam; PF00735; Septin; 1.
DR PIRSF; PIRSF006698; Septin; 1.
DR PRINTS; PR01742; SEPTIN7.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51719; G_SEPTIN; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cell cycle; Cell division; Cell projection; Centromere;
KW Chromosome; Cilium; Coiled coil; Cytoplasm; Cytoskeleton; Differentiation;
KW Flagellum; GTP-binding; Kinetochore; Mitosis; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Spermatogenesis.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q16181"
FT CHAIN 2..437
FT /note="Septin-7"
FT /id="PRO_0000173527"
FT DOMAIN 47..316
FT /note="Septin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 47..317
FT /note="Interaction with SEPTIN12"
FT /evidence="ECO:0000250|UniProtKB:Q16181"
FT REGION 57..64
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 113..116
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 378..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 332..433
FT /evidence="ECO:0000255"
FT COMPBIAS 378..413
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 57..64
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 90
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 116
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 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"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q16181"
FT MOD_RES 30
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O55131"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O55131"
FT MOD_RES 228
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q16181"
FT MOD_RES 334
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16181"
FT MOD_RES 373
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O55131"
FT MOD_RES 424
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16181"
FT MOD_RES 426
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q16181"
SQ SEQUENCE 437 AA; 50680 MW; 946A08C54B7124FF CRC64;
MSVSARSAAA EERSVNSSTM VAQQKNLEGY VGFANLPNQV YRKSVKRGFE FTLMVVGESG
LGKSTLINSL FLTDLYSPEY PGPSHRIKKT VQVEQSKVLI KEGGVQLLLT IVDTPGFGDA
VDNSNCWQPV IDYIDSKFED YLNAESRVNR RQMPDNRVQC CLYFIAPSGH GLKPLDIEFM
KRLHEKVNII PLIAKADTLT PEECQQFKKQ IMKEIQEHKI KIYEFPETDD EEENKLVKKI
KDRLPLAVVG SNTIIEVNGK RVRGRQYPWG VAEVENGEHC DFTILRNMLI RTHMQDLKDV
TNNVHYENYR SRKLAAVTYN GVDNNKNKGQ LTKSPLAQME EERREHVAKM KKMEMEMEQV
FEMKVKEKVQ KLKDSEAELQ RRHEQMKKNL EAQHKELEEK RRQFEDEKAN WEAQQRILEQ
QNSSRTLEKN KKKGKIF
