CYH1_RAT
ID CYH1_RAT Reviewed; 398 AA.
AC P97694;
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-1;
DE AltName: Full=PH, SEC7 and coiled-coil domain-containing protein 1;
DE AltName: Full=SEC7 homolog A;
DE Short=rSec7-1;
GN Name=Cyth1; Synonyms=Pscd1, Sec7a;
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 CHARACTERIZATION, AND MUTAGENESIS OF GLU-157.
RX PubMed=9927699; DOI=10.1073/pnas.96.3.1094;
RA Ashery U., Koch H., Scheuss V., Brose N., Rettig J.;
RT "A presynaptic role for the ADP ribosylation factor (ARF)-specific GDP/GTP
RT exchange factor msec7-1.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:1094-1099(1999).
RN [3]
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, ARF5 and ARF6.
CC Promotes the activation of ARF factors through replacement of GDP with
CC GTP. Plays an important role in membrane trafficking, during junctional
CC remodeling and epithelial polarization, through regulation of ARF6
CC activity. {ECO:0000250|UniProtKB:Q9QX11}.
CC -!- SUBUNIT: Interacts with TRIM23 and CYTIP (By similarity). Interacts
CC (via coiled-coil domain) with FRMD4A (via coiled-coil domain) (By
CC similarity). Interacts with FRMD4B (By similarity). Found in a complex
CC with PARD3, CYTH1 and FRMD4A (By similarity). Interacts (via N-terminal
CC domain) with INAVA (via N-terminal domain) (By similarity).
CC {ECO:0000250|UniProtKB:Q15438, ECO:0000250|UniProtKB:Q9QX11}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9QX11};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:Q9QX11}. Cytoplasm,
CC cytosol {ECO:0000250|UniProtKB:Q9QX11}. Cell junction, tight junction
CC {ECO:0000250|UniProtKB:Q9QX11}. Cell junction, adherens junction
CC {ECO:0000250|UniProtKB:Q9QX11}. Note=Colocalized with TJP1 during
CC epithelial polarization. {ECO:0000250|UniProtKB:Q9QX11}.
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, expression is
CC seen in the mantle and ventricular germinal zones throughout the
CC neuraxis. On postnatal days 0 (P0) and P7, expression is seen in the
CC cerebral neocortex, olfactory mitral and granule cell layers,
CC hippocampal pyramidal and dentate granule cells and the striatum. A
CC lower expression is seen in gray matter in di-, mes- and met-encephali.
CC In the cerebellum, the expression is evident in the external and
CC internal granule cell layers and Purkinje cell layer. On P14, a
CC decreased expression is seen in the di-, mes- and met-encephali. On P21
CC and thereafter, expression is seen in the olfactory mitral and granule
CC cells, dentate granule cells and the cerebellar granule cells and
CC Purkinje 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.
CC {ECO:0000250|UniProtKB:Q9QX11}.
CC -!- PTM: Ubiquitinated by SCF(FBXW11) E3 ubiquitin-protein ligase complex.
CC Ubiquitination induces proteasomal degradation.
CC {ECO:0000250|UniProtKB:Q15438}.
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DR EMBL; U83895; AAB41443.1; -; mRNA.
DR RefSeq; NP_446362.1; NM_053910.1.
DR AlphaFoldDB; P97694; -.
DR SMR; P97694; -.
DR BioGRID; 250573; 1.
DR STRING; 10116.ENSRNOP00000004196; -.
DR iPTMnet; P97694; -.
DR PhosphoSitePlus; P97694; -.
DR jPOST; P97694; -.
DR PaxDb; P97694; -.
DR PRIDE; P97694; -.
DR Ensembl; ENSRNOT00000004196; ENSRNOP00000004196; ENSRNOG00000043381.
DR GeneID; 116691; -.
DR KEGG; rno:116691; -.
DR UCSC; RGD:620397; rat.
DR CTD; 9267; -.
DR RGD; 620397; Cyth1.
DR eggNOG; KOG0930; Eukaryota.
DR GeneTree; ENSGT00940000157519; -.
DR InParanoid; P97694; -.
DR OrthoDB; 657055at2759; -.
DR PhylomeDB; P97694; -.
DR Reactome; R-RNO-6811438; Intra-Golgi traffic.
DR PRO; PR:P97694; -.
DR Proteomes; UP000002494; Chromosome 10.
DR GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005923; C:bicellular tight junction; ISS:UniProtKB.
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:0098888; C:extrinsic component of presynaptic membrane; IDA:SynGO.
DR GO; GO:0031594; C:neuromuscular junction; IDA:SynGO.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0090162; P:establishment of epithelial cell polarity; ISS:UniProtKB.
DR GO; GO:0032012; P:regulation of ARF protein signal transduction; IEA:InterPro.
DR GO; GO:0030155; P:regulation of cell adhesion; ISO:RGD.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IDA:SynGO.
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 1: Evidence at protein level;
KW Acetylation; Cell junction; Cell membrane; Coiled coil; Cytoplasm;
KW Guanine-nucleotide releasing factor; Lipid-binding; Membrane;
KW Reference proteome; Tight junction; Ubl conjugation.
FT CHAIN 1..398
FT /note="Cytohesin-1"
FT /id="PRO_0000120196"
FT DOMAIN 73..202
FT /note="SEC7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00189"
FT DOMAIN 260..377
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 388..396
FT /note="C-terminal autoinhibitory region"
FT /evidence="ECO:0000250"
FT COILED 10..67
FT /evidence="ECO:0000255"
FT BINDING 269..277
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 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 292
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 302
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 351
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 MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q15438"
FT MUTAGEN 157
FT /note="E->K: Loss of ARF translocation."
FT /evidence="ECO:0000269|PubMed:9927699"
SQ SEQUENCE 398 AA; 46274 MW; 79E06E2364282E85 CRC64;
MEDDDSYVPS DLTAEERQEL ENIRRRKQEL LADIQRLKEE IAEVANEIES LGSTEERKNM
QRNKQVAMGR KKFNMDPKKG IQFLIENGLL KNTCEDIAQF LYKGEGLNKT AIGDYLGERD
EFSIQVLHAF VELHEFTDLN LVQALRQFLW SFRLPGEAQK IDRMMEAFAQ RYCQCNTGVF
QSTDTCYVLS FAIIMLNTSL HNPNVKDKPT VERFIAMNRG INDGGDLPEE LLRNLYESIK
NEPFKIPEDD GNDLTHTFFN PDREGWLLKL GGGRVKTWKR RWFILTDNCL YYFEYTTDKE
PRGIIPLENL SIREVEDSKK PNCFELYIPD NKDQVIKACK TEADGRVVEG NHTVYRISAP
TPEEKEDWIK CIKAAISRDP FYEMLAARKK KVSSTKRH
