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Database: UniProt
Entry: A0A3B4D314_PYGNA
LinkDB: A0A3B4D314_PYGNA
Original site: A0A3B4D314_PYGNA 
ID   A0A3B4D314_PYGNA        Unreviewed;      1051 AA.
AC   A0A3B4D314;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Disabled homolog 2-interacting protein-like {ECO:0000313|Ensembl:ENSPNAP00000017935.1};
GN   Name=DAB2IP {ECO:0000313|Ensembl:ENSPNAP00000017935.1};
OS   Pygocentrus nattereri (Red-bellied piranha).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC   Characoidei; Pygocentrus.
OX   NCBI_TaxID=42514 {ECO:0000313|Ensembl:ENSPNAP00000017935.1, ECO:0000313|Proteomes:UP000261440};
RN   [1] {ECO:0000313|Ensembl:ENSPNAP00000017935.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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DR   AlphaFoldDB; A0A3B4D314; -.
DR   Ensembl; ENSPNAT00000038753.1; ENSPNAP00000017935.1; ENSPNAG00000024529.1.
DR   GeneTree; ENSGT00940000155853; -.
DR   Proteomes; UP000261440; Unplaced.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   CDD; cd04013; C2_SynGAP_like; 1.
DR   CDD; cd05136; RasGAP_DAB2IP; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR021887; DAB2P_C.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR039360; Ras_GTPase.
DR   InterPro; IPR023152; RasGAP_CS.
DR   InterPro; IPR001936; RasGAP_dom.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   PANTHER; PTHR10194:SF26; DISABLED HOMOLOG 2-INTERACTING PROTEIN; 1.
DR   PANTHER; PTHR10194; RAS GTPASE-ACTIVATING PROTEINS; 1.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF12004; DAB2P_C; 1.
DR   Pfam; PF00616; RasGAP; 2.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00323; RasGAP; 1.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR   SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS00509; RAS_GTPASE_ACTIV_1; 1.
DR   PROSITE; PS50018; RAS_GTPASE_ACTIV_2; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   GTPase activation {ECO:0000256|ARBA:ARBA00022468}.
FT   DOMAIN          1..78
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          69..187
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          247..439
FT                   /note="Ras-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50018"
FT   REGION          597..691
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          707..860
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1025..1051
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          897..963
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          993..1020
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        597..656
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        668..685
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        719..739
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        740..755
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        757..782
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        796..852
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1051 AA;  117642 MW;  9C0A8AB5EB3FD556 CRC64;
     MPRLKESRSH ESLLSPSSAV EALDLSMEEE VLIKPVHSSI LGQDFCFEVT TSTGSKCFSC
     RSAAEREKWM ENLRRAVHPN KDNSRRVENM LKCWIIEAKD LPAKKKYFCE LCLDDTLYAR
     TTCKLKTDNV FWGEHFEFNN LPSVKSITVH LYKETDKKKK KDKNNYIGLV NVPIVAVTGR
     QFVEKWYTVS TPNPNKGKTP GPMVRMKCRY QSMSILPMEL YKEFAEYITN NYMLLCSILE
     PALSVKSKEE MACALVHILQ STGKAKDFLT DLMMSEVDRC GDNEHLIFRE NTLATKAIEE
     YLKLVGQKYL QDALGEFIKA LYESDENCEV DPSKCSSSDL PEHQGNLKMC CELAFCKIIN
     SYCVFPRELK EVFASWRQEC GNRGRPDISE RLISASLFLR FLCPAIMSPS LFDLMQEYPD
     DRTARTLTLI AKVTQNLANF TKFGSKEEYM SFMNQFLEHE WTNMQRFLLE ISNPETISNT
     AGFEGYIDLG RELSTLHSLL SEAVTQLDQS TAAKLGPLVR ILRDVNMALT NPTGVPVASP
     TERVGSPSLP SCSVSTGLQK LVMDTELTGL VDFTRLPSPT PENKDLFFVT RNSVIQPSPA
     RSSSYSEANE PDIQLPNGSK SLSMVDLQDS RSLESGPCTS SSDPANDLQG SGAWNAPTLK
     GNMAAGPTLR KTGQTPTTPS TETAPGRPQL LAPLSFQNPV YQMAAGLPVS PRGGGTADSG
     SECHSSISSQ GNVEDSATTG AKHHSSDEFV RRSGEFTRRQ LSLTETQHQA NVPRQNSAGP
     QRRIDQPPPP TITRGRTPPS MLNTAPYPRP SSGSMMSSSP DWPSGGARLR QQSSSSKGDS
     PETKQRTLHK QAPSPVNPGA LDRTAAWLLN MNVQYLEQEG IDPDSRHRED LPNKDELTQT
     EKEIAMLQER LRLSAKKLEE YEVRLQGQDE QTQKMLLEYQ ARLEDAEDRL RRQQEDKELQ
     MKSIITRLMS VEEELKKDHA DMQAIVDSKQ KIIEAQEKRI ASLDAANARL MSALSQLKER
     YSMQTRNGIS PTNPSKLQIT ENGEFRNSSN C
//
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