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Database: UniProt
Entry: A0A2D0Q9X1_ICTPU
LinkDB: A0A2D0Q9X1_ICTPU
Original site: A0A2D0Q9X1_ICTPU 
ID   A0A2D0Q9X1_ICTPU        Unreviewed;      1458 AA.
AC   A0A2D0Q9X1;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Rho guanine nucleotide exchange factor 12 isoform X3 {ECO:0000313|RefSeq:XP_017315493.1};
GN   Name=arhgef12b {ECO:0000313|RefSeq:XP_017315493.1};
OS   Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC   Ictaluridae; Ictalurus.
OX   NCBI_TaxID=7998 {ECO:0000313|RefSeq:XP_017315493.1};
RN   [1] {ECO:0000313|RefSeq:XP_017315493.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_017315493.1};
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_017315493.1; XM_017460004.3.
DR   STRING; 7998.ENSIPUP00000034002; -.
DR   GeneID; 108260059; -.
DR   CTD; 571031; -.
DR   OrthoDB; 2875542at2759; -.
DR   Proteomes; UP000221080; Chromosome 28.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   CDD; cd00992; PDZ_signaling; 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; 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; 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};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT   DOMAIN          66..143
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          782..972
FT                   /note="DH"
FT                   /evidence="ECO:0000259|PROSITE:PS50010"
FT   DOMAIN          1014..1127
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          26..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          146..198
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          224..319
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          610..736
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1126..1229
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1286..1349
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1364..1388
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        31..52
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        161..189
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        265..286
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        610..673
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        711..731
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1132..1151
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1158..1181
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1210..1229
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1286..1304
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1458 AA;  162748 MW;  4590BB3B0B0E9EB8 CRC64;
     MHRSDAEARS TCIGLRRWIT IRFPKKPTRP GSILNKDHPP DKKPKSEKVS VPPTHDFDPT
     GLVQRCVIIQ KDENGFGLTV SGDNPVFVQL VKEDGAAMRA GVQTGDRIIK VNGTLVTHSN
     HVEVVELIKS GSYVALTVLG RPPGLPQIPL SEGEGDGDPL SSLSSPHSPG PTVAERSSSS
     STSPSDRITS PLPAWAMKEE YGRNPTARLL KDIQEAQKHI PLLQGQLGKA TTAGQDGLLS
     RRPGEGDSEE GGGLGDVDAS PSWHFDSESP VNSNSTPVTP SMIPESPYQR DTPCHSPKPM
     PRFSLNSCPS PDGEDAVDLD SSYQCSAGSP LSRLPPPIIG AEDDDFDTEQ EQVNGQCSCF
     QTMELLKSRP AHLAVFLHHV VSQFDPAPLL CYLYAELYKQ SNPKETRRIY GELHSTFMDR
     SAQLKVAVPD SISADMERWK PDLIPEDVQR QHVQHLQDTF LPDIQKHLED FRQKRSMGLT
     LAEAELSRLD SERVRDRAAL EKERSCSEHI ITRINEVLLT TSATEEEKCT AMQFVIQAYM
     KHLGVKVKES RGFEPKPKLI NLLPKIKKTI KPEKDGGVEV LKKSRFQIMR SHNKRPSRTD
     VSSITKALEQ NKQRTQKQLS QNALAPTEQP EAPSAGRIRS SQSSDGPDGS PGSINSPTFS
     ASPVQSSDST ARELEPGATP LSALPRLGEV GPQAEGQDSS SSGTHFDFTY PPDHLQEEEP
     ETDRNPDGGT PRPIRRMEPL CTGEVQSEDD QAFEVEPEQD PPHWQTLVST EVLALLSPHE
     IKRQEVINEL FYTERAHLRM LKVLDNVFYQ RMTRESILPP ADIKNIFTNL EEIVQLHVSI
     TEQMTAIRKK YETAVVDLIG DDLLSWFSGT EEEKIKRAVG TFCSNQPFAL ELIKSRQKKD
     QRFAAFVQEA ESNRQCRRLQ LKDMIPVEMQ RLTKYPLLLE NIAKYTDDTE EKSKVKRACE
     CCRQILNHVN QEVKEAENKQ RLEDYQRRLD LSSLKQSEYP MIAEFKNLNL TKRKMVHEGP
     LSWKVNKDKT IELYTLLLED ILVLLQRQDE KLILKCHSKN LAGTAETKHI FSPIIKLSTV
     LVRSVATDNK SFFVVSMSDY GAQIYELMAQ TVSEQKTWHD LIGQRADSMK SLPQNDGERE
     ADDEMNSGMP KMSKDPDRIS TGSVQSPEKD ATSSTEIMQI PPAGSNPFDT KSEDEEEAEG
     EHLPQVQDEV QDEVQDEVQD EAEEDEEEAF LDPELADRLP FLKQRSRHAI AVEEKDLDTF
     DLPPLMADEA LRTLAALRQL LINHMDGQED VDRDRERGEA RLRELKAGSL QGSEENAAPG
     GSVENGAERT ETAHVKSENR LELPSGDTGF FETSEDFGSY MVLEGYGGSG ESSTDDDGQV
     CSTEPAAAGD SGIDLKKLLS SVSSQSRGPN FSRQIMTHLR LLQANLQHLK DVESKYNQLC
     QRHSEQAATE SEENKDKS
//
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