SEPT6_BOVIN
ID SEPT6_BOVIN Reviewed; 427 AA.
AC Q3SZN0;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Septin-6;
GN Name=SEPTIN6 {ECO:0000250|UniProtKB:Q14141}; Synonyms=SEPT6;
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=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Filament-forming cytoskeletal GTPase. Required for normal
CC organization of the actin cytoskeleton. Involved in cytokinesis. Forms
CC a filamentous structure with SEPTIN12, SEPTIN6, SEPTIN2 and probably
CC SEPTIN4 at the sperm annulus which is required for the structural
CC integrity and motility of the sperm tail during postmeiotic
CC differentiation (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:Q14141}.
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 SEPTIN2 and SEPTIN7. Also interacts with SEPTIN9 and SEPTIN12.
CC Interaction with SEPTIN12 alters filament structure. 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. Interacts with SOCS7. Interacts
CC with HNRNPA1 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton, spindle.
CC Chromosome, centromere, kinetochore {ECO:0000250}. Cleavage furrow
CC {ECO:0000250}. Midbody {ECO:0000250}. Cell projection, cilium,
CC flagellum {ECO:0000250|UniProtKB:Q14141}. Note=In metaphase cells,
CC localized within the microtubule spindle. At the metaphase plate, in
CC close apposition to the kinetochores of the congressed chromosomes. In
CC cells undergoing cytokinesis, localized to the midbody, the ingressing
CC cleavage furrow, and the central spindle. Found in the sperm annulus
CC (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q14141}.
CC -!- MISCELLANEOUS: Coordinated expression with SEPTIN2 and SEPTIN7.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC102779; AAI02780.1; -; mRNA.
DR RefSeq; NP_001030507.1; NM_001035430.2.
DR AlphaFoldDB; Q3SZN0; -.
DR SMR; Q3SZN0; -.
DR STRING; 9913.ENSBTAP00000005629; -.
DR PaxDb; Q3SZN0; -.
DR PRIDE; Q3SZN0; -.
DR Ensembl; ENSBTAT00000005629; ENSBTAP00000005629; ENSBTAG00000004291.
DR GeneID; 540783; -.
DR KEGG; bta:540783; -.
DR CTD; 23157; -.
DR VEuPathDB; HostDB:ENSBTAG00000004291; -.
DR VGNC; VGNC:34457; SEPTIN6.
DR eggNOG; KOG3859; Eukaryota.
DR GeneTree; ENSGT00940000158026; -.
DR HOGENOM; CLU_017718_8_1_1; -.
DR InParanoid; Q3SZN0; -.
DR OMA; NNGIHIY; -.
DR OrthoDB; 845354at2759; -.
DR TreeFam; TF101080; -.
DR Proteomes; UP000009136; Chromosome X.
DR Bgee; ENSBTAG00000004291; Expressed in thymus and 106 other tissues.
DR ExpressionAtlas; Q3SZN0; baseline and differential.
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; IBA:GO_Central.
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; IPR030644; SEPT6.
DR InterPro; IPR016491; Septin.
DR PANTHER; PTHR18884:SF55; PTHR18884:SF55; 1.
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 Acetylation; Cell cycle; Cell division; Cell projection; Centromere;
KW Chromosome; Cilium; Coiled coil; Cytoplasm; Cytoskeleton; Differentiation;
KW Flagellum; GTP-binding; Kinetochore; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Spermatogenesis.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q14141"
FT CHAIN 2..427
FT /note="Septin-6"
FT /id="PRO_0000239733"
FT DOMAIN 39..305
FT /note="Septin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 49..56
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 101..104
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 184..187
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 405..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 321..416
FT /evidence="ECO:0000255"
FT BINDING 49..56
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 104
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 185..193
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 239
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 254
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q14141"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14141"
FT MOD_RES 367
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q14141"
FT MOD_RES 416
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14141"
FT MOD_RES 418
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14141"
SQ SEQUENCE 427 AA; 48775 MW; CFA5CE139BA29739 CRC64;
MAATDIARQV GEGCRTVPLA GHVGFDSLPD QLVNKSVSQG FCFNILCVGE TGLGKSTLMD
TLFNTKFEGE PATHTQPGVQ LRSNTYDLQE SNVGLKLTIV STVGFGDQIN KEDSYKPIVE
FIDAQFEAYL QEELKIRRVL HTYHDSRIHA CLYFIAPTGH SLKSLDLVTM KKLDSKVNII
PIIAKSDAIS KSELTKFKIK ITSELVNNGV QIYQFPTDDE SVAEINGTMN AHLPFAVIGS
TEELKIGNKM MKARQYPWGT VQVENEAHCD FVKLREMLIR VNMEDLREQT HSRHYELYRR
CKLEEMGFKD TDPDSKPFSL QETYEAKRNE FLGELQKKEE EMRQMFVQRV KEKEAELKEA
EKELHEKFDR LKKLHQDEKK KLEDKKKSLD DEVNAFKQRK TAAELLQSQG SQAGGSQTLK
RDKEKKN
