SEP2B_XENLA
ID SEP2B_XENLA Reviewed; 352 AA.
AC Q63ZQ1;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Septin-2B;
GN Name=sept2-b;
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=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION.
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. Plays a role in the biogenesis
CC of polarized columnar-shaped epithelium. Required for the progression
CC through mitosis through regulation of chromosome congression. During
CC anaphase, may be required for chromosome segregation and spindle
CC elongation (By similarity). Probably plays a role in ciliogenesis and
CC collective cell movements including convergent extension during
CC gastrulation. In cilia, required for the integrity of the diffusion
CC barrier at the base of the primary cilium that prevents diffusion of
CC transmembrane proteins between the cilia and plasma membranes. Controls
CC cell shape and not polarization of cells during convergent extension.
CC {ECO:0000250, ECO:0000269|PubMed:20671153}.
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. Can form heterooligomers with other family members and form
CC filaments. Interacts with wdpcp (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton
CC {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Cleavage
CC furrow {ECO:0000250}. Midbody {ECO:0000250}. Cell projection, cilium
CC membrane {ECO:0000250}. Note=Localizes at the base of the cilia near
CC the morphological distinction between the cilia and plasma membranes.
CC Cytoplasm, cell cortex. {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; BC082859; AAH82859.1; -; mRNA.
DR RefSeq; NP_001088062.1; NM_001094593.1.
DR AlphaFoldDB; Q63ZQ1; -.
DR SMR; Q63ZQ1; -.
DR IntAct; Q63ZQ1; 1.
DR DNASU; 494757; -.
DR GeneID; 494757; -.
DR CTD; 494757; -.
DR Xenbase; XB-GENE-6255319; septin2.S.
DR Proteomes; UP000186698; Genome assembly.
DR Bgee; 494757; Expressed in blastula and 19 other tissues.
DR GO; GO:0060170; C:ciliary membrane; ISS:UniProtKB.
DR GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
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; ISS:UniProtKB.
DR GO; GO:0007224; P:smoothened signaling pathway; 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 InterPro; IPR008113; Septin2.
DR Pfam; PF00735; Septin; 1.
DR PIRSF; PIRSF006698; Septin; 1.
DR PRINTS; PR01740; SEPTIN2.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51719; G_SEPTIN; 1.
PE 2: Evidence at transcript level;
KW Cell cycle; Cell division; Cell membrane; Cell projection; Cytoplasm;
KW Cytoskeleton; GTP-binding; Membrane; Mitosis; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..352
FT /note="Septin-2B"
FT /id="PRO_0000363222"
FT DOMAIN 33..305
FT /note="Septin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 43..50
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 100..103
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 181..184
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 259..269
FT /note="Important for dimerization"
FT /evidence="ECO:0000250"
FT BINDING 43..50
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 77
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 103
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 182..190
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 240
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 255
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT SITE 155
FT /note="Important for dimerization"
FT /evidence="ECO:0000250"
SQ SEQUENCE 352 AA; 40450 MW; 9CBEDFC81A4B42FC CRC64;
MSKQQAQFTN PETPGYVGFA NLPNQVHRKS VRKGFEFTLM VVGESGLGKS TLINSLFLTD
LYPERVVPGA ANKIERTVEI EASTVEIEER GVKLRLTVVD TPGYGDAMNC VDCFKPIISY
VDNQFERYLH DESGLNRRHI VDNRVHCCFY FISPFGHGLK PLDVEFMKAL HNKVNIVPVI
AKADTLTLRE RERLKRRVLD EIEERGIKIY HLPDAESDED EDFKEQTRLL KASIPFTVVG
SNQLIEAKGK KVRGRLYPWG VVEVENPEHN DFLKLRTMLI THMQDLQEVT QDLHYENFRS
ERLKKGGASK VENVEVTKDQ MLQEKEAELR RMQEMIARMQ AQMQIQSQSG DV
