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Database: UniProt
Entry: A0A3Q1AR17_AMPOC
LinkDB: A0A3Q1AR17_AMPOC
Original site: A0A3Q1AR17_AMPOC 
ID   A0A3Q1AR17_AMPOC        Unreviewed;       782 AA.
AC   A0A3Q1AR17;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Rho GTPase-activating protein 26-like {ECO:0000313|Ensembl:ENSAOCP00000003713.1};
GN   Name=ARHGAP26 {ECO:0000313|Ensembl:ENSAOCP00000003713.1};
OS   Amphiprion ocellaris (Clown anemonefish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Amphiprion.
OX   NCBI_TaxID=80972 {ECO:0000313|Ensembl:ENSAOCP00000003713.1, ECO:0000313|Proteomes:UP000257160};
RN   [1] {ECO:0000313|Ensembl:ENSAOCP00000003713.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion
CC       {ECO:0000256|ARBA:ARBA00004246}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004370}.
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DR   AlphaFoldDB; A0A3Q1AR17; -.
DR   Ensembl; ENSAOCT00000009317.1; ENSAOCP00000003713.1; ENSAOCG00000007075.1.
DR   GeneTree; ENSGT00940000157254; -.
DR   OMA; YALITSQ; -.
DR   OrthoDB; 5395569at2759; -.
DR   Proteomes; UP000257160; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd01249; BAR-PH_GRAF_family; 1.
DR   CDD; cd07636; BAR_GRAF; 1.
DR   Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   InterPro; IPR027267; AH/BAR_dom_sf.
DR   InterPro; IPR004148; BAR_dom.
DR   InterPro; IPR035483; GRAF_BAR.
DR   InterPro; IPR047234; GRAF_fam.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR047225; PH_GRAF.
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; PTHR12552; OLIGOPHRENIN 1; 1.
DR   PANTHER; PTHR12552:SF4; RHO GTPASE-ACTIVATING PROTEIN 26; 1.
DR   Pfam; PF16746; BAR_3; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   Pfam; PF14604; SH3_9; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR   SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000257160};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          265..369
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          383..567
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   DOMAIN          724..782
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   REGION          573..617
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          629..721
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          87..140
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        573..591
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        602..617
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        629..693
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        706..721
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   782 AA;  88941 MW;  F716ACE62D99A6C2 CRC64;
     MGLPALEFSD CYLDSPQFRE RLKSHELELD KTNKFIKELI KDGKALIQAL KSLSTAKRKF
     ADSLNEFKFQ CIGDAETDDE MCIAKSLQEF AAVLQNLEDE RTRMIENAND VLIMPLERFR
     KEQISAAKEA KKKYDKETEK YCAVLEKHLS LSARKKESHL HEADNQVDNV RQHFYEVSLE
     YVFKVQEVQE RKMFDFVEPL LAFLQGLFTY YHHGYELAKD FNHFKTDLTI SIQNTRNRFE
     STRSEVESLM RKMKENPHEH KSVSQHTMEG YLFVQEKRSF VSTWVKYYCT YHREPKKVTM
     VLFDPKSGGK TGEEESFLLK SCTRRKTDSI EKRFCFDVEA VDRPGVITMQ AMSEEDRRLW
     MEAMDGREPV YNLNKDNQAE GMAHLDVIGF NVMKKFIYAV DTRGIDEQGL YRIVGVNSRV
     QKLLSLAMDP KTCADVELEN SEWEIKTITS AIKHYLRMLP APLMTYQYQR SFIKAAKMDN
     PEARVTEIHA LVHRLPEKNR QMLELLMKHL ANVASHHQQN LMTIANLGVV FGPTLLRPQE
     ETVAAIMDIK FQNIVVEILI EHHERIFRDV SNSAGGSANM QLNLSRRRSA ESKAPSCSER
     PLTLFHTPTH SQKGEKRNSV VNTADLQQPV SSSANCNSSS SSSSGSSSQS RTPRHSLTSN
     DGEQDSRQIR PSSLLNPKSR GSVPTSATSP SPTSPRSPSW PMFSAPSSPQ PTSSASSDSS
     PVSIAGRKAR ALYACKAEHD SELSFIAGTI FENVHASREP GWLEGTLDGR TGLIPENYVE
     FL
//
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