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Database: UniProt
Entry: A0A2K6UNG0_SAIBB
LinkDB: A0A2K6UNG0_SAIBB
Original site: A0A2K6UNG0_SAIBB 
ID   A0A2K6UNG0_SAIBB        Unreviewed;      1014 AA.
AC   A0A2K6UNG0;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=DAB2 interacting protein {ECO:0000313|Ensembl:ENSSBOP00000033392.1};
GN   Name=DAB2IP {ECO:0000313|Ensembl:ENSSBOP00000033392.1};
OS   Saimiri boliviensis boliviensis (Bolivian squirrel monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC   Saimiriinae; Saimiri.
OX   NCBI_TaxID=39432 {ECO:0000313|Ensembl:ENSSBOP00000033392.1, ECO:0000313|Proteomes:UP000233220};
RN   [1] {ECO:0000313|Ensembl:ENSSBOP00000033392.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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DR   AlphaFoldDB; A0A2K6UNG0; -.
DR   Ensembl; ENSSBOT00000050306.1; ENSSBOP00000033392.1; ENSSBOG00000032859.1.
DR   GeneTree; ENSGT00940000155853; -.
DR   Proteomes; UP000233220; 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   GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233220}.
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          529..554
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          567..596
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          654..677
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          697..719
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          749..852
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          869..889
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        567..589
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        654..669
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        703..719
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        751..769
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        770..786
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        788..811
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        818..832
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        873..889
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1014 AA;  111856 MW;  D49DD7981FDE4CD5 CRC64;
     MPRLKESRSH ESLLSPSSAV EALDLSMEEE VVIKPVHSSI LGQDYCFEVT TSSGSKCFSC
     RSAAERDKWM ENLRRAVHPN KDNSRRVEHI LKLWVIEAKD LPAKKKYLCE LCLDDVLYAR
     TTGKLKTDNV FWGEHFEFHN LPPLRTVTVH LYRETDKKKK KERNSYLGLV SLPAASVAGR
     QFVEKWYPVV TPNPKGGKGP GPMIRIKARY QTITILPMEM YKEFAEHITN HYLGLCAALE
     PILSAKTKEE MASALVHILQ STGKVKDFLT DLMMSEVDRC GDNEHLIFRE NTLATKAIEE
     YLKLVGQKYL QDALGEFIKA LYESDENCEV DPSKCSAADL PEHQGNLKMC CELAFCKIIN
     SYCVFPRELK EVFASWRQEC SSRGRPDISE RLISASLFLR FLCPAIMSPS LFNLLQEYPD
     DRTARTLTLI AKVTQNLANF AKFGSKEEYM SFMNQFLEHE WTNMQRFLLE ISNPETLSNT
     AGFEGYIDLG RELSSLHSLL WEAVSQLEQS IVSKLGPLPR ILRDVHTALS TPGSGQLPGT
     NDLASTPGSG SSSISAGLQK MVIENDLSGS SGVQPSPARS SSYSEANEPD LQMANGGKSL
     SMVDLQDARA LDGEAGSPAG PDVLPTDGQA PAAQLVAGWP ARATPVSLTG LATVRRAGQT
     PTTPGTSEGA PGRPQLLAPL SFQNPVYQMA AGLPLSPRGL GDSGSEGHSS LSSHSNSEEL
     AAAAKLGSFS TAAEELARRP GELARRQMSL TEKGGQPTMP RQNSAGPQRR IDQPPPPPPP
     PHTLKTGRTP PNLLSTLQYP RPSSGTLASA SPDWAGPSAR LRQQSSSSKG DSPELKPRAV
     HKQGPSPVSP NALDRTAAWL LTMNAQLLED EGLGPDPPHR DRLRSKDELS QAEKDLAVLQ
     DKLRISTKKL EEYETLFKCQ EETTQKLVLE YQARLEEGEE RLRRQQEDKD IQMKGIISRL
     MSVEEELKKD HAEMQAAVDS KQKIIDAQEK RIASLDAANA RLMSALTQLK ESMH
//
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