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Database: UniProt
Entry: A0A2I3TET3_PANTR
LinkDB: A0A2I3TET3_PANTR
Original site: A0A2I3TET3_PANTR 
ID   A0A2I3TET3_PANTR        Unreviewed;      1600 AA.
AC   A0A2I3TET3;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=IQ motif containing GTPase activating protein 2 {ECO:0000313|Ensembl:ENSPTRP00000087767.1};
GN   Name=IQGAP2 {ECO:0000313|Ensembl:ENSPTRP00000087767.1,
GN   ECO:0000313|VGNC:VGNC:4048};
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000087767.1, ECO:0000313|Proteomes:UP000002277};
RN   [1] {ECO:0000313|Ensembl:ENSPTRP00000087767.1, ECO:0000313|Proteomes:UP000002277}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16136131; DOI=10.1038/nature04072;
RG   Chimpanzee sequencing and analysis consortium;
RT   "Initial sequence of the chimpanzee genome and comparison with the human
RT   genome.";
RL   Nature 437:69-87(2005).
RN   [2] {ECO:0000313|Ensembl:ENSPTRP00000087767.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   EMBL; AACZ04061838; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AACZ04061839; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AACZ04061840; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   Ensembl; ENSPTRT00000099789.1; ENSPTRP00000087767.1; ENSPTRG00000017002.7.
DR   VGNC; VGNC:4048; IQGAP2.
DR   GeneTree; ENSGT00950000183076; -.
DR   InParanoid; A0A2I3TET3; -.
DR   Proteomes; UP000002277; Chromosome 5.
DR   Bgee; ENSPTRG00000017002; Expressed in bone marrow and 20 other cell types or tissues.
DR   GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR   GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR   GO; GO:0030175; C:filopodium; IEA:Ensembl.
DR   GO; GO:0030027; C:lamellipodium; IEA:Ensembl.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005902; C:microvillus; IEA:Ensembl.
DR   GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR   GO; GO:0071933; F:Arp2/3 complex binding; IEA:Ensembl.
DR   GO; GO:0005516; F:calmodulin binding; IBA:GO_Central.
DR   GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR   GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; IEA:Ensembl.
DR   GO; GO:0031267; F:small GTPase binding; IEA:Ensembl.
DR   GO; GO:0034314; P:Arp2/3 complex-mediated actin nucleation; IEA:Ensembl.
DR   GO; GO:1903479; P:mitotic actomyosin contractile ring assembly actin filament organization; IBA:GO_Central.
DR   GO; GO:0032956; P:regulation of actin cytoskeleton organization; IEA:Ensembl.
DR   GO; GO:0070493; P:thrombin-activated receptor signaling pathway; IEA:Ensembl.
DR   CDD; cd05131; RasGAP_IQGAP2; 1.
DR   Gene3D; 1.20.5.190; -; 1.
DR   Gene3D; 1.10.418.10; Calponin-like domain; 1.
DR   InterPro; IPR001715; CH_dom.
DR   InterPro; IPR036872; CH_dom_sf.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR000593; RasGAP_C.
DR   InterPro; IPR023152; RasGAP_CS.
DR   InterPro; IPR001936; RasGAP_dom.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR001202; WW_dom.
DR   PANTHER; PTHR14149; RAS GTPASE-ACTIVATING PROTEIN WITH IQ MOTIF; 1.
DR   PANTHER; PTHR14149:SF12; RAS GTPASE-ACTIVATING-LIKE PROTEIN IQGAP2; 1.
DR   Pfam; PF00307; CH; 1.
DR   Pfam; PF00612; IQ; 2.
DR   Pfam; PF00616; RasGAP; 1.
DR   Pfam; PF03836; RasGAP_C; 1.
DR   SMART; SM00033; CH; 1.
DR   SMART; SM00015; IQ; 3.
DR   SMART; SM00323; RasGAP; 1.
DR   SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR   SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR   SUPFAM; SSF143885; RGC domain-like; 1.
DR   PROSITE; PS50021; CH; 1.
DR   PROSITE; PS50096; IQ; 3.
DR   PROSITE; PS00509; RAS_GTPASE_ACTIV_1; 1.
DR   PROSITE; PS50018; RAS_GTPASE_ACTIV_2; 1.
DR   PROSITE; PS01159; WW_DOMAIN_1; 1.
DR   PROSITE; PS50020; WW_DOMAIN_2; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002277};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        15..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        170..190
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          66..181
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000259|PROSITE:PS50021"
FT   DOMAIN          619..652
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          942..1175
FT                   /note="Ras-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50018"
FT   COILED          190..217
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1436..1463
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1600 AA;  183297 MW;  66BC55D8511A7FEF CRC64;
     MWLTPGAEPS LQPSASPWLV ISCLFFFSFF LFETESRSVA QAGVQWRDLC SLQAPPPGKL
     PNWNHFNIFF NLFRWMEVCL VEELPPTTEL EEGLRNGVYL AKLAKFFAPK MVSEKKIYDV
     EQTRYKKSGL HFRHTDNTVQ WLRAMESIGL PKIFYPETTD VYDRKNIPRM IYCIHALSLY
     LFKLGIAPQI QDLLGKVDFT EEEISNMRKE LEKYGIQMPS FSKIGGILAN ELSVDEAALH
     AAVIAINEAV EKGIAEQTVV TLRNPNAVLT LVDDNLAPEY QKELWDAKKK KEENARLKNS
     CISEEERDAY EELLTQAEIQ GNINKVNRQA AVDHINAVIP EGDPENTLLA LKKQEAQLPA
     VYPFAAAMYQ NELFNLQKQN TMNYLAHEEL LIAVEMLSAV ALLNQALESN DLVSVQNQLR
     SPAIGLNNLD KAYVERYANT LLSVKLEVLS QGQDNLSWNE IQNCIDMVNA QIQEENDRVV
     AVGYINEAID EGNPLRTLET LLLPTANISD VDPAHAQHYQ DVLYHAKSQK LRDSESVSKV
     LWLDEIQQAV DEANVDEDRA KQWVTLVVDV NQCLEGKKSS DILSVLKSST SNANDIIPEC
     ADKYYDALVK AKELKSERVS SDGSWLKLNL HEKYDYYYNI DSKESSWVTP ESCLYKESWL
     TGKEIEDIIE EVTVGYIREN IWSASEELLL RFQATSSGPI LREEFEARKS FLHEQEENVV
     KIQAFWKGYK QRKEYMHRRQ TFIDNTDSIV KIQSWFRMAT ARKSYLSRLQ YFRDHNNEIV
     KIQSLLRANK ARDDYKTLVG SENPPLTVIR KFVYLLDQSD LDFQEELEVA RLREEVVTKI
     RANQQLEKDL NLMDIKIGLL VKNRITLEDV ISHSKKLNKK KGGEMEILNN TDNQGIKSLS
     KERRKTLETY QQLFYLLQTN PLYLAKLIFQ MPQNKSTKFM DTVIFTLYNY ASNQREEYLL
     LKLFKTALEE EIKSKVDQVQ DIVTGNPTVI KMVVSFNRGA RGQNTLRQLL APVVKEIIDD
     KSLIINTNPV EVYKAWVNQL ETQTGEASKL PYDVTTEQAL TYPEVKNKLE ASIENLRRVT
     DKVLNSIISS LDLLPYGLRY IAKVLKNSIH EKFPDATEDE LLKIVGNLLY YRYMNPAIVA
     PDGFDIIDMT AGGQINSDQR RNLGSVAKVL QHAASNKLFE GENEHLSSMN NYLSETYQEF
     RKYFKEACNV PEPEEKFNMD KYTDLVTVSK PVIYISIEEI ISTHSLLLEH QDAIAPEKND
     LLSELLGSLG EVPTVESFLG EGAVDPNDPN KANTLSQLSK TEISLVLTSK YDIEDGEAID
     SRSLMIKTKK LIIDVIRNQP GNTLTEILET PATAQQEVDH ATDMVSRAMI DSRTPEEMKH
     SQSMIEDAQL PLEQKKRKIQ RNLRTLEQTG HVSSENKYQD ILNEIAKDIR NQRIYRKLRK
     AELAKLQQTL NALNKKAAFY EEQINYYDTY IKTCLDNLKR KNTRRSIKLD GKGEPKGAKR
     AKPVKYTAAK LHEKGVLLDI DDLQTNQFKN VTFDIIATED VGIFDVRSKF LGVEMEKVQL
     NIQDLLQMQY EGVAVMKMFD KVKVNVNLLI YLLNKKFYGK
//
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