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Database: UniProt
Entry: A0A2Y9FFH6_PHYMC
LinkDB: A0A2Y9FFH6_PHYMC
Original site: A0A2Y9FFH6_PHYMC 
ID   A0A2Y9FFH6_PHYMC        Unreviewed;      1525 AA.
AC   A0A2Y9FFH6;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Rho guanine nucleotide exchange factor 12 isoform X2 {ECO:0000313|RefSeq:XP_007121769.1};
GN   Name=ARHGEF12 {ECO:0000313|RefSeq:XP_007121769.1};
OS   Physeter macrocephalus (Sperm whale) (Physeter catodon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Physeteridae; Physeter.
OX   NCBI_TaxID=9755 {ECO:0000313|Proteomes:UP000248484, ECO:0000313|RefSeq:XP_007121769.1};
RN   [1] {ECO:0000313|RefSeq:XP_007121769.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_007121769.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC       Membrane {ECO:0000256|ARBA:ARBA00004370}.
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DR   RefSeq; XP_007121769.1; XM_007121707.4.
DR   Ensembl; ENSPCTT00005032645; ENSPCTP00005029692; ENSPCTG00005021172.
DR   GeneID; 102996900; -.
DR   CTD; 23365; -.
DR   OrthoDB; 2875542at2759; -.
DR   Proteomes; UP000248484; Chromosome 16.
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   4: Predicted;
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248484}.
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          18..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          228..294
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          553..631
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          651..698
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1118..1182
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1367..1386
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1407..1441
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        231..247
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        553..577
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        609..629
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        651..687
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1525 AA;  170968 MW;  CA2C003DADDED576 CRC64;
     MSGTQSTITD RFPLKKPIRH GSILNRESPT DKKQKVERST SHDFDPTGLV HRCVIIQKDD
     NGFGLTVSGD NPVFVQSVKE DGAAMRAGVQ TGDRIIKVNG TLVTHSNHLE VVKLIRSGSY
     VALTVQGRPP GSPQFPLADS EVEPSVVGHM SPIMTSPHSP GASGNMERIT SPVLMGEENN
     VVHNQKVEIL RKMLQKEQER LQLLQEDYSR TPAQRLLKEI QEAKKHIPQL QEQLSKATGS
     AQDGAAVTSS KPLGDGLAVS EIEADPGDGL GRIDYGSGDA SRPGSDSADS PKSGLKERIY
     LEENPDKSEV IQDADTQSLI GSPSTRIAPH IIGAEDDDFG TEHEQINGQC SCFQSIELLK
     SRPAHLAVFL HHVVSQFDPA TLLCYLYSDL YKQTNSKETR RVFLEFHQFF LDRSAHLKVS
     VPDEISVDLE KRRPELIPED LHRHYIQTMQ ERVHPEVQRH LEDFRQKRSM GLTLAESELT
     KIDAERDKDR VTLEKERACA EQIVAKIEEV LMTAQAVEED KSSTMQYVIL MYMKHLGVKV
     KEPRNLEHKR GRIGFLPKIK QSMKKDREGE EKGKRRGFPS ILGPPRRPSR HDNSAIGRAM
     ELQKQRHPKH ISTPSSVSPE PQDSAKLRQS GLASEGADIG YLPANSMSSM VSGATLSQEG
     GKENDMGSKQ VGETPASGDS LDGTPRTPST IFDFPPPPLD QVQEEEWEVE RVTEHGTPKP
     FRKFDSIAFG ESQSEDEQFE NDLETDPPNW QQLVSREVLL ALKPCEIKRQ EVINELFYTE
     RAHVRTLKVL DQVFYQRVSR EGILSPSELR KIFSNLEDIL QLHIGLNEQM KAVRKRNETS
     VIDQIGEDLL TWFSGPGEEK LKHAAATFCS NQPFALEMIK SRQKKDSRFQ TFVQDAESNP
     LCRRLQLKDI IPTQMQRLTK YPLLLDNIAK YTEWPTEREK VKKAADHCRQ ILNYVNQAVK
     EAENKQRLED YQRRLDTSNL KLSEYPNVEE LRNLDLTKRK MIHEGPLVWK VNRDKTIDLY
     TLLLEDILVL LQKQDDRLVL RCHSKILAST GDSKHTFSPV IKLNTVLVRQ VATDNKALFV
     ISMSDNGAQI YELVAQTVSE KTVWQDLICR MAASVKEQST KPIPLPQSPP CEGDNDEEEP
     PKLKVEHHGI SVTGLQSPDR DLGLESPLMS SKPQSHSLDT SGKSEVDDLF VAERQFAKEQ
     HADGTLKEVG VNYQITIPDP HLPVSEERWA LDALRNLGLL KQLLVQQLGL TEKSTQEDWP
     HFPRCRTASL GLQADSGTQN PENIKAYHPC EGQMPFRTGT GDISTCYSPR TSTESSAPRD
     SVVLAFQDSQ ASNILVMDHM IMTPEMPPAE PEGGLDESGE HFFDAREAHS DDNPSEGDGA
     VKKEEKDVNL RISGTCLILD GYETVQESST DEEVASSLPP QPATGIPSMD STPRQQRSPQ
     NAHFDGAVSP FTPEFLVQQR WGAMEDSCFE IRSPSSCADS QSQIMEYIRK IEADLEHLKK
     VEESYTILCQ RLAGSALTDK HSDKS
//
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