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Database: UniProt
Entry: A0A3Q1F8X2_9TELE
LinkDB: A0A3Q1F8X2_9TELE
Original site: A0A3Q1F8X2_9TELE 
ID   A0A3Q1F8X2_9TELE        Unreviewed;       820 AA.
AC   A0A3Q1F8X2;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=ABR activator of RhoGEF and GTPase {ECO:0000313|Ensembl:ENSAPOP00000003690.1};
GN   Name=ABR {ECO:0000313|Ensembl:ENSAPOP00000003690.1};
OS   Acanthochromis polyacanthus (spiny chromis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Acanthochromis.
OX   NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000003690.1, ECO:0000313|Proteomes:UP000257200};
RN   [1] {ECO:0000313|Ensembl:ENSAPOP00000003690.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cell projection, axon
CC       {ECO:0000256|ARBA:ARBA00004489}. Cell projection, dendritic spine
CC       {ECO:0000256|ARBA:ARBA00004552}. Synapse
CC       {ECO:0000256|ARBA:ARBA00034103}.
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DR   AlphaFoldDB; A0A3Q1F8X2; -.
DR   Ensembl; ENSAPOT00000011326.1; ENSAPOP00000003690.1; ENSAPOG00000005363.1.
DR   GeneTree; ENSGT00940000153491; -.
DR   Proteomes; UP000257200; Unplaced.
DR   GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR   GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   CDD; cd08686; C2_ABR; 1.
DR   CDD; cd04387; RhoGAP_Bcr; 1.
DR   CDD; cd00160; RhoGEF; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 1.
DR   Gene3D; 1.20.900.10; Dbl homology (DH) 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   InterPro; IPR037769; Abr/Bcr.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR035899; DBL_dom_sf.
DR   InterPro; IPR000219; DH-domain.
DR   InterPro; IPR001331; GDS_CDC24_CS.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   PANTHER; PTHR23182:SF5; ACTIVE BREAKPOINT CLUSTER REGION-RELATED PROTEIN; 1.
DR   PANTHER; PTHR23182; BREAKPOINT CLUSTER REGION PROTEIN BCR; 1.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF19057; PH_19; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   Pfam; PF00621; RhoGEF; 1.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SMART; SM00325; RhoGEF; 1.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR   SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR   SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS00741; DH_1; 1.
DR   PROSITE; PS50010; DH_2; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
PE   4: Predicted;
KW   Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW   GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW   Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658};
KW   Reference proteome {ECO:0000313|Proteomes:UP000257200};
KW   Synapse {ECO:0000256|ARBA:ARBA00023018}.
FT   DOMAIN          50..243
FT                   /note="DH"
FT                   /evidence="ECO:0000259|PROSITE:PS50010"
FT   DOMAIN          260..418
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          443..572
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          606..806
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
SQ   SEQUENCE   820 AA;  94247 MW;  9BDA5996EF0AF1BF CRC64;
     MEEEEEEALC YLDRVLEEDE EVFDYGDGEL EPITPIHRQF KGDIEKGLEM KKLVLSGFLA
     SEEIYINQLE ALLLPMRPLK ATATTSQPVL TIQQIETIFY KIQDIFEIHK EFYDALLPSI
     QQWDEKVTVG HLFQKLASQL GVYKAFVDNY KVALETAEKC SQANIQFQKI SENLKVKGPK
     DSKECTTSTS MEALLYKPID RVTRSTLVLH DLLKHTPKDH PDFPLLQDAL RISQNFLSSI
     NEEIDPRRTA VTTPKGEARQ LVKDGFLVEV SESSRKLRHV FLFTDLLLCA KMKKTAVGRH
     QQYECKWYIP LADLTFQTLD DSDSCPSIQV LPEHEIEEMK IKISVLKSEI QKEKKAPKGQ
     SRVERLRKKM NEQESWLLLH SPTIPFRIHN KHGKSYLFLL SSDYERSEWR ESIQKLQKKD
     LQACVLSSVE LQVLTSSCFK LRTVHNIPVT SNKDDEETPG LYGFLHVIVH SAKGFKESAN
     LYCTLEVDSY GYFVSKAKTR VFRDTTEPQW NEEFEIELEG SQYLRILCYE KCYDKSMLNK
     DDNEIVDKIM GKGQVQLDPQ TVQSKNWHMD VIEMNGIKVE FSMKFTSRDL SLKRTPSKKQ
     SGVFGVKINV VTKRERSKVP YIVRQCIEEV EKRGIDEVGI YRISGVATDI QALKLAFDTN
     TKDILVMLSD MDINAIAGTL KLYFRELPEP LLTDRLYPAF MEGIALSDPA AKENCMMHLL
     RSLPDPNLMT FLTLLEHLKR VADKEPINKM SLHNLATVFG PTLLRPSESE STKGQHITSA
     SDIWSHDVMA QVQVLLYYLQ HPPISFAELK RNTLYFSTDV
//
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