ID G3TI61_LOXAF Unreviewed; 752 AA.
AC G3TI61;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein {ECO:0000256|RuleBase:RU369028};
DE Short=Cnt-b {ECO:0000256|RuleBase:RU369028};
DE AltName: Full=Centaurin-beta {ECO:0000256|RuleBase:RU369028};
GN Name=ACAP2 {ECO:0000313|Ensembl:ENSLAFP00000014316.3};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000014316.3, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000014316.3, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000014316.3,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000014316.3}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000014316.3};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: GTPase-activating protein (GAP) for ADP ribosylation factor 6
CC (ARF6). {ECO:0000256|ARBA:ARBA00037592}.
CC -!- FUNCTION: GTPase-activating protein for the ADP ribosylation factor
CC family. {ECO:0000256|RuleBase:RU369028}.
CC -!- ACTIVITY REGULATION: GAP activity stimulated by phosphatidylinositol
CC 4,5-bisphosphate (PIP2) and phosphatidic acid.
CC {ECO:0000256|RuleBase:RU369028}.
CC -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000256|ARBA:ARBA00004481,
CC ECO:0000256|RuleBase:RU369028}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004481, ECO:0000256|RuleBase:RU369028}.
CC Membrane {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004170}.
CC -!- DOMAIN: PH domain binds phospholipids including phosphatidic acid,
CC phosphatidylinositol 3-phosphate, phosphatidylinositol 3,5-bisphosphate
CC (PIP2) and phosphatidylinositol 3,4,5-trisphosphate (PIP3). May mediate
CC protein binding to PIP2 or PIP3 containing membranes.
CC {ECO:0000256|RuleBase:RU369028}.
CC -!- DOMAIN: The BAR domain mediates homodimerization, it can neither bind
CC membrane nor impart curvature, but instead requires the neighboring PH
CC domain to achieve these functions. {ECO:0000256|RuleBase:RU369028}.
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DR AlphaFoldDB; G3TI61; -.
DR Ensembl; ENSLAFT00000017078.3; ENSLAFP00000014316.3; ENSLAFG00000017077.3.
DR GeneTree; ENSGT00940000156389; -.
DR HOGENOM; CLU_012513_0_1_1; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd08851; ArfGap_ACAP2; 1.
DR CDD; cd07638; BAR_ACAP2; 1.
DR CDD; cd13250; PH_ACAP; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 1.10.220.150; Arf GTPase activating protein; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR045258; ACAP1/2/3-like.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR037278; ARFGAP/RecO.
DR InterPro; IPR001164; ArfGAP_dom.
DR InterPro; IPR038508; ArfGAP_dom_sf.
DR InterPro; IPR004148; BAR_dom.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR23180:SF241; ARF-GAP WITH COILED-COIL, ANK REPEAT AND PH DOMAIN-CONTAINING PROTEIN 2; 1.
DR PANTHER; PTHR23180; CENTAURIN/ARF; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF01412; ArfGap; 1.
DR Pfam; PF16746; BAR_3; 1.
DR Pfam; PF00169; PH; 1.
DR PRINTS; PR00405; REVINTRACTNG.
DR SMART; SM00248; ANK; 3.
DR SMART; SM00105; ArfGap; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF57863; ArfGap/RecO-like zinc finger; 1.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 2.
DR PROSITE; PS50088; ANK_REPEAT; 2.
DR PROSITE; PS50115; ARFGAP; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Endosome {ECO:0000256|ARBA:ARBA00022753, ECO:0000256|RuleBase:RU369028};
KW GTPase activation {ECO:0000256|RuleBase:RU369028};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU369028};
KW Reference proteome {ECO:0000313|Proteomes:UP000007646};
KW Repeat {ECO:0000256|RuleBase:RU369028};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU369028};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00288}.
FT DOMAIN 249..344
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 382..511
FT /note="Arf-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50115"
FT REPEAT 614..646
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 647..679
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 354..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 506..552
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 100..130
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 200..231
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 527..552
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 752 AA; 84946 MW; E93E1953D49B921C CRC64;
RAALEEVEGD VAELELKLDK LVKLCIAMID TGKAFCVANK QFMNGIRDLA QYSSNDAVVE
TSLTKFSDSL QEMINFHTIL FDQTQRSIKA QLQNFVKEDL RKFKDAKKQF EKVSEEKENA
LVKNAQVQRN KQHEVEEATN ILTATRKCFR HIALDYVLQI NVLQSKRRSE ILKSMLSFMY
AHLAFFHQGY DLFSELGPYM KDLGAQLDQL VVDAAKEKRE MEQKHSTIQQ KDFSSDDSKL
EYNVDAANGI VMEGYLFKRA SNAFKTWNRR WFSIQNNQLV YQKKFKDNPT VVVEDLRLCT
VKHCEDIERR FCFEVVSPTK SCMLQADSEK LRQAWIKAVQ TSIATAYRDK SDESEKLDKK
SSPSTGSLES GSESKEKLLK GESALQRVQC IPGNASCCDC GLADPRWASI NLGITLCIEC
SGIHRSLGVH FSKVRSLTLD TWEPELLKLM CELGNDVINR VYEAKVEKMG IKKPQPGQRQ
EKEAYIRAKY VERKFVDKYA ISASPPEQEE KTVSKSCEEK RLSISKPGPV TSLQSNDSGI
QQSSDDGRES LPSMVSANSL YEPEGERQDS AFLDSKHLNP GLQLYRASYE KNLPKMAEAL
AHGADVNWAN LEENQATPLI QAVLGGSLVT CEFLLQNGAN VNQRDVQGRG PLHHATVLGH
TGQVCLFLKR GANQHATDEE GKDPLTIAVE AANADIVTLL RLARMNEEMR ESEGLYGQPG
DETYQDIFRD FSQMASNNPE KLNRFQQESQ KF
//
