SEP2A_XENTR
ID SEP2A_XENTR Reviewed; 350 AA.
AC Q5BKN4;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Septin-2A;
GN Name=sept2-A; Synonyms=sept2; ORFNames=TNeu051p22.1;
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=Neurula;
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAR-2005) 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; CR761939; CAJ82844.1; -; mRNA.
DR EMBL; BC091009; AAH91009.1; -; mRNA.
DR RefSeq; NP_001017039.1; NM_001017039.2.
DR RefSeq; XP_012818671.1; XM_012963217.2.
DR AlphaFoldDB; Q5BKN4; -.
DR SMR; Q5BKN4; -.
DR STRING; 8364.ENSXETP00000062024; -.
DR PaxDb; Q5BKN4; -.
DR DNASU; 549793; -.
DR Ensembl; ENSXETT00000040281; ENSXETP00000040281; ENSXETG00000018605.
DR GeneID; 549793; -.
DR KEGG; xtr:549793; -.
DR CTD; 549793; -.
DR eggNOG; KOG2655; Eukaryota.
DR HOGENOM; CLU_017718_0_0_1; -.
DR InParanoid; Q5BKN4; -.
DR OrthoDB; 845354at2759; -.
DR PhylomeDB; Q5BKN4; -.
DR Proteomes; UP000008143; Chromosome 1.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000018605; Expressed in heart and 16 other tissues.
DR ExpressionAtlas; Q5BKN4; 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..350
FT /note="Septin-2A"
FT /id="PRO_0000363223"
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 350 AA; 40322 MW; 6C7B1E416A72CC15 CRC64;
MSQTGEKVKF SDSAGYVGFA NLPNQVHRKS VKKGFEFTLM VVGESGLGKS TLINSLFLTD
LYPERYIPGA AEKIERTVQI EASTVEIEER GVKLRLTVVD TPGYGDAINS QDCFKTIIHY
IDNQFERYLH DESGLNRRHI IDNRVHCCFY FISPFGHGLK PLDVEFMKAL HGKVNIVPVI
AKADTLTLKE RDRLKRRVLD EIAEHGIRIY QLPDADSDED EEFKEQTRVL KASIPFAVIG
SNQLIEVKGK KIRGRLYPWG VVEVENPEHN DFLKLRTMLV THMQDLQEVT QDLHYENFRS
ERLKRTGKPV EEEVLDKDMI LQQKEAELRR MQEMIAQMQA QMRMKPSGEE
