SEP8A_XENLA
ID SEP8A_XENLA Reviewed; 427 AA.
AC Q6AXA6;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Septin-8-A;
GN Name=sept8-a;
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=Ovary;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC079687; AAH79687.1; -; mRNA.
DR RefSeq; NP_001087375.1; NM_001093906.1.
DR AlphaFoldDB; Q6AXA6; -.
DR SMR; Q6AXA6; -.
DR BioGRID; 104059; 1.
DR IntAct; Q6AXA6; 1.
DR DNASU; 447199; -.
DR GeneID; 447199; -.
DR KEGG; xla:447199; -.
DR CTD; 447199; -.
DR Xenbase; XB-GENE-1032912; septin8.L.
DR OrthoDB; 845354at2759; -.
DR Proteomes; UP000186698; Chromosome 3L.
DR Bgee; 447199; Expressed in internal ear and 19 other tissues.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
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 Coiled coil; GTP-binding; Nucleotide-binding; Reference proteome.
FT CHAIN 1..427
FT /note="Septin-8-A"
FT /id="PRO_0000363231"
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 376..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 320..409
FT /evidence="ECO:0000255"
FT COMPBIAS 376..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; 49738 MW; 0039E52F2D503798 CRC64;
MAATDVQRAS NEEKRSLAMS GHVGFDSLPD QLVSKSVTQG FCFNILCVGE TGIGKSTLMN
TLFNTTFETE EASHYENGVC LRPRTYDLQE SNVHLKLTIV DTVGFGDQIN KDDSYRSVVD
YIDTQFENYL QEELKIRRSL FNFHDSRIHV CLYFITPTGH SLKSLDLVTM KKLDSKVNII
PIIAKADTIS KSELHKFKIK IMSELVSNGV QIYQFPTDDD AVAEINSVMN AHLPFAVVGS
TEEVKVGNKL VRARQYPWGV VQVENESHCD FVKLREMLIR VNMEDLREQT HTRHYELYRR
CKLEEMGFKD NDPDTQPFSL QETYEAKRKE FLSELQRKEE EMRQMFVNKV KETEAELKER
ERELQEKFMQ LKRIHQEESK KVEDKRRDLE EEMNSFNRRK AAMEALQSQS FQATSQQPLK
KDKDRKN