SEPT7_XENLA
ID SEPT7_XENLA Reviewed; 425 AA.
AC Q6GLZ5;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Septin-7;
GN Name=septin7 {ECO:0000250|UniProtKB:Q16181}; Synonyms=sept7;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
RX PubMed=20671153; DOI=10.1126/science.1191184;
RA Kim S.K., Shindo A., Park T.J., Oh E.C., Ghosh S., Gray R.S., Lewis R.A.,
RA Johnson C.A., Attie-Bittach T., Katsanis N., Wallingford J.B.;
RT "Planar cell polarity acts through septins to control collective cell
RT movement and ciliogenesis.";
RL Science 329:1337-1340(2010).
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 (By similarity). Plays a role
CC in ciliogenesis and collective cell movements including convergent
CC extension during gastrulation. Controls cell elongation but not
CC polarization during convergent extension. {ECO:0000250,
CC ECO:0000269|PubMed:20671153}.
CC -!- SUBUNIT: Monomer, and homodimer. Nucleotide binding promotes
CC oligomerization. Can form heterooligomers with other family members and
CC form filaments (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Chromosome, centromere,
CC kinetochore {ECO:0000250}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000250}. Cleavage furrow {ECO:0000250}. Midbody {ECO:0000250}.
CC Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:20671153}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the mesoderm during gastrulation.
CC Expressed in the notochord of neurula stage embryos.
CC {ECO:0000269|PubMed:20671153}.
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}.
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DR EMBL; BC074298; AAH74298.1; -; mRNA.
DR RefSeq; NP_001086183.1; NM_001092714.1.
DR AlphaFoldDB; Q6GLZ5; -.
DR SMR; Q6GLZ5; -.
DR BioGRID; 102775; 1.
DR IntAct; Q6GLZ5; 2.
DR MaxQB; Q6GLZ5; -.
DR DNASU; 444612; -.
DR GeneID; 444612; -.
DR KEGG; xla:444612; -.
DR CTD; 444612; -.
DR Xenbase; XB-GENE-957468; septin7.L.
DR OrthoDB; 845354at2759; -.
DR Proteomes; UP000186698; Chromosome 6L.
DR Bgee; 444612; Expressed in spleen and 19 other tissues.
DR GO; GO:0005930; C:axoneme; IDA:UniProtKB.
DR GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR GO; GO:0031105; C:septin complex; IEA:InterPro.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR GO; GO:0060031; P:mediolateral intercalation; IMP:UniProtKB.
DR GO; GO:0016476; P:regulation of embryonic cell shape; IMP: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 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 Cell cycle; Cell division; Cell projection; Centromere; Chromosome; Cilium;
KW Coiled coil; Cytoplasm; Cytoskeleton; GTP-binding; Kinetochore; Mitosis;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..425
FT /note="Septin-7"
FT /id="PRO_0000406216"
FT DOMAIN 28..297
FT /note="Septin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 38..45
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 94..97
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 175..178
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT COILED 324..421
FT /evidence="ECO:0000255"
FT BINDING 38..45
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 71
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 97
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 176..184
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 231
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 246
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 425 AA; 49469 MW; 6DE9A2D5CA4D3A7C CRC64;
MVAQQKNLEG YVGFANLPNQ VYRKSVKRGF EFTLMVVGES GLGKSTLINS LFLTDLYAPD
YPGPSHRIKK TVQVEQSKVL IKEGGVQLLL TIVDTPGFGD AVDNSNCWQP VIDYIDSKFE
DYLNAESRVN RRQMPDNRVQ CCLYFIAPSG HGLKPLDIEF MKRLHEKVNI IPLIAKADTL
TPEECQQFKK QIMKEIQEHK IKIYEFPETD DEEENKLVKK IKDGLPLAVV GSNTIIEVNG
KRVRGRQYPW GVAEVENGEH CDFTILRNML IRTHMQDLKD VTNNVHYENY RSRKLAAVTY
NGVDNNKNKG QLTKYDTGEG MSPLAQMEEE RREHVAKMKK MEMEMEQVFE MKVKEKVQKL
KDSEAELQRR HEQMKKNLEA QHKELEEKRR QFEEEKVNWE TQQRILEQQN TSRTLEKNKK
KGKIF
