CYH3_RAT
ID CYH3_RAT Reviewed; 400 AA.
AC P97696;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Cytohesin-3;
DE AltName: Full=PH, SEC7 and coiled-coil domain-containing protein 3;
DE AltName: Full=SEC7 homolog C;
DE Short=rSec7-3;
GN Name=Cyth3; Synonyms=Pscd3, Sec7c;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9352219;
RA Telemenakis I., Benseler F., Stenius K., Suedhof T.C., Brose N.;
RT "Rat homologues of yeast sec7p.";
RL Eur. J. Cell Biol. 74:143-149(1997).
RN [2]
RP DEVELOPMENTAL STAGE.
RX PubMed=11834294; DOI=10.1016/s0169-328x(01)00312-6;
RA Suzuki I., Owada Y., Suzuki R., Yoshimoto T., Kondo H.;
RT "Localization of mRNAs for subfamily of guanine nucleotide-exchange
RT proteins (GEP) for ARFs (ADP-ribosylation factors) in the brain of
RT developing and mature rats under normal and postaxotomy conditions.";
RL Brain Res. Mol. Brain Res. 98:41-50(2002).
CC -!- FUNCTION: Promotes guanine-nucleotide exchange on ARF1. Promotes the
CC activation of ARF factors through replacement of GDP with GTP (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with TAMALIN. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Cell membrane;
CC Peripheral membrane protein. Note=Translocates from the cytosol to
CC membranes enriched in phosphatidylinositol 3,4,5-trisphosphate.
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Present in all tissues tested, with highest protein
CC levels in brain and adrenal.
CC -!- DEVELOPMENTAL STAGE: On embryonic days 15 (E15) and E18, expressed in
CC the cortical plate of the cerebrum. On postnatal days 0 (P0) and P7, a
CC moderate expression is seen in the cerebral neocortex, hippocampal
CC pyramidal and dentate granule cell layers. In the cerebellum, expressed
CC in the cerebellar Purkinje cells. On P14, a decreased expression is
CC seen throughout the brain. On P21, expression is seen in the cerebellar
CC Purkinje cells, dentate granule cells and the hippocampal pyramidal
CC cells. {ECO:0000269|PubMed:11834294}.
CC -!- DOMAIN: Binds via its PH domain to the inositol head group of
CC phosphatidylinositol 3,4,5-trisphosphate. {ECO:0000250}.
CC -!- DOMAIN: Autoinhibited by its C-terminal basic region. {ECO:0000250}.
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DR EMBL; U83897; AAB41445.1; -; mRNA.
DR AlphaFoldDB; P97696; -.
DR BMRB; P97696; -.
DR SMR; P97696; -.
DR IntAct; P97696; 1.
DR MINT; P97696; -.
DR STRING; 10116.ENSRNOP00000001412; -.
DR BindingDB; P97696; -.
DR ChEMBL; CHEMBL1914274; -.
DR jPOST; P97696; -.
DR PaxDb; P97696; -.
DR PRIDE; P97696; -.
DR RGD; 620399; Cyth3.
DR eggNOG; KOG0930; Eukaryota.
DR InParanoid; P97696; -.
DR PhylomeDB; P97696; -.
DR Reactome; R-RNO-6811438; Intra-Golgi traffic.
DR PRO; PR:P97696; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005912; C:adherens junction; ISO:RGD.
DR GO; GO:0005923; C:bicellular tight junction; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0001726; C:ruffle; ISO:RGD.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; ISS:UniProtKB.
DR GO; GO:0090162; P:establishment of epithelial cell polarity; ISO:RGD.
DR GO; GO:0048193; P:Golgi vesicle transport; ISS:UniProtKB.
DR GO; GO:0045785; P:positive regulation of cell adhesion; ISO:RGD.
DR GO; GO:0032012; P:regulation of ARF protein signal transduction; IEA:InterPro.
DR CDD; cd00171; Sec7; 1.
DR Gene3D; 1.10.1000.11; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR023394; Sec7_C_sf.
DR InterPro; IPR000904; Sec7_dom.
DR InterPro; IPR035999; Sec7_dom_sf.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF01369; Sec7; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00222; Sec7; 1.
DR SUPFAM; SSF48425; SSF48425; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50190; SEC7; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Coiled coil; Cytoplasm; Guanine-nucleotide releasing factor;
KW Lipid-binding; Membrane; Reference proteome.
FT CHAIN 1..400
FT /note="Cytohesin-3"
FT /id="PRO_0000120202"
FT DOMAIN 77..206
FT /note="SEC7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00189"
FT DOMAIN 265..381
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 392..400
FT /note="C-terminal autoinhibitory region"
FT /evidence="ECO:0000250"
FT COILED 14..61
FT /evidence="ECO:0000255"
FT BINDING 273..281
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3,4,5-trisphosphate)"
FT /ligand_id="ChEBI:CHEBI:57836"
FT /evidence="ECO:0000250"
FT BINDING 285
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3,4,5-trisphosphate)"
FT /ligand_id="ChEBI:CHEBI:57836"
FT /evidence="ECO:0000250"
FT BINDING 296
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3,4,5-trisphosphate)"
FT /ligand_id="ChEBI:CHEBI:57836"
FT /evidence="ECO:0000250"
FT BINDING 306
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3,4,5-trisphosphate)"
FT /ligand_id="ChEBI:CHEBI:57836"
FT /evidence="ECO:0000250"
FT BINDING 355
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3,4,5-trisphosphate)"
FT /ligand_id="ChEBI:CHEBI:57836"
FT /evidence="ECO:0000250"
SQ SEQUENCE 400 AA; 46337 MW; C8C19A2B611CB828 CRC64;
MDEGGGGEGG SVPEDLSLEE REELLDIRRR KKELIDDIER LKYEIAEVMT EIDNLTSVEE
SKTTQRNKQI AMGRKKFNMD PKKGIQFLIE NDLLQSSPED VAQFLYKGEG LNKTVIGDYL
GERDDFNIKV LQAFVELHEF ADLNLVQALR QFLWSFRLPG EAQKIDRMME AFASRYCLCN
PGVFQSTDTC YVLSFAIIML NTSLHNHNVR DKPTAERFIT MNRGINEGGD LPEELLRNLY
ESIKNEPFKI PEDDGNDLTH TFFNPDREGW LLKLGGGRVK TWKRRWFILT DNCLYYFEYT
TDKEPRGIIP LENLSIREVE DPRKPNCFEL YNPSHKGQVI KACKTEADGR VVEGNHVVYR
ISAPSPEEKE EWMKSIKASI SRDPFYDMLA TRKRRIANKK
