SEP2A_XENLA
ID SEP2A_XENLA Reviewed; 356 AA.
AC Q9DE33; A0JMX2;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Septin-2A;
DE AltName: Full=Septin-A;
DE Short=XlSeptA;
GN Name=sept2-a; Synonyms=septa;
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 [MRNA], AND SUBUNIT.
RC TISSUE=Kidney;
RX PubMed=12419187; DOI=10.1016/s0960-9822(02)01258-7;
RA Mendoza M., Hyman A.A., Glotzer M.;
RT "GTP binding induces filament assembly of a recombinant septin.";
RL Curr. Biol. 12:1858-1863(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH WDPCP.
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. {ECO:0000269|PubMed:12419187,
CC ECO:0000269|PubMed:20671153}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20671153}.
CC Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000250}. Cleavage furrow {ECO:0000250}. Midbody {ECO:0000250}.
CC Cell projection, cilium membrane {ECO:0000250}. Note=Localizes at the
CC base of the cilia near the morphological distinction between the cilia
CC and plasma membranes (By similarity). Cytoplasm, cell cortex.
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 -!- SEQUENCE CAUTION:
CC Sequence=AAI26038.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF212298; AAG43543.1; -; mRNA.
DR EMBL; BC126037; AAI26038.1; ALT_TERM; mRNA.
DR RefSeq; NP_001082061.1; NM_001088592.1.
DR RefSeq; XP_018117214.1; XM_018261725.1.
DR RefSeq; XP_018117215.1; XM_018261726.1.
DR RefSeq; XP_018117217.1; XM_018261728.1.
DR AlphaFoldDB; Q9DE33; -.
DR SMR; Q9DE33; -.
DR BioGRID; 99538; 1.
DR IntAct; Q9DE33; 1.
DR MaxQB; Q9DE33; -.
DR GeneID; 398203; -.
DR KEGG; xla:398203; -.
DR CTD; 398203; -.
DR Xenbase; XB-GENE-865354; septin2.L.
DR OMA; XILDEIE; -.
DR OrthoDB; 845354at2759; -.
DR Proteomes; UP000186698; Chromosome 5L.
DR Bgee; 398203; Expressed in spleen 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; IDA: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 1: Evidence at protein 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..356
FT /note="Septin-2A"
FT /id="PRO_0000363221"
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 356 AA; 40928 MW; 80693736E084A126 CRC64;
MSKQQAQFTN PETPGYVGFA NLPNQVHRKS VRKGFEFTLM VVGESGLGKS TLINSLFLTD
LYPERVVPGA ADKIERTVDI EASTVEIEER GVKLRLTVVD TPGYGDAMNC VDCFKPIISY
VDNQFERYLH DESGLNRRHI VDNRVHCCFY FISPFGHGLK PLDVEFMKAL HNKVNIVPVI
AKADTLTLRE RERLKRRVLD EIEEHGIKIY QLPDAESDED EDFKEQTRLL KASIPFTVVG
SNQLIEAKGK KVRGRLYPWG VVEVENTEHN DFLKLRTMLI THMQDLQEVT QDLHYENFRS
ERLKKGVTSS KVEHVEVTKD QILQEKEAEL RRMQEMITRM QAQMQIQGQS GDAQHL
