Full text data of ARF5
ARF5
[Confidence: low (only semi-automatic identification from reviews)]
ADP-ribosylation factor 5
Note: presumably soluble (membrane word is not in UniProt keywords or features)
ADP-ribosylation factor 5
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P84085
ID ARF5_HUMAN Reviewed; 180 AA.
AC P84085; P26437;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 2.
DT 22-JAN-2014, entry version 106.
DE RecName: Full=ADP-ribosylation factor 5;
GN Name=ARF5;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1993656;
RA Tsuchiya M., Price S.R., Tsai S.-C., Moss J., Vaughan M.;
RT "Molecular identification of ADP-ribosylation factor mRNAs and their
RT expression in mammalian cells.";
RL J. Biol. Chem. 266:2772-2777(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=9169151; DOI=10.1006/geno.1997.4689;
RA McGuire R.E., Daiger S.P., Green E.D.;
RT "Localization and characterization of the human ADP-ribosylation
RT factor 5 (ARF5) gene.";
RL Genomics 41:481-484(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
RT "cDNA clones of human proteins involved in signal transduction
RT sequenced by the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, and Skin;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP INTERACTION WITH ASAP2.
RX PubMed=10022920;
RA Andreev J., Simon J.-P., Sabatini D.D., Kam J., Plowman G.,
RA Randazzo P.A., Schlessinger J.;
RT "Identification of a new Pyk2 target protein with Arf-GAP activity.";
RL Mol. Cell. Biol. 19:2338-2350(1999).
RN [7]
RP INTERACTION WITH RAB11FIP3 AND RAB11FIP4.
RX PubMed=17030804; DOI=10.1073/pnas.0605357103;
RA Shiba T., Koga H., Shin H.-W., Kawasaki M., Kato R., Nakayama K.,
RA Wakatsuki S.;
RT "Structural basis for Rab11-dependent membrane recruitment of a family
RT of Rab11-interacting protein 3 (FIP3)/Arfophilin-1.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15416-15421(2006).
RN [8]
RP INTERACTION WITH NCS1, AND SUBCELLULAR LOCATION.
RX PubMed=17555535; DOI=10.1111/j.1600-0854.2007.00594.x;
RA Haynes L.P., Sherwood M.W., Dolman N.J., Burgoyne R.D.;
RT "Specificity, promiscuity and localization of ARF protein interactions
RT with NCS-1 and phosphatidylinositol-4 kinase-III beta.";
RL Traffic 8:1080-1092(2007).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS) OF 8-180 IN COMPLEX WITH GDP.
RG Structural genomics consortium (SGC);
RT "Structure of human ADP-ribosylation factor 5.";
RL Submitted (AUG-2007) to the PDB data bank.
CC -!- FUNCTION: GTP-binding protein that functions as an allosteric
CC activator of the cholera toxin catalytic subunit, an ADP-
CC ribosyltransferase. Involved in protein trafficking; may modulate
CC vesicle budding and uncoating within the Golgi apparatus.
CC -!- SUBUNIT: Binds ASAP2. Interacts with NCS1/FREQ at the Golgi
CC complex. Interacts with RAB11FIP3 and RAB11FIP4.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus. Cytoplasm, perinuclear
CC region.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; M57567; AAA90927.1; -; mRNA.
DR EMBL; U73002; AAC51299.1; -; Genomic_DNA.
DR EMBL; AF493884; AAM12598.1; -; mRNA.
DR EMBL; BT007087; AAP35750.1; -; mRNA.
DR EMBL; BC003043; AAH03043.1; -; mRNA.
DR EMBL; BC033104; AAH33104.1; -; mRNA.
DR PIR; A23741; A23741.
DR RefSeq; NP_001653.1; NM_001662.3.
DR UniGene; Hs.653202; -.
DR PDB; 2B6H; X-ray; 1.76 A; A=8-179.
DR PDBsum; 2B6H; -.
DR ProteinModelPortal; P84085; -.
DR SMR; P84085; 7-180.
DR IntAct; P84085; 2.
DR MINT; MINT-4825056; -.
DR STRING; 9606.ENSP00000000233; -.
DR ChEMBL; CHEMBL5986; -.
DR PhosphoSite; P84085; -.
DR DMDM; 51316990; -.
DR PeptideAtlas; P84085; -.
DR PRIDE; P84085; -.
DR DNASU; 381; -.
DR Ensembl; ENST00000000233; ENSP00000000233; ENSG00000004059.
DR GeneID; 381; -.
DR KEGG; hsa:381; -.
DR UCSC; uc003vmb.2; human.
DR CTD; 381; -.
DR GeneCards; GC07P127228; -.
DR HGNC; HGNC:658; ARF5.
DR MIM; 103188; gene.
DR neXtProt; NX_P84085; -.
DR PharmGKB; PA24941; -.
DR eggNOG; COG1100; -.
DR HOGENOM; HOG000163691; -.
DR HOVERGEN; HBG002073; -.
DR InParanoid; P84085; -.
DR KO; K07940; -.
DR OMA; MVQEDEL; -.
DR OrthoDB; EOG77WWDV; -.
DR PhylomeDB; P84085; -.
DR ChiTaRS; ARF5; human.
DR EvolutionaryTrace; P84085; -.
DR GeneWiki; ARF5; -.
DR GenomeRNAi; 381; -.
DR NextBio; 1595; -.
DR PRO; PR:P84085; -.
DR ArrayExpress; P84085; -.
DR Bgee; P84085; -.
DR CleanEx; HS_ARF5; -.
DR Genevestigator; P84085; -.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; TAS:ProtInc.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR024156; Small_GTPase_ARF.
DR InterPro; IPR006689; Small_GTPase_ARF/SAR.
DR Pfam; PF00025; Arf; 1.
DR PRINTS; PR00328; SAR1GTPBP.
DR SMART; SM00177; ARF; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51417; ARF; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Cytoplasm; ER-Golgi transport;
KW Golgi apparatus; GTP-binding; Lipoprotein; Myristate;
KW Nucleotide-binding; Protein transport; Reference proteome; Transport.
FT INIT_MET 1 1 Removed (Potential).
FT CHAIN 2 180 ADP-ribosylation factor 5.
FT /FTId=PRO_0000207396.
FT NP_BIND 24 31 GTP.
FT NP_BIND 67 71 GTP.
FT NP_BIND 126 129 GTP.
FT LIPID 2 2 N-myristoyl glycine (Potential).
FT HELIX 8 11
FT TURN 12 15
FT STRAND 18 25
FT HELIX 30 37
FT STRAND 43 48
FT STRAND 51 58
FT STRAND 61 67
FT HELIX 78 83
FT STRAND 87 93
FT HELIX 97 99
FT HELIX 100 111
FT HELIX 114 116
FT STRAND 120 126
FT HELIX 136 142
FT HELIX 145 147
FT STRAND 153 157
FT TURN 160 163
FT HELIX 166 176
FT TURN 177 179
SQ SEQUENCE 180 AA; 20530 MW; 25EF3D4895408147 CRC64;
MGLTVSALFS RIFGKKQMRI LMVGLDAAGK TTILYKLKLG EIVTTIPTIG FNVETVEYKN
ICFTVWDVGG QDKIRPLWRH YFQNTQGLIF VVDSNDRERV QESADELQKM LQEDELRDAV
LLVFANKQDM PNAMPVSELT DKLGLQHLRS RTWYVQATCA TQGTGLYDGL DWLSHELSKR
//
ID ARF5_HUMAN Reviewed; 180 AA.
AC P84085; P26437;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 2.
DT 22-JAN-2014, entry version 106.
DE RecName: Full=ADP-ribosylation factor 5;
GN Name=ARF5;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1993656;
RA Tsuchiya M., Price S.R., Tsai S.-C., Moss J., Vaughan M.;
RT "Molecular identification of ADP-ribosylation factor mRNAs and their
RT expression in mammalian cells.";
RL J. Biol. Chem. 266:2772-2777(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=9169151; DOI=10.1006/geno.1997.4689;
RA McGuire R.E., Daiger S.P., Green E.D.;
RT "Localization and characterization of the human ADP-ribosylation
RT factor 5 (ARF5) gene.";
RL Genomics 41:481-484(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
RT "cDNA clones of human proteins involved in signal transduction
RT sequenced by the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, and Skin;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP INTERACTION WITH ASAP2.
RX PubMed=10022920;
RA Andreev J., Simon J.-P., Sabatini D.D., Kam J., Plowman G.,
RA Randazzo P.A., Schlessinger J.;
RT "Identification of a new Pyk2 target protein with Arf-GAP activity.";
RL Mol. Cell. Biol. 19:2338-2350(1999).
RN [7]
RP INTERACTION WITH RAB11FIP3 AND RAB11FIP4.
RX PubMed=17030804; DOI=10.1073/pnas.0605357103;
RA Shiba T., Koga H., Shin H.-W., Kawasaki M., Kato R., Nakayama K.,
RA Wakatsuki S.;
RT "Structural basis for Rab11-dependent membrane recruitment of a family
RT of Rab11-interacting protein 3 (FIP3)/Arfophilin-1.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15416-15421(2006).
RN [8]
RP INTERACTION WITH NCS1, AND SUBCELLULAR LOCATION.
RX PubMed=17555535; DOI=10.1111/j.1600-0854.2007.00594.x;
RA Haynes L.P., Sherwood M.W., Dolman N.J., Burgoyne R.D.;
RT "Specificity, promiscuity and localization of ARF protein interactions
RT with NCS-1 and phosphatidylinositol-4 kinase-III beta.";
RL Traffic 8:1080-1092(2007).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS) OF 8-180 IN COMPLEX WITH GDP.
RG Structural genomics consortium (SGC);
RT "Structure of human ADP-ribosylation factor 5.";
RL Submitted (AUG-2007) to the PDB data bank.
CC -!- FUNCTION: GTP-binding protein that functions as an allosteric
CC activator of the cholera toxin catalytic subunit, an ADP-
CC ribosyltransferase. Involved in protein trafficking; may modulate
CC vesicle budding and uncoating within the Golgi apparatus.
CC -!- SUBUNIT: Binds ASAP2. Interacts with NCS1/FREQ at the Golgi
CC complex. Interacts with RAB11FIP3 and RAB11FIP4.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus. Cytoplasm, perinuclear
CC region.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; M57567; AAA90927.1; -; mRNA.
DR EMBL; U73002; AAC51299.1; -; Genomic_DNA.
DR EMBL; AF493884; AAM12598.1; -; mRNA.
DR EMBL; BT007087; AAP35750.1; -; mRNA.
DR EMBL; BC003043; AAH03043.1; -; mRNA.
DR EMBL; BC033104; AAH33104.1; -; mRNA.
DR PIR; A23741; A23741.
DR RefSeq; NP_001653.1; NM_001662.3.
DR UniGene; Hs.653202; -.
DR PDB; 2B6H; X-ray; 1.76 A; A=8-179.
DR PDBsum; 2B6H; -.
DR ProteinModelPortal; P84085; -.
DR SMR; P84085; 7-180.
DR IntAct; P84085; 2.
DR MINT; MINT-4825056; -.
DR STRING; 9606.ENSP00000000233; -.
DR ChEMBL; CHEMBL5986; -.
DR PhosphoSite; P84085; -.
DR DMDM; 51316990; -.
DR PeptideAtlas; P84085; -.
DR PRIDE; P84085; -.
DR DNASU; 381; -.
DR Ensembl; ENST00000000233; ENSP00000000233; ENSG00000004059.
DR GeneID; 381; -.
DR KEGG; hsa:381; -.
DR UCSC; uc003vmb.2; human.
DR CTD; 381; -.
DR GeneCards; GC07P127228; -.
DR HGNC; HGNC:658; ARF5.
DR MIM; 103188; gene.
DR neXtProt; NX_P84085; -.
DR PharmGKB; PA24941; -.
DR eggNOG; COG1100; -.
DR HOGENOM; HOG000163691; -.
DR HOVERGEN; HBG002073; -.
DR InParanoid; P84085; -.
DR KO; K07940; -.
DR OMA; MVQEDEL; -.
DR OrthoDB; EOG77WWDV; -.
DR PhylomeDB; P84085; -.
DR ChiTaRS; ARF5; human.
DR EvolutionaryTrace; P84085; -.
DR GeneWiki; ARF5; -.
DR GenomeRNAi; 381; -.
DR NextBio; 1595; -.
DR PRO; PR:P84085; -.
DR ArrayExpress; P84085; -.
DR Bgee; P84085; -.
DR CleanEx; HS_ARF5; -.
DR Genevestigator; P84085; -.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; TAS:ProtInc.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR024156; Small_GTPase_ARF.
DR InterPro; IPR006689; Small_GTPase_ARF/SAR.
DR Pfam; PF00025; Arf; 1.
DR PRINTS; PR00328; SAR1GTPBP.
DR SMART; SM00177; ARF; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51417; ARF; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Cytoplasm; ER-Golgi transport;
KW Golgi apparatus; GTP-binding; Lipoprotein; Myristate;
KW Nucleotide-binding; Protein transport; Reference proteome; Transport.
FT INIT_MET 1 1 Removed (Potential).
FT CHAIN 2 180 ADP-ribosylation factor 5.
FT /FTId=PRO_0000207396.
FT NP_BIND 24 31 GTP.
FT NP_BIND 67 71 GTP.
FT NP_BIND 126 129 GTP.
FT LIPID 2 2 N-myristoyl glycine (Potential).
FT HELIX 8 11
FT TURN 12 15
FT STRAND 18 25
FT HELIX 30 37
FT STRAND 43 48
FT STRAND 51 58
FT STRAND 61 67
FT HELIX 78 83
FT STRAND 87 93
FT HELIX 97 99
FT HELIX 100 111
FT HELIX 114 116
FT STRAND 120 126
FT HELIX 136 142
FT HELIX 145 147
FT STRAND 153 157
FT TURN 160 163
FT HELIX 166 176
FT TURN 177 179
SQ SEQUENCE 180 AA; 20530 MW; 25EF3D4895408147 CRC64;
MGLTVSALFS RIFGKKQMRI LMVGLDAAGK TTILYKLKLG EIVTTIPTIG FNVETVEYKN
ICFTVWDVGG QDKIRPLWRH YFQNTQGLIF VVDSNDRERV QESADELQKM LQEDELRDAV
LLVFANKQDM PNAMPVSELT DKLGLQHLRS RTWYVQATCA TQGTGLYDGL DWLSHELSKR
//
MIM
103188
*RECORD*
*FIELD* NO
103188
*FIELD* TI
*103188 ADP-RIBOSYLATION FACTOR 5; ARF5
*FIELD* TX
DESCRIPTION
ADP-ribosylation factors (ARFs) are guanine nucleotide-binding proteins,
read moreapproximately 20 kD in size, that serve as GTP-dependent allosteric
activators of cholera toxin ADP-ribosyltransferase activity (summary by
Tsuchiya et al., 1991).
CLONING
To the 4 species of mammalian ARF, termed ARF1-4, previously identified
by cloning, Tsuchiya et al. (1991) added new ARF-like genes, ARF5 and 6
(600464), encoding proteins of 180 and 175 amino acids, respectively.
Both proteins contain consensus sequences believed to be involved in
guanine nucleotide binding and GTP hydrolysis. ARF5 was more similar in
deduced amino acid sequence to ARF4, which also has 180 amino acids.
GENE STRUCTURE
McGuire et al. (1997) determined that the ARF5 gene contains 6 coding
exons spanning approximately 3.2 kb of genomic DNA.
MAPPING
McGuire et al. (1997) mapped the ARF5 gene to a YAC contig on chromosome
7q31.3.
*FIELD* RF
1. McGuire, R. E.; Daiger, S. P.; Green, E. D.: Localization and
characterization of the human ADP-ribosylation factor 5 (ARF5) gene. Genomics 41:
481-484, 1997.
2. Tsuchiya, M.; Price, S. R.; Tsai, S.-C.; Moss, J.; Vaughan, M.
: Molecular identification of ADP-ribosylation factor mRNAs and their
expression in mammalian cells. J. Biol. Chem. 266: 2772-2777, 1991.
*FIELD* CN
Carol A. Bocchini - updated: 4/23/1999
*FIELD* CD
Victor A. McKusick: 6/17/1994
*FIELD* ED
carol: 05/22/2012
terry: 4/26/1999
carol: 4/23/1999
dkim: 6/26/1998
mark: 3/23/1995
jason: 6/17/1994
*RECORD*
*FIELD* NO
103188
*FIELD* TI
*103188 ADP-RIBOSYLATION FACTOR 5; ARF5
*FIELD* TX
DESCRIPTION
ADP-ribosylation factors (ARFs) are guanine nucleotide-binding proteins,
read moreapproximately 20 kD in size, that serve as GTP-dependent allosteric
activators of cholera toxin ADP-ribosyltransferase activity (summary by
Tsuchiya et al., 1991).
CLONING
To the 4 species of mammalian ARF, termed ARF1-4, previously identified
by cloning, Tsuchiya et al. (1991) added new ARF-like genes, ARF5 and 6
(600464), encoding proteins of 180 and 175 amino acids, respectively.
Both proteins contain consensus sequences believed to be involved in
guanine nucleotide binding and GTP hydrolysis. ARF5 was more similar in
deduced amino acid sequence to ARF4, which also has 180 amino acids.
GENE STRUCTURE
McGuire et al. (1997) determined that the ARF5 gene contains 6 coding
exons spanning approximately 3.2 kb of genomic DNA.
MAPPING
McGuire et al. (1997) mapped the ARF5 gene to a YAC contig on chromosome
7q31.3.
*FIELD* RF
1. McGuire, R. E.; Daiger, S. P.; Green, E. D.: Localization and
characterization of the human ADP-ribosylation factor 5 (ARF5) gene. Genomics 41:
481-484, 1997.
2. Tsuchiya, M.; Price, S. R.; Tsai, S.-C.; Moss, J.; Vaughan, M.
: Molecular identification of ADP-ribosylation factor mRNAs and their
expression in mammalian cells. J. Biol. Chem. 266: 2772-2777, 1991.
*FIELD* CN
Carol A. Bocchini - updated: 4/23/1999
*FIELD* CD
Victor A. McKusick: 6/17/1994
*FIELD* ED
carol: 05/22/2012
terry: 4/26/1999
carol: 4/23/1999
dkim: 6/26/1998
mark: 3/23/1995
jason: 6/17/1994