ID A0A2U3XGP3_LEPWE Unreviewed; 1448 AA.
AC A0A2U3XGP3;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Arf-GAP with Rho-GAP domain, ANK repeat and PH domain-containing protein 1 isoform X2 {ECO:0000313|RefSeq:XP_006730498.1};
GN Name=ARAP1 {ECO:0000313|RefSeq:XP_006730498.1};
OS Leptonychotes weddellii (Weddell seal) (Otaria weddellii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Pinnipedia; Phocidae;
OC Leptonychotes.
OX NCBI_TaxID=9713 {ECO:0000313|Proteomes:UP000245341, ECO:0000313|RefSeq:XP_006730498.1};
RN [1] {ECO:0000313|RefSeq:XP_006730498.1}
RP IDENTIFICATION.
RC TISSUE=Liver {ECO:0000313|RefSeq:XP_006730498.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_006730498.1; XM_006730435.2.
DR GeneID; 102747346; -.
DR CTD; 116985; -.
DR OrthoDB; 4835at2759; -.
DR Proteomes; UP000245341; 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; cd08837; ArfGap_ARAP; 1.
DR CDD; cd13253; PH1_ARAP; 1.
DR CDD; cd13254; PH2_ARAP; 1.
DR CDD; cd13256; PH3_ARAP; 1.
DR CDD; cd13257; PH4_ARAP; 1.
DR CDD; cd13259; PH5_ARAP; 1.
DR CDD; cd17226; RA_ARAP1; 1.
DR CDD; cd04385; RhoGAP_ARAP; 1.
DR CDD; cd09490; SAM_Arap1_2_3; 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 PANTHER; PTHR45899:SF3; ARF-GAP WITH RHO-GAP DOMAIN, ANK REPEAT AND PH DOMAIN-CONTAINING PROTEIN 1; 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 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:UP000245341};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00288};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00288}.
FT DOMAIN 10..64
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT DOMAIN 336..428
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 449..538
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 544..669
FT /note="Arf-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50115"
FT DOMAIN 752..859
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 967..1148
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT DOMAIN 1181..1270
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 1283..1394
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 95..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 179..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 272..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..224
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..292
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1448 AA; 161562 MW; F14E0BD194293A41 CRC64;
MAEAGDAALS VAEWLRALHL EQYAGLFEQH GLVWATECQG LSDARLQDMG MLLPGHRRRI
LAGLLRAHTP PTPAPRPTAR PVPMKRHVFR SLPAPALPPA ALPEPLPTAG EEAGLPTAPP
IPPRRSCLPP ACFSAPSAAA PDPVLPPLPA KRHLAELSVP PVPPRTGPPR LLVSLPSKEE
ELLSPLLSSP PQPEPEEPPA TLPRVPPQPP SPPPSPPEIP PKPLRLLPEF DDSDYDEVPE
EGPGAPAGLM TKKEELPVSH FPRAVRVASL LSEGEELSGD DDQGDEDEDD HAYEGVPNGG
WHASSLSSSL PSSLLIPELP PPPMDGLPGD PTPITPVIKA GWLDKNPPQG SYIYQKRWVR
LDADHLRYFD SNKDAYSKRF ISVACISRVA AIGDQKFEVI TNNRTFAFRA ESDAERKEWV
RALQQAAAEQ GARARLSSTY PLGVRGPELP DHAGSLELRG FKNKLYVAVV GDKVQLYKNL
EEYHLGIGIT FIDMSVGNVK EADRRSFDLT TPYRIFSFSA ESELEKEQWL EAMQGAIAEA
LSTSEVAERI WAVAPNRFCA DCGAAQPDWA SINLCVVICK RCAGEHRGLG AGVSKVRSLK
MDRKVWTETL IELFLHLGNG TGNRFWAANV PPSEALQPNS SPGARRRHLE AKYREGKYRC
YHPLFGNQEE LDKALCATVT TTDLAETQAL LGCGAGVNCF SGDPEAPTPL ALAEQAGQIL
QMEFLRNNRT TEVPRLESTK PLEKHYSVVL PTVSHSGFLY KTASAGKLLQ DRRAREEFSR
RWCVLSDGVL SYYENERAVT PNGEIRASEI VCLAVPPPDT HGFEHTFEVY TEGERLYLFG
LESAELAREW VKCIAKAFIP PLAEDLLTRD FERLGRLPYK AGLSLQRAQE GWFSLTGSEL
RAVFPEGPCE EPLQLRKLQE LSVQGDSENQ VLVLVERRRT LYIQGERRLD FTGWLGAIQK
AAASSGDTLS EQQLGDSDIP VIVYRCVDYI TQCGLTSEGI YRKCGQTSKT QRLLESLRQD
ARSVRLKEGE QHVDDVSSAL KRFLRDLPDG LFTRAQRLAW LDTSEIEDEE EKVSRYRELL
ARLPPVNRAT VKALISHLYC VQCFSDTNQM NTHNLAIVFG PTLFQTDGQD YKAGRVVEDL
ISHYVVVFSV DEEELRKQRE EITAIVKMRV AGTASGTQHA GDFICTVYLE EKKADTEQHI
KIPASMTAEE LTLEILDRRN VGVRERDYWT CFEVNEREEA ERPLHFAEKV LPILHGLGTD
SYLVVKKHQS MEAMLLYLAS HVGDTKHGMM KFREDRSLLG LGLPSGGFHD RYFILNSSCL
RLYKEIRSHR PEKEWPVRSL KVYLGVKKKL RPPTCWGFTV VHETEKHEKQ QWYLCCETQM
ELREWFATFL FVQHDGLVWP SEPSRVSRAV PEVRLGSVSL IPLRGSENEM RRSVAAFAAD
PLSLLRNV
//
