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
//