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Database: UniProt
Entry: K9J6B3_DESRO
LinkDB: K9J6B3_DESRO
Original site: K9J6B3_DESRO 
ID   K9J6B3_DESRO            Unreviewed;      1532 AA.
AC   K9J6B3;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   SubName: Full=Putative guanine nucleotide exchange factor {ECO:0000313|EMBL:JAA53249.1};
DE   Flags: Fragment;
OS   Desmodus rotundus (Vampire bat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Phyllostomidae;
OC   Desmodontinae; Desmodus.
OX   NCBI_TaxID=9430 {ECO:0000313|EMBL:JAA53249.1};
RN   [1] {ECO:0000313|EMBL:JAA53249.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Salivary gland {ECO:0000313|EMBL:JAA53249.1};
RA   Francischetti I.M.B., Assumpcao T.C.F., Ma D., Vicente E.C.,
RA   Ribeiro J.M.C.;
RT   "The Vampirome: Transcriptome and Proteome Analysis of the Submandibular
RT   and Accessory Glands of the Vampire Bat and Vector of Human Rabies,
RT   Desmodus rotundus.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC       Membrane {ECO:0000256|ARBA:ARBA00004370}.
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DR   EMBL; GABZ01000276; JAA53249.1; -; mRNA.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0001664; F:G protein-coupled receptor binding; IEA:InterPro.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:InterPro.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IEA:InterPro.
DR   GO; GO:0007266; P:Rho protein signal transduction; IEA:InterPro.
DR   CDD; cd00992; PDZ_signaling; 1.
DR   CDD; cd13390; PH_LARG; 1.
DR   CDD; cd08754; RGS_LARG; 1.
DR   CDD; cd00160; RhoGEF; 1.
DR   Gene3D; 2.30.42.10; -; 1.
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   Gene3D; 1.10.167.10; Regulator of G-protein Signalling 4, domain 2; 1.
DR   InterPro; IPR037801; ARHGEF12_PH.
DR   InterPro; IPR035899; DBL_dom_sf.
DR   InterPro; IPR000219; DH-domain.
DR   InterPro; IPR001331; GDS_CDC24_CS.
DR   InterPro; IPR037884; LARG_RGS.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR041020; PH_16.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR015212; RGS-like_dom.
DR   InterPro; IPR036305; RGS_sf.
DR   InterPro; IPR044926; RGS_subdomain_2.
DR   PANTHER; PTHR45872:SF3; RHO GUANINE NUCLEOTIDE EXCHANGE FACTOR 12; 1.
DR   PANTHER; PTHR45872; RHO GUANINE NUCLEOTIDE EXCHANGE FACTOR 2, ISOFORM D; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   Pfam; PF17838; PH_16; 1.
DR   Pfam; PF09128; RGS-like; 1.
DR   Pfam; PF00621; RhoGEF; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00325; RhoGEF; 1.
DR   SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR   SUPFAM; SSF50156; PDZ domain-like; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF48097; Regulator of G-protein signaling, RGS; 1.
DR   PROSITE; PS00741; DH_1; 1.
DR   PROSITE; PS50010; DH_2; 1.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT   DOMAIN          62..126
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          776..966
FT                   /note="DH"
FT                   /evidence="ECO:0000259|PROSITE:PS50010"
FT   DOMAIN          1008..1121
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          1..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          323..343
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          563..601
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          613..647
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          667..695
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1414..1452
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          196..249
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        10..50
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        563..585
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        616..639
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        678..695
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1434..1452
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:JAA53249.1"
SQ   SEQUENCE   1532 AA;  173253 MW;  8E9303FD83E6A433 CRC64;
     RFPLKKPIRH GSILNRESPT DKKQKVERSV SHDFDPTDSS SKKTRSSSEE SRSEIYGLVQ
     RCVVIQKDDN GFGLTVSGDN PVFVQSVKED GAAMRAGVQT GDRIIKVNGT LVTHSNHLEV
     VKLIKSGSYV ALTVQGRPPG SAQIPLSDSE VEPLVIGHMS PIMTSPHSPG TSGNMERITS
     PVLMEEENNV VHNQKVEILR KMLRKEQERL QLLQEDYNRT PAQRLLKEIQ EAKKHIPQLQ
     EQLSKATGSA QDGAIITSSK PLGDTLTVSE LEADPGDGLC KIDYSRDVSW PSSDNANSPK
     SGQKEKIYLE ENLEKNEVIQ DTDTQSLIGS PSTHTAPHII GAEDDDFGTE HEQINGQCSC
     FQSIELLKSR PAHLAVFLHH VVSQFDPATL LCYLYSDLYK QTNSKETRRV FLEFHQFFLD
     RSAHLKVSVP DEISVDLEKR RPELIPEDLH RHYIQSVQER VHPEIQRHLE DFRQKRSMGL
     TLAESELTKL DVERDKDRVT LEKERACAEQ IVAKIEEVLM TAQAIEEDKS STMQYVIFMY
     MKHLGVKVKE PRNLEHKRGR IGFLPKIKQT MKKDREGEEK GKRRGFSSIL GPPRRPSRHD
     NSAIGRAMEL QKQRYPKHLS TPSSVSPEPQ DSAKLRQSGL ASEGSDIGYL PANSMSSMAS
     VATLFQEGGK DNDMGSKQVG ETPASGDSLD STPRTSNTIF DFLPLQLDQV QEEEWEVERI
     PEHGTPKPFR KFDSIGFGES QSEDELFEND LETDPPNWQQ LVSREVLLGL KPCEIKRQEV
     INELFYTERA HVRTLKVLDQ VFYQRVSREG ILSPSEIRKI FSNLEDILQL HIVLNEQMKA
     VRKRNETSVI DQIGEDLLTW FSGPGEEKLK HAAATFCSNQ PFALEMIKSR QKKDSRFHTF
     VQDAESNPLC RRLQLKDIIP TQMQRLTKYP LLLDNIAKYT EWPMEREKVK KAADHCRRIL
     NYVNQAVKEA ENKQRLEDYQ RRLDTSNLKL SEYPNVEELR NLDLTKRKMI HEGPLVWKVN
     RDKTIDLYTL LLEDILVLLQ KQDDRLVLRC HSKILASTAD SKHTFSPVIK LNTVLVRQVA
     TDNKAFFVIS MSDNGAQIYE LVAQTVSEKT VWQDLICQMA ASVKEQSTKP IPLPQSPPCE
     GDNDEEPPKI KVEHHGISVT CLQSTDRDLG LESPLMSSKA QPHSLDVSEK SEVDDLFVAE
     RQFAKEQHAE GTVKKVGVKY PITIPDSHLP VSEGQWALDA LRNLGLLKQL LVQKLSLTEK
     STQEDWPHFS TYRTASPGVQ TDSGTQNFEI IKAYHTGERQ RPFRTGTGDI SACYSPRAST
     DSYVPRDSVV LAFQDSQASN ILVMDHMIMT PEIPPAEPEG GLDESGEHFF DAREVHSDDN
     PLEGDGAVKM EEKDANLHIS GNYLILDGYE TVQESSTDEE VTSSLPPQPM KGLPFVDSTQ
     QPQHSLQNAL SDGAVSPFTP EFLVQQCWEA GEDTCYEIQS PYTCADSERQ IMEYIHKIEA
     DLEHLKKVEE SYTILWQRLA ESALTDNHSD KS
//
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