ID A0A3Q1FRI8_9TELE Unreviewed; 348 AA.
AC A0A3Q1FRI8;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Septin-2 {ECO:0000313|Ensembl:ENSAPOP00000018272.1};
OS Acanthochromis polyacanthus (spiny chromis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Acanthochromis.
OX NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000018272.1, ECO:0000313|Proteomes:UP000257200};
RN [1] {ECO:0000313|Ensembl:ENSAPOP00000018272.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium membrane
CC {ECO:0000256|ARBA:ARBA00004309}. Cleavage furrow
CC {ECO:0000256|ARBA:ARBA00004626}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000256|ARBA:ARBA00004186}. Membrane
CC {ECO:0000256|ARBA:ARBA00004370}. Midbody
CC {ECO:0000256|ARBA:ARBA00004214}.
CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC GTPase superfamily. Septin GTPase family.
CC {ECO:0000256|RuleBase:RU004560}.
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DR AlphaFoldDB; A0A3Q1FRI8; -.
DR STRING; 80966.ENSAPOP00000018272; -.
DR Ensembl; ENSAPOT00000034368.1; ENSAPOP00000018272.1; ENSAPOG00000021616.1.
DR GeneTree; ENSGT00940000164668; -.
DR InParanoid; A0A3Q1FRI8; -.
DR OrthoDB; 5396944at2759; -.
DR Proteomes; UP000257200; Unplaced.
DR GO; GO:0060170; C:ciliary membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
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:InterPro.
DR CDD; cd01850; CDC_Septin; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR030379; G_SEPTIN_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR016491; Septin.
DR InterPro; IPR008113; Septin2.
DR PANTHER; PTHR18884; SEPTIN; 1.
DR PANTHER; PTHR18884:SF64; SEPTIN-2; 1.
DR Pfam; PF00735; Septin; 1.
DR PIRSF; PIRSF006698; Septin; 1.
DR PRINTS; PR01740; SEPTIN2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51719; G_SEPTIN; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW Cell division {ECO:0000256|ARBA:ARBA00022776};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|PIRSR:PIRSR006698-
KW 2}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Mitosis {ECO:0000256|ARBA:ARBA00022776};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR006698-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000257200}.
FT DOMAIN 33..305
FT /note="Septin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51719"
FT COILED 321..348
FT /evidence="ECO:0000256|SAM:Coils"
FT SITE 155
FT /note="Important for dimerization"
FT /evidence="ECO:0000256|PIRSR:PIRSR006698-2"
SQ SEQUENCE 348 AA; 39999 MW; CA3A244311057B39 CRC64;
MSQSGEKGKF PDTAGYVGFA NLPNQVHRKS VKKGFEFTLM VVGESGLGKS TLINSLFLTD
LYPERYIPGA AEKIERTVQI EASTVEIEER GVKLRLTVVD TPGYGDAINS QDCFKTIIQY
IDNQFERYLH DESGLNRRHI VDNRVHCCFY FISPFGHGLK PLDVEFMKAI HSKVNIVPVI
AKADTLTLKE RDRLKRRILD EIAEHGIKIY QLPDADSDED EEFKEQTRVL KASIPFAVIG
SNQLIEVKGK KIRGRLYPWG VVEVENPEHN DFLKLRTMLV THMQDLQEVT QDLHYENFRS
ERLKRAGRAV DEDVVDKDQI LLQKEAELRR MQEMIAQMQA QMKMKSDE
//
