ID A0A3Q2C6C8_CYPVA Unreviewed; 1737 AA.
AC A0A3Q2C6C8;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Rho guanine nucleotide exchange factor 28 {ECO:0000313|Ensembl:ENSCVAP00000000137.1};
OS Cyprinodon variegatus (Sheepshead minnow).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Cyprinodontidae;
OC Cyprinodon.
OX NCBI_TaxID=28743 {ECO:0000313|Ensembl:ENSCVAP00000000137.1, ECO:0000313|Proteomes:UP000265020};
RN [1] {ECO:0000313|Ensembl:ENSCVAP00000000137.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR Ensembl; ENSCVAT00000015578.1; ENSCVAP00000000137.1; ENSCVAG00000001016.1.
DR GeneTree; ENSGT00940000155831; -.
DR Proteomes; UP000265020; Unplaced.
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:0048468; P:cell development; IEA:UniProt.
DR CDD; cd20876; C1_p190RhoGEF; 1.
DR CDD; cd14680; PH_p190RhoGEF; 1.
DR CDD; cd00160; RhoGEF; 1.
DR Gene3D; 3.30.60.20; -; 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 InterPro; IPR037819; ARHGEF28_PH.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR041020; PH_16.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR13944; AGAP007712-PA; 1.
DR PANTHER; PTHR13944:SF22; RHO GUANINE NUCLEOTIDE EXCHANGE FACTOR 28; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF17838; PH_16; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000265020};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 717..764
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 913..1110
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 1152..1254
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 408..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 460..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 490..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 560..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 607..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 692..718
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 800..867
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1363..1391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1473..1574
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 509..524
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..540
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..640
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 700..716
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 819..867
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1737 AA; 196245 MW; 253FFEE73670413A CRC64;
MSTLLISPFQ VIPERYLDDI HCFFASHLSE LILDIGFSST GHDLVEVVSV TAYISTNDGF
YPYACKSFLE YSKDVAQDAA EYLSGKWDRF GPHRYQEVLR RFPVLAQTAD EEDCGRLLQC
REGETLLGGS SADDTDLRHL DENITLALAN MDYPQQWKNT DTEPGEGAED HLKETLLHLA
VRLHLVHLAR FLIHQTRGQR LLSLPDEGGE APIQLAHSNA LHSTLRDLAV PSGAAINPLP
GVFCLWADSS CMLRVCPRTE SVFLTQRQSP DMRHQDSIMV LRERLEDPRV CREINILRDA
AGEHKRRRNE AHLIKQRDTK ELNVDGNALL DNVFEDQPTL FLIDTDSEEE TSSSLSVNVH
LKQSTEVQNQ FSQRASDPSL SMINGNDQTF AQHTQACEED IKFRVDDVTS DSTNTDGSLW
DPEDLLLATD TPPPHSHLRE LPASLPSSLS LSPVDQALTR LIRRPSTEPN SHRDSPTMET
CDISLVALEV DSEEEPPEPK SLLSRLFSDV GKSEEKKETR RPNPDLTCTR SQSASACEPN
SKDLSEEGVR LRSYSYSHSK FCPSRSNRDN HTSEGSPDGV LHSVSHSRSL LQALSLSKST
LSLSLLHPGK QRTSSISEPS HDKREVRFRK RAQSADDEGS VELAESLHHL TLSEFLKEIE
EEELEKCNIP NKAESEKYKV IRTFSFLKNR MSSTRNKSKV NKGKGKDREA KDRQLNGHRF
GAGPCLGPTV CVVCDKPASG KDLLHCSGCT AIVHKSCKES VPPCLKKLQD RHATTGIKSK
TASLPQNFIV RESPPHSVIP ISVSQPVLTP KERKDTVTHS GSLPGSLPNS DSLLSESSET
ESEALKPNSL SEELLPTPGS SASNESSFGE DCVDSYIHTY SDILADSADY EAESWSLTVE
HKFCKRQDKR AVKRQDVIYE LMQTELHHLQ TLHIMAEVFR RGMKEEVQLD TESVERVFPC
LDQLLVLHHA FFTAMKERRQ TSGQPQGHRN YLIQQIGDIL LHQFSEENGE KMKQVYGEFC
SHHNEAVSFF KDLLLHNKRF QSFVKQQGHN SLVRRREIPE CILLVTQRIT KYPVLLERIL
HYTQEETDEH GNISKALAHI REVIAAVDSR VSEYERHQRL QEVCNRMENR STAKLKSGRT
FRKQDMMGPG QTLRYQGVLL WKTATGRLKD VLALLLTDSL IFLQEKDQKY AFAAVDQKPP
VIALQKLIVR EVANEEKGMF LISASSAGPE MYEVHTSSKE ERNTWMRLIR EAVESCPEET
EGSASESEEE KRAAEVRFQK ILKLQESLTS QDQQICSSLE EKLQIYTELS ALSGRMEAVS
AEPRLLVQMQ SEELPQAAGL LAAALQEAEN LKAALSSKAR SLSSHSQDSD SMFPVSPDAL
ADPTFEENGG SLTDAFESQS AADLQKRDGS CIDFKAAESV QTLTQLLYSL QAAVTIQDTC
YEVQRLLLQA SEHTSPRSHC LPLHGLRSNT LQEQEKQRNL EKRKEEVAAA QRLRERLRQE
KERWERECQA RESQQVEQES KLEEREKKCQ LAAEKLRRER QELEEQLEEY QQSLERLREG
QRSVERERER LEDQHKLLQA WKHGRQSSLP AVIPHMVIPL DVQQASPPYN SRRHAGNGSV
FVNEAAYAGD SFNNRHVHHK RNDPNAHNSF NSLLDRSNRQ YPVVSNPLGS GYIYSPIGRL
QHSTSDHSYN GETWMSTADL NPQLTHPSEH QLELNTLVSL ETDSDQEDGR EETIVFL
//
