ID A0A2R9ABW2_PANPA Unreviewed; 1126 AA.
AC A0A2R9ABW2;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Rho GTPase activating protein 33 {ECO:0000313|Ensembl:ENSPPAP00000012942.1};
GN Name=ARHGAP33 {ECO:0000313|Ensembl:ENSPPAP00000012942.1};
OS Pan paniscus (Pygmy chimpanzee) (Bonobo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9597 {ECO:0000313|Ensembl:ENSPPAP00000012942.1, ECO:0000313|Proteomes:UP000240080};
RN [1] {ECO:0000313|Ensembl:ENSPPAP00000012942.1, ECO:0000313|Proteomes:UP000240080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22722832; DOI=10.1038/nature11128;
RA Prufer K., Munch K., Hellmann I., Akagi K., Miller J.R., Walenz B.,
RA Koren S., Sutton G., Kodira C., Winer R., Knight J.R., Mullikin J.C.,
RA Meader S.J., Ponting C.P., Lunter G., Higashino S., Hobolth A., Dutheil J.,
RA Karakoc E., Alkan C., Sajjadian S., Catacchio C.R., Ventura M.,
RA Marques-Bonet T., Eichler E.E., Andre C., Atencia R., Mugisha L.,
RA Junhold J., Patterson N., Siebauer M., Good J.M., Fischer A., Ptak S.E.,
RA Lachmann M., Symer D.E., Mailund T., Schierup M.H., Andres A.M., Kelso J.,
RA Paabo S.;
RT "The bonobo genome compared with the chimpanzee and human genomes.";
RL Nature 486:527-531(2012).
RN [2] {ECO:0000313|Ensembl:ENSPPAP00000012942.1}
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 EMBL; AJFE02054455; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A2R9ABW2; -.
DR Ensembl; ENSPPAT00000035610.1; ENSPPAP00000012942.1; ENSPPAG00000029621.1.
DR GeneTree; ENSGT00940000155110; -.
DR Proteomes; UP000240080; Chromosome 19.
DR Bgee; ENSPPAG00000029621; Expressed in testis and 6 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; cd07299; PX_TCGAP; 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; 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:SF11; RHO GTPASE-ACTIVATING PROTEIN 33; 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:UP000240080};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 186..248
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 315..510
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 551..671
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 696..873
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 895..914
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 929..949
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 954..973
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 985..1126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 571..586
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 621..646
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 709..736
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 748..763
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 796..810
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 895..911
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1017..1032
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1033..1048
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1057..1074
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1126 AA; 121095 MW; C9C8607DC92143F9 CRC64;
MVARSTDSLD GPGEGSVQPL PTAGGPSVKG KPGKRLSAPR GPFPRLADCA HFHYENVDFG
HIQLLLSPDR EGPSLSGENE LVFGVQVTCQ GRSWPVLRSY DDFRSLDAHL HRCIFDRRFS
CLPELPPPPE GARAAQMLVP LLLQYLETLS GLVDSNLNCG PVLTWMELDN HGRRLLLSEE
ASLNIPAVAA AHVIKRYTAQ APDELSFEVG DIVSVIDMPP TEDRSWWRGK RGFQVGFFPS
ECVELFTERP GPGLKADADG PPCGIPAPQG ISSLTSAVPR PRGKLAGLLR TFMRSRPSRQ
RLRQRGILRQ RVFGCDLGEH LSNSGQDVPQ VLRCCSEFIE AHGVVDGIYR LSGVSSNIQR
LRHEFDSERI PELSGPAFLQ DIHSVSSLCK LYFRELPNPL LTYQLYGKFS EAMSVPGEEE
RLVRVHDVIQ QLPPPHYRTL EYLLRHLARM ARHSANTSMH ARNLAIVWAP NLLRSMELES
VGMGGAAAFR EVRVQSVVVE FLLTHVDVLF SDTFTSAGLD PAGRCLLPRP KSLAGSCPST
RLLTLEEAQA RTQGRLGTPT EPTTPKAPAS PAERRKGERG EKQRKPGGSS WKTFFALGRG
PSVPRKKPLP WLGGTRAPPQ PSGSRPDTVT LRSAKSEESL SSQASGAELL GAGGAPASAT
PTPALSPGRS LRPHLIPLLL RGAEAPLTDA CQQEMCSKLR GAQGPLGPDM ESPLPPPPLS
LLRPGGAPPP PPKNPARLMA LALAERAQQV AEQQSQQECG GTPPAPQSPF HRSLSLEVGE
EPLGTSGSGP PPNSLAHPGA WVPGPPPYLP RQQSDGSLLR SQRPMGTSRR GLRGPAQVSA
QLRAGGGGRD APEAAAQSPC SVPSQVPTPG FFSPAPRECL PPFLGVPKPG LYPLGPPSFQ
PSSPAPVWRS SLGPPAPLDR GENLYYEIGA SEGSPYSGPT RSWSPFRSMP PDRLNASYGM
LGQSPPLHRS PDFLLSYPPA PSCFPPDHLG YSAPQHPARR PTPPEPLYVN LALGPRGPSP
ASSSSSSPPA HPRSRSDPGP PVPRLPQKQR APWGPCTPHR VPGPWGPPEP LLLYRAAPPA
YGRGGELHRG SLYRNGGQRG EGAGPPPPYP TPSWSLHSEG QTRSYC
//
