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Database: UniProt
Entry: A0A2Y9NXW8_DELLE
LinkDB: A0A2Y9NXW8_DELLE
Original site: A0A2Y9NXW8_DELLE 
ID   A0A2Y9NXW8_DELLE        Unreviewed;      1164 AA.
AC   A0A2Y9NXW8;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Disabled homolog 2-interacting protein isoform X6 {ECO:0000313|RefSeq:XP_022434533.1};
GN   Name=DAB2IP {ECO:0000313|RefSeq:XP_022434533.1};
OS   Delphinapterus leucas (Beluga whale).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Monodontidae; Delphinapterus.
OX   NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022434533.1};
RN   [1] {ECO:0000313|RefSeq:XP_022434533.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_022434533.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   RefSeq; XP_022434533.1; XM_022578825.2.
DR   AlphaFoldDB; A0A2Y9NXW8; -.
DR   Proteomes; UP000248483; 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; SM00233; PH; 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:UP000248483}.
FT   DOMAIN          172..206
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          197..315
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          375..566
FT                   /note="Ras-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50018"
FT   REGION          1..68
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          660..683
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          718..745
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          806..826
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          846..868
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          898..1004
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1018..1038
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        49..65
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        718..738
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        852..868
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        919..938
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        940..959
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1022..1038
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1164 AA;  128291 MW;  042E99AF9478C3A8 CRC64;
     MSAGGARKST GRPSYYYRLL RRPRLQRQRS RSRSRTRPAR ESPQERPGSR RSLPGSLSEK
     SPSMEASAAT PFRVTGFLSR RLKGSIKRTK SQPKLDRNHS FRHILPGFRS AAAAASSASA
     ADNERSHLMP RLKESRSHES LLSPSSAVEA LDLSMEEEVV IKPVHSSILG QDYCFEVTTS
     SGSKCFSCRS AAERDKWMEN LRRAVHPNKD NSRRVEHILK LWVIEAKDLP AKKKYLCELC
     LDDVLYARTT GKLKTDNVFW GEHFEFHNLP PLRTVTVHLY RETDKKKKKE RNSYLGLVSL
     PAASVAGRQF VEKWYPVVTP NPKSGKGPGP MIRIKARYQT ITILPMEMYK EFAEHITNHY
     LGLCAALEPI LSAKTKEEMA SALVHILQST GKVKDFLTDL MMSEVDRCGD EHLIFRENTL
     ATKAIEEYLK LVGQKYLQDA LGEFIKALYE SDENCEVDPS KCSAADLPEH QGNLKMCCEL
     AFCKIINSYC VFPRELKEVF ASWRQECSNR GRPDISERLI SASLFLRFLC PAIMSPSLFN
     LLQEYPDDRT ARTLTLIAKV TQNLANFAKF GSKEEYMSFM NQFLEHEWTS MQRFLLEISN
     PETVSNTAGF EGYIDLGREL SSLHSLLWEA VSQLEQSIVS KLGPLPRILR DVHTALSAPG
     SGQLAGTSDL ASPPGSGSSS VSAGLQKVAI ENDVSGLIDF TRLPSPTPEN KDLFFVTRSS
     GVQPSPARSS SYSEANEPDL QMANGGKSLS MVDLQDARTL DGEAGSPAGP DALAVDGQAP
     AVQLVAGWPA RVAPVSLAGL ATVRRAGQTP STAGTSEGAP GRPQLLAPLS FQNPVYQMAA
     GLPLSPRGLG DSGSEGHSSL SSHSNSEDLA AAAKLGSFSS TAEELGRRPG ELARRQVSLT
     EKGGQPPGPR QNSAGPQRRI DQPPPPPPPP PPAPRGRTPP TLLSTLQYPR PSSGTLASAS
     PDWAGPGARL RQQSSSSKGD SPELKPRAVH KQGPSPVSPN ALDRTAAWLL TMNAQLLEDE
     GLGPDPPHRD RLRSKEELSQ AEKQDLAVLQ DKLRISTKKL EEYETLFKCQ EETTQKLVLE
     YQARLEEGEE RLRRQQEDKD IQMKGIISRL MSVEEELKKD HAEMQAAVDS KQKIIDAQEK
     RIASLDAANA RLMSALTQLK ESMH
//
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