SEP2B_XENTR
ID SEP2B_XENTR Reviewed; 355 AA.
AC A1L0Y5;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Septin-2B;
GN Name=sept2-B;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
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. Plays a role in ciliogenesis and collective cell movements
CC including convergent extension during gastrulation. In cilia, required
CC for the integrity of the diffusion barrier at the base of the primary
CC cilium that prevents diffusion of transmembrane proteins between the
CC cilia and plasma membranes. Controls cell shape and not polarization of
CC cells during convergent extension (By similarity). {ECO:0000250}.
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}. Cytoplasm, cell cortex
CC {ECO:0000250}. Cell projection, cilium membrane {ECO:0000250}.
CC Note=Localizes at the base of the cilia near the morphological
CC distinction between the cilia and plasma membranes. {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; BC127290; AAI27291.1; -; mRNA.
DR RefSeq; NP_001090723.1; NM_001097254.1.
DR RefSeq; XP_012825381.1; XM_012969927.2.
DR RefSeq; XP_012825382.1; XM_012969928.2.
DR AlphaFoldDB; A1L0Y5; -.
DR SMR; A1L0Y5; -.
DR STRING; 8364.ENSXETP00000044933; -.
DR PaxDb; A1L0Y5; -.
DR DNASU; 100036706; -.
DR Ensembl; ENSXETT00000026555; ENSXETP00000026555; ENSXETG00000012166.
DR GeneID; 100036706; -.
DR KEGG; xtr:100036706; -.
DR CTD; 4735; -.
DR Xenbase; XB-GENE-480201; septin2.
DR eggNOG; KOG2655; Eukaryota.
DR HOGENOM; CLU_017718_0_0_1; -.
DR InParanoid; A1L0Y5; -.
DR OMA; EASHAEI; -.
DR OrthoDB; 845354at2759; -.
DR PhylomeDB; A1L0Y5; -.
DR TreeFam; TF101079; -.
DR Proteomes; UP000008143; Chromosome 5.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000012166; Expressed in embryo and 15 other tissues.
DR ExpressionAtlas; A1L0Y5; baseline and differential.
DR GO; GO:0032153; C:cell division site; IBA:GO_Central.
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:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR GO; GO:0031105; C:septin complex; IBA:GO_Central.
DR GO; GO:0005940; C:septin ring; IBA:GO_Central.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0008021; C:synaptic vesicle; 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: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:0017157; P:regulation of exocytosis; IBA:GO_Central.
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..355
FT /note="Septin-2B"
FT /id="PRO_0000363224"
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 355 AA; 40798 MW; D690DCC1D7B6E9D2 CRC64;
MSKQQAQFTN PETPGYVGFA NLPNQVHRKS VRKGFEFTLM VVGESGLGKS TLINSLFLTD
LYPERVVPGA ADKIERTVEI EASTVEIEER GVKLRLTVVD TPGYGDAMNC VDCFKPIISY
VDNQFERYLH DESGLNRRHI VDNRVHCCFY FISPFGHGLK PLDVEFMKAL HNKVNIVPVI
AKADTLTLRE RERLKRRVLD EIEEHGIKIY QLPDAESDED EDFKEQTRLL KASIPFTVVG
SNQLIEAKGK KVRGRLYPWG VVEVENPEHN DFLKLRTMLI THMQDLQEVT QDLHYENFRS
ERLKKGVASK VENVEVTKDQ ILQEKEAELR RMQEMIARMQ AQMQIQSQSG DAQHL
