ID   B4E2K6_HUMAN            Unreviewed;      1278 AA.
AC   B4E2K6;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 97.
DE   SubName: Full=cDNA FLJ60405, highly similar to Rho guanine nucleotide exchange factor 12 {ECO:0000313|EMBL:BAG65168.1};
DE   Flags: Fragment;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|EMBL:BAG65168.1};
RN   [1] {ECO:0000313|EMBL:BAG65168.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Trachea {ECO:0000313|EMBL:BAG65168.1};
RA   Wakamatsu A., Yamamoto J., Kimura K., Ishii S., Watanabe K., Sugiyama A.,
RA   Murakawa K., Kaida T., Tsuchiya K., Fukuzumi Y., Kumagai A., Oishi Y.,
RA   Yamamoto S., Ono Y., Komori Y., Yamazaki M., Kisu Y., Nishikawa T.,
RA   Sugano S., Nomura N., Isogai T.;
RT   "NEDO human cDNA sequencing project focused on splicing variants.";
RL   Submitted (OCT-2007) 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; AK304316; BAG65168.1; -; mRNA.
DR   RefSeq; NP_001185594.1; NM_001198665.1.
DR   RefSeq; NP_056128.1; NM_015313.2.
DR   AlphaFoldDB; B4E2K6; -.
DR   PeptideAtlas; B4E2K6; -.
DR   DNASU; 23365; -.
DR   GeneID; 23365; -.
DR   KEGG; hsa:23365; -.
DR   CTD; 23365; -.
DR   OrthoDB; 2875542at2759; -.
DR   BioGRID-ORCS; 23365; 25 hits in 1151 CRISPR screens.
DR   GenomeRNAi; 23365; -.
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:0051056; P:regulation of small GTPase mediated signal transduction; IEA:UniProt.
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.
DR   Genevisible; B4E2K6; HS.
PE   2: Evidence at transcript level;
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT   DOMAIN          53..117
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          768..958
FT                   /note="DH"
FT                   /evidence="ECO:0000259|PROSITE:PS50010"
FT   DOMAIN          1000..1113
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          229..327
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          549..688
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1119..1160
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        231..245
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        291..310
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        549..577
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        609..631
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        641..687
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1278
FT                   /evidence="ECO:0000313|EMBL:BAG65168.1"
SQ   SEQUENCE   1278 AA;  143947 MW;  A6279845201B370A CRC64;
     MSGTQSTITD RFPLKKPIRH GSILNRESPT DKKQKVERIA SHDFDPTGLV QRCVIIQKDD
     NGFGLTVSGD NPVFVQSVKE DGAAMRAGVQ TGDRIIKVNG TLVTHSNHLE VVKLIKSGSY
     VALTVQGRPP GSPQIPLADS EVEPSVIGHM SPIMTSPHSP GASGNMERIT SPVLMGEENN
     VVHNQKVEIL RKMLQKEQER LQLLQEDYNR TPAQRLLKEI QEAKKHIPQL QEQLSKATGS
     AQDGAVVTPS RPLGDTLTVS EAETDPGDVL GRTDCSSGDA SRPSSDNADS PKSGPKERIY
     LEENPEKSET IQDTDTQSLV GSPSTRIAPH IIGAEDDDFG TEHEQINGQC SCFQSIELLK
     SRPAHLAVFL HHVVSQFDPA TLLCYLYSDL YKHTNSKETR RIFLEFHQFF LDRSAHLKVS
     VPDEMSADLE KRRPELIPED LHRHYIQTMQ ERVHPEVQRH LEDFRQKRSM GLTLAESELT
     KLDAERDKDR LTLEKERTCA EQIVAKIEEV LMTAQAVEED KSSTMQYVIL MYMKHLGVKV
     KEPRNLEHKR GRIGFLPKIK QSMKKDKEGE EKGKRRGFPS ILGPPRRPSR HDNSAIGRAM
     ELQKARHPKH LSTPSSVSPE PQDSAKLRQS GLANEGTDAG YLPANSMSSV ASGASFSQEG
     GKENDTGSKQ VGETSAPGDT LDGTPRTLNT VFDFPPPPLD QVQEEECEVE RVTEHGTPKP
     FRKFDSVAFG ESQSEDEQFE NDLETDPPNW QQLVSREVLL GLKPCEIKRQ EVINELFYTE
     RAHVRTLKVL DQVFYQRVSR EGILSPSELR KIFSNLEDIL QLHIGLNEQM KAVRKRNETS
     VIDQIGEDLL TWFSGPGEEK LKHAAATFCS NQPFALEMIK SRQKKDSRFQ TFVQDAESNP
     LCRRLQLKDI IPTQMQRLTK YPLLLDNIAK YTEWPTEREK VKKAADHCRQ ILNYVNQAVK
     EAENKQRLED YQRRLDTSSL KLSEYPNVEE LRNLDLTKRK MIHEGPLVWK VNRDKTIDLY
     TLLLEDILVL LQKQDDRLVL RCHSKILAST ADSKHTFSPV IKLSTVLVRQ VATDNKALFV
     ISMSDNGAQI YELVAQTVSE KTVWQDLICR MAASVKEQST KPIPLPQSTP GEGDNDEEDP
     SKLKEEQHGI SVTGLQSPDR DLGLESTLIS SKPQSHSLST SGKSEVRDLF VAERQFAKEQ
     HTDGTLKEVG EDYQIAIPDS HLPVSEERWA LDALRNLGLL KQLLVQQLGL TEKSVQEDWQ
     HFPRYRTASQ GPQTDSVI
//