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Database: UniProt
Entry: A0A3Q3GUZ4_9LABR
LinkDB: A0A3Q3GUZ4_9LABR
Original site: A0A3Q3GUZ4_9LABR 
ID   A0A3Q3GUZ4_9LABR        Unreviewed;      2028 AA.
AC   A0A3Q3GUZ4;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Rho GTPase activating protein 32 {ECO:0000313|Ensembl:ENSLBEP00000038302.1};
GN   Name=ARHGAP32 {ECO:0000313|Ensembl:ENSLBEP00000038302.1};
OS   Labrus bergylta (ballan wrasse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Labriformes; Labridae; Labrus.
OX   NCBI_TaxID=56723 {ECO:0000313|Ensembl:ENSLBEP00000038302.1, ECO:0000313|Proteomes:UP000261660};
RN   [1] {ECO:0000313|Ensembl:ENSLBEP00000038302.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the PX domain-containing GAP family.
CC       {ECO:0000256|ARBA:ARBA00008795}.
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DR   Ensembl; ENSLBET00000039875.1; ENSLBEP00000038302.1; ENSLBEG00000028551.1.
DR   GeneTree; ENSGT00940000154313; -.
DR   Proteomes; UP000261660; Unplaced.
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; PF07653; SH3_2; 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:UP000261660};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          252..314
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          390..585
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   REGION          718..809
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          838..860
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          930..957
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          991..1200
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1252..1379
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1524..1543
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1607..1630
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1824..2028
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        752..778
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1001..1031
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1056..1080
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1094..1197
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1253..1273
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1284..1305
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1310..1341
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1350..1367
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1829..1856
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1857..1885
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1895..1953
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1990..2010
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2028 AA;  223528 MW;  1B771FBA1EE9B218 CRC64;
     MEAGSGAAAA VGSTALGLLG ATATSSHDIL DRGLRSGRHL EDDDIVPELA YIHPRERPDW
     EETISAMARS AEIPELRAEP LMRSCSSSTA SMKVKNVKKL CFTKGHFPKL AECAHFHYEN
     VDFGTIQLSL GDEQCEVTRN GFESKELVYL VHIYCQGRSW IVKRSYEDFR VLDKHLHLCI
     YDRRFSQLPE LPRLDSLTDQ SESVSQMLLA YLSRLSAIAD NKINCGPALT WMEVDNKGNH
     LLVHEESSIN VPAIAAAHVI KRYIAQASDE LSFEVGDIVS VIDMPPKEDT TWWRGKHGFQ
     VGFFPSECVE LINDKVPQSM TNTVPKPDLE MESVIQDNAW VADPLNHYSI SSVSKKHGKL
     ITFLRTFMKS RPTKQKLKQR GILRERVFGC DLGEHLLNSA HDVPQVLKSC TEFIEKHGVV
     DGIYRLSGIA SNIQKLRHEF DSEQIPDLTK DVYIQDIHCV GSLCKLYFRE LPNPLLTYQL
     YEKFSEAVSA ATDEERLIKI HDVIQQLPPP HYRTLEFLMR HLSHLAAFSY ITNMHSKNLA
     IVWAPNLLRS KQIESACFSG TAAFMEVRIQ SVVVEFILNH VDVLFSSKLS SLIREGAGHN
     SLSRPKSLLV SSPSTKLLSL EEAQARTQAQ INSPVTEDSK YIEVGEGPAA LQGKFHTVIE
     FPTERKRPPI KSKKSPVGSW RSFFNLGKSS SMSKRKLTRN PSEPNELKAM ALAGGRGDTA
     TLRSAKSEES LSSLHNVEGE SKVYRPRRPR SSSDALSASF NGDLLDSRQH CNSYDNLDGT
     EDSDGDDGPI CVPALISPPR SAGEDVDLSP PDIGMASLDF DPMSFQCSLP DTSYAFPLDD
     SPAGAEGSTL KRSPGSKSNG SDLMSASFLG SLTSPLLSGD FCYREKIESK KLTTSYSYTD
     KPTQAVSPIK CAKTTSLTPL ATSELFSVEK PDDRNTAAHP VSSQPLSPPA AAKDSPPLMG
     SVLLRAAEPS LSEAFQMELH SKLATFDSVD SQELKGDDSV QQEPAASSQE QQGVVAPDSS
     KDLTPRFLSS TAPSAAPPPP PPKNAARMLA LALAESAQQV SVQSQFRSSE PPTPVSPLQT
     HEESDLLGVA HPKVQHFQTS SEDGAERESS LPPNSTAPTV TTTSSYPSAS SPAIKLQPLE
     LTSTITKLPD SAKSSTTPLG PHPDTDSSST DTTLYKCVPL PSSTSLSSPT RKSPERQQSV
     PAHVPVHIPV HVPVHVPVHV PVHVPVHVPV HVPVHVPVHV PVHVPVHVPV HVPVHTNSSS
     NTPATTPSGS RKDTRVLPQP VPEVKPGETS PRPILPKPSD QPPPIKPKRQ ALSQHQTQTQ
     QQSQAQIQAH LQTQSNSQPH PPSQPNTQPQ TPALPQTHTQ PPSKASARVA PTSAEPVEKP
     WEAIKPVQPC TEPVKYHEVY GPPAPPVRTI ESKLATAALS QSEASYHVLA EGPTPGHLEE
     ALPHHPPSPR KSSTHQPAYL YHAKAEPVLM EPPGAAYYHQ RPVPLGPQTM PHHYRPDSVP
     PHLSFVSKSE PQIPYSARVD NRYSTLGPRS YHHSIKSRGN SRGVYVSPGP GHQGYSHDRT
     HGYPTIRRVH SLHVPSTIRT VPIQRTEVPP DDEIFFYHRP VYPCKAYQQP PQQQQPPQQQ
     QQQQQSSQGD YHVTQLQPYF ENGRVQYRYS PYSGSGPVEA PYYDIDPYGT IRVRHFHSRD
     PGAAAGRPGG KATGYHYLAR HVLPPGKEHS FVSRDMPPGH ASMEAPAYLS WDPEESERLR
     FQSIRRESRA RQKVKGPVLS QYDNVGLFAP ADISGYEMLH LRSKSDPGKA VLAAAESKDG
     RYLPRHMTSD PDVVLYMETD KHVQGDRSEG LAKQSTSKKC QSSHSFPSSL SHSLSHQQES
     SRHDAKPADD KQGTDGSRSK HWQQEYPSKR SFTPRYECPD SDHKGKSGYH STEEQPSDPR
     DQHAHSKPER SHSVREPPHY SKPEPDRDYS YQKHSSKAAQ SHYDNLDDYR PVPQPQAPLH
     KRGGSGSYPG PGFSVSQNNR AYSTALGQGG YIQTDLALPR PETEIRTE
//
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