Full text data of ATP6V1F
ATP6V1F
(ATP6S14, VATF)
[Confidence: low (only semi-automatic identification from reviews)]
V-type proton ATPase subunit F; V-ATPase subunit F (V-ATPase 14 kDa subunit; Vacuolar proton pump subunit F)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
V-type proton ATPase subunit F; V-ATPase subunit F (V-ATPase 14 kDa subunit; Vacuolar proton pump subunit F)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q16864
ID VATF_HUMAN Reviewed; 119 AA.
AC Q16864; C9J2K4; Q6IBA8;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 20-FEB-2007, sequence version 2.
DT 22-JAN-2014, entry version 121.
DE RecName: Full=V-type proton ATPase subunit F;
DE Short=V-ATPase subunit F;
DE AltName: Full=V-ATPase 14 kDa subunit;
DE AltName: Full=Vacuolar proton pump subunit F;
GN Name=ATP6V1F; Synonyms=ATP6S14, VATF;
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] (ISOFORM 1).
RC TISSUE=Fetal brain;
RX PubMed=8581736; DOI=10.1093/dnares/2.3.107;
RA Fujiwara T., Kawai A., Shimizu F., Hirano H., Okuno S., Takeda S.,
RA Ozaki K., Shimada Y., Nagata M., Watanabe T., Takaichi A.,
RA Nakamura Y., Shin S.;
RT "Cloning, sequencing and expression of a novel cDNA encoding human
RT vacuolar ATPase (14-kDa subunit).";
RL DNA Res. 2:107-111(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
RA Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
RA Waterston R.H., Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Lung adenocarcinoma;
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 [5]
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).
CC -!- FUNCTION: Subunit of the peripheral V1 complex of vacuolar ATPase
CC essential for assembly or catalytic function. V-ATPase is
CC responsible for acidifying a variety of intracellular compartments
CC in eukaryotic cells.
CC -!- SUBUNIT: V-ATPase is a heteromultimeric enzyme composed of a
CC peripheral catalytic V1 complex (components A to H) attached to an
CC integral membrane V0 proton pore complex (components: a, c, c',
CC c'' and d).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q16864-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q16864-2; Sequence=VSP_045952;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the V-ATPase F subunit 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; D49400; BAA08392.1; -; mRNA.
DR EMBL; CR456896; CAG33177.1; -; mRNA.
DR EMBL; AC025594; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC104230; AAI04231.1; -; mRNA.
DR EMBL; BC104231; AAI04232.1; -; mRNA.
DR EMBL; BC107854; AAI07855.1; -; mRNA.
DR EMBL; BU956696; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; JC4193; JC4193.
DR RefSeq; NP_001185838.1; NM_001198909.1.
DR RefSeq; NP_004222.2; NM_004231.3.
DR UniGene; Hs.78089; -.
DR ProteinModelPortal; Q16864; -.
DR SMR; Q16864; 7-91.
DR IntAct; Q16864; 1.
DR MINT; MINT-1426240; -.
DR STRING; 9606.ENSP00000249289; -.
DR TCDB; 3.A.2.2.4; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR PhosphoSite; Q16864; -.
DR DMDM; 126302612; -.
DR PaxDb; Q16864; -.
DR PeptideAtlas; Q16864; -.
DR PRIDE; Q16864; -.
DR Ensembl; ENST00000249289; ENSP00000249289; ENSG00000128524.
DR Ensembl; ENST00000492758; ENSP00000417378; ENSG00000128524.
DR GeneID; 9296; -.
DR KEGG; hsa:9296; -.
DR UCSC; uc022all.1; human.
DR CTD; 9296; -.
DR GeneCards; GC07P128502; -.
DR HGNC; HGNC:16832; ATP6V1F.
DR HPA; CAB009529; -.
DR MIM; 607160; gene.
DR neXtProt; NX_Q16864; -.
DR PharmGKB; PA38421; -.
DR eggNOG; COG1436; -.
DR HOGENOM; HOG000056545; -.
DR HOVERGEN; HBG004488; -.
DR InParanoid; Q16864; -.
DR KO; K02151; -.
DR OMA; RHVIDAH; -.
DR OrthoDB; EOG7JMGGM; -.
DR BioCyc; MetaCyc:HS05192-MONOMER; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_15518; Transmembrane transport of small molecules.
DR GeneWiki; ATP6V1F; -.
DR GenomeRNAi; 9296; -.
DR NextBio; 34831; -.
DR PRO; PR:Q16864; -.
DR ArrayExpress; Q16864; -.
DR Bgee; Q16864; -.
DR CleanEx; HS_ATP6V1F; -.
DR Genevestigator; Q16864; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0033180; C:proton-transporting V-type ATPase, V1 domain; IEA:InterPro.
DR GO; GO:0016471; C:vacuolar proton-transporting V-type ATPase complex; IDA:UniProtKB.
DR GO; GO:0042624; F:ATPase activity, uncoupled; NAS:UniProtKB.
DR GO; GO:0015078; F:hydrogen ion transmembrane transporter activity; NAS:UniProtKB.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro.
DR GO; GO:0006879; P:cellular iron ion homeostasis; TAS:Reactome.
DR GO; GO:0008286; P:insulin receptor signaling pathway; TAS:Reactome.
DR GO; GO:0051701; P:interaction with host; TAS:Reactome.
DR GO; GO:0090382; P:phagosome maturation; TAS:Reactome.
DR GO; GO:0033572; P:transferrin transport; TAS:Reactome.
DR Gene3D; 3.40.50.10580; -; 1.
DR InterPro; IPR008218; ATPase_V1-cplx_f_g_su.
DR InterPro; IPR005772; ATPase_V1-cplx_fsu_euk.
DR PANTHER; PTHR13861; PTHR13861; 1.
DR Pfam; PF01990; ATP-synt_F; 1.
DR PIRSF; PIRSF015945; ATPase_V1_F_euk; 1.
DR TIGRFAMs; TIGR01101; V_ATP_synt_F; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Hydrogen ion transport;
KW Ion transport; Polymorphism; Reference proteome; Transport.
FT CHAIN 1 119 V-type proton ATPase subunit F.
FT /FTId=PRO_0000144799.
FT VAR_SEQ 52 52 F -> FRSLGSLPGSVVEANPNQRDPPLWDEIDS (in
FT isoform 2).
FT /FTId=VSP_045952.
FT VARIANT 24 24 G -> V (in dbSNP:rs10958).
FT /FTId=VAR_048348.
FT CONFLICT 8 8 I -> T (in Ref. 1; BAA08392).
SQ SEQUENCE 119 AA; 13370 MW; 9FE5A8BD249A85FA CRC64;
MAGRGKLIAV IGDEDTVTGF LLGGIGELNK NRHPNFLVVE KDTTINEIED TFRQFLNRDD
IGIILINQYI AEMVRHALDA HQQSIPAVLE IPSKEHPYDA AKDSILRRAR GMFTAEDLR
//
ID VATF_HUMAN Reviewed; 119 AA.
AC Q16864; C9J2K4; Q6IBA8;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 20-FEB-2007, sequence version 2.
DT 22-JAN-2014, entry version 121.
DE RecName: Full=V-type proton ATPase subunit F;
DE Short=V-ATPase subunit F;
DE AltName: Full=V-ATPase 14 kDa subunit;
DE AltName: Full=Vacuolar proton pump subunit F;
GN Name=ATP6V1F; Synonyms=ATP6S14, VATF;
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] (ISOFORM 1).
RC TISSUE=Fetal brain;
RX PubMed=8581736; DOI=10.1093/dnares/2.3.107;
RA Fujiwara T., Kawai A., Shimizu F., Hirano H., Okuno S., Takeda S.,
RA Ozaki K., Shimada Y., Nagata M., Watanabe T., Takaichi A.,
RA Nakamura Y., Shin S.;
RT "Cloning, sequencing and expression of a novel cDNA encoding human
RT vacuolar ATPase (14-kDa subunit).";
RL DNA Res. 2:107-111(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
RA Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
RA Waterston R.H., Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Lung adenocarcinoma;
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 [5]
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).
CC -!- FUNCTION: Subunit of the peripheral V1 complex of vacuolar ATPase
CC essential for assembly or catalytic function. V-ATPase is
CC responsible for acidifying a variety of intracellular compartments
CC in eukaryotic cells.
CC -!- SUBUNIT: V-ATPase is a heteromultimeric enzyme composed of a
CC peripheral catalytic V1 complex (components A to H) attached to an
CC integral membrane V0 proton pore complex (components: a, c, c',
CC c'' and d).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q16864-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q16864-2; Sequence=VSP_045952;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the V-ATPase F subunit 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; D49400; BAA08392.1; -; mRNA.
DR EMBL; CR456896; CAG33177.1; -; mRNA.
DR EMBL; AC025594; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC104230; AAI04231.1; -; mRNA.
DR EMBL; BC104231; AAI04232.1; -; mRNA.
DR EMBL; BC107854; AAI07855.1; -; mRNA.
DR EMBL; BU956696; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; JC4193; JC4193.
DR RefSeq; NP_001185838.1; NM_001198909.1.
DR RefSeq; NP_004222.2; NM_004231.3.
DR UniGene; Hs.78089; -.
DR ProteinModelPortal; Q16864; -.
DR SMR; Q16864; 7-91.
DR IntAct; Q16864; 1.
DR MINT; MINT-1426240; -.
DR STRING; 9606.ENSP00000249289; -.
DR TCDB; 3.A.2.2.4; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR PhosphoSite; Q16864; -.
DR DMDM; 126302612; -.
DR PaxDb; Q16864; -.
DR PeptideAtlas; Q16864; -.
DR PRIDE; Q16864; -.
DR Ensembl; ENST00000249289; ENSP00000249289; ENSG00000128524.
DR Ensembl; ENST00000492758; ENSP00000417378; ENSG00000128524.
DR GeneID; 9296; -.
DR KEGG; hsa:9296; -.
DR UCSC; uc022all.1; human.
DR CTD; 9296; -.
DR GeneCards; GC07P128502; -.
DR HGNC; HGNC:16832; ATP6V1F.
DR HPA; CAB009529; -.
DR MIM; 607160; gene.
DR neXtProt; NX_Q16864; -.
DR PharmGKB; PA38421; -.
DR eggNOG; COG1436; -.
DR HOGENOM; HOG000056545; -.
DR HOVERGEN; HBG004488; -.
DR InParanoid; Q16864; -.
DR KO; K02151; -.
DR OMA; RHVIDAH; -.
DR OrthoDB; EOG7JMGGM; -.
DR BioCyc; MetaCyc:HS05192-MONOMER; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_15518; Transmembrane transport of small molecules.
DR GeneWiki; ATP6V1F; -.
DR GenomeRNAi; 9296; -.
DR NextBio; 34831; -.
DR PRO; PR:Q16864; -.
DR ArrayExpress; Q16864; -.
DR Bgee; Q16864; -.
DR CleanEx; HS_ATP6V1F; -.
DR Genevestigator; Q16864; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0033180; C:proton-transporting V-type ATPase, V1 domain; IEA:InterPro.
DR GO; GO:0016471; C:vacuolar proton-transporting V-type ATPase complex; IDA:UniProtKB.
DR GO; GO:0042624; F:ATPase activity, uncoupled; NAS:UniProtKB.
DR GO; GO:0015078; F:hydrogen ion transmembrane transporter activity; NAS:UniProtKB.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro.
DR GO; GO:0006879; P:cellular iron ion homeostasis; TAS:Reactome.
DR GO; GO:0008286; P:insulin receptor signaling pathway; TAS:Reactome.
DR GO; GO:0051701; P:interaction with host; TAS:Reactome.
DR GO; GO:0090382; P:phagosome maturation; TAS:Reactome.
DR GO; GO:0033572; P:transferrin transport; TAS:Reactome.
DR Gene3D; 3.40.50.10580; -; 1.
DR InterPro; IPR008218; ATPase_V1-cplx_f_g_su.
DR InterPro; IPR005772; ATPase_V1-cplx_fsu_euk.
DR PANTHER; PTHR13861; PTHR13861; 1.
DR Pfam; PF01990; ATP-synt_F; 1.
DR PIRSF; PIRSF015945; ATPase_V1_F_euk; 1.
DR TIGRFAMs; TIGR01101; V_ATP_synt_F; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Hydrogen ion transport;
KW Ion transport; Polymorphism; Reference proteome; Transport.
FT CHAIN 1 119 V-type proton ATPase subunit F.
FT /FTId=PRO_0000144799.
FT VAR_SEQ 52 52 F -> FRSLGSLPGSVVEANPNQRDPPLWDEIDS (in
FT isoform 2).
FT /FTId=VSP_045952.
FT VARIANT 24 24 G -> V (in dbSNP:rs10958).
FT /FTId=VAR_048348.
FT CONFLICT 8 8 I -> T (in Ref. 1; BAA08392).
SQ SEQUENCE 119 AA; 13370 MW; 9FE5A8BD249A85FA CRC64;
MAGRGKLIAV IGDEDTVTGF LLGGIGELNK NRHPNFLVVE KDTTINEIED TFRQFLNRDD
IGIILINQYI AEMVRHALDA HQQSIPAVLE IPSKEHPYDA AKDSILRRAR GMFTAEDLR
//
MIM
607160
*RECORD*
*FIELD* NO
607160
*FIELD* TI
*607160 ATPase, H+ TRANSPORTING, LYSOSOMAL, 14-KD, V1 SUBUNIT F; ATP6V1F
;;VACUOLAR ATPase, 14-KD SUBUNIT
read more*FIELD* TX
CLONING
The vacuolar ATPase (V-ATPase) is a multisubunit complex that mediates
acidification of intracellular organelles. By large-scale sequencing of
a human fetal brain cDNA library and database searching, Fujiwara et al.
(1995) identified a sequence showing homology with the 14-kD subunit of
M. sexta V-ATPase. Using 5-prime RACE, they cloned a full-length cDNA
encoding a deduced 119-amino acid protein with a molecular mass of 14
kD. The protein is predominantly hydrophilic and shares 69% and 70%
sequence identity with the M. sexta and Drosophila homologs,
respectively. Northern blot analysis detected ubiquitous expression of a
0.8-kb transcript.
*FIELD* RF
1. Fujiwara, T.; Kawai, A.; Shimizu, F.; Hirano, H.; Okuno, S.; Takeda,
S.; Ozaki, K.; Shimada, Y.; Nagata, M.; Watanabe, T.; Takaichi, A.;
Takahashi, E.; Nakamura, Y.; Shin, S.: Cloning, sequencing and expression
of a novel cDNA encoding human vacuolar ATPase (14-kDa subunit). DNA
Res. 2: 107-111, 1995.
*FIELD* CD
Carol A. Bocchini: 8/23/2002
*FIELD* ED
carol: 08/23/2002
mgross: 8/23/2002
carol: 8/23/2002
*RECORD*
*FIELD* NO
607160
*FIELD* TI
*607160 ATPase, H+ TRANSPORTING, LYSOSOMAL, 14-KD, V1 SUBUNIT F; ATP6V1F
;;VACUOLAR ATPase, 14-KD SUBUNIT
read more*FIELD* TX
CLONING
The vacuolar ATPase (V-ATPase) is a multisubunit complex that mediates
acidification of intracellular organelles. By large-scale sequencing of
a human fetal brain cDNA library and database searching, Fujiwara et al.
(1995) identified a sequence showing homology with the 14-kD subunit of
M. sexta V-ATPase. Using 5-prime RACE, they cloned a full-length cDNA
encoding a deduced 119-amino acid protein with a molecular mass of 14
kD. The protein is predominantly hydrophilic and shares 69% and 70%
sequence identity with the M. sexta and Drosophila homologs,
respectively. Northern blot analysis detected ubiquitous expression of a
0.8-kb transcript.
*FIELD* RF
1. Fujiwara, T.; Kawai, A.; Shimizu, F.; Hirano, H.; Okuno, S.; Takeda,
S.; Ozaki, K.; Shimada, Y.; Nagata, M.; Watanabe, T.; Takaichi, A.;
Takahashi, E.; Nakamura, Y.; Shin, S.: Cloning, sequencing and expression
of a novel cDNA encoding human vacuolar ATPase (14-kDa subunit). DNA
Res. 2: 107-111, 1995.
*FIELD* CD
Carol A. Bocchini: 8/23/2002
*FIELD* ED
carol: 08/23/2002
mgross: 8/23/2002
carol: 8/23/2002