ID A0A3Q1I5G6_ANATE Unreviewed; 1735 AA.
AC A0A3Q1I5G6;
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 (GEF) 28a {ECO:0000313|Ensembl:ENSATEP00000015405.1};
GN Name=ARHGEF28 {ECO:0000313|Ensembl:ENSATEP00000015405.1};
OS Anabas testudineus (Climbing perch) (Anthias testudineus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000015405.1, ECO:0000313|Proteomes:UP000265040};
RN [1] {ECO:0000313|Ensembl:ENSATEP00000015405.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR Ensembl; ENSATET00000015648.2; ENSATEP00000015405.1; ENSATEG00000010673.2.
DR GeneTree; ENSGT00940000155831; -.
DR Proteomes; UP000265040; 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; 1.25.40.20; Ankyrin repeat-containing domain; 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; IPR036770; Ankyrin_rpt-contain_sf.
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; 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 Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000265040};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 698..745
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 892..1089
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 1131..1233
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 319..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 504..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 579..623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 676..700
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 782..851
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1335..1381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1443..1476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1694..1735
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 600..622
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 681..699
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 795..851
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1335..1352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1362..1381
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1443..1471
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1735 AA; 195301 MW; C9A326174BA309A2 CRC64;
MEVNRREVPL YGQVEALVRL QATAPEDAEF YVLVQGTRLT HVTAAKIGDD GLNLCFTVPG
HDLAEVVSVT PYFYAEDQVK PCEGETCLKY IKDVAQEAAE YMSARRDQLG PQSYQEVLKR
FPIWTQGDEE VSAGELNHIE QDVCIGQSSG EARLKQLDEK ITQAMANMDH PQQWKNTDSQ
SREAAEQHPK ETLLHLAVRL GLVHLSRFLI HQPRGQRALT LPNQEGDTPL QLAQKAGQHA
MFRVLAAPPG PVVGPVPGVW CVWSDSCCML RFCSCTDSLS LTVRQGSSSC PQDAIMVLRD
RLGDHNILKL ISVLRTDSDG DKRRDEVGSS NEGRSKERVE EQVLVDNVFE EQLVLSLDDD
EEDYPSSLSV NGHPMQSGRL QSPITQCAPD PPLSMISSSD QTVTQQLEDV DIKYSISGVT
RDSTGTDSGL WDTVDSEDLL QATDTPPPCS DVFCLPSVPS HPLSPVDQSL ARLNCPNFFE
TTNHRHSPTM DACDLSPSQV ALEVDSEEDG AEPKSPLSPL SSDEQSEAIR EAFHVSPNLT
CTRSQSASSA CEPTTKDLAD QGIRLRSYSY SSSKISLRPA RFGRDNHTSD ISPEQRASSI
SEQSHEKREI RFRKRAQSAD DEGSMELAES LQHLTLSEFL KEIEEEDLNN YNIPAKVESE
KYKVIRTFSF LKSRMSSTRN KAKGKGKDRE SKDRPPHGHR FLTGSCLGPT MCVVCDKPAS
GKDLLHCSVC TTIVHKGCKD SIPPCLKKLQ DKYSVTMVKN KTASLPQNFT VRDSTPQRVI
PISTSLPVMT PKEKKDAVTQ SSSLSRSFPN SDSRLSETSE TESDALKVTS QSEELLPTPT
SSTSTESSFG EDCVDTYTHS DVSADEDDYK AESWSLIVEH KFCKKQDKQT IKRQDVIYEL
MQTELHHLQT LHIMAEVFRR GMREEVQLDT EVVERVFPCL DQLILFHHAF FTAMKERRQT
SAEPRGHRNY LIQRIGDILL HQFSDENGEK MKQVYGDFCS RHTEAVSFFK ELQQHNKRFQ
NFIKQQGNNS LVRRREIPEC ILLVTQRITK YPVLLERILQ YTQEETEEHA DLSKSLTQIR
EVIAAVDLRV SENEQHQKLQ EVWNRMENRS SAKLKNGHTF RKQDMMGPGQ ILKYQGVLLW
KTATGRLKDV MALLLTDTLI FLQEKDQKYT FATVDQKPPV IALQKLIVRQ VANEERGMFL
ISASAAGPEM YEVHTSSKEE RNTWMRLIRE AVESCPEEEE EYTSESEEEK RAAEARVQKI
YKLQESLMSQ DQQICSSLEE KLHIYTELSG LSGRTDPSLV EPRLLVQPDS EELPQAAVLL
AAALQEAENL KATLSSKTCL PSSDSPETDT PDSVFPVSPA PLVDTLSNSS EASPEIPDAN
ENSWTENLAL QSPTNLQKAD TNDIDCKVAQ SVQSLTQLLY SLQAAVTIQD SCYEVQKLLL
QETGRPSQSA PRQHLSSFRG STLQEQEKQR NLAQQLQERL HQEKERWEKE CQARESQQEE
QESKLEERER QCHLEAERLR RKREELDEQL EEYQQSLERL REGQRKVEME REHLKNQQKV
LQSWRNGQQK SLATGIPHMV ISLDGQQDSE LNESRDHAGN GSVFVNEAAF VSTSINNRHI
HHKRNDPSAH NCLNTLLARS NSRQSPTANA PHSQGWVMGT GCLFSPGGRL GMQHLSTDHN
SHSYIGETWS STASRADPYP VLPHPSDSQL DLSAPVSLET DSGGEEGREE TIVYL
//
