ID F6XFM6_XENTR Unreviewed; 1821 AA.
AC F6XFM6;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 4.
DT 27-MAR-2024, entry version 74.
DE SubName: Full=Dedicator of cytokinesis 2 {ECO:0000313|Ensembl:ENSXETP00000043109};
GN Name=dock2 {ECO:0000313|Ensembl:ENSXETP00000043109};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364 {ECO:0000313|Ensembl:ENSXETP00000043109};
RN [1] {ECO:0000313|Ensembl:ENSXETP00000043109}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nigerian {ECO:0000313|Ensembl:ENSXETP00000043109};
RX PubMed=20431018; DOI=10.1126/science.1183670;
RA Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L.,
RA Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R.,
RA Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J.,
RA Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H.,
RA Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K.,
RA Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A.,
RA Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T.,
RA Khokha M.K., Richardson P.M., Rokhsar D.S.;
RT "The genome of the Western clawed frog Xenopus tropicalis.";
RL Science 328:633-636(2010).
RN [2] {ECO:0000313|Ensembl:ENSXETP00000043109}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUN-2011) to UniProtKB.
CC -!- SIMILARITY: Belongs to the DOCK family. {ECO:0000256|PROSITE-
CC ProRule:PRU00983}.
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DR Ensembl; ENSXETT00000043109; ENSXETP00000043109; ENSXETG00000019922.
DR AGR; Xenbase:XB-GENE-990617; -.
DR Xenbase; XB-GENE-990617; dock2.
DR eggNOG; KOG1998; Eukaryota.
DR HOGENOM; CLU_000595_2_1_1; -.
DR TreeFam; TF300423; -.
DR Bgee; ENSXETG00000019922; Expressed in liver.
DR ExpressionAtlas; F6XFM6; baseline.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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 Gene3D; 1.20.58.740; -; 1.
DR Gene3D; 1.25.40.410; -; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 1.20.1270.350; Dedicator of cytokinesis N-terminal subdomain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
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; IPR032376; DOCK_N.
DR InterPro; IPR042455; DOCK_N_sub1.
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; PTHR45653; DEDICATOR OF CYTOKINESIS; 1.
DR PANTHER; PTHR45653:SF6; DEDICATOR OF CYTOKINESIS PROTEIN 2; 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 Pfam; PF16172; DOCK_N; 1.
DR PROSITE; PS51650; C2_DOCK; 1.
DR PROSITE; PS51651; DOCKER; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT DOMAIN 411..592
FT /note="C2 DOCK-type"
FT /evidence="ECO:0000259|PROSITE:PS51650"
FT DOMAIN 1196..1607
FT /note="DOCKER"
FT /evidence="ECO:0000259|PROSITE:PS51651"
FT REGION 1653..1729
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1752..1782
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1662..1676
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1752..1779
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1821 AA; 211060 MW; 5AE84FF336D95964 CRC64;
MRHLTALFYV PPAICNFKSN GVPQISLQIG DVVHIQESCE GKGKPGIFPK SFIHIKDVTV
QRKRNMENIV PAEIPLVREV TTTLREWGNI WKQLYAVRSK TEKFKQVQSM MYDLMEWRSQ
LLSGTLPKDE LKELKQKVTS KIDYGNKILE LDLIVRDEDG NILDPDKTSV ISLFHAHNEA
TEKITERIKE EMAQNEYTLH GRITSSPTHG LYVFVRNFVC RIGEDAELFM SLYDPLKQTI
ISENYLVRWG SKGFPKEIDM LNNLKVVFTD LGNKDLNREK IYLVCQIVRI GRMDLKDSNL
KKYTQGLRRP FGVAVMDITD VIKGKIESDE EKQHFIPFHP VVAENDFLHS LLTKVTSSKG
DSGGQGLWVT VKMLVGDSVQ IRKDYPHLVD RTTVVARKLG FPEIIMPGDV RNDIYVTLLQ
GDFDRATQRN VEVIMCVCDE EGKIIPNAIC SGAGDKPVSE YRSVLYYQIK QPRWMETIKV
AVPIEEMQRI HLRFMFRHRS SQESKDKGER NFAMAFVRLM KEDGTTLHDG NHDLVVLKGD
SKKMEDGSTY LHFPFTRQQM DNKGSTFSRN SSSSGGLSVS SRDAFSISTL VCSTKLTQNV
GLLGLLKWRT KPEHLQENLE KLKIVDGEEV VKFLQDTLDA LFNIMMENSQ TEKYDILVFD
ALIYIIGLIA DRKFQHFNTV LEAYIKQHFS ATLAYKKLMC VLKKYLDISS RGEQCEPILR
TLKALEYVFK FIVRSRTLFS QLYEGKEQNE FEESMRNLFE SINNLMECEH KTTILLQVAA
LKYLPSVLHD VETVFDARLL SQLLYEFYTC IPPVKLQQQK VQSMIEIVRS NLFKKQECRD
ILLPMITKEL KDWLEQGRQD ASHGKEKKFC VDLLNNILEV LSCQDEASTY HHIQEITIQL
LRTVIRTVIM LDREQDLTSH FVACMTAILN QMTNQHYTVY IETFKSNYDL VDFLMETFIM
FKDLIGKNVY PCDWITMSMV QNRVFLRAIN KFAETMNQKF LENMNFEVQL WNNYFHLAVA
FITQDSLQLE NFSHDKRNEI LNKYGDMRCL IGFAIRDMWY KLGQNKICFI PGMVGPILEM
TLIPEVELRR STIPIFFDMM LCEYHHSGDF RKFENEIILK LDHEVEGGRG DWQYMQLFEA
ILLDYSINHS YIFKAIETFV ILIKGLLERL LDYRAVVTDE SKDNRMSCTV NLLNFYKDIN
REAMYIRYLY KLRDLHLDCE NYTEAAYTLL LHTRLLKWSD EQCSPQVMQT EFQSSQTYRH
LKETLYGVII GYFDKGKMWE EAIALCKQLA DQYEMEVFDY ELLSQCLTQQ AKFYENIMKI
LRPKPDYFAV GYYGQGFPTF LRNKVFIYRG KEYERREDFL AQLMAQFPFS EKLNTTSSPG
EDITNSPGQY IQCFTVQPVL EEQTRFKNKP VPDQILNFYK SNYVQRFHYS KPVRKGSIDP
ENEFASMWIE RTTFFTAYRL PGILRWFEVT SMSHATISPL ENAIETMSAT NEKILMLINQ
YQSDENLPIN PLSMCLNGIV DPAVMGGFAK YEKAFFTDEY IQEHPEDNEK LNRLKDLIAW
QTPLLGAGIR IHEKRVTDDL RPFHDRMEEC FKSLKIKVEK QYGVRELPDF DDGRVGRPRS
MLRSYRQMSI ISMSSVGSDC FTPVKPANES FELDVPVPKA KHQETETNSS QGTAEPEVKL
RRSKKKNKRS SVVFTEEISG PESSLSKRLS RKHEFMSDTN LSEHTVNQQA PSVLKQMSFA
SRSMPTIPAL TLSVANGPSS EEQSPSQKMS QQNLFSTGEG DKRTLKKNKV NQFFRTMVNT
PKMSAAGNDE SFSMDLATAP V
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