ID A0A0K3ATL6_CAEEL Unreviewed; 1505 AA.
AC A0A0K3ATL6;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=DH domain-containing protein {ECO:0000313|EMBL:CTQ86343.1};
GN ORFNames=CELE_Y105E8A.25 {ECO:0000313|EMBL:CTQ86343.1}, Y105E8A.25
GN {ECO:0000313|EMBL:CTQ86343.1, ECO:0000313|WormBase:Y105E8A.25a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000313|EMBL:CTQ86343.1, ECO:0000313|Proteomes:UP000001940};
RN [1] {ECO:0000313|EMBL:CTQ86343.1, ECO:0000313|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000313|EMBL:CTQ86343.1,
RC ECO:0000313|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RA Sulson J.E., Waterston R.;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR EMBL; BX284601; CTQ86343.1; -; Genomic_DNA.
DR RefSeq; NP_001300404.1; NM_001313475.1.
DR SMR; A0A0K3ATL6; -.
DR PeptideAtlas; A0A0K3ATL6; -.
DR EnsemblMetazoa; Y105E8A.25a.1; Y105E8A.25a.1; WBGene00013682.
DR GeneID; 3564893; -.
DR KEGG; cel:CELE_Y105E8A.25; -.
DR AGR; WB:WBGene00013682; -.
DR WormBase; Y105E8A.25a; CE50251; WBGene00013682; -.
DR OrthoDB; 2917157at2759; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00013682; Expressed in pharyngeal muscle cell (C elegans) and 4 other cell types or tissues.
DR ExpressionAtlas; A0A0K3ATL6; baseline and differential.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR Gene3D; 1.20.900.10; Dbl homology (DH) domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR041020; PH_16.
DR PANTHER; PTHR13944; AGAP007712-PA; 1.
DR PANTHER; PTHR13944:SF21; CYSTS, ISOFORM C; 1.
DR Pfam; PF17838; PH_16; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50010; DH_2; 1.
PE 1: Evidence at protein level;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Proteomics identification {ECO:0007829|EPD:A0A0K3ATL6,
KW ECO:0007829|PeptideAtlas:A0A0K3ATL6};
KW Reference proteome {ECO:0000313|Proteomes:UP000001940}.
FT DOMAIN 705..899
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 208..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 443..608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1199..1286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1435..1505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1384..1425
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 27..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..267
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..293
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..418
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..468
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..494
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 527..545
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..608
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1225..1277
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1435..1497
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1505 AA; 166485 MW; 19C9DB452109DFBF CRC64;
MNWDEEEASS LPPLPSSPPP EPVDPTRITF TLSNESSSPR YEFNNLVTSS SPSYFSYQPY
TSPGIYLLPD REQQPYFGAD FQTESSISWN SPTSPPPPPM IVEEEMRSGG GTARPVTPRS
IANSLDSLSE CAQHHHHHSD VVNANSNSDR SRSLGDLLAA TMQDGNDDSL RNGSYDTLVT
TTTKGGGLTD SGIGGGLLLM KGEDEMDIMD DHNSSSSPDH HRIPTDISSP DSFTYPPVSF
TSYDPVNGSG SVPSYSNENT NPLDSTPRGH SADDRKHSDL PAISEESEHE QQSIHIPYNH
YPPHSSSVGP GAAPAVREVV EHTYPMVHCN SAPSNTVFNS DRIAHRRVVS DDVTETTRLK
RSEELENMDK VGRISFEKRS ASTNHLSKSR KGATLVFHND PNEKDETDDE EEYEDAADGY
SKDNEMLILE KSGGEERYRM ASVKKKNGSP LRHFDNHSNL TSISSTEPPP VRLPRRVSAV
SSTSRSSPQR ATDQSWKDKM PPFGIVGHSM YSPQSLPSRD AIPRTPFDGS TISSGASSNI
GGSQRIGKNA KKEKSGSDTF TFGNLFRKKP PTSRPNLADI ISDLDQRSTT GGRGGGSLSA
GATNRRSTSA TILPMSSAGG CDPTTPFDSA CSLDGLPDHI SRMVSPSDSP HHATSSSTLN
GANSMSSLYV QLDRIYGKHD LFANDEYQSW HEKYRHNTLS TKQVKKQDAI FELYLMEKRH
CANIAFLLHG YRRRMLDENI ITKQDMDVLI PDVLEPLLIF HLNVLERITA RMKENYEVGT
ISDIISEELA IDGGQHTKLC CDAYTDFGVA KERSDVLYHH LMNKNAKFAE FFKKTYSEET
FYKHYDFRPL ITKIIGRATK YSLLLETILK NEQPFSEYHD LTKTALETAR KFAHKIDGNL
SMAHMSMKWE ELKAQIDSSS ATTLYVSDPS VANATIRYTF DLDSLNSATN RKLVHLGEAL
IKIPVNPVGS GGGTHSSSSG KQVDKKDQCY IVLFDDIIVI LIRKSSRQLI FMQDQGVMPV
QSLLIRTAAR GHSIMLISGA KPVLFEISFH TSTDRKKWVT LLELAPKNVP PEGIRITTGD
ADGVLRDRVA AQQDAEDKWL KELEAIFDTR LPEEEALAKY LETRLEFFDN VREHVSNLPF
KTRTDISNRI REAVKGRFRE LRRARVIPLN RLVERITESR DADLWSYFDE KADAADVLEK
SSDLSEDSDN SGDSAARGAK PRRIQTFHGT SQQPGSSNGG GAIESKNNGI RRHTTVPRMN
SDGGSGSSSS AAAAAGSSTT DRIPIPDDVA FDEENISASA QGSARGRGDS ELDRKTYGEM
LSDLPIRQTM RARRASTNLI KEVISLRKEN HLLKNDNALT KSRCALLERV RGGGAMMTST
ATAVDDSMEM LRKKEKEIRE LQQKVLADRD ELAEKQKAID AQEEEIQTKW AALQARSIEQ
QQSPMHVRSS SSHSQVSSPT YKTPQIQLPP SSSASSSSSS QNNTTDWSPM LTSLATKTET
KKLKK
//
