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Database: UniProt
Entry: A0A2U4BVZ8_TURTR
LinkDB: A0A2U4BVZ8_TURTR
Original site: A0A2U4BVZ8_TURTR 
ID   A0A2U4BVZ8_TURTR        Unreviewed;      1498 AA.
AC   A0A2U4BVZ8;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   07-OCT-2020, sequence version 2.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Rho guanine nucleotide exchange factor 12 isoform X4 {ECO:0000313|RefSeq:XP_019797314.2};
GN   Name=ARHGEF12 {ECO:0000313|RefSeq:XP_019797314.2};
OS   Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Delphinidae; Tursiops.
OX   NCBI_TaxID=9739 {ECO:0000313|Proteomes:UP000245320, ECO:0000313|RefSeq:XP_019797314.2};
RN   [1] {ECO:0000313|RefSeq:XP_019797314.2}
RP   IDENTIFICATION.
RC   TISSUE=Spleen {ECO:0000313|RefSeq:XP_019797314.2};
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_019797314.2; XM_019941755.2.
DR   Proteomes; UP000245320; Chromosome 8.
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, ECO:0000256|SAM:Coils};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245320}.
FT   DOMAIN          72..136
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          740..930
FT                   /note="DH"
FT                   /evidence="ECO:0000259|PROSITE:PS50010"
FT   DOMAIN          972..1085
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          1..62
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          521..676
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1090..1157
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1340..1359
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1380..1424
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          206..259
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        13..60
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        521..549
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        581..659
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1380..1420
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1498 AA;  168528 MW;  4841E46659916606 CRC64;
     MSGTQSTITD RFPLKKPIRH GSILNRESPT DKKQKVERST SHDFDPTDSS SKKTKSSSEE
     SRSEIYGLVQ RCVIIQKDDN GFGLTVSGDN PVFVQSVKED GAAMRAGVQT GDRIIKVNGT
     LVTHSNHLEV VKLIKSGSYV ALTVQGRPPG SPQFPLADSE VEPSVVGHMS PIMTSPHSPG
     ASGNMERITS PVLMGEENNV VHNQKVEILR KMLQKEQERL QLLQEDYSRT PAQRLLKEIQ
     EAKKHIPQLQ EQLSKATGSA QSPKSGLKER IYLEENPEKS EVIQDTDTQS LIGSPSTRIA
     PHIIGAEDDD FGTEHEQING QCSCFQSIEL LKSRPAHLAV FLHHVVSQFD PATLLCYLYS
     DLYKQTNSKE TRRVFLEFHQ FFLDRSAHLK VSVPDEISVD LEKRRPELIP EDLHRHYIQT
     MQERVHPEVQ RHLEDFRQKR SMGLTLAESE LTKIDAERDK DRVTLEKERA CAEQIVAKIE
     EVLMTAQAVE EDKSSTMQYV ILMYMKHLGV KVKEPRNLEH KRGRIGFLPK IKQSMKKDRE
     GEEKGKRRGF PSILGPPRRP SRHDNSAIGR AMELQKQRHP KHISTPSSVS PEPQDSAKLR
     QSGLTSEGVD TGYLPANSMS SMVSGATLSQ EGGKENDMGS KQVGETPASG DSLDGTPRTP
     STIFDFPPPP LDQVQEEEWE VERVTEHGTP KPFRKFDSIA FGESQSEDEQ FENDLETDPP
     NWQQLVSREV LLALKPCEIK RQEVINELFY TERAHVRTLK VLDQVFYQRV SREGILSPSE
     LRKIFSNLED ILQLHIGLNE QMKAVRKRNE TSVIDQIGED LLTWFSGPGE EKLKHAAATF
     CSNQPFALEM IKSRQKKDSR FQTFVQDAES NPLCRRLQLK DIIPTQMQRL TKYPLLLDNI
     AKYTEWPTER EKVKKAADHC RQILNYVNQA VKEAENKQRL EDYQRRLDTS NLKLSEYPNV
     EELRNLDLTK RKMIHEGPLV WKVNRDKTID LYTLLLEDIL VLLQKQDDRL VLRCHSKILA
     STGDSKHTFS PVIKLNTVLV RQVATDNKAL FVISMSDNGA QIYELVAQTV SEKTVWQDLI
     CRMAASVKEQ STKPIPLPQS PPCEGDNDEE EPPKLKVEHH GISVSGLQSP DRDLGLESPL
     MSSKPQSHSL DTSGKSEVDD DLFVADRQFA KEQHADGTLK EVGVNYQITV PDPHLPVSEE
     RWALDALRNL GLLKQLLVQQ LGLTEKSTQE DWPHFPRCRT ASLGAQADSG TQKPGNIKAY
     HPCEGQMPFR TGTGDISTCY SPRTSTESSA PRDSVVLAFQ DSQASNILVM DHMIMTPEMP
     PAEPEGGLDE SGEHFFDARE AHSDDNPSEG DGAVKKEEKD VNLRISGTCL ILDGYETVQE
     SSTDEEIASS LPPQPATGIP SMDSTRRQQR SPQNAHSDGA VSPFTPEFLV QQRWGAMEDS
     CLEIRSPSSC ADSQSQIMEC IRKIEADLEH LKKVEESYSI LCQRLAGSAL TDKHSDKS
//
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