ID A0A0V1KUU6_9BILA Unreviewed; 1655 AA.
AC A0A0V1KUU6;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Rho guanine nucleotide exchange factor 12 {ECO:0000313|EMBL:KRZ51055.1};
GN Name=Arhgef12 {ECO:0000313|EMBL:KRZ51055.1};
GN ORFNames=T02_2537 {ECO:0000313|EMBL:KRZ51055.1};
OS Trichinella nativa.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6335 {ECO:0000313|EMBL:KRZ51055.1, ECO:0000313|Proteomes:UP000054721};
RN [1] {ECO:0000313|EMBL:KRZ51055.1, ECO:0000313|Proteomes:UP000054721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS10 {ECO:0000313|EMBL:KRZ51055.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Membrane {ECO:0000256|ARBA:ARBA00004370}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the eukaryotic
CC ribosomal protein eS31 family. {ECO:0000256|ARBA:ARBA00009891}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the ubiquitin family.
CC {ECO:0000256|ARBA:ARBA00008373}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRZ51055.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JYDW01000240; KRZ51055.1; -; Genomic_DNA.
DR Proteomes; UP000054721; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005840; C:ribosome; IEA:InterPro.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR CDD; cd00029; C1; 1.
DR CDD; cd00992; PDZ_signaling; 1.
DR CDD; cd00160; RhoGEF; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 3.30.60.20; -; 1.
DR Gene3D; 6.20.50.150; -; 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; IPR046349; C1-like_sf.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR001331; GDS_CDC24_CS.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR002219; PE/DAG-bd.
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 InterPro; IPR002906; Ribosomal_eS31.
DR InterPro; IPR038582; Ribosomal_eS31_euk-type_sf.
DR InterPro; IPR011332; Ribosomal_zn-bd.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR45872; RHO GUANINE NUCLEOTIDE EXCHANGE FACTOR 2, ISOFORM D; 1.
DR PANTHER; PTHR45872:SF2; RHO GUANINE NUCLEOTIDE EXCHANGE FACTOR 2, ISOFORM D; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF17838; PH_16; 1.
DR Pfam; PF09128; RGS-like; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR Pfam; PF01599; Ribosomal_S27; 1.
DR Pfam; PF00240; ubiquitin; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SMART; SM01402; Ribosomal_S27; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 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 SUPFAM; SSF54236; Ubiquitin-like; 1.
DR SUPFAM; SSF57829; Zn-binding ribosomal proteins; 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 PROSITE; PS50053; UBIQUITIN_2; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658};
KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000054721};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 13..75
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 531..581
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 803..998
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 1040..1155
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1505..1565
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS50053"
FT REGION 85..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1160..1183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 160..187
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 85..99
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..126
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1168..1182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1655 AA; 187229 MW; 11D31B91E6E0499A CRC64;
MHFHGEHFAE ERNVLIKRDE NGYGLTVCGN NPVFVQSVRE GSAAAKAGVH VGECIIKVNG
VTVTSLDHLE VVKLISVAPY TTLTLSGGPS SSSAASSMGN DHYEKRDRCL ERRSTENAIR
PNSKKKQSEW HLKRKKIIQQ ILTEEKRQLQ VMLKGSDAHA DADQRIIEKM TRRIHNLEDQ
LNEVEKLDFE QVELFYKNLI NQENISLSNS GFRSHSDDLS SSLTMKSSKF HSDDVVASSS
TDDERLLTKS GNIDEIRDHQ IPVPVSEVPP ESPLLVHTLS MSNECDSAAV EFNSSSFDEP
FSKLPMLKTH LGHLAVFLHY LLSNSDPSYL LFYLLTDIFA LYIGKESKKW AYEIHSSFLL
PYSPCRVSFT DSSSWETVDA VLNDPNKHAD SAQWRRLFST ARGLAVQAIN EQLADFRSKR
ILGLGNVFGE SMLQRLQAGD SAHERKIFDA LIAPHLIAFF EEAADFDQLP KRIQVIVAAL
ATLYKHNNVK CRNAAMEKLL ERCPTYIAKE KQRFARPLLP KASRRALQIK AHCFNIAPVL
QTTFCYQCQK LIWGIGAMSL FCGKCGVVLH KSCVENLAES CFGSMNLRRP LILKKIVGRK
NVESSMDNIE QSIEEGKVST AKTDASMLLK ENSGEGDGSS EKNLTRNFDK SGVTNAAVSK
QSAHIHNLSR SQSMNIEVAY KTLSYECAFR KNLTEVPDVE VVIPAGEAIG SLFYCDADKT
ESLTRISTTE SSTTVSVQDV SRERSPMISE LDSPLTSSVS FSNTLHDIHI ELDSDFKVEN
EIPLLEDLLD LESFQYLDKR EKNRLEVIYE LFHTEQTHVR NLKILYRLFY KQLLNFNVIS
FEFASLLFSN LEDVLNLHVE MNEAMKNMMQ NNKLIGDISI MMLQFDGKER MRNIDSLHCQ
KLQSAIEALK HRVVKDQKLR EFLQVVESLP VCRKLQLKDM LPMEMQRLTK YPLLLENVLK
YTEEVITVYH LLDPSEEADR LRTCIECSRS ILESVNSAKR NAENVLRLQR LQQMLDTTQF
DKVNHPIVSE FCPLDVRRFS LIHEGPLIWR LNKSKIVDLH VVLLDEILLL LSPTSDGHLA
LRFHNINISC GKDEVKWTHC PLLKLNSLIA KDVATDKKAF FLVSTSPSGP QIYELATQSK
AEKQNWFKFI VEQIEASKEH EQKTSVRHGQ AGQESKSGDS FYEIPNSARK KSLTVRSQRT
MKNPNFDERV RVTCQPRLIS PSEINICQPT VFQHSKPILN PLEKLKQEDK LVIRLLNEKL
QIISSFFGQK NDLPPSSAVD SRTSREAREF VISAIKQTNR LLEAINEQTR LIEMENFENG
SVKYQVPEVE CPSVPCYQLT QIAAGLMTCL TNLLHSLQIM GDDLKRVQRE LHQYKLSPER
LVPFPEKICQ AVGTDIPTDV THEAACRKSL TDAAVQTEPA SFLQTNNCDA VKKNAGKSTE
NFHTDDQPTE LSGRSIIKDA LPTGSCNTAA SEKPILRNGK MGTDGLCLFD TDIAKLEEQP
CSEIITIESN CTIGEIKKQI QEEEESLCSS YLVLGGRPLE DDWTLAQCNI QEFSTLDLSY
RLLGGAKKRK KKMYTTPKKI KHKKKKVKLA VLKYYKIDEN GKVSRLRKEC TSESCGAGVF
MANHYNRQYC GKCYCTMVVQ DPVQREQKAG KGKGH
//
