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Database: UniProt
Entry: A0A3L8SPR2_CHLGU
LinkDB: A0A3L8SPR2_CHLGU
Original site: A0A3L8SPR2_CHLGU 
ID   A0A3L8SPR2_CHLGU        Unreviewed;      1542 AA.
AC   A0A3L8SPR2;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   13-SEP-2023, entry version 20.
DE   RecName: Full=C2 DOCK-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=DV515_00004668 {ECO:0000313|EMBL:RLW06004.1};
OS   Chloebia gouldiae (Gouldian finch) (Erythrura gouldiae).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Passeridae;
OC   Chloebia.
OX   NCBI_TaxID=44316 {ECO:0000313|EMBL:RLW06004.1, ECO:0000313|Proteomes:UP000276834};
RN   [1] {ECO:0000313|EMBL:RLW06004.1, ECO:0000313|Proteomes:UP000276834}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Red01 {ECO:0000313|EMBL:RLW06004.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:RLW06004.1};
RX   PubMed=30282656;
RA   Toomey M.B., Marques C.I., Andrade P., Araujo P.M., Sabatino S.,
RA   Gazda M.A., Afonso S., Lopes R.J., Corbo J.C., Carneiro M.;
RT   "A non-coding region near Follistatin controls head colour polymorphism in
RT   the Gouldian finch.";
RL   Proc. R. Soc. B 285:0-0(2018).
CC   -!- SIMILARITY: Belongs to the DOCK family. {ECO:0000256|PROSITE-
CC       ProRule:PRU00983}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RLW06004.1}.
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DR   EMBL; QUSF01000010; RLW06004.1; -; Genomic_DNA.
DR   STRING; 44316.ENSEGOP00005019554; -.
DR   Proteomes; UP000276834; Unassembled WGS sequence.
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; cd08696; C2_Dock-C; 1.
DR   CDD; cd11703; DHR2_DOCK7; 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; IPR037808; C2_Dock-C.
DR   InterPro; IPR027007; C2_DOCK-type_domain.
DR   InterPro; IPR035892; C2_domain_sf.
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; IPR046769; DOCKER_Lobe_A.
DR   InterPro; IPR046770; DOCKER_Lobe_B.
DR   InterPro; IPR046773; DOCKER_Lobe_C.
DR   PANTHER; PTHR23317; DEDICATOR OF CYTOKINESIS DOCK; 1.
DR   PANTHER; PTHR23317:SF78; DEDICATOR OF CYTOKINESIS PROTEIN 7; 1.
DR   Pfam; PF06920; DHR-2_Lobe_A; 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   Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000276834}.
FT   DOMAIN          5..171
FT                   /note="C2 DOCK-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51650"
FT   DOMAIN          1082..1516
FT                   /note="DOCKER"
FT                   /evidence="ECO:0000259|PROSITE:PS51651"
FT   REGION          335..362
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        335..358
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1542 AA;  174795 MW;  A889A594C7A2676C CRC64;
     MVRPRNLLYV YPQSLNFANR QGSARNITVK VQFMYGEDPS NAMPVIFGKS SCPEFSKEAY
     TAVVYHNRSP DFHEEIKIKL PATLTDHHHL LFTFYHVSCQ QKQNTPLETP VGYTWIPMLQ
     NGRLKTGQFC LPVSLEKPPQ AYSVLSPEVP LPGMKWVDNH KGVFNVEVVA VSSLHTQDPY
     LDKFFALVHA LDEHMFPVRI GDMRIMENNL ENELKSSISA LNSSQLEPVV RFLHLLLDKL
     ILLVVRPPVI AGQIVNLGQA SFEAMASIIN RLHKNLDGNQ DQHGRNSLLA SYIYYVFRLP
     NTYPNSPSPG PGGLGGSVHY ATMARSAVRP ASLNLNRSRS LSNSNPDISG TPTSPDDEVR
     SIIGTKATDR SCNRMSSHTE TSSFLQTLTG RLPTKKLFHE ELALQWVVCS GSVREAALQQ
     AWFFFELMVK SMVHHLYFAD KLDAARKNRF PERFMDDVSA LVSTIAGDIV SRFQKDTEMV
     ERLNTSLAFF LNDLLSIMDR GFVFTLIKTC YKQVSSKVYT LTNPSNLASL KLDFLRIICS
     HEHYVTLNLP CSLLTPPASP SPSVSSATSQ SSGFSTNVQD QKIANMFELS VPFRQQHYLA
     GLVLTELAVI LDPDAEGLFG LHKKVINMVH NLLSSHDSDP RYADPQVKAR VAMLYLPLIG
     VIMETVPQLY DFTESHNQRG RPSCVTVDDY ESEGGSMINQ TVAMAIAGTS VPQLTRPSSF
     LLPSSSGRQH STFSTESSRS LLICLLWVLK NADEGVLQKW FTDLSVLQLN RLLDLLYLCV
     SCFEYKGKKV FERMNSLTFK KSKDMRAKLE EAILGSIGAR QEMVRRSRGQ LERSPSGSAF
     GSQENLRWRK DMTHWRQNTE KLDKSRAEIE HEALIDGNLA TEANLIILDT LEIVVQTVSV
     TESKESILGG VLKVLLHSMA CNQSALYLQH CFATQRALVS KFPELLFEEE TEQCADLCLR
     LLRHCSSSVN TIRSHASASL YLLMRQNFEI GNNFARVKMQ VTMSLSSLVG TSQNFNEEFL
     RRSLKTILTY AEEDLELRET TFPDQVQDLV FNLHMILSDT VKMKEHQEDP EMLIDLMYRI
     AKGYQNSPDL RLTWLQNMAG KHSERSNHAE SAQCLVHSAA LVAEYLSMLE DRKYLPVGCV
     TFQNISSNVL EESAVSDDVV SPDEEGICSG KYFTEAGLVG LLEQAAASFS MAGMYEAVNE
     VYKVLIPIHE ANRDAKKLST IHGKLQEAFS KIVHQDGKRM FGTYFRVGFY GTKFGDLDEQ
     EFVYKEPAIT KLAEISHRLE GFYGERFGED VLEVIKDSNP VDKCKLDPNK AYIQITYVEP
     YFDTYEMKDR ITYFDKNYNL RRFMYCTPFT LDGRAHGDLH EQFKRKTILT TSHAFPYIKT
     RINVIHKEEI ILTPIEVAIE DMQKKTQELA FATHQDPADP KMLQMVLQGS VGTTVNQGPL
     EVAQVFLAEI PNDPKLFRHH NKLRLCFKDF TKRCEDALRK NKSLIGPDQK EYQRELERNY
     HRLKEALQPL INRKIPQLYK AVLPVTCHRD SFSRMSLRKM EI
//
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