ID A0A3Q2C6E3_CYPVA Unreviewed; 1724 AA.
AC A0A3Q2C6E3;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Rho guanine nucleotide exchange factor 28 {ECO:0000313|Ensembl:ENSCVAP00000000133.1};
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:ENSCVAP00000000133.1, ECO:0000313|Proteomes:UP000265020};
RN [1] {ECO:0000313|Ensembl:ENSCVAP00000000133.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR Ensembl; ENSCVAT00000015581.1; ENSCVAP00000000133.1; ENSCVAG00000001016.1.
DR GeneTree; ENSGT00940000155831; -.
DR OMA; NDINTHS; -.
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 704..751
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 900..1097
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 1139..1241
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 427..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 479..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 509..567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 579..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 679..705
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 787..854
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1350..1378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1460..1561
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 528..543
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 544..559
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 603..628
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..703
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 806..854
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1724 AA; 194915 MW; ED52602150CEBBDF CRC64;
MEVNRKEVPL YGQVDGSILL QETAPEDGEF YVVAQGSRLT HVTTAKRGCD EHTLNFTVPG
HDLVEVVSVT AYISTNDGFY PYACKSFLEY SKDVAQDAAE YLSGKWDRFG PHRYQEVLRR
FPVLAQTADE EDCGRLLQCR EGETLLGGSS ADDTDLRHLD ENITLALANM DYPQQWKNTD
TEPGEGAEDH LKETLLHLAV RLHLVHLARF LIHQTRGQRL LSLPDEGGEA PIQLAHSNAL
HSTLRDLAVP SGAAINPLPG VFCLWADSSC MLRVCPRTES VFLTQRQSPD MRHQDSIMVL
RERLEDPRVC REINILRDAA GEHKRRRNEA HLIKQRDTKE LNVDGNALLD NVFEDQPTLF
LIDTDSEEET SSSLSVNVHL KQSTEVQNQF SQRASDPSLS MINGNDQTFA QHTQACEEDI
KFRVDDVTSD STNTDGSLWD PEDLLLATDT PPPHSHLREL PASLPSSLSL SPVDQALTRL
IRRPSTEPNS HRDSPTMETC DISLVALEVD SEEEPPEPKS LLSRLFSDVG KSEEKKETRR
PNPDLTCTRS QSASACEPNS KDLSEEGVRL RSYSYSHSKF CPSRSNRDNH TSEGSPEQRT
SSISEPSHDK REVRFRKRAQ SADDEGSVEL AESLHHLTLS EFLKEIEEEE LEKCNIPNKA
ESEKYKVIRT FSFLKNRMSS TRNKSKVNKG KGKDREAKDR QLNGHRFGAG PCLGPTVCVV
CDKPASGKDL LHCSGCTAIV HKSCKESVPP CLKKLQDRHA TTGIKSKTAS LPQNFIVRES
PPHSVIPISV SQPVLTPKER KDTVTHSGSL PGSLPNSDSL LSESSETESE ALKPNSLSEE
LLPTPGSSAS NESSFGEDCV DSYIHTYSDI LADSADYEAE SWSLTVEHKF CKRQDKRAVK
RQDVIYELMQ TELHHLQTLH IMAEVFRRGM KEEVQLDTES VERVFPCLDQ LLVLHHAFFT
AMKERRQTSG QPQGHRNYLI QQIGDILLHQ FSEENGEKMK QVYGEFCSHH NEAVSFFKDL
LLHNKRFQSF VKQQGHNSLV RRREIPECIL LVTQRITKYP VLLERILHYT QEETDEHGNI
SKALAHIREV IAAVDSRVSE YERHQRLQEV CNRMENRSTA KLKSGRTFRK QDMMGPGQTL
RYQGVLLWKT ATGRLKDVLA LLLTDSLIFL QEKDQKYAFA AVDQKPPVIA LQKLIVREVA
NEEKGMFLIS ASSAGPEMYE VHTSSKEERN TWMRLIREAV ESCPEETEGS ASESEEEKRA
AEVRFQKILK LQESLTSQDQ QICSSLEEKL QIYTELSALS GRMEAVSAEP RLLVQMQSEE
LPQAAGLLAA ALQEAENLKA ALSSKARSLS SHSQDSDSMF PVSPDALADP TFEENGGSLT
DAFESQSAAD LQKRDGSCID FKAAESVQTL TQLLYSLQAA VTIQDTCYEV QRLLLQASEH
TSPRSHCLPL HGLRSNTLQE QEKQRNLEKR KEEVAAAQRL RERLRQEKER WERECQARES
QQVEQESKLE EREKKCQLAA EKLRRERQEL EEQLEEYQQS LERLREGQRS VERERERLED
QHKLLQAWKH GRQSSLPAVI PHMVIPLDVQ QASPPYNSRR HAGNGSVFVN EAAYAGDSFN
NRHVHHKRND PNAHNSFNSL LDRSNRQYPV VSNPLGSGYI YSPIGRLQHS TSDHSYNGET
WMSTADLNPQ LTHPSEHQLE LNTLVSLETD SDQEDGREET IVFL
//
