ID A0A3Q3AC65_KRYMA Unreviewed; 1677 AA.
AC A0A3Q3AC65;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Arf-GAP with Rho-GAP domain, ANK repeat and PH domain-containing protein 2-like {ECO:0000313|Ensembl:ENSKMAP00000013866.1};
OS Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000013866.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000013866.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_017281738.1; XM_017426249.1.
DR RefSeq; XP_017281741.1; XM_017426252.1.
DR RefSeq; XP_017281742.1; XM_017426253.1.
DR STRING; 37003.ENSKMAP00000013817; -.
DR Ensembl; ENSKMAT00000014024.1; ENSKMAP00000013817.1; ENSKMAG00000010353.1.
DR Ensembl; ENSKMAT00000014074.1; ENSKMAP00000013866.1; ENSKMAG00000010353.1.
DR GeneID; 108241816; -.
DR KEGG; kmr:108241816; -.
DR CTD; 116984; -.
DR GeneTree; ENSGT00940000167169; -.
DR OMA; FAHSCET; -.
DR OrthoDB; 4835at2759; -.
DR Proteomes; UP000264800; 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; 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); 5.
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 PANTHER; PTHR45899:SF1; ARF-GAP WITH RHO-GAP DOMAIN, ANK REPEAT AND PH DOMAIN-CONTAINING PROTEIN 2; 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; 5.
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; 5.
DR SUPFAM; SSF47769; SAM/Pointed domain; 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, ECO:0000256|SAM:Coils};
KW GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00288};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000264800};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00288};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00288}.
FT DOMAIN 6..70
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT DOMAIN 431..523
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 541..630
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 627..750
FT /note="Arf-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50115"
FT DOMAIN 837..947
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1060..1241
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT DOMAIN 1273..1367
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 1379..1482
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 71..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 235..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 317..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 371..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1488..1677
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1107..1139
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 84..124
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..343
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1488..1555
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1594..1617
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1662..1677
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1677 AA; 187807 MW; E0C1A6B1B82A3614 CRC64;
MLAPPEPSHE VAEWLSTLHL SQYVSFFEQG GYRALEDCKD LTEERLLQLK VLPTGHRRRI
LRSLEALGVS QLSGEEGEDE ESLESGETKP KLYPRHIFRE YGRKGTSFQH TQTKEKREYD
SEGSRSLPAR AGLAGDEENL PDGRYDSPPV PAPRSLQHIQ TSAQVQTRGP ASTLSSSSSS
DSVSTSDIPS DCEASAEEHF SSAAEVPLRA VADNKGFHIQ MVDNSIYETQ MSVKDAAGPR
LSRSYRLRHR PVPEIPNPAA VSPQERSTQT SSPEHLTGSE RPTGANDAQK APLQRTFTPI
VPYGEIFLFN NPEPALEQSA KKGLQRGFKA KMKQQKKRKK SKDKERPPGS SVSDGDDYST
VSALPEITLQ RSLSSTPAAA SPPSSGPKDE SLIMVECDLY SQRADVLSSC TKRAQPDISP
YACFYGAPKH QVLKVGWLDK LSPQGNCVFQ RRWVRFDGNS LAYYNNDKEM YSKGLILASA
VRQVRGLGDN KFEVVTSLRT FVFRAEKEGE RREWMETLQM ATRPPACSSQ KRSDSLPHLS
STNKRGLLEL RGYKGRVLVS LVGSKVRLCK TEQDYRAGLG IAEVDLTAAN VREVDRKGFE
INTPFKNFCF VADSEKEKAQ WIEAVQESIV ETLSDYEVAE KIWFNEANRS CADCCAPQPE
WASVNLGVVL CKKCAGQHRS LGPHLSKVRS LKLDSSIWSN ELVELFLEVG NKNVNAFWAA
NLPMEEELHS MASAEQRATF VRRKYRERKY RRILEGLYDV EQLNQALCAA VVTPDVLQTM
ALVFSGADVM CATGDPTYST PYLLAQRAGQ KLQMEFLHQN KLSDFSCSEN ASSSDASLFM
DGFLYISTGS AKTTVERRGR DDMARRWCTL EGGFLSYYES ERSASAMGRV DVTEVVCLAI
SNTETMSGAG AVFTVELYLQ TERMLIVGAE TQATQHDWIQ ALTKCFVPSK VEGLVQKDGE
LIGRLQYKEG HDLYHWRTGW FTLEGSALHF SSGEEEGEEE VLQLKQLQEL TVSTHTEGED
KIQVLLMVEC GRTIYIRGFN KMDFSLWHSA ITLAAGTDGK ALSDQQLTKN GVPIIVDSCI
AFVTQYGLCQ EGVYQRTGDP ARVSLLLEEF TRDARNVKLR EKEHQLEDVT DTLKSFLSQA
EDALLTKELY PFWVSALDET NESQRVKKYS TFIESLPKIN KSTLEALLQH LYRIQQCSHL
NQMSSEKLAT VFSSCLFQTQ GQTPQEISVV HDLISNYITL FSVNEDQVQQ MERENGFITR
WNEKKDTSFS PAGDLIFEVY LEKRVPEQCC LIKVSPSMRP SELAEIALSM KNATFRADDL
WTTFEVIENG ELERPLHHSE KILEQVLEWS TLECPSSAFL LIKKFPGAKR MANDKDSQQF
IKGDYLKFND GSSKLLPGHK FQDKYVALHA EKLLLYREIK NTKAEKTIQL KTVKCYLGLK
KKLKPPTNWG FTVYTDKQQW HFCCDKRETQ VSWVTDIIAT KFGSDLHSKG TSDLKTSRGT
AGTESSKLPL YNHSYNKQVI PQQMDRRVSL GNGESKTTKV CDLPLKSQTL PNSPKPSDRH
KTKSVPNSPK PGGDLKTKPL PSSPKPGGDL KTKPVLNNPQ TLEVPQRRTS VDVSLPPQLP
SPSLPRHLRP MPQFVSPQSS SKPLNKRPFL GGEGGMPPNL MNELNSVLSK TGRKSSD
//
