SEPT8_XENTR
ID SEPT8_XENTR Reviewed; 427 AA.
AC B1H120;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Septin-8;
GN Name=septin8 {ECO:0000250|UniProtKB:Q92599}; Synonyms=sept8;
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=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:B0BNF1}.
CC Cytoplasm, cytoskeleton {ECO:0000250}. Synapse
CC {ECO:0000250|UniProtKB:B0BNF1}. Cell projection, axon
CC {ECO:0000250|UniProtKB:B0BNF1}. Cytoplasmic vesicle, secretory vesicle,
CC synaptic vesicle membrane {ECO:0000250|UniProtKB:B0BNF1}. Presynapse
CC {ECO:0000250|UniProtKB:B0BNF1}. Note=Expressed in axons of immature
CC neurons, localizes to synapses in mature neurons.
CC {ECO:0000250|UniProtKB:B0BNF1}.
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; BC160437; AAI60437.1; -; mRNA.
DR RefSeq; NP_001116199.1; NM_001122727.1.
DR AlphaFoldDB; B1H120; -.
DR SMR; B1H120; -.
DR STRING; 8364.ENSXETP00000062946; -.
DR GeneID; 100126684; -.
DR KEGG; xtr:100126684; -.
DR CTD; 23176; -.
DR Xenbase; XB-GENE-1032907; septin8.
DR eggNOG; KOG3859; Eukaryota.
DR InParanoid; B1H120; -.
DR OrthoDB; 845354at2759; -.
DR Proteomes; UP000008143; Chromosome 3.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000030617; Expressed in brain and 13 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0032153; C:cell division site; IBA:GO_Central.
DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR GO; GO:0098793; C:presynapse; ISS:UniProtKB.
DR GO; GO:0031105; C:septin complex; IBA:GO_Central.
DR GO; GO:0005940; C:septin ring; IBA:GO_Central.
DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
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:0061640; P:cytoskeleton-dependent cytokinesis; IBA:GO_Central.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:0035542; P:regulation of SNARE complex assembly; 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; IPR030646; SEPT8.
DR InterPro; IPR016491; Septin.
DR PANTHER; PTHR18884:SF54; PTHR18884:SF54; 1.
DR Pfam; PF00735; Septin; 1.
DR PIRSF; PIRSF006698; Septin; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51719; G_SEPTIN; 1.
PE 2: Evidence at transcript level;
KW Cell projection; Coiled coil; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton;
KW GTP-binding; Membrane; Nucleotide-binding; Reference proteome; Synapse.
FT CHAIN 1..427
FT /note="Septin-8"
FT /id="PRO_0000363233"
FT DOMAIN 39..305
FT /note="Septin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 49..56
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 101..104
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 184..187
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 373..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 321..409
FT /evidence="ECO:0000255"
FT COMPBIAS 373..398
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..417
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 49..56
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 104
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 185..193
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 239
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 254
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 427 AA; 49764 MW; C398FE9A25904D88 CRC64;
MAATDVERVS NEEKRSLAMT GHVGFDSLPD QLVSKSVTQG FCFNILCVGE TGIGKSTLMN
TLFNTTFETE EASHYENGVR LRPRTYDLQE SNVHLKLTIV DTVGFGDQIN KDDSYRSVVD
YIDTQFENYL QEELKIRRSL FNYHDSRIHV CLYFITPTGH SLKSLDLVTM KKLDSKVNII
PIIAKADTIS KSELHKFKIK IMSELVSNGV QIYQFPTDDD AVAEINSVMN AHLPFAVVGS
TEEVKVGNKL VRARQYPWGV VQVENESHCD FVKLREMLIR VNMEDLREQT HTRHYELYRR
CKLEEMGFKD NDPDTQPFSL QETYEAKRKE FLGELQRKEE EMRQMFVNKV KETEAELKDK
ERELQEKFMQ LKRVHQEESK KVEDKRRDLE EEMNSFNRRK AAMEALQSQS FQATSQQPLK
KDKDRKN
