ID R0KC01_ANAPL Unreviewed; 1538 AA.
AC R0KC01;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Rap guanine nucleotide exchange factor 6 {ECO:0000313|EMBL:EOB07382.1};
DE Flags: Fragment;
GN ORFNames=Anapl_09850 {ECO:0000313|EMBL:EOB07382.1};
OS Anas platyrhynchos (Mallard) (Anas boschas).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC Anatinae; Anas.
OX NCBI_TaxID=8839 {ECO:0000313|EMBL:EOB07382.1, ECO:0000313|Proteomes:UP000296049};
RN [1] {ECO:0000313|Proteomes:UP000296049}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23749191; DOI=10.1038/ng.2657;
RA Huang Y., Li Y., Burt D.W., Chen H., Zhang Y., Qian W., Kim H., Gan S.,
RA Zhao Y., Li J., Yi K., Feng H., Zhu P., Li B., Liu Q., Fairley S.,
RA Magor K.E., Du Z., Hu X., Goodman L., Tafer H., Vignal A., Lee T.,
RA Kim K.W., Sheng Z., An Y., Searle S., Herrero J., Groenen M.A.,
RA Crooijmans R.P., Faraut T., Cai Q., Webster R.G., Aldridge J.R.,
RA Warren W.C., Bartschat S., Kehr S., Marz M., Stadler P.F., Smith J.,
RA Kraus R.H., Zhao Y., Ren L., Fei J., Morisson M., Kaiser P., Griffin D.K.,
RA Rao M., Pitel F., Wang J., Li N.;
RT "The duck genome and transcriptome provide insight into an avian influenza
RT virus reservoir species.";
RL Nat. Genet. 45:776-783(2013).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
CC -!- SIMILARITY: Belongs to the RAPGEF2 family.
CC {ECO:0000256|ARBA:ARBA00010829}.
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DR EMBL; KB742531; EOB07382.1; -; Genomic_DNA.
DR Proteomes; UP000296049; Unassembled WGS sequence.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005770; C:late endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR CDD; cd00038; CAP_ED; 1.
DR CDD; cd00992; PDZ_signaling; 1.
DR CDD; cd01785; RA_PDZ-GEF1; 1.
DR CDD; cd00155; RasGEF; 1.
DR CDD; cd06224; REM; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR Gene3D; 1.10.840.10; Ras guanine-nucleotide exchange factors catalytic domain; 1.
DR Gene3D; 1.20.870.10; Son of sevenless (SoS) protein Chain: S domain 1; 1.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR018490; cNMP-bd_dom_sf.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR000159; RA_dom.
DR InterPro; IPR000651; Ras-like_Gua-exchang_fac_N.
DR InterPro; IPR023578; Ras_GEF_dom_sf.
DR InterPro; IPR001895; RASGEF_cat_dom.
DR InterPro; IPR036964; RASGEF_cat_dom_sf.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR45161; CYTOSKELETON-ASSOCIATED PROTEIN 4; 1.
DR PANTHER; PTHR45161:SF4; RAP GUANINE NUCLEOTIDE EXCHANGE FACTOR 6; 1.
DR Pfam; PF00027; cNMP_binding; 1.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF00788; RA; 1.
DR Pfam; PF00617; RasGEF; 1.
DR Pfam; PF00618; RasGEF_N; 1.
DR SMART; SM00100; cNMP; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00314; RA; 1.
DR SMART; SM00147; RasGEF; 1.
DR SMART; SM00229; RasGEFN; 1.
DR SUPFAM; SSF51206; cAMP-binding domain-like; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF48366; Ras GEF; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50200; RA; 1.
DR PROSITE; PS50009; RASGEF_CAT; 1.
DR PROSITE; PS50212; RASGEF_NTER; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658,
KW ECO:0000256|PROSITE-ProRule:PRU00168};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Neurogenesis {ECO:0000256|ARBA:ARBA00022902};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000296049}.
FT DOMAIN 218..318
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 350..463
FT /note="N-terminal Ras-GEF"
FT /evidence="ECO:0000259|PROSITE:PS50212"
FT DOMAIN 468..538
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 688..774
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 799..1027
FT /note="Ras-GEF"
FT /evidence="ECO:0000259|PROSITE:PS50009"
FT REGION 118..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1082..1115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1137..1216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1365..1425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1512..1538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..179
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1098..1115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1140..1183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1195..1216
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1372..1425
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1512..1528
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EOB07382.1"
FT NON_TER 1538
FT /evidence="ECO:0000313|EMBL:EOB07382.1"
SQ SEQUENCE 1538 AA; 172816 MW; D6810A8C81642978 CRC64;
YSSETIARCW YILLSGSVLM KDSMFLPPCS FGKQSGGKRG CECIILEPSE MIVVENSKDN
EENILQREVP LRQSRRRFRK INQRGERQTI TDNVDASSYI SLPADLTKMH LTDNPHPQVT
HVPSSQSGCS IASDSGSSSL SDIYQATESE MGDVDLTGLP EAPVDSEDEE EEEDEDIDRT
SDPLLGRDVV RECLEKEPAD KTDDDIEQLL EFMHQLPAFA NMTMSVRREL CSVMIFEVVE
QAGAIILEDG QELDSWYVIL NGTVEISYPD GKSESLCMGN SFGITPSLDK QYMNGVVRTK
VDDCQFVCIA QQDYWRILNH VEKNTHKVEE EGEIVMVKEH RELDRSGTRK GHIVIKATPE
RLIMHLIEEH SIVDPTYIED FLLTYRTFLT SPLEVGNKLL EWFTVDSLRD KVTRVVLLWV
NNHFNDFEGD PAMTRFLEEF EKNLENTKMK GHLRLLNIAC AAKAKWRQIT LQKPSRDSPL
FFSLLGGSDK GFGIFVETVE TGSKAAEAGL KRGDQIMEVN GQNFENITFV KALEILRNNT
HLSITVKTNI FVFKELLCRI GQEKNGIPHI PKIAEKKNNR YSIPDMPGDV EQMFPREKGN
KKMKANTVSG GRNRIRKILD KTRFSILPPK LFSDGSVSQS QDDSIVGTRQ CRHSLAIMPI
PGTLSSSSPD LLQPTTSILD FSNPSDIPDQ VIRVFKADQQ SCYIIISKDT TAKEVVSHAV
HEFNLTGAPE TYSLCEVSVS PEGVIKQRRL PDQFSKLADR IQLNGRYYLK NNMETETLCS
DEDAQELLRE SQISLLQLST IEVATQLSMR DFELFRNIEP TEYIDDLYKL DSKTGNAHLK
QFEDVINQET FWVAMEILAE PNQLKRMKII KHFIKIALHC RECKNFNSMF AVISGLNLAP
VARLRGTWEK LPSKYEKHLR DLQDLFDPSR NMAKYRNILS SQSMQPPIIP LFPVVKKDIT
FLHEGNDSKV DGLVNFEKLR MIAKEIRQVV RMTSANMDPA VMFRQRSLSQ GSTNSNMLDV
QGGAHKKRAR RSSLLNAKKL YEDAQMARKV KQYLSNLNVE TDEEKIQILS LQCEPAYSTL
TKNLSERRGA KSSEMSPVPM RSIGQTTKAH QHQQNRMSQV LQVPTVNLYP SRKKGLTKDH
VTFSTGSPQK SLSLSEEVST KKQTEDTMSM ASSLHSSPPA SPQGSPRKGY ALIPSTKSDN
FSDSSHSEIS SRSSIVSNCS VDSMSAALQD ERGLSQSLTV VDAAGADRKE HPQPLTDYGQ
PCPGWSITRP ALIRGMAFTS SMSNEEISHD HITVEAADSG RGSWTSCSSS SHDNFQNIPN
QKSWDLLNSY RHTQLDGPIA EVDPTNCYSE EAYLYSEAFS KNNRQSKASV EHDQSRQSWA
SSSSLSDTYE TNYGTIKRRG LENSTSEQTE VLDSKPGTDT TYKTVTSSTE KGLIVYCVTS
PKKDDRYREP PPTPPGYMGI SLADIKEGSP HHPHLKPPDY SVAVQRSKML PSDLSRLSSA
SLSSEPVACI SSKMPQWHSR QPSNPKLADM TDADSEED
//
