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Database: UniProt
Entry: A0A3B4UZS2_SERDU
LinkDB: A0A3B4UZS2_SERDU
Original site: A0A3B4UZS2_SERDU 
ID   A0A3B4UZS2_SERDU        Unreviewed;      1302 AA.
AC   A0A3B4UZS2;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=RAS protein activator like 2 {ECO:0000313|Ensembl:ENSSDUP00000023792.1};
GN   Name=RASAL2 {ECO:0000313|Ensembl:ENSSDUP00000023792.1};
OS   Seriola dumerili (Greater amberjack) (Caranx dumerili).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Carangiformes; Carangidae; Seriola.
OX   NCBI_TaxID=41447 {ECO:0000313|Ensembl:ENSSDUP00000023792.1, ECO:0000313|Proteomes:UP000261420};
RN   [1] {ECO:0000313|Ensembl:ENSSDUP00000023792.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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DR   STRING; 41447.ENSSDUP00000023792; -.
DR   Ensembl; ENSSDUT00000024236.1; ENSSDUP00000023792.1; ENSSDUG00000017264.1.
DR   GeneTree; ENSGT00940000157702; -.
DR   Proteomes; UP000261420; 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   CDD; cd22265; UDM1_RNF168; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 1.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR021887; DAB2P_C.
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:SF52; RAS GTPASE-ACTIVATING PROTEIN NGAP; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   GTPase activation {ECO:0000256|ARBA:ARBA00022468}.
FT   DOMAIN          32..281
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          272..390
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          450..643
FT                   /note="Ras-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50018"
FT   REGION          85..154
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          175..218
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          843..1017
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1039..1102
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1127..1147
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1282..1302
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1155..1214
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        95..113
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        135..154
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        195..209
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        906..1004
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1055..1102
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1128..1147
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1302 AA;  145271 MW;  DB809F65C8E5BA29 CRC64;
     METDSVAGDV ESLHGGLSLL DPLVDRILVD TVSQQQGWLR VYDVKGPPAH RFSCGQSPYT
     DSGAWERKYC ILTDTQLILL HKDDEAAGDA QESPTDSAKG RSLRRTVSVP SEGQFPEFQA
     EGATMLEVSS ERSPRRRSIS GLGSSEKSVA IDNPNSSPFK VPGFFSKRLK GSIKRTKSQT
     KLDRNTSFRL PSLRPAEPDR SRGLPKLKES SSHESLLSPG SAVEALDLSM EEDVFIKPLH
     SSILGQEFCF EVTYSGGSKC FSCTSASERD KWMENLRRTI QPNKDNCRRA ENLLRLWIIE
     AKDLPPKKKY FCELCLDDVL YARTTSKTRH DSLFWGEYFD FSSLPAVHSV TVHIYRDVDK
     KKKKDKNNYV GLVNIPVSGV TGRQFVEKWY PVSTPTTSKA KGGGPSIRIK SRFQTISILP
     MEQYKEFAEF ITNNYTMLCS VLEPVISVKN KEEMACALVH ILQSTGRAKD FLTDLVMSEV
     DRCADHDVLI FRENTLATKA IEEYLKLVGQ KYLHDALGEF IKALYESDEN CEVDPSRCPS
     GDLSEHQSNL KMCCELAFCK IINSYCVFPR ELKEVFASWK QQCVVRGHQQ DISKRLISAS
     LFLRFLCPAI MSPSLFNLMQ EYPDDRTSRT LTLIAKVIQN LANFTKFGNK EEYMAFMNDF
     LEHEWAGMMR FLSEISNQET LSNTPGFEGY IDLGRELSVL HALLWEVVSQ LDKGENSFLQ
     ATVAKLGPLP RILGDISRSL AAPTPVQQQL RRFQDHSSAH NISGSLSSGL QRIFEDPVDS
     HCEVRSLQSP GGDRMEGYVR GQRPLLAHQH PSVHSSFSDQ EERDNLLPNG RSISLVDLQD
     AQSLHGPAAP PPHHEAPPRL SRVGSQASIG QGPPPLNYPH SNPLTPQPHQ MKAPPRDGQP
     QSAPQVRRPL HPSLSQQRSL QPLSFQNPVY HLSNPTHSLS TRSAHSLRQD SSSENLSTES
     SHNSHSNSDD YGSQVGVKGR VASNSSLDEL GSRRSTQSEE CSTPRRNVPP DLPPGVATAV
     AIPRQSTTAG TAHIVKVEQQ SRGGAGARAP RSLPHSASLR SSSSANTEPT PTSGHTNRQQ
     STCSVENMAP PPRSATKQPQ QVASPVEAVA VALSPVERTA AWVLNNGQYE EKEEEGGGDR
     SREEGRNTEK YELEISRLKE RLRVSGRRLE EYERRLLAQE QQMQKLLLEY KNRLEDSEER
     LRRQQEEKDS QMKSIICRLM AVEEELKRDH AEMQAVIEAK QKIIDAQEKR IGSLDAANSR
     LMAALTQVKE RYSAPNLCNG LSPSNPTKLS ITENGEFKNS SC
//
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