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Database: UniProt
Entry: A0A2U3WSA0_ODORO
LinkDB: A0A2U3WSA0_ODORO
Original site: A0A2U3WSA0_ODORO 
ID   A0A2U3WSA0_ODORO        Unreviewed;      2089 AA.
AC   A0A2U3WSA0;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Rho GTPase-activating protein 32 isoform X1 {ECO:0000313|RefSeq:XP_004412102.1};
GN   Name=ARHGAP32 {ECO:0000313|RefSeq:XP_004412102.1};
OS   Odobenus rosmarus divergens (Pacific walrus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Pinnipedia; Odobenidae;
OC   Odobenus.
OX   NCBI_TaxID=9708 {ECO:0000313|Proteomes:UP000245340, ECO:0000313|RefSeq:XP_004412102.1};
RN   [1] {ECO:0000313|RefSeq:XP_004412102.1}
RP   IDENTIFICATION.
RG   RefSeq;
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   RefSeq; XP_004412102.1; XM_004412045.2.
DR   STRING; 9708.A0A2U3WSA0; -.
DR   GeneID; 101370367; -.
DR   KEGG; oro:101370367; -.
DR   CTD; 9743; -.
DR   InParanoid; A0A2U3WSA0; -.
DR   OrthoDB; 5314555at2759; -.
DR   Proteomes; UP000245340; Unplaced.
DR   GO; GO:1901981; F:phosphatidylinositol phosphate binding; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd07298; PX_RICS; 1.
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; IPR042139; PX_ARHGAP32.
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   Reference proteome {ECO:0000313|Proteomes:UP000245340};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          259..321
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          372..567
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   REGION          27..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          671..708
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          720..739
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          824..856
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          954..1035
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1111..1162
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1206..1257
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1291..1312
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1337..1359
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1800..1865
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1880..2003
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        992..1026
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1232..1257
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1812..1847
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1938..1974
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2089 AA;  229874 MW;  B25CEBD3FE72B5A7 CRC64;
     METECESSTS GDDSVFWLDF EVLTEMTGSE EGERDDNFRK MKSSVHSEED DFVPELHRNV
     HPRERPDWEE TLSTMARGAD VPEIPGDLSL KTCGSTASMK VKHVKKLPFT KGHFPKMAEC
     AHFHYENVEF GSIQLSLSEE QNEITKNGCE SKELVYLVHI ACQGKSWIVK RSYEDFRVLD
     KHLHLCIYDR RFSQLSELPR SDALKDSPES VTQMLMAYLS RLSAIAGNKI NCGPALTWME
     IDNKGNHLLV HEESSINTPA VGAAHVIKRY TARAPDELTL EVGDIVSVID MPPKVLSTWW
     RGKHGFQVGL FPGHCVELIN QKVPQSVTNS VPKPVSKKHG KLITFLRTFM KSRPTKQKLK
     QRGILKERVF GCDLGEHLLN SGFEVPQVLQ SCTAFIERYG IVDGIYRLSG VASNIQRLRH
     EFDSEHVPDL TKEPYVQDIH SVGSLCKLYF RELPNPLLTY QLYEKFSDAV SAATDEERLI
     KIHDVIQQLP PPHYRTLEFL MRHLSLLADY CSITNMHAKN LAIVWAPNLL RSKQIESACF
     SGTAAFMEVR IQSVVVEFIL NHVDVLFSGK ISAVIQDGAA SLSRPKSLLV SSPSTKLLTL
     EEAQARTQAQ VSSPIVTENK YIEVGEGPAA LQGKFHTIIE FPLERRRPQN KMKKSPVGSW
     RSFFNLGKSS SVSKRKLQRN ESEPSEMKAL SLKGGRAEGT LRSAKSEESL TSLHAVDGDS
     KLFRPRRPRS SSDALSASFN GEMLGNRCNS YDNLPHDNES EEEVGLLHIP ALMSSHTAED
     VDLSPPDIGV ASLDFDPMSF QCSPPKAESE CLESGASFLD SLGYSQEKSS SNKKDTEAGG
     SQSQTPGSTA SSEAVSPLQE KLSPFFTLDL SPTEEKSSKP SSFTEKVVYA FSPKIGRKLS
     KSPSMNISEP ISVTLPTRVS EVIGTVSNTA APNASSPTWS KSVEDSDVIN RSPTQVGKMK
     TNEREAQGGC ESEVQPLDQG AAAEVESPGK EEQVVASSQS KAVPSGQTQT GAVTHDPPQD
     SVPVSSVSLI PPPPPPKNVA RLLALALAES AQQASTQSLK RPGTSQAAYS HYGDIAVAAT
     EDKLPSPYSS VTLDKAYFQT DRPAEEFHLQ HGVSGDCDQP SPDPAAPGNP PHASATEAGE
     QLDQADFPGS YPYRTHLPGD PDKARITSVA LTDSKSDDHL SFLEDQSGKT SMPTVSFMDQ
     DQGQLHFYSG EQPPYLGASM DKPHHHPSEL ADKSPTPSNL PRDKSYPPSG SPEENPSTAT
     MAYLTTALAT AEMSTREASW DVVEQATAAD CPAVTLQRPP RTNRPLPPPP SQRSAELLPV
     MGQVQAATNI GLNNSHKVRR GGIVPAPERP PDPRAMDDPA PILGSDGAAA QCPISGPALQ
     PSLPEKAREG ARAPPLPLRA DSVPVFSSCG FPAPVPPTRT MESKMATAIH SSSADAPSSS
     GYHPFVTASS ASVDDALPLP LPVPQPKHAS QKTTYSTFAR PDVTTEPFGP ENCLHFNMNP
     NCQYRPQSVP PHHNKLEQHQ VYGSRSEPPA SMGPRYNTYV APGRNASGHH AKPCSRVEYV
     SSLGSTIRSS CYPEDIPPYP TIRRVQSLHA PPSSMIRSVP ISRTEVPPDD EPAYCPRPLY
     QYKPYQSSQA RSDYHVTQLQ PYFENGRVHY RYSPYSSSSS SYYSPEGALC DVDAYGTVQL
     RPLHRLPNRD FAFYNPRLQG KNLYSYAGLL PRPRANMTGY FSGNDHNVVN MPPTADVKHT
     YTSWDLEDME KYRMQSIRRE SRARQKVKGP VMSQYDNMTP AVQDDLGGIY VIHLRSKSDP
     GKTGLLSVAE GKEGRHPAKA VSPEGEDRFY RKHPEPEFDR AHHHGGYGNG QSEKPTLPQK
     QSSLRNRKLH DMGCSLPEHR AHQEASHRQL CESKNGPPYP QGAGQLDYGP KGIPDTSEPV
     SYHNSGGKYI PSGQESLRLN HKEVRLSKEL ERPRARQPPA PEKHSRDCYK EEEHLPQSIV
     PPPKPERSHS LKLHHTQNVE RDPGVLYQYQ THGKRQSSMT VVSQYDNLEG YHSPPQHQRG
     GFGGGAMGTY VAPGFPHPQN RTYATALGQG AFLPTELSLQ HPETQIHAE
//
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