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Database: UniProt
Entry: A0A3Q7SHN2_VULVU
LinkDB: A0A3Q7SHN2_VULVU
Original site: A0A3Q7SHN2_VULVU 
ID   A0A3Q7SHN2_VULVU        Unreviewed;      1440 AA.
AC   A0A3Q7SHN2;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Rho guanine nucleotide exchange factor 12 isoform X5 {ECO:0000313|RefSeq:XP_025854836.1, ECO:0000313|RefSeq:XP_025854837.1};
GN   Name=ARHGEF12 {ECO:0000313|RefSeq:XP_025854836.1,
GN   ECO:0000313|RefSeq:XP_025854837.1};
OS   Vulpes vulpes (Red fox).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX   NCBI_TaxID=9627 {ECO:0000313|Proteomes:UP000286640, ECO:0000313|RefSeq:XP_025854836.1};
RN   [1]
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (JAN-2019) to UniProtKB.
RN   [2] {ECO:0000313|RefSeq:XP_025854836.1, ECO:0000313|RefSeq:XP_025854837.1}
RP   IDENTIFICATION.
RC   STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025854836.1,
RC   ECO:0000313|RefSeq:XP_025854837.1};
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_025854836.1,
RC   ECO:0000313|RefSeq:XP_025854837.1};
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_025854836.1; XM_025999051.1.
DR   RefSeq; XP_025854837.1; XM_025999052.1.
DR   Proteomes; UP000286640; Unplaced.
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; PF17838; PH_16; 1.
DR   Pfam; PF09128; RGS-like; 1.
DR   Pfam; PF00621; RhoGEF; 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:UP000286640}.
FT   DOMAIN          1..33
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          684..874
FT                   /note="DH"
FT                   /evidence="ECO:0000259|PROSITE:PS50010"
FT   DOMAIN          916..1029
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          153..210
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          471..543
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          570..612
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1035..1054
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1064..1099
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1180..1212
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1322..1364
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        471..493
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        525..539
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1084..1098
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1183..1203
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1440 AA;  161290 MW;  377D37006F589F6E CRC64;
     MRAGVQTGDR IIKVNGTLVT HSNHLEVVKL IKSGSYVALT VQGRPPGSPQ IPLADSEVEP
     SVIGHMSPIM TSPHSPGASG NMERITSPVL MGEENNVVHN QKVEILRKML QKEQERLQLL
     QEDYNRTPAQ RLLKEIQEAK KHIPQLQEQL SKATGSAQDG AVVTSSKPVG EPLTASEVEA
     DPGEGIGRLD YCTGDASRPG SDSADSPKSA LKERICLEEN PEKSEVIQDT DTQSLFGSPS
     PRIAAHIIGA EDDDFGTEHE QINGQCSCFQ SIELLKSRPA HLAVFLHHVV SQFDPATLLC
     YLYSDLYKQT NSKETRRVFL EFHQFFLDRS AHLKVSVPDE ISVDLEKRRP ELIPEDLHRH
     YIQTMQERVH PEVQRHLEDF RQKRSMGLTL AESELTKLDA ERDKDRVTLE KERACAEQIV
     AKIEEVLMTA QPVEEDKSST MQYVILMYMK HLGVKVKEPR NLEHKRGRIG FLPKIKQSMK
     KDREGEEKGK RRGFPSILGP PRRPSRHDNS AIGRAMELQK QRHPKHLSTP SSVSPEPQDP
     AKLRQSALAG EGTEVGYLPA NPMSSVAAGA ALSQEGGKEN DTGSKQVGET PASGDCIDNT
     PRTPNTVFDF PPPPLDQVQE EEWEVERVTE HGTPKPFRKF DSIAFGESQS EDEQFENDLE
     TDPPNWQQLV SREVLLGLKP SEIKRQEVIN ELFYTERAHV RTLKVLDQVF YQRVSREGIL
     SPSELRKIFS NLEDILQLHI GLNEQMKAVR KRNETSVIDQ IGEDLLTWFS GPGEDKLKHA
     AATFCSNQPF ALEMIKSRQK KDSRFQTFVQ DAESNPLCRR LQLKDIIPTQ MQRLTKYPLL
     LDNIAKYTEW PMEREKVKKA ADHCRQILNY VNQAVKEAEN KQRLEDYQRR LDTSNLKLSE
     YPNVEELRNL DLTKRKMIHE GPLVWKVNRD KTIDLYTLLL EDILVLLQKQ DDRLVLRCHS
     KILASTADSK HTFSPVIKLN TVLVRQVATD NKALFVISMS DNGAQIYELV AQTVSEKTVW
     QDLICRMAAS VKEQSAKPIP LPQSPPCEGD NDEEAAPKLK VEHHSISVPG LQSPDRDLGL
     ESPLISSKPQ SHSLGTSGKS EVDDLFVAER QFAKEQHTDG TLQEAGGSYQ ITIPDPHLPA
     SEERWALDAL RNLGLLKQLL VQQLGLTEKS AQEDWPHFPR YRTASSGVQT DSGTQNSENS
     KAYPPGEGQM PFRTGTGDIS TCYSPRTSTE SSAPRDSVVL AFQESQASNI LVMDHMIMTP
     EMPPAEPEGS LDESGEHFFD AREAHSDDNP SEGDGAVKKE EDVNLRISGN YLILDGYEAV
     QESSTDEEVA SSLPPPPTAG IPAMDCARPQ QHSPQHAHSD GAASPFTPEF LVQQRWGAME
     DSCFEIQSPP SCADSQSQIM EYIRKIEADL EHLKKVEESY SILCQRLAGS ALTDKHSDKS
//
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