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Database: UniProt
Entry: A0A2K6SKP2_SAIBB
LinkDB: A0A2K6SKP2_SAIBB
Original site: A0A2K6SKP2_SAIBB 
ID   A0A2K6SKP2_SAIBB        Unreviewed;      1543 AA.
AC   A0A2K6SKP2;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Rho guanine nucleotide exchange factor 12 {ECO:0000313|Ensembl:ENSSBOP00000007952.1};
GN   Name=ARHGEF12 {ECO:0000313|Ensembl:ENSSBOP00000007952.1};
OS   Saimiri boliviensis boliviensis (Bolivian squirrel monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC   Saimiriinae; Saimiri.
OX   NCBI_TaxID=39432 {ECO:0000313|Ensembl:ENSSBOP00000007952.1, ECO:0000313|Proteomes:UP000233220};
RN   [1] {ECO:0000313|Ensembl:ENSSBOP00000007952.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC       Membrane {ECO:0000256|ARBA:ARBA00004370}.
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DR   RefSeq; XP_003923639.1; XM_003923590.2.
DR   STRING; 39432.ENSSBOP00000007952; -.
DR   Ensembl; ENSSBOT00000024710.1; ENSSBOP00000007952.1; ENSSBOG00000020565.1.
DR   GeneID; 101040423; -.
DR   KEGG; sbq:101040423; -.
DR   CTD; 23365; -.
DR   GeneTree; ENSGT00940000157662; -.
DR   OMA; QSEYPMI; -.
DR   OrthoDB; 2875542at2759; -.
DR   Proteomes; UP000233220; 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:Ensembl.
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:Ensembl.
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};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233220}.
FT   DOMAIN          72..136
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          786..976
FT                   /note="DH"
FT                   /evidence="ECO:0000259|PROSITE:PS50010"
FT   DOMAIN          1018..1131
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          247..346
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          577..612
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          624..708
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1136..1202
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        13..60
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        250..264
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        310..329
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        577..596
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        634..691
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1181..1202
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1543 AA;  173123 MW;  8A2CA85E3CAFF4C1 CRC64;
     MSGTQSTITD RFPLKKPIRH GSILNRESPT DKKQKVERIA SHDFDPTDSS SKKTKSSSEE
     SRSEIYGLVQ RCVIIQKDDN GFGLTVSGDN PVFVQSVKED GAAMRAGVQT GDRIIKVNGT
     LVTHSNHLEV VKLIKSGSYV ALTVQGRPPG SPQIPLADSE VEPSVIGHMS PIMTSPHSPG
     ASGNMERITS PVLMGEENNV VHNQKVEILR KMLQKEQERL QLLQEDYNRT PAQRLLKEIQ
     EAKKHIPQLQ EQLSKATGSA QDGAVVTPSR PLGDTLTVSE AEADPGDGLG RTDCSSGDAS
     RPSSDNADSP KSGPKERIYL EENPEKSETI QDTDTQSLVG SPSTRIAPHI IGAEDDDFGT
     EHEQINGQCS CFQSIELLKS RPAHLAVFLH HVVSQFDPAT LLCYLYSDLY KHTNSKETRR
     IFLEFHQFFL DRSAHLKVSV PDEMSVDLEK RRPELIPEDL HRHYIQTMQE RVHPEVQRHL
     EDFRQKRSMG LTLAESELTK LDAERDKDRL TLEKERTCAE QIVAKIEEVL MTAQAVEEDK
     SSTMQYVILM YMKHLGVKVK EPRNLEHKRG RIGFLPKIKQ SMKKDKEGEE KGKRRGFPSI
     LGPPRRPSRH DNSAIGRAME LQKARHPKHL STPLSVSPEP QDSAKLRQSG LANEGTDTGY
     LPASMSSLAS GASFSQEGGK ENDTGSKQVG ETPAPGDTLD GTPRTLNTVF DFPTPPLDQV
     QEEECEVERV TEHGTPKPFR KFDSVAFGES QSEDEQFEND LETDPPNWQQ LVSREVLLGL
     KPCEIKRQEV INELFYTERA HVRTLKVLDQ VFYQRVSREG ILSPSELRKI FSNLEDILQL
     HIGLNEQMKA VRKRNETSVI DQIGEDLLTW FSGPGEEKLK HAAATFCSNQ PFALEMIKSR
     QKKDSRFQTF VQDAESNPLC RRLQLKDIIP TQMQRLTKYP LLLDNIAKYT EWSTEREKVK
     KAADHCRQIL NYVNQAVKEA ENKQRLEDYQ RRLDTSSLKL SEYPNVEELR NLDLTKRKMI
     HEGPLVWKVN RDKTIDLYTL LLEDILVLLQ KQDDRLVLRC HSKILASTAD SKHTFSPVIK
     LNTVLVRQVA TDNKALFVIS MSDNGAQIYE LVAQTVSEKT VWQDLICRMA ASVKEQSTKP
     IPLPQSPPGE GDNDEEDPSK LKEEQHGISV TGLQSPDRDL GLESTLMSSK PQSHSLSTSG
     KSEVRDLFVA ERQFAKEQHP DGTLKETGED YQITIPDSHL PISEERWALD ALRNLGLLKQ
     LLVQQLGLAE KSTQEDWQHF PRYRTASQGA QTDTVIQNSE NIRAYHSSEG HLPFRTGTGD
     IATCYSPRTS TESSAPRDSV VLAPQDSQAS NILVMDHMIM TPEMPTTEPE GGLDDSGEHF
     FDAREAHSDE NPSEGDGVVN KEEKEINLRI SGNYLILDGY DTVQESSTDE EVASSLTLQP
     VTGISAVDST HQQQHSPQNA HSDGVVSPFT PEFLVQQRWG AMEDSCFEIQ SPSSCADSQS
     QIMEYIHKIE ADLEHLKKVE ESYTILCQRL AGSALTDKHS DKS
//
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