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Database: UniProt
Entry: A0A3Q1H2X1_9TELE
LinkDB: A0A3Q1H2X1_9TELE
Original site: A0A3Q1H2X1_9TELE 
ID   A0A3Q1H2X1_9TELE        Unreviewed;      1603 AA.
AC   A0A3Q1H2X1;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=Dedicator of cytokinesis protein 4-like {ECO:0000313|Ensembl:ENSAPOP00000034097.1};
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:ENSAPOP00000034097.1, ECO:0000313|Proteomes:UP000257200};
RN   [1] {ECO:0000313|Ensembl:ENSAPOP00000034097.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the DOCK family. {ECO:0000256|PROSITE-
CC       ProRule:PRU00983}.
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DR   STRING; 80966.ENSAPOP00000019607; -.
DR   Ensembl; ENSAPOT00000029529.1; ENSAPOP00000019607.1; ENSAPOG00000023197.1.
DR   Ensembl; ENSAPOT00000029570.1; ENSAPOP00000034097.1; ENSAPOG00000023197.1.
DR   Ensembl; ENSAPOT00000029625.1; ENSAPOP00000019676.1; ENSAPOG00000023197.1.
DR   Ensembl; ENSAPOT00000029679.1; ENSAPOP00000034153.1; ENSAPOG00000023197.1.
DR   GeneTree; ENSGT00940000155659; -.
DR   OrthoDB; 8258at2759; -.
DR   Proteomes; UP000257200; Unplaced.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:InterPro.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   CDD; cd08695; C2_Dock-B; 1.
DR   CDD; cd11705; DHR2_DOCK4; 1.
DR   Gene3D; 1.20.58.740; -; 1.
DR   Gene3D; 1.25.40.410; -; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 1.
DR   InterPro; IPR037811; C2_Dock-B.
DR   InterPro; IPR027007; C2_DOCK-type_domain.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR037014; DHR2_DOCK4.
DR   InterPro; IPR026791; DOCK.
DR   InterPro; IPR043161; DOCK_C_lobe_A.
DR   InterPro; IPR043162; DOCK_C_lobe_C.
DR   InterPro; IPR027357; DOCKER_dom.
DR   InterPro; IPR046770; DOCKER_Lobe_B.
DR   InterPro; IPR046773; DOCKER_Lobe_C.
DR   PANTHER; PTHR45653; DEDICATOR OF CYTOKINESIS; 1.
DR   PANTHER; PTHR45653:SF7; DEDICATOR OF CYTOKINESIS PROTEIN 4; 1.
DR   Pfam; PF20422; DHR-2_Lobe_B; 1.
DR   Pfam; PF20421; DHR-2_Lobe_C; 1.
DR   Pfam; PF14429; DOCK-C2; 1.
DR   PROSITE; PS51650; C2_DOCK; 1.
DR   PROSITE; PS51651; DOCKER; 1.
PE   3: Inferred from homology;
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000257200}.
FT   DOMAIN          26..198
FT                   /note="C2 DOCK-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51650"
FT   DOMAIN          826..1232
FT                   /note="DOCKER"
FT                   /evidence="ECO:0000259|PROSITE:PS51651"
FT   REGION          1239..1603
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1239..1253
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1269..1332
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1335..1349
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1392..1408
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1433..1496
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1553..1572
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1603 AA;  183189 MW;  B614A3E95C4EDD60 CRC64;
     MVLFTRGVSI TRKLGFSDVI MPGEMRNDLY ITLEKGEFEK GGKSVARNVE ITVYVLDIDG
     QVLKSHVAAG SGEPGGDEYH SLVLYHNNSP RWAEQIKLPI PVDMFRGSHV RFEFRHCSTK
     DKGEKKLFGY SFVPLMQEDG RTLPDGTHEL IIHKCEENTS LADCSRYLKQ PFSKANLPSN
     NQTLKGTKES FWITSFLCST KLTQNGDMLD LLKWRAHPER INDSLSKLKE IDGSEIVKFL
     QDTLDTLFGI LDESSQRYGL KVFDSLVHII NLLQDSKFQH FKPVMDTYIE SHFAGALSYR
     DLIKVLKWYV DRIVDAEHQD HIQQVLKASE YIFKYIIQSR RLFSLATGGQ NEEEFRVCIH
     ELFMSIRFFL SQENKGTSPV AQTQAVFLRT FPAIYGELLK IFTVREVAGF VRETLGSLPT
     TVHADCPLEA IKLQCIAKTV ESQLYINPES RCILLPVVLR VLQAHMQEQR DLVMCARILT
     SMLSLIKKEE NGSAEPVVSE EVELIVESLL GVLLRTILEI SNRPQPAGPA MRLQFQDVTG
     EFVACLLALL RQMSDRHYQQ LLQAFSSKDD LRDFLLHIFT VFRILIRPEM FPKDWTVMRL
     VTNNVIITTV LYLSDALRKN FLNDKFDYKV WDSYFYLSVI FINQPCLQLE SFSPSKRKKI
     LEKYGDMRVM MGCEIFSMWQ NLGEHKLNFI PAMIGPFLEV TLVPQPDLRN VMIPIFHDMM
     DWEQRRSGNF KQVEAKLIDK LDSLMSEGKG DETYRELFNS IIPLFGPYPS LLKKIERETW
     RESGISLIAT VTRLMERLLD YRDCMKLGEV DGKKIGCTVS LLNFYKTELN KEEMYIRYIH
     KLYDLHLKAQ NYTEASYTLL LYDELLEWSD RPLREFLNYP MQSEWQRKEY LHLTIVQNFD
     RGKCWENGII LCRELADQYE SYYDYRNLSK MRMMEASLYD KIMDQQRLEP EFFRVGFYGK
     KFPFFLRNKE FVCRGHDYER LEAFQQRMLN EFPHAIAMQH VNQPDQTIYQ ADAQYLQIYA
     VTPIPESQDV LQRDGVPDNI KSFYKFNHIW RFRYDRPFHK GTKDKENEFK SLWVERTTLT
     LVQSLPGISR WFEVEKRELV EVSPLENAIE VIENKNLQLR TLITQCQSRQ MQNINPLTMC
     LNGVIDAAVN GGLARYQEAF FVKDYIMNHP EDGEKIGRLR ELMFEQAHIL EYGLAVHEKF
     VPQDMRPLHK KLVDQFHLMK SSLGIQEFPA YVRASPVHFT NGSPRTCRNS VPSIISPDGG
     RGVTRRSYPA VNRYSSSSLS SQASNEVSNI TGQSESSDEV FNMQPSPSTS SLSSNHSASP
     NVTSSAPSSA RGSPQMAEKH KHSRENACLS PRERPVSAIF PNPLDPAQRA PAHQIGDTTL
     PRSDPNLSAP DKVRPTPSSW SLDSVKEGAP SFSDSVGKLL CPPVPPRPPY SGSSAKNMRS
     QSPVPTSRSP QKTTVPPFTP SPTECQSASL VSNSPVLSGS YSSGISSLSR CSVSEASGTE
     LPAGDHPPHT LPPPTTLPNS ISSSSDEPIR RENKTPPPYS VYERNNPRRP VPLPHSLSIP
     PQTDPPALPP KPHQLRTGSM KLDGTADPRV PRPRPLPRKV SQL
//
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