CYH1_CHLAE
ID CYH1_CHLAE Reviewed; 398 AA.
AC Q76MZ1;
DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Cytohesin-1;
DE AltName: Full=PH, SEC7 and coiled-coil domain-containing protein 1;
GN Name=CYTH1; Synonyms=PSCD1;
OS Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Chlorocebus.
OX NCBI_TaxID=9534;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Kim H.-S.;
RT "Identification and characterization of cytohesin-1 gene in the African
RT green monkey (Cercopithecus aethiops): alternative splicing of mRNA
RT transcript, sequence and phylogeny.";
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
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. Interacts (via N-terminal domain) with
CC INAVA (via N-terminal domain) (By similarity).
CC {ECO:0000250|UniProtKB:Q15438, ECO:0000250|UniProtKB:Q9QX11}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q15438};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:Q15438}. 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 -!- 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; AB022021; BAA87918.1; -; mRNA.
DR AlphaFoldDB; Q76MZ1; -.
DR SMR; Q76MZ1; -.
DR GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
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:0005085; F:guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
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 Acetylation; Cell junction; Cell membrane; Coiled coil; Cytoplasm;
KW Guanine-nucleotide releasing factor; Lipid-binding; Membrane;
KW Tight junction; Ubl conjugation.
FT CHAIN 1..398
FT /note="Cytohesin-1"
FT /id="PRO_0000120193"
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"
SQ SEQUENCE 398 AA; 46413 MW; 067FEE0FEA7A4C86 CRC64;
MEEDDSYVPS DLTAEERQEL ENIRRRKQEL LADIQRLKDE IAEVANEIEN LGSTEERKNM
QRNKQVAMGR KKFNMDPKKG IQFLIENDLL KNTCEDIAQF LYKGEGLNKT AIGDYLGERD
EFNIQVLHAF VELHEFTDLN LVQALRQFLW SFRLPGEAQK IDRMMEAFAQ RYCQCNNGVF
QSTDTCYVLS FAIIMLNTSL HNPNVKDKPT VERFIAMNRG INDGGDLPEE LLRNLYESIK
NEPFKIPEDD GNDLTHTFFN PDREGWLLKL GGGRVKTWKR RWFILTDNCL YYFEYTTDKE
PRGIIPLENL SIREVEDSKK PNCFELYIPD NKDQVIKACK TEADGRVVEG NHTVYRISAP
TPEEKEEWIK CIKAAISRDP FYEMLAARKK KVSSTKRH
