ID A0A2D0QAD8_ICTPU Unreviewed; 1789 AA.
AC A0A2D0QAD8;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Rho guanine nucleotide exchange factor 28 isoform X1 {ECO:0000313|RefSeq:XP_017315254.1};
GN Name=arhgef28a {ECO:0000313|RefSeq:XP_017315254.1};
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_017315254.1};
RN [1] {ECO:0000313|RefSeq:XP_017315254.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_017315254.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR RefSeq; XP_017315254.1; XM_017459765.3.
DR Ensembl; ENSIPUT00000008742; ENSIPUP00000008377; ENSIPUG00000005745.
DR GeneID; 108259943; -.
DR KEGG; ipu:108259943; -.
DR CTD; 559941; -.
DR OMA; THIFIFQ; -.
DR OrthoDB; 2917157at2759; -.
DR Proteomes; UP000221080; Chromosome 28.
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 GO; GO:0007160; P:cell-matrix adhesion; IEA:Ensembl.
DR GO; GO:0007030; P:Golgi organization; IEA:Ensembl.
DR GO; GO:0060415; P:muscle tissue morphogenesis; IEA:Ensembl.
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; 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; PS00479; ZF_DAG_PE_1; 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 Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 759..806
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 955..1152
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 1193..1295
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 394..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 449..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 546..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 663..686
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1398..1459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1522..1541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1298..1328
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 395..418
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 561..613
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 663..684
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1398..1426
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1443..1459
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1789 AA; 202892 MW; 756B37B0F1467F3B CRC64;
MELNRDEVPV YGQVEVYAVL QDTQSIQEKA EYYVLLKGSH IHHVTKAQRK EKCHLLSFII
PGHNVAEKVS VRLYSWEDGN RCSQPAPMSE ELSLEYKWDT VQEVADLLIS DPDNLTSSMH
VDIQRKFCLV ESIQPGQNSL DVNEQHGTSR LDENLGLDQR LKLKTESGKH NPEENPGCWE
PDPGGCKLEP CSAIDVKITQ AVSNMYSLLE WNNQKTQESQ APRQMETPLH IAVRLGLYHL
TLFYLQQSGG QEMATLPNEE GHTPTELAQS RGHAATISAL ANLSACSEES PVWMSQIWAD
ESHLLRLCPL TTSFILTVKN RINFDPQRSI QLYREKHRYL ESHMQEVVLT EVEGKSRQNQ
TDDTSEGDLT SWTNIEDCVL LESVFEEQLV LSLDEDEENP TTYNSEKSCS PPGFSSPFQL
QSTDITAARL TAMLNRTGKN DDHRKYIATV PNNSSATDPQ PAVKVEGTRE QRPFSHPFLP
SFTQFSPTSS AGLVLDRFLR GSSHSEHNNH SASSPPESYE ISPSLVALEM DSEEEDDDLL
MKKPLPQISS ENKDNGDKQD RFNPSSGLSC TRCHSASSDC NHASQKDSAD QGVRLRSYSY
SSPKISLLSP RSSRDTPRPP ADLSHDGVFT NNSNGSRSLL QALSLSKSLS LLNPVKQRAL
SLTEQPQEKR ELRFRRRTQS ADDESSVELA DSLQHLTLSE FLKEIEEEGW DKYIIPSKTE
PEKYKVSRTF SFIKSRMYST RSKKGKAKEK EVKEKQGSGH QFAAGPVLGT SVCEVCDKPV
SGKETLHCTN CAVCIHKGCK DSAAQCLKKV QDKYAVSRMK ARAATLPQNF VLRESIPSSQ
ISTSASLPVV TQRDRRDTTP LPCPISRSVP LVPEWLAESP EGDTEFSSWR SHGQSEELLQ
TMESSTSTDS SLVEETVDAP LQNSFGTDTL YLEAESWSLA VETQFCQNQE KRTIKRQDVI
YELMQTELHH LQTLTIMAEV FRRGMREEVG LDAEAIGRIF PCLDELLVLH RDFLSAMTER
RNNSTQPDNE KNYLIHHVGD ILLQQFSQEN AENMKRVYGE FCSRHIEAVS FFKELQQQNK
RFQLFIKQQS SNLLVKRREI PECILLVTQR ITKYPVLLER ILQYTEEGTQ EHSDISGALS
LVRELISAVD LRVSEREQSQ WLSDVLGRME SKSLARLKSG AAFRKHDMTN GRTLLHHGPL
LWKTATGRLK DVLALLLTDL LIFLQEKDQK YIFATVDQKC PVISLQKLIV REVANEERGM
FLISASSSGP EMYEVHAATK DERKAWMRLI REAVEICHEK EEVTASESEE ERSAAEAKNQ
RIQKLQESLC SHDQLICSSL EEKLHIYAEL AAMVGHRDIS PEPKLLVCPN TEELPNAAVL
LNAALKEAEN LKEALSFHCN STSRPGPLPV SEEQKTSDTT TQLEATLPAP SPPPVPAEEE
PQAADAVRSE EEELREDSLE LQLRNQSSTT DNHNMYLKVC QSIQSLTQLL YSLQAVVTIQ
DSRYEVRRLL LLLLSSSAHQ RISQGSLQEQ ERQREAERRR QDLARAARER QRWARECQAQ
HLRYEERESE LAQREQRCHE EVQRLQRQRE ELEEQQQEYQ QSLERLREGQ RSVERERERL
EMQQRMMGKW RHERQHNLPV TSIKLEAHQG SGDETKNFHH GHHSGLDEDG SIFVNEAAFL
ATSMNNRRLH HYQHQYQHNT HLHPGYVNSP SAQNSLNSLL ALSNHTHPTI STQDELWTED
VGPAIHSTRT AGAVGPGIYQ GDALLVPQAF VSMETENQDP DGEEKIVYL
//
