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Database: UniProt
Entry: A0A2K5LK01_CERAT
LinkDB: A0A2K5LK01_CERAT
Original site: A0A2K5LK01_CERAT 
ID   A0A2K5LK01_CERAT        Unreviewed;      1453 AA.
AC   A0A2K5LK01;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=ArfGAP with RhoGAP domain, ankyrin repeat and PH domain 1 {ECO:0000313|Ensembl:ENSCATP00000013276.1};
GN   Name=ARAP1 {ECO:0000313|Ensembl:ENSCATP00000013276.1};
OS   Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Cercocebus.
OX   NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000013276.1, ECO:0000313|Proteomes:UP000233060};
RN   [1] {ECO:0000313|Ensembl:ENSCATP00000013276.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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DR   STRING; 9531.ENSCATP00000013276; -.
DR   Ensembl; ENSCATT00000037414.1; ENSCATP00000013276.1; ENSCATG00000030588.1.
DR   GeneTree; ENSGT00940000157424; -.
DR   Proteomes; UP000233060; Unplaced.
DR   Bgee; ENSCATG00000030588; Expressed in lung and 12 other cell types or tissues.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; IEA:Ensembl.
DR   GO; GO:0051497; P:negative regulation of stress fiber assembly; IEA:Ensembl.
DR   GO; GO:0051491; P:positive regulation of filopodium assembly; IEA:Ensembl.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:Ensembl.
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; 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); 3.
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; 2.
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; 4.
DR   SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR   PROSITE; PS50115; ARFGAP; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 3.
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:UP000233060};
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          326..418
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          439..528
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          534..659
FT                   /note="Arf-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50115"
FT   DOMAIN          742..849
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          953..1138
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   DOMAIN          1171..1260
FT                   /note="Ras-associating"
FT                   /evidence="ECO:0000259|PROSITE:PS50200"
FT   REGION          68..144
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          175..301
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        70..102
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        186..219
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        271..285
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1453 AA;  162709 MW;  AA3FF1D3B01B4D97 CRC64;
     MAEAGDAALS VAEWLRALHL EQYTGLFEQH GLVWATECQG LSDARLMDMG MLLPGHRRRI
     LAGLLRAHTP PAPAPRPTPR PVPMKRHIFR SPPAPATPPE PLPTATEDEG LPTAPPIPPR
     RSCLPPTCFT TPSTAAPDPV LPPLPAKRHL AELSVPPVPP RTGPPRLLLS LPTKEEESLL
     PLSSLPQPEP EDPLSALPQG PPQPHSPPPC PPEIPPKPVR LFPEFDDSDY DEVPEEGPGA
     PARVMTKKEE PPLSRVPRAV RVASLLSEGE ELSGDDQEDG DEDDHAYEGV PNGGWHTSSL
     SLSLPSTIAA PHPMDGPPGG STPVTPVIKA GWLDKNPPQG SYIYQKRWVR LDTDHLRYFD
     SNKDAYSKRF ISVACISRVA AIGDQKFEVI TNNRTFAFRA ESDVERKEWM QALQQAMAEQ
     RARARLSSAY LLGVPGSEQP DRAGSLELRG FKNKLYVAVV GDKVQLYKNL EEYHLGIGIT
     FIDMSVGNVK EVDRRSFDLT TPYRIFSFSA DSELEKEQWL EAMQGAVAEA LSTSEVAERV
     WAAAPNRFCA DCGAPQPDWA SINLCVVICK RCAGEHRGLG AGVSKVRSLK MDRKVWTETL
     IELFLQLGNG AGNRFWAANV PPSEALQPSS SPSTRRCHLE AKYREGKYRR YHPLFGNQEE
     LDKALCAAVT TTDLAETQAL LGCGAGISCF SGDPEAPTPL ALAEQAGQTL QMEFLRNNRT
     TEVPRLDSMK PLEKHYSVIL PTVSHSGFLY KTASAGKLLQ DRRAREEFSR RWCVLSDGVL
     SYYENERAVT PNGEIRASEI VCLAVPLPDT HGFEHTFEVY TEGERLYLFG LESMEQAHEW
     VKCIAKAFVP PLAEDLLARD FERLGRLPYK AGLSLQRAQE GWFSLSGSEL RAVFPEGPCE
     EPLQLRKLQE LSIQGDSENQ VLVLVERRRT LYIQGERRLD FMGWLGAIQK AAASMGDTLS
     EQQLGDSDIP VIVYRCVDYI TQCGLTSEGI YRKCGQTSKT QRLLESLRQD ARSVHLKEGE
     QHVDDVSSAL KRFLRDLPDG LFTRAQRLAW LEASEIEDEE EKVSRYRELL VWLPPVNRAT
     VKALISHLYC VQCFSDTNQM NVHNLAIVFG PTLFQTDGQD YKAGRVVEDL INHYVVVFSV
     DEEELRKQRE EITAIVKMRV AGTASGTQHA GDFICTVYLE EKKAETEQHV KIPASMTAEE
     LTLEILDRRN VGIREKDYWT CFEVNEREEA ERPLHFAEKV LPILHGLGTD SHLVVKKHQA
     MEAMLLYLAS RVSDTKHGMM KFREDRSLLG LGLPSGGFHD RYFILNSSCL RLYKEVRSQR
     PWSGAPETSH RPEKEWPVKS LRVYLGVKKK LRPPTCWRHF WEGWADLRLN VWPRPLSAPQ
     HDGLVWPSEP SRVSRAVPEV RLGSVSLIPL RGSENEMRRS VAAFTADPLS VPSRCLRNWR
     YMAGDWNRFL ESC
//
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