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Database: UniProt
Entry: A0A0V1NNU2_9BILA
LinkDB: A0A0V1NNU2_9BILA
Original site: A0A0V1NNU2_9BILA 
ID   A0A0V1NNU2_9BILA        Unreviewed;      1713 AA.
AC   A0A0V1NNU2;
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:KRZ85695.1};
GN   Name=Arhgef12 {ECO:0000313|EMBL:KRZ85695.1};
GN   ORFNames=T08_3365 {ECO:0000313|EMBL:KRZ85695.1};
OS   Trichinella sp. T8.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=92180 {ECO:0000313|EMBL:KRZ85695.1, ECO:0000313|Proteomes:UP000054924};
RN   [1] {ECO:0000313|EMBL:KRZ85695.1, ECO:0000313|Proteomes:UP000054924}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS272 {ECO:0000313|EMBL:KRZ85695.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-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:KRZ85695.1}.
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DR   EMBL; JYDM01000135; KRZ85695.1; -; Genomic_DNA.
DR   STRING; 92180.A0A0V1NNU2; -.
DR   Proteomes; UP000054924; 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   SMART; SM00213; UBQ; 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:UP000054924};
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          785..971
FT                   /note="DH"
FT                   /evidence="ECO:0000259|PROSITE:PS50010"
FT   DOMAIN          1013..1128
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          1551..1623
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50053"
FT   REGION          85..130
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          216..244
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          656..725
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1133..1156
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        656..678
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        679..705
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        706..725
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1141..1155
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1713 AA;  194388 MW;  BF40BBFADB4D8FA7 CRC64;
     MHFHGEHFAE ERNVLIKRDE NGYGLTVCGN NPVFVQSVRE GSAAAKAGVH VGECIIKVNG
     VTVTSLDHLE VVKLISVAPY TTLTLSGGPS SSSAASSMGN DHYEKRDRCL ERRSTENAIR
     PNSKKKQSEW HLKRKKIIQQ ILTEEKRQLQ VMLKGSDAHA DADQRIIEKM TRRIHNLEDQ
     LNEVEKLDFE QVELFYKNLI YQENISLSNS GFRSHSDDLS SSLTMKSSKS HSDDVVASSS
     TDDERLLTKS GNIDEIRDHQ IPVPVSEVPP ESPLLVHTLS MSNECDSAAV ELNSSSFDEP
     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 SQSMNIEEES YRGARRRSSD TSRRSHSDAD KTESLTRIST TESSTTVSVQ
     DVSRERSPMI SELDSPLTSS VSFSNTLHDI HIELDSDFKV ENEIPLLEDL LDLESFQYLD
     KREKNRLEVI YELFHTEQTH VRNLKILYRL FYKQLLNFNV ISFEFASLLF SNLEDVLNLH
     VEMNEAMKNM MQNNKLIGDI SIMMLQFDGK ERMRNIDSLH CQKLQSAIEA LKHRVVKDQK
     LREFLQVVES LPVCRKLQLK DMLPMEMQRL TKYPLLLENV LKYTEDPSEE ADRLRTCIEC
     SRSILESVNS AKRNAENVLR LQRLQQMLDT TQFDKVNHPI VSEFCPLDVR RFSLIHEGPL
     IWRLNKSKIV DLHVVLLDEI LLLLSPTSDG HLALRFHNIN ISCGKDEVKW THCPLLKLNS
     LIAKDVATDK KAFFLVSTSP SGPQIYELAT QSKAEKQNWF KFIVEQIEAS KEHEQKTSVR
     HGQAGQESKS GDSFYEIPNS ARKKSLTVRS QRTMKNPNFD ERVRVTCQPR LISPSEINIC
     QPTVFQHSKP ILNPLEKLKQ EDKLVIRLLN EKLQIISSFF GQKNDLPPSS AVDSRTSREA
     REFVISAIKQ KSQDLYIFVL ANRLLEAINE QTRLIEMENF ENGSVKYQVP EVECPSVPCY
     QLTQIAAGLM TCLTNLLHSL QIMGDDLKRV QRELHQYKLS PERLLPFPEK ICQAVGTDIP
     TDVTHEAACR KSLTDAAVQT EPASFLQTNN CDAVKKNAGK STENFHTDDQ PTELSGRSII
     KDALPTGSCN TAASEKPILR NGKMGTDGLC LFDTDIAKLE EQPCSEIITK SKNFSNVLHL
     QNFTWKEIFQ NNHSDVAFHF LNCCSVMLCV FVREVLVQFW QTVKKLEIEA MQIFVRSGRL
     IALNIESNCT IGEIKKQIQE EEESLCSSYL VLGGRPLEDD WTLAQCNIQE FSTLDLSYRL
     LGGAKKRKKK MYTTPKKIKH KKKKVKLAVL KYYKIDENGK VSRLRKECTS ESCGAGVFMA
     NHYNRQYCGK CYCTMVVQDP VQREQKPGKG KGH
//
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