CYH4_MOUSE
ID CYH4_MOUSE Reviewed; 393 AA.
AC Q80YW0;
DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Cytohesin-4;
DE AltName: Full=PH, SEC7 and coiled-coil domain-containing protein 4;
GN Name=Cyth4; Synonyms=Pscd4;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Liu D., Zhang H., Lu J.;
RT "Mouse cytohesin-4, a novel Sec7 and PH domain containing and integrin
RT associated protein.";
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Promotes guanine-nucleotide exchange on ARF1 and ARF5.
CC Promotes the activation of ARF factors through replacement of GDP with
CC GTP (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF079972; AAD46734.1; -; mRNA.
DR CCDS; CCDS27620.1; -.
DR RefSeq; NP_082471.2; NM_028195.3.
DR AlphaFoldDB; Q80YW0; -.
DR SMR; Q80YW0; -.
DR BioGRID; 215305; 2.
DR STRING; 10090.ENSMUSP00000042698; -.
DR iPTMnet; Q80YW0; -.
DR PhosphoSitePlus; Q80YW0; -.
DR EPD; Q80YW0; -.
DR MaxQB; Q80YW0; -.
DR PaxDb; Q80YW0; -.
DR PRIDE; Q80YW0; -.
DR ProteomicsDB; 285444; -.
DR Antibodypedia; 25912; 196 antibodies from 25 providers.
DR DNASU; 72318; -.
DR Ensembl; ENSMUST00000043069; ENSMUSP00000042698; ENSMUSG00000018008.
DR GeneID; 72318; -.
DR KEGG; mmu:72318; -.
DR UCSC; uc007wps.2; mouse.
DR CTD; 27128; -.
DR MGI; MGI:2441702; Cyth4.
DR VEuPathDB; HostDB:ENSMUSG00000018008; -.
DR eggNOG; KOG0930; Eukaryota.
DR GeneTree; ENSGT00940000160865; -.
DR HOGENOM; CLU_032820_3_0_1; -.
DR InParanoid; Q80YW0; -.
DR OMA; MLNTGLH; -.
DR OrthoDB; 657055at2759; -.
DR PhylomeDB; Q80YW0; -.
DR TreeFam; TF352091; -.
DR Reactome; R-MMU-6811438; Intra-Golgi traffic.
DR BioGRID-ORCS; 72318; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Cyth4; mouse.
DR PRO; PR:Q80YW0; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q80YW0; protein.
DR Bgee; ENSMUSG00000018008; Expressed in granulocyte and 113 other tissues.
DR ExpressionAtlas; Q80YW0; baseline and differential.
DR Genevisible; Q80YW0; MM.
DR GO; GO:0034451; C:centriolar satellite; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0045171; C:intercellular bridge; ISO:MGI.
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: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 1: Evidence at protein level;
KW Cell membrane; Coiled coil; Guanine-nucleotide releasing factor;
KW Lipid-binding; Membrane; Reference proteome.
FT CHAIN 1..393
FT /note="Cytohesin-4"
FT /id="PRO_0000120204"
FT DOMAIN 54..241
FT /note="SEC7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00189"
FT DOMAIN 259..375
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 386..393
FT /note="C-terminal autoinhibitory region"
FT /evidence="ECO:0000250"
FT COILED 13..56
FT /evidence="ECO:0000255"
FT BINDING 268..275
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 279
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 290
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 300
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 393 AA; 45285 MW; A021643E86DC57A8 CRC64;
MDVCHTDPAE LSSGEAKELQ QIKWHRKQLL EDIQKLKDEI ADVFAQIDCF ESTEESRMAQ
KEKEMCIGRK KFNMDPNKGI QYLIEHKLLT SDVQDIAQFL YKGDGLNKTA IGTYLGEKDP
INLQVLQAFV DCHEFANLNL VQALRQFLWS FRLPGEAQKI DRMMEAFAAR YCLCNPGVFR
STDTCYVLSF SVIMLNTGLH NPNVRDRPPF ERFVTMNRGI NSGSDLPEEQ LRNLFDSIKS
EPFSIPEDDG GDLTHTFFNP DREGWLLKLG GRVKTWKRRW FILTDNCLYY FEFTTDKEPR
GIIPLENLSV QKVEDPKKPF CLELYNPSCR GQKIKACKTD GDGKVVEGKH ESYRISAANA
EERDQWIEAI RASITRVPFY DLLSARKKKI VGK
