ID U3F9C8_MICFL Unreviewed; 175 AA.
AC U3F9C8;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=ADP-ribosylation factor 6 {ECO:0000256|ARBA:ARBA00017741};
OS Micrurus fulvius (Eastern coral snake) (Coluber fulvius).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Micrurus.
OX NCBI_TaxID=8637 {ECO:0000313|EMBL:JAB54732.1};
RN [1] {ECO:0000313|EMBL:JAB54732.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Venom gland {ECO:0000313|EMBL:JAB54732.1};
RX PubMed=23915248; DOI=10.1186/1471-2164-14-531;
RA Margres M.J., Aronow K., Loyacano J., Rokyta D.R.;
RT "The venom-gland transcriptome of the eastern coral snake (Micrurus
RT fulvius) reveals high venom complexity in the intragenomic evolution of
RT venoms.";
RL BMC Genomics 14:531-531(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2;
CC Evidence={ECO:0000256|ARBA:ARBA00000249};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000256|ARBA:ARBA00000249};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004193};
CC Lipid-anchor {ECO:0000256|ARBA:ARBA00004193}. Cell projection,
CC filopodium membrane {ECO:0000256|ARBA:ARBA00004527}; Lipid-anchor
CC {ECO:0000256|ARBA:ARBA00004527}. Cell projection, ruffle
CC {ECO:0000256|ARBA:ARBA00004466}. Cleavage furrow
CC {ECO:0000256|ARBA:ARBA00004626}. Endosome membrane
CC {ECO:0000256|ARBA:ARBA00004455}; Lipid-anchor
CC {ECO:0000256|ARBA:ARBA00004455}. Midbody, Midbody ring
CC {ECO:0000256|ARBA:ARBA00004476}. Recycling endosome membrane
CC {ECO:0000256|ARBA:ARBA00004139}; Lipid-anchor
CC {ECO:0000256|ARBA:ARBA00004139}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family.
CC {ECO:0000256|RuleBase:RU003925}.
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DR EMBL; GAEP01000089; JAB54732.1; -; mRNA.
DR AlphaFoldDB; U3F9C8; -.
DR GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR GO; GO:0031527; C:filopodium membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0090543; C:Flemming body; IEA:UniProtKB-SubCell.
DR GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0001726; C:ruffle; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR CDD; cd04149; Arf6; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR041838; Arf6.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR024156; Small_GTPase_ARF.
DR InterPro; IPR006689; Small_GTPase_ARF/SAR.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR11711; ADP RIBOSYLATION FACTOR-RELATED; 1.
DR PANTHER; PTHR11711:SF322; ADP-RIBOSYLATION FACTOR 6; 1.
DR Pfam; PF00025; Arf; 1.
DR PRINTS; PR00328; SAR1GTPBP.
DR SMART; SM00177; ARF; 1.
DR SMART; SM00175; RAB; 1.
DR SMART; SM00178; SAR; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51417; ARF; 1.
PE 2: Evidence at transcript level;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|RuleBase:RU003925};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU003925}.
SQ SEQUENCE 175 AA; 20140 MW; E0DB1CD914860F3B CRC64;
MGKMLSKIFG NKEMRILMLG LDAAGKTTIL YKLKLGQPVT TIPTVGFNVE TVTYKNVKFN
VWDVGGQDKI RPLWRHYYTG TQGLIFVVDC ADRDRIDEGR QELHRIINDR EMRDAIILVF
ANKQDLPDAM KPHEIQEKLG LTRIRDRNWY VQPSCATSGE GLYEGLMWLT SNYKS
//