ID A0A3Q0RQZ2_AMPCI Unreviewed; 1625 AA.
AC A0A3Q0RQZ2;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=ArfGAP with RhoGAP domain, ankyrin repeat and PH domain 3 {ECO:0000313|Ensembl:ENSACIP00000013036.1};
OS Amphilophus citrinellus (Midas cichlid) (Cichlasoma citrinellum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; New World cichlids;
OC Cichlasomatinae; Heroini; Amphilophus.
OX NCBI_TaxID=61819 {ECO:0000313|Ensembl:ENSACIP00000013036.1, ECO:0000313|Proteomes:UP000261340};
RN [1] {ECO:0000313|Ensembl:ENSACIP00000013036.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR Ensembl; ENSACIT00000013398.1; ENSACIP00000013036.1; ENSACIG00000010029.1.
DR GeneTree; ENSGT00940000158869; -.
DR Proteomes; UP000261340; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd13253; PH1_ARAP; 1.
DR CDD; cd13254; PH2_ARAP; 1.
DR CDD; cd17228; RA_ARAP3; 1.
DR CDD; cd04385; RhoGAP_ARAP; 1.
DR Gene3D; 1.10.220.150; Arf GTPase activating protein; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 4.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR InterPro; IPR037278; ARFGAP/RecO.
DR InterPro; IPR001164; ArfGAP_dom.
DR InterPro; IPR038508; ArfGAP_dom_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR000159; RA_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR037858; RhoGAP_ARAP.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR45899:SF4; ARF-GAP WITH RHO-GAP DOMAIN, ANK REPEAT AND PH DOMAIN-CONTAINING PROTEIN 3; 1.
DR PANTHER; PTHR45899; RHO GTPASE ACTIVATING PROTEIN AT 15B, ISOFORM C; 1.
DR Pfam; PF01412; ArfGap; 1.
DR Pfam; PF00169; PH; 3.
DR Pfam; PF00788; RA; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR Pfam; PF00536; SAM_1; 1.
DR PRINTS; PR00405; REVINTRACTNG.
DR SMART; SM00105; ArfGap; 1.
DR SMART; SM00233; PH; 4.
DR SMART; SM00324; RhoGAP; 1.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF57863; ArfGap/RecO-like zinc finger; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR SUPFAM; SSF50729; PH domain-like; 4.
DR SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS50115; ARFGAP; 1.
DR PROSITE; PS50003; PH_DOMAIN; 4.
DR PROSITE; PS50200; RA; 1.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00288};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00288};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00288}.
FT DOMAIN 21..80
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT DOMAIN 417..509
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 524..613
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 610..744
FT /note="Arf-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50115"
FT DOMAIN 804..917
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 928..1026
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1030..1211
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT DOMAIN 1240..1334
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT REGION 196..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..214
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..325
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1625 AA; 183080 MW; FE675019CDA7F838 CRC64;
MKPSPESTLV IMASLDGSTP VETLLSVIHL ERYLDTFHQA GLLLARDFTH LDNDALVSLG
ITATGHRKRI LRLVSYIKRT EGQRANQKVD LPRDRCQSVC SSESGCTAAS THQEVFRNSS
APDLAAMLTN SNSSRVAVKP VPKPRTVFNR RRTTPVHFCP TPDPAPPLPR RLSQESICFT
VLEGLSSGDT LAADNSLTSD LSDKATSPSR RSSQTERTRP GRSRSLSDAG GLLPPVPPRL
NRGVLTALMQ GSPPTSSSSP VPTEQVQALS SLTSCSGSSD SSRLSGSSPS GSPRGGGMEM
VSNEIYWGTS PSSAAHSGGR SYYSPQSAPP TPPRQTTDRN CERNSFSLYF RGCRFSWTKR
FSQPFHAGDS PGYSTVGETP PSLRCLSLPR HTFPPEADED LTISPYASYT SLTERAPPII
SGWLDKLSPQ GNYVFQKRYV KFDGKNLMYF GSEKDAYPKG VIPLAAIQMT RPAKDNKFEI
VTTHRIFVFR TDSEVLRRRW VSTLQEHVRD QLVFGRRRFG PGAHCQKHGV LELKGTKSKV
YAAINTDQIW LYKSEQCFRN GIGITVIEAR GATIRDGKHK SFDLITPYKT FSFTADSDRE
KRDWMEALQE SIAETLSDYE VAEKIWSNRS NRTCADCKAP NPDWASINLC VVICKNCAGQ
HRGLGTMVSK VQSLKLDTSV WSNEIVQLFI MLGNDRANDF WAARLSASEE LDCDASPEQR
REFIVQKYRE GRYRLAHPAF SSQEELLKVL CSAVSEQTLL KTVTQIFSEA ESAHIANESN
GRNPHSPDPC STSDPSVYDE IMQPVLHSGY LYKSSSVNRG TMSRKNREDF QKFWCSVDRS
LVFYESDRSG DPCLQIGAKD IVCLGVGRPD SSSSSGFIDR FRYTFELYLT SEKLYQFGLE
TADDLHSWTK AIGKAATPLS CHCLLTREFE RVGLLRYRAM LDPQQWKEAY FVLQKSNLFI
CPRNDGAAED IINLNRLQEL SIASENENQE KKDILVLVEK GRTLHLQGVG RTDFSLWYSD
IQRAAGGKGN ALRDQQMSRN DIPIIVDSCI AFITQYGLGH EGIYRKNGAK SRIKLLMEEF
RKDARNVKLR IGDHFIEDVT DVLKRFFREI DDPIFMADLH PLWQEAAKIP LKRPRLDCYK
EIIRSLPRVN RTTLAALISH LYRVQKCADL NQMCTKNLSL LFAPSLFQTD GKGEHEVKIV
EDLIDNYLYV FDIDEEHQTQ IELEISLITT WKDTQLSQAG DLIIEVYLEM KIPDCCITLK
VSPTMCAEEL TNQVLYMRNI PAGDKDVWMT FEAIEDGQLE RPLHPKEKVL EQALQWCKMA
DPSSAYLVVK RVPKGEGITL LTSYKSEIMK VGLLRCREEP PKLLQGNRFQ ERTFQIQDHK
LLLLKDKKSI KPEKEWALKT MKIYIGIRKK LKAPTSSGTF TCRLVWDQLT LLVFMDLLLF
QNDDPGPPVL RRHSSSDISK QKFGTMPLVP IRGDESNSSM LSANQTLRKL HNRRTLSMYF
PMKVQQDSFE ERSESPDLPE PLYEEVGDFG LQVLKSLETS FLSSSIAETQ EVPDHPPLRL
VPVETGHLDH MMIPEAVRTA GGSVETLERQ TLQGVCTPSQ ELLLQELSSA FIKKTEEEEE
RPYDV
//
