CYH4_HUMAN
ID CYH4_HUMAN Reviewed; 394 AA.
AC Q9UIA0; Q5R3F9; Q9UGT6;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Cytohesin-4;
DE AltName: Full=PH, SEC7 and coiled-coil domain-containing protein 4;
GN Name=CYTH4; Synonyms=CYT4, PSCD4;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=10652308; DOI=10.1074/jbc.275.5.3221;
RA Ogasawara M., Kim S.C., Adamik R., Togawa A., Ferrans V.J., Takeda K.,
RA Kirby M., Moss J., Vaughan M.;
RT "Similarities in function and gene structure of cytohesin-4 and cytohesin-
RT 1, guanine nucleotide-exchange proteins for ADP-ribosylation factors.";
RL J. Biol. Chem. 275:3221-3230(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RA Liu D., Zhang H., Lu J.;
RT "cDNA cloning and genomic organization of cytohesin-4.";
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Blood;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=17398095; DOI=10.1016/j.cub.2007.03.007;
RA Hofmann I., Thompson A., Sanderson C.M., Munro S.;
RT "The Arl4 family of small G proteins can recruit the cytohesin Arf6
RT exchange factors to the plasma membrane.";
RL Curr. Biol. 17:711-716(2007).
CC -!- FUNCTION: Promotes guanine-nucleotide exchange on ARF1 and ARF5.
CC Promotes the activation of ARF factors through replacement of GDP with
CC GTP. {ECO:0000269|PubMed:10652308}.
CC -!- INTERACTION:
CC Q9UIA0; Q8NA61-2: CBY2; NbExp=3; IntAct=EBI-11521003, EBI-11524851;
CC Q9UIA0; Q96HB5: CCDC120; NbExp=8; IntAct=EBI-11521003, EBI-744556;
CC Q9UIA0; Q8NCU1: CCDC197; NbExp=3; IntAct=EBI-11521003, EBI-750686;
CC Q9UIA0; Q4G0X9-5: CCDC40; NbExp=3; IntAct=EBI-11521003, EBI-11943297;
CC Q9UIA0; Q16204: CCDC6; NbExp=3; IntAct=EBI-11521003, EBI-1045350;
CC Q9UIA0; Q969H4: CNKSR1; NbExp=4; IntAct=EBI-11521003, EBI-741671;
CC Q9UIA0; P78358: CTAG1B; NbExp=3; IntAct=EBI-11521003, EBI-1188472;
CC Q9UIA0; Q9UHG0: DCDC2; NbExp=3; IntAct=EBI-11521003, EBI-10303987;
CC Q9UIA0; P53539: FOSB; NbExp=3; IntAct=EBI-11521003, EBI-2806743;
CC Q9UIA0; Q96ED9-2: HOOK2; NbExp=3; IntAct=EBI-11521003, EBI-10961706;
CC Q9UIA0; Q8WWN9: IPCEF1; NbExp=6; IntAct=EBI-11521003, EBI-4401965;
CC Q9UIA0; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-11521003, EBI-2556193;
CC Q9UIA0; Q86T90: KIAA1328; NbExp=3; IntAct=EBI-11521003, EBI-3437878;
CC Q9UIA0; P08779: KRT16; NbExp=3; IntAct=EBI-11521003, EBI-356410;
CC Q9UIA0; O76011: KRT34; NbExp=3; IntAct=EBI-11521003, EBI-1047093;
CC Q9UIA0; Q15154-3: PCM1; NbExp=3; IntAct=EBI-11521003, EBI-11742977;
CC Q9UIA0; P20618: PSMB1; NbExp=3; IntAct=EBI-11521003, EBI-372273;
CC Q9UIA0; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-11521003, EBI-739895;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17398095};
CC Peripheral membrane protein {ECO:0000269|PubMed:17398095}.
CC -!- TISSUE SPECIFICITY: Expressed predominantly in peripheral blood
CC leukocytes. {ECO:0000269|PubMed:10652308}.
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; AF125349; AAF28896.1; -; mRNA.
DR EMBL; AF075458; AAF15389.1; -; mRNA.
DR EMBL; CR456551; CAG30437.1; -; mRNA.
DR EMBL; Z94160; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC041161; AAH41161.1; -; mRNA.
DR CCDS; CCDS13946.1; -.
DR RefSeq; NP_001304953.1; NM_001318024.1.
DR RefSeq; NP_037517.1; NM_013385.4.
DR AlphaFoldDB; Q9UIA0; -.
DR SMR; Q9UIA0; -.
DR BioGRID; 118019; 40.
DR IntAct; Q9UIA0; 23.
DR MINT; Q9UIA0; -.
DR STRING; 9606.ENSP00000248901; -.
DR iPTMnet; Q9UIA0; -.
DR PhosphoSitePlus; Q9UIA0; -.
DR BioMuta; CYTH4; -.
DR DMDM; 13124094; -.
DR jPOST; Q9UIA0; -.
DR MassIVE; Q9UIA0; -.
DR MaxQB; Q9UIA0; -.
DR PaxDb; Q9UIA0; -.
DR PeptideAtlas; Q9UIA0; -.
DR PRIDE; Q9UIA0; -.
DR ProteomicsDB; 84482; -.
DR Antibodypedia; 25912; 196 antibodies from 25 providers.
DR DNASU; 27128; -.
DR Ensembl; ENST00000248901.11; ENSP00000248901.6; ENSG00000100055.21.
DR GeneID; 27128; -.
DR KEGG; hsa:27128; -.
DR MANE-Select; ENST00000248901.11; ENSP00000248901.6; NM_013385.5; NP_037517.1.
DR UCSC; uc003arf.4; human.
DR CTD; 27128; -.
DR DisGeNET; 27128; -.
DR GeneCards; CYTH4; -.
DR HGNC; HGNC:9505; CYTH4.
DR HPA; ENSG00000100055; Tissue enhanced (bone marrow, lymphoid tissue).
DR MIM; 606514; gene.
DR neXtProt; NX_Q9UIA0; -.
DR OpenTargets; ENSG00000100055; -.
DR PharmGKB; PA164718621; -.
DR VEuPathDB; HostDB:ENSG00000100055; -.
DR eggNOG; KOG0930; Eukaryota.
DR GeneTree; ENSGT00940000160865; -.
DR HOGENOM; CLU_032820_3_0_1; -.
DR InParanoid; Q9UIA0; -.
DR OMA; MLNTGLH; -.
DR OrthoDB; 657055at2759; -.
DR PhylomeDB; Q9UIA0; -.
DR TreeFam; TF352091; -.
DR PathwayCommons; Q9UIA0; -.
DR Reactome; R-HSA-6811438; Intra-Golgi traffic.
DR SignaLink; Q9UIA0; -.
DR BioGRID-ORCS; 27128; 13 hits in 1070 CRISPR screens.
DR ChiTaRS; CYTH4; human.
DR GeneWiki; CYTH4; -.
DR GenomeRNAi; 27128; -.
DR Pharos; Q9UIA0; Tbio.
DR PRO; PR:Q9UIA0; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q9UIA0; protein.
DR Bgee; ENSG00000100055; Expressed in granulocyte and 139 other tissues.
DR ExpressionAtlas; Q9UIA0; baseline and differential.
DR Genevisible; Q9UIA0; HS.
DR GO; GO:0034451; C:centriolar satellite; IDA:HPA.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0045171; C:intercellular bridge; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA: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..394
FT /note="Cytohesin-4"
FT /id="PRO_0000120203"
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..394
FT /note="C-terminal autoinhibitory region"
FT /evidence="ECO:0000250"
FT COILED 12..65
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"
FT VARIANT 74
FT /note="M -> V (in dbSNP:rs16998061)"
FT /id="VAR_051920"
SQ SEQUENCE 394 AA; 45672 MW; 0C9C8E8AD6890F34 CRC64;
MDLCHPEPAE LSSGETEELQ RIKWHRKQLL EDIQKLKDEI ADVFAQIDCF ESAEESRMAQ
KEKELCIGRK KFNMDPAKGI QYFIEHKLLT PDVQDIARFL YKGEGLNKTA IGTYLGERDP
INLQVLQAFV DCHEFANLNL VQALRQFLWS FRLPGEAQKI DRMMEAFATR YCLCNPGVFQ
STDTCYVLSF SIIMLNTSLH NPNVRDRPPF ERFVSMNRGI NNGSDLPEDQ LRNLFDSIKS
EPFSIPEDDG NDLTHTFFNP DREGWLLKLG GRVKTWKRRW FILTDNCLYY FEFTTDKEPR
GIIPLENLSV QKVDDPKKPF CLELYNPSCR GQKIKACKTD GDGRVVEGKH ESYRISATSA
EERDQWIESI RASITRVPFY DLVSTRKKKI ASKQ
