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Database: UniProt
Entry: A0A3P8YF49_ESOLU
LinkDB: A0A3P8YF49_ESOLU
Original site: A0A3P8YF49_ESOLU 
ID   A0A3P8YF49_ESOLU        Unreviewed;      1806 AA.
AC   A0A3P8YF49;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   02-DEC-2020, sequence version 2.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Rho GTPase-activating protein 32 {ECO:0000313|Ensembl:ENSELUP00000015232.2};
GN   Name=ARHGAP32 {ECO:0000313|Ensembl:ENSELUP00000015232.2};
OS   Esox lucius (Northern pike).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC   Esocidae; Esox.
OX   NCBI_TaxID=8010 {ECO:0000313|Ensembl:ENSELUP00000015232.2, ECO:0000313|Proteomes:UP000265140};
RN   [1] {ECO:0000313|Ensembl:ENSELUP00000015232.2, ECO:0000313|Proteomes:UP000265140}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=25069045;
RA   Rondeau E.B., Minkley D.R., Leong J.S., Messmer A.M., Jantzen J.R.,
RA   von Schalburg K.R., Lemon C., Bird N.H., Koop B.F.;
RT   "The genome and linkage map of the northern pike (Esox lucius): conserved
RT   synteny revealed between the salmonid sister group and the Neoteleostei.";
RL   PLoS ONE 9:e102089-e102089(2014).
RN   [2] {ECO:0000313|Ensembl:ENSELUP00000015232.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the PX domain-containing GAP family.
CC       {ECO:0000256|ARBA:ARBA00008795}.
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DR   Ensembl; ENSELUT00000039254.2; ENSELUP00000015232.2; ENSELUG00000015466.2.
DR   GeneTree; ENSGT00940000154313; -.
DR   Proteomes; UP000265140; LG07.
DR   Bgee; ENSELUG00000015466; Expressed in spleen and 15 other cell types or tissues.
DR   GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd04384; RhoGAP_CdGAP; 1.
DR   CDD; cd11835; SH3_ARHGAP32_33; 1.
DR   Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR   Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   InterPro; IPR036871; PX_dom_sf.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   PANTHER; PTHR15729; CDC42 GTPASE-ACTIVATING PROTEIN; 1.
DR   PANTHER; PTHR15729:SF13; RHO GTPASE-ACTIVATING PROTEIN 32; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   Pfam; PF14604; SH3_9; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR   SUPFAM; SSF64268; PX domain; 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265140};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          246..308
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          359..554
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   REGION          687..725
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1027..1187
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1265..1292
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1560..1586
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1605..1716
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1742..1778
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1027..1041
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1042..1070
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1076..1095
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1102..1122
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1123..1145
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1165..1181
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1608..1625
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1658..1699
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1754..1778
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1806 AA;  200047 MW;  1685E69FD9BC233F CRC64;
     LNSLDCVVSV TKKYNNWITS SGTVHQGLRP GRHPEEDDIV PELARLVYPR ERPDWEETIS
     AMARSAEVPE LNAEPLLRSC SSTASMKVKN IKKLSFTKGH FPKLAECAHF HYENVDFGTI
     QLALADEQSE VTRNGFESKE LVYLVQIYCQ GRSWIVKRSY EDFRVLDKHL HLCIYDRRFS
     QLPELPRVSS LKDRAEAVSQ MLMAYLSRFS AIADNKINCG PALTWMEVDN KGNHLLVHEE
     SSINVPAIAA AHVIKRYTAQ AADELSFEVG DIVSVIDMPP KEDTTWWRGK HGFQVGFFPS
     ECVELINDKV PQSVTNSVPK PVSKKHGKLI TFLRTFMKSR PTKQKLKQRG ILRERVFGCD
     LGEHLLNSGH DVPQVLKSCT DFIEKHGVVD GMYRLSGIAS NIQKLRHEFD SEQIPDLTKD
     VYIQDIHCVG SLCKLYFREL PNPLLTYQLY EKFSEAVSAA TDEERLIKIH DVIQQLPPPH
     YRTLEFLMRH LSHLATFSYV TNMHSKNLAI VWAPNLLRSK QIESACFSGT AAFMEVRIQS
     VVVEFILNHV DVLFSPKLSS LIREGAGHNS LSRPKSLLVS SPSTKLLTLE EAQARTQAQI
     NSPVTADSKY IEVGEGPAAL QGKFHTVIQF PTERKRPPVK SKKSPVGSWR SFFNLGKSSS
     MSKRKLQRNP SEPSELKTMA LAGGRGDTAT LRSAKSEESL TSLHNVEGES KVYRPRRPRS
     SSDALSASFN GDLLDSHTRQ HCNAFEKLAQ GNSVGSTRDR AGSDEDEGPI CVPALISPPR
     SSGEDVDLSP PDIGMASLDF DPMSFQCSLP DGSFSFPMGL SDAATGVAGQ GSAENNSAPV
     SPSFLGKFTS PFLSPDLSPA MGKKAESKKM TCSVSFPDKT LQAVSPIKSK SAILAPLTIS
     EPFAVEFPAK PTESHCVPQP SSPPTGLLRD SPPLMGSVLL RTGEPSLSEA FQMEMHSCLF
     PLLFSCPQAP FLFSVLTLQC PSVFVPLPGA VASLDSPKAS PSVSLLHPPP PPKNAARMLA
     LALAESAQQA SILTQRRPSK SQPPTPLSPV RPMEPSHSLD WPPPPPMHPH TSLEEGLQTG
     AAQTPNQTPT TITPNLTPSS SPPPTITTDK QPSQSSSEQP QPAPHPQSKP QLQPHPKPQS
     HPQPNARLAP APAESVERPW EAIKPIQPPT EPVPHHNAHG PPTPPVRSIE SKLATAALSH
     TEAANPAIFH NILAEASMPE EALAHPPPPL RKTSNHQSAY LYHTKGDAAS LEPMGEDYYH
     QRAIPTGQPS YHYRPDSVPP HHSYVSKSEP QIPYSARTDQ RYYTLAHPRS YHQTMKHRGP
     PRAGEYISPS LGHRGQAYGP MEGGPVYPTI RRVHSLHVPS NVRSVPFQRA EVPPDNELFY
     YQRPVYQCKA YQPPQQSPQA DYHVTQLQPY FENGRVQYRY SPYSPSTNPL DSPYYDVDPY
     GTVRLRHFHS FGSRDLGPAL GRSGGKAGSY HYLSRHVFPP GKEHSFVSRD MPPVHGSKGA
     AVYIAWDPDE SERLRMHSIR RESRARQKVK GPVMSQYDNV GMFVPGDLGR YETLHLRSKS
     DPGKAMLMSA EGKDGHYGVH PGSQHAPRHL VSDLDLLMYM EPEKHCQGNG TGDQQISSRN
     CPASHLHQAQ HLPRKQPHQQ DPSQHDPGDS ARGFQPSYER LDPDRHLNRA KTPGGHQKHD
     DQQQPTPVKP ERLHSVRERP QQHYSQTPMP EPDRDYSYQL HGRQQRHSTV TVQSHYDNLD
     DYHPAAVPQP QAPMPNSHGG SSGSFPTNPG FTGSHSNRAY STALGQGAFI PAELALQRPE
     TEIHAE
//
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