Full text data of AGTRAP
AGTRAP
(ATRAP)
[Confidence: low (only semi-automatic identification from reviews)]
Type-1 angiotensin II receptor-associated protein (AT1 receptor-associated protein)
Type-1 angiotensin II receptor-associated protein (AT1 receptor-associated protein)
UniProt
Q6RW13
ID ATRAP_HUMAN Reviewed; 159 AA.
AC Q6RW13; A8MVQ5; Q5SNV4; Q5SNV5; Q96AC0; Q96PL4; Q9NRW9;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 05-JUL-2004, sequence version 1.
DT 22-JAN-2014, entry version 87.
DE RecName: Full=Type-1 angiotensin II receptor-associated protein;
DE AltName: Full=AT1 receptor-associated protein;
GN Name=AGTRAP; Synonyms=ATRAP;
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), TISSUE SPECIFICITY, AND
RP INTERACTION WITH GNB2L1 AND AGTR1.
RC TISSUE=Fetal brain;
RX PubMed=11733189; DOI=10.1016/S1357-2725(01)00094-2;
RA Wang W., Huang Y., Zhou Z., Tang R., Zhao W., Zeng L., Xu M.,
RA Cheng C., Gu S., Ying K., Xie Y., Mao Y.;
RT "Identification and characterization of AGTRAP, a human homolog of
RT murine angiotensin II receptor-associated protein (Agtrap).";
RL Int. J. Biochem. Cell Biol. 34:93-102(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
RA Ye R.D., He R.;
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Pancreas islet cell;
RA Melton D., Brown J., Kenty G., Permutt A., Lee C., Kaestner K.,
RA Lemishka I., Scearce M., Brestelli J., Gradwohl G., Clifton S.,
RA Hillier L., Marra M., Pape D., Wylie T., Martin J., Blistain A.,
RA Schmitt A., Theising B., Ritter E., Ronko I., Bennett J., Cardenas M.,
RA Gibbons M., McCann R., Cole R., Tsagareishvili R., Williams T.,
RA Jackson Y., Bowers Y.;
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT VAL-143.
RG SeattleSNPs variation discovery resource;
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 5).
RC TISSUE=Colon, and Eye;
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 [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH AGTR1.
RX PubMed=12960423; DOI=10.1091/mbc.E03-06-0383;
RA Lopez-Ilasaca M., Liu X., Tamura K., Dzau V.J.;
RT "The angiotensin II type I receptor-associated protein, ATRAP, is a
RT transmembrane protein and a modulator of angiotensin II signaling.";
RL Mol. Biol. Cell 14:5038-5050(2003).
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).
CC -!- FUNCTION: Appears to be a negative regulator of type-1 angiotensin
CC II receptor-mediated signaling by regulating receptor
CC internalisation as well as mechanism of receptor desensitization
CC such as phosphorylation. Induces also a decrease in cell
CC proliferation and angiotensin II-stimulated transcriptional
CC activity.
CC -!- SUBUNIT: Interacts with GNB2L1/RACK1, and with the C-terminal
CC region of AGTR1.
CC -!- INTERACTION:
CC Q96AL5:PBX3; NbExp=3; IntAct=EBI-741181, EBI-741171;
CC Q9UKF7:PITPNC1; NbExp=3; IntAct=EBI-741181, EBI-749241;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC membrane protein. Golgi apparatus membrane; Multi-pass membrane
CC protein. Cytoplasmic vesicle membrane; Multi-pass membrane
CC protein. Note=Present in perinuclear vesicular membranes,
CC Endoplasmic reticulum, Golgi and endocytic vesicles.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q6RW13-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6RW13-2; Sequence=VSP_014839;
CC Name=3;
CC IsoId=Q6RW13-3; Sequence=VSP_039290;
CC Note=No experimental confirmation available;
CC Name=5;
CC IsoId=Q6RW13-5; Sequence=VSP_040406;
CC Name=4;
CC IsoId=Q6RW13-4; Sequence=VSP_039291;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Ubiquitous but more abundant in kidney, heart,
CC pancreas and thyroid.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAI15876.1; Type=Erroneous gene model prediction;
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/agtrap/";
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DR EMBL; AF312374; AAL26806.1; -; mRNA.
DR EMBL; AF165187; AAF89547.1; -; mRNA.
DR EMBL; CA866314; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AY488088; AAR25556.1; -; Genomic_DNA.
DR EMBL; AL953897; CAI15876.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL953897; CAI15877.1; -; Genomic_DNA.
DR EMBL; AL953897; CAI15878.1; -; Genomic_DNA.
DR EMBL; AL953897; CAI15879.1; -; Genomic_DNA.
DR EMBL; CH471130; EAW71702.1; -; Genomic_DNA.
DR EMBL; BC017328; AAH17328.1; -; mRNA.
DR EMBL; BE782705; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_001035284.1; NM_001040194.1.
DR RefSeq; NP_001035285.1; NM_001040195.1.
DR RefSeq; NP_001035286.1; NM_001040196.1.
DR RefSeq; NP_001035287.1; NM_001040197.1.
DR RefSeq; NP_065083.3; NM_020350.4.
DR UniGene; Hs.464438; -.
DR ProteinModelPortal; Q6RW13; -.
DR IntAct; Q6RW13; 10.
DR STRING; 9606.ENSP00000319713; -.
DR PhosphoSite; Q6RW13; -.
DR DMDM; 71152303; -.
DR PaxDb; Q6RW13; -.
DR PeptideAtlas; Q6RW13; -.
DR PRIDE; Q6RW13; -.
DR DNASU; 57085; -.
DR Ensembl; ENST00000314340; ENSP00000319713; ENSG00000177674.
DR Ensembl; ENST00000376629; ENSP00000365816; ENSG00000177674.
DR Ensembl; ENST00000376637; ENSP00000365824; ENSG00000177674.
DR Ensembl; ENST00000400895; ENSP00000383688; ENSG00000177674.
DR Ensembl; ENST00000452018; ENSP00000408505; ENSG00000177674.
DR GeneID; 57085; -.
DR KEGG; hsa:57085; -.
DR UCSC; uc001asv.3; human.
DR CTD; 57085; -.
DR GeneCards; GC01P011796; -.
DR HGNC; HGNC:13539; AGTRAP.
DR HPA; HPA044120; -.
DR MIM; 608729; gene.
DR neXtProt; NX_Q6RW13; -.
DR PharmGKB; PA38363; -.
DR eggNOG; NOG45277; -.
DR HOGENOM; HOG000034218; -.
DR HOVERGEN; HBG080881; -.
DR InParanoid; Q6RW13; -.
DR OMA; DAISMFL; -.
DR OrthoDB; EOG7SFHZD; -.
DR PhylomeDB; Q6RW13; -.
DR ChiTaRS; AGTRAP; human.
DR GeneWiki; AGTRAP; -.
DR GenomeRNAi; 57085; -.
DR NextBio; 62875; -.
DR PRO; PR:Q6RW13; -.
DR ArrayExpress; Q6RW13; -.
DR Bgee; Q6RW13; -.
DR CleanEx; HS_AGTRAP; -.
DR Genevestigator; Q6RW13; -.
DR GO; GO:0005938; C:cell cortex; IEA:Ensembl.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0004945; F:angiotensin type II receptor activity; IEA:Ensembl.
DR GO; GO:0008217; P:regulation of blood pressure; IEA:Ensembl.
DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR InterPro; IPR009436; Angiotensin_II_typ1_rcpt-assoc.
DR Pfam; PF06396; AGTRAP; 1.
DR ProDom; PD357679; PD357679; 1.
DR SMART; SM00805; AGTRAP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Cytoplasmic vesicle;
KW Endoplasmic reticulum; Golgi apparatus; Membrane; Polymorphism;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1 159 Type-1 angiotensin II receptor-associated
FT protein.
FT /FTId=PRO_0000064735.
FT TOPO_DOM 1 23 Extracellular (Potential).
FT TRANSMEM 24 44 Helical; (Potential).
FT TOPO_DOM 45 55 Cytoplasmic (Potential).
FT TRANSMEM 56 76 Helical; (Potential).
FT TOPO_DOM 77 86 Extracellular (Potential).
FT TRANSMEM 87 107 Helical; (Potential).
FT TOPO_DOM 108 159 Cytoplasmic (Potential).
FT REGION 110 122 Interaction with AGTR1.
FT VAR_SEQ 10 159 VILLGHWLLTTWGCIVFSGSYAWANFTILALGVWAVAQRDS
FT IDAISMFLGGLLATIFLDIVHISIFYPRVSLTDTGRFGVGM
FT AILSLLLKPLSCCFVYHMYRERGGELLVHTGFLGSSQDRSA
FT YQTIDSAEAPADPFAVPEGRSQDARGY -> GLHCILRLLC
FT LGQLHHPGLGRVGCGSAGLHRRHKHVSGWLAGHHLPGHRAH
FT QHLLPAGQPHGHGPLWRGHGHPQLAAQAALLLLRLPHVPGA
FT RGFPWVFSGP (in isoform 4).
FT /FTId=VSP_039291.
FT VAR_SEQ 21 159 WGCIVFSGSYAWANFTILALGVWAVAQRDSIDAISMFLGGL
FT LATIFLDIVHISIFYPRVSLTDTGRFGVGMAILSLLLKPLS
FT CCFVYHMYRERGGELLVHTGFLGSSQDRSAYQTIDSAEAPA
FT DPFAVPEGRSQDARGY -> CFWRHFSAKPRLETIELTCAL
FT CKLRSAAHRATAGLHCILRLLCLGQLHHPGLGRVGCGSAGL
FT HRRHKHVSGWLAGHHLPGHRAHQHLLPAGQPHGHGPLWRGH
FT GHPQLAAQAALLLLRLPHVPGARG (in isoform 3).
FT /FTId=VSP_039290.
FT VAR_SEQ 21 159 WGCIVFSGSYAWANFTILALGVWAVAQRDSIDAISMFLGGL
FT LATIFLDIVHISIFYPRVSLTDTGRFGVGMAILSLLLKPLS
FT CCFVYHMYRERGGELLVHTGFLGSSQDRSAYQTIDSAEAPA
FT DPFAVPEGRSQDARGY -> CFWRHFSAKPRLETIELTCAL
FT CKLRSAAHRATAGLHCILRLLCLGQLHHPGLGRVGCGSAGL
FT HRRHKHVSGWLAGHHLPGHRAHQHLLPAGQPHGHGPLWRGH
FT GHPQLAAQAALLLLRLPHVPGARGFPWVFSGP (in
FT isoform 5).
FT /FTId=VSP_040406.
FT VAR_SEQ 115 121 Missing (in isoform 2).
FT /FTId=VSP_014839.
FT VARIANT 143 143 A -> V (in dbSNP:rs17875960).
FT /FTId=VAR_023075.
FT CONFLICT 158 158 G -> R (in Ref. 2; AAF89547).
FT CONFLICT 159 159 Y -> S (in Ref. 1; AAL26806).
SQ SEQUENCE 159 AA; 17419 MW; 7E1D5C7E79AE6BC5 CRC64;
MELPAVNLKV ILLGHWLLTT WGCIVFSGSY AWANFTILAL GVWAVAQRDS IDAISMFLGG
LLATIFLDIV HISIFYPRVS LTDTGRFGVG MAILSLLLKP LSCCFVYHMY RERGGELLVH
TGFLGSSQDR SAYQTIDSAE APADPFAVPE GRSQDARGY
//
ID ATRAP_HUMAN Reviewed; 159 AA.
AC Q6RW13; A8MVQ5; Q5SNV4; Q5SNV5; Q96AC0; Q96PL4; Q9NRW9;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 05-JUL-2004, sequence version 1.
DT 22-JAN-2014, entry version 87.
DE RecName: Full=Type-1 angiotensin II receptor-associated protein;
DE AltName: Full=AT1 receptor-associated protein;
GN Name=AGTRAP; Synonyms=ATRAP;
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), TISSUE SPECIFICITY, AND
RP INTERACTION WITH GNB2L1 AND AGTR1.
RC TISSUE=Fetal brain;
RX PubMed=11733189; DOI=10.1016/S1357-2725(01)00094-2;
RA Wang W., Huang Y., Zhou Z., Tang R., Zhao W., Zeng L., Xu M.,
RA Cheng C., Gu S., Ying K., Xie Y., Mao Y.;
RT "Identification and characterization of AGTRAP, a human homolog of
RT murine angiotensin II receptor-associated protein (Agtrap).";
RL Int. J. Biochem. Cell Biol. 34:93-102(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
RA Ye R.D., He R.;
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Pancreas islet cell;
RA Melton D., Brown J., Kenty G., Permutt A., Lee C., Kaestner K.,
RA Lemishka I., Scearce M., Brestelli J., Gradwohl G., Clifton S.,
RA Hillier L., Marra M., Pape D., Wylie T., Martin J., Blistain A.,
RA Schmitt A., Theising B., Ritter E., Ronko I., Bennett J., Cardenas M.,
RA Gibbons M., McCann R., Cole R., Tsagareishvili R., Williams T.,
RA Jackson Y., Bowers Y.;
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT VAL-143.
RG SeattleSNPs variation discovery resource;
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 5).
RC TISSUE=Colon, and Eye;
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 [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH AGTR1.
RX PubMed=12960423; DOI=10.1091/mbc.E03-06-0383;
RA Lopez-Ilasaca M., Liu X., Tamura K., Dzau V.J.;
RT "The angiotensin II type I receptor-associated protein, ATRAP, is a
RT transmembrane protein and a modulator of angiotensin II signaling.";
RL Mol. Biol. Cell 14:5038-5050(2003).
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).
CC -!- FUNCTION: Appears to be a negative regulator of type-1 angiotensin
CC II receptor-mediated signaling by regulating receptor
CC internalisation as well as mechanism of receptor desensitization
CC such as phosphorylation. Induces also a decrease in cell
CC proliferation and angiotensin II-stimulated transcriptional
CC activity.
CC -!- SUBUNIT: Interacts with GNB2L1/RACK1, and with the C-terminal
CC region of AGTR1.
CC -!- INTERACTION:
CC Q96AL5:PBX3; NbExp=3; IntAct=EBI-741181, EBI-741171;
CC Q9UKF7:PITPNC1; NbExp=3; IntAct=EBI-741181, EBI-749241;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC membrane protein. Golgi apparatus membrane; Multi-pass membrane
CC protein. Cytoplasmic vesicle membrane; Multi-pass membrane
CC protein. Note=Present in perinuclear vesicular membranes,
CC Endoplasmic reticulum, Golgi and endocytic vesicles.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q6RW13-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6RW13-2; Sequence=VSP_014839;
CC Name=3;
CC IsoId=Q6RW13-3; Sequence=VSP_039290;
CC Note=No experimental confirmation available;
CC Name=5;
CC IsoId=Q6RW13-5; Sequence=VSP_040406;
CC Name=4;
CC IsoId=Q6RW13-4; Sequence=VSP_039291;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Ubiquitous but more abundant in kidney, heart,
CC pancreas and thyroid.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAI15876.1; Type=Erroneous gene model prediction;
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/agtrap/";
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DR EMBL; AF312374; AAL26806.1; -; mRNA.
DR EMBL; AF165187; AAF89547.1; -; mRNA.
DR EMBL; CA866314; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AY488088; AAR25556.1; -; Genomic_DNA.
DR EMBL; AL953897; CAI15876.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL953897; CAI15877.1; -; Genomic_DNA.
DR EMBL; AL953897; CAI15878.1; -; Genomic_DNA.
DR EMBL; AL953897; CAI15879.1; -; Genomic_DNA.
DR EMBL; CH471130; EAW71702.1; -; Genomic_DNA.
DR EMBL; BC017328; AAH17328.1; -; mRNA.
DR EMBL; BE782705; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_001035284.1; NM_001040194.1.
DR RefSeq; NP_001035285.1; NM_001040195.1.
DR RefSeq; NP_001035286.1; NM_001040196.1.
DR RefSeq; NP_001035287.1; NM_001040197.1.
DR RefSeq; NP_065083.3; NM_020350.4.
DR UniGene; Hs.464438; -.
DR ProteinModelPortal; Q6RW13; -.
DR IntAct; Q6RW13; 10.
DR STRING; 9606.ENSP00000319713; -.
DR PhosphoSite; Q6RW13; -.
DR DMDM; 71152303; -.
DR PaxDb; Q6RW13; -.
DR PeptideAtlas; Q6RW13; -.
DR PRIDE; Q6RW13; -.
DR DNASU; 57085; -.
DR Ensembl; ENST00000314340; ENSP00000319713; ENSG00000177674.
DR Ensembl; ENST00000376629; ENSP00000365816; ENSG00000177674.
DR Ensembl; ENST00000376637; ENSP00000365824; ENSG00000177674.
DR Ensembl; ENST00000400895; ENSP00000383688; ENSG00000177674.
DR Ensembl; ENST00000452018; ENSP00000408505; ENSG00000177674.
DR GeneID; 57085; -.
DR KEGG; hsa:57085; -.
DR UCSC; uc001asv.3; human.
DR CTD; 57085; -.
DR GeneCards; GC01P011796; -.
DR HGNC; HGNC:13539; AGTRAP.
DR HPA; HPA044120; -.
DR MIM; 608729; gene.
DR neXtProt; NX_Q6RW13; -.
DR PharmGKB; PA38363; -.
DR eggNOG; NOG45277; -.
DR HOGENOM; HOG000034218; -.
DR HOVERGEN; HBG080881; -.
DR InParanoid; Q6RW13; -.
DR OMA; DAISMFL; -.
DR OrthoDB; EOG7SFHZD; -.
DR PhylomeDB; Q6RW13; -.
DR ChiTaRS; AGTRAP; human.
DR GeneWiki; AGTRAP; -.
DR GenomeRNAi; 57085; -.
DR NextBio; 62875; -.
DR PRO; PR:Q6RW13; -.
DR ArrayExpress; Q6RW13; -.
DR Bgee; Q6RW13; -.
DR CleanEx; HS_AGTRAP; -.
DR Genevestigator; Q6RW13; -.
DR GO; GO:0005938; C:cell cortex; IEA:Ensembl.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0004945; F:angiotensin type II receptor activity; IEA:Ensembl.
DR GO; GO:0008217; P:regulation of blood pressure; IEA:Ensembl.
DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR InterPro; IPR009436; Angiotensin_II_typ1_rcpt-assoc.
DR Pfam; PF06396; AGTRAP; 1.
DR ProDom; PD357679; PD357679; 1.
DR SMART; SM00805; AGTRAP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Cytoplasmic vesicle;
KW Endoplasmic reticulum; Golgi apparatus; Membrane; Polymorphism;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1 159 Type-1 angiotensin II receptor-associated
FT protein.
FT /FTId=PRO_0000064735.
FT TOPO_DOM 1 23 Extracellular (Potential).
FT TRANSMEM 24 44 Helical; (Potential).
FT TOPO_DOM 45 55 Cytoplasmic (Potential).
FT TRANSMEM 56 76 Helical; (Potential).
FT TOPO_DOM 77 86 Extracellular (Potential).
FT TRANSMEM 87 107 Helical; (Potential).
FT TOPO_DOM 108 159 Cytoplasmic (Potential).
FT REGION 110 122 Interaction with AGTR1.
FT VAR_SEQ 10 159 VILLGHWLLTTWGCIVFSGSYAWANFTILALGVWAVAQRDS
FT IDAISMFLGGLLATIFLDIVHISIFYPRVSLTDTGRFGVGM
FT AILSLLLKPLSCCFVYHMYRERGGELLVHTGFLGSSQDRSA
FT YQTIDSAEAPADPFAVPEGRSQDARGY -> GLHCILRLLC
FT LGQLHHPGLGRVGCGSAGLHRRHKHVSGWLAGHHLPGHRAH
FT QHLLPAGQPHGHGPLWRGHGHPQLAAQAALLLLRLPHVPGA
FT RGFPWVFSGP (in isoform 4).
FT /FTId=VSP_039291.
FT VAR_SEQ 21 159 WGCIVFSGSYAWANFTILALGVWAVAQRDSIDAISMFLGGL
FT LATIFLDIVHISIFYPRVSLTDTGRFGVGMAILSLLLKPLS
FT CCFVYHMYRERGGELLVHTGFLGSSQDRSAYQTIDSAEAPA
FT DPFAVPEGRSQDARGY -> CFWRHFSAKPRLETIELTCAL
FT CKLRSAAHRATAGLHCILRLLCLGQLHHPGLGRVGCGSAGL
FT HRRHKHVSGWLAGHHLPGHRAHQHLLPAGQPHGHGPLWRGH
FT GHPQLAAQAALLLLRLPHVPGARG (in isoform 3).
FT /FTId=VSP_039290.
FT VAR_SEQ 21 159 WGCIVFSGSYAWANFTILALGVWAVAQRDSIDAISMFLGGL
FT LATIFLDIVHISIFYPRVSLTDTGRFGVGMAILSLLLKPLS
FT CCFVYHMYRERGGELLVHTGFLGSSQDRSAYQTIDSAEAPA
FT DPFAVPEGRSQDARGY -> CFWRHFSAKPRLETIELTCAL
FT CKLRSAAHRATAGLHCILRLLCLGQLHHPGLGRVGCGSAGL
FT HRRHKHVSGWLAGHHLPGHRAHQHLLPAGQPHGHGPLWRGH
FT GHPQLAAQAALLLLRLPHVPGARGFPWVFSGP (in
FT isoform 5).
FT /FTId=VSP_040406.
FT VAR_SEQ 115 121 Missing (in isoform 2).
FT /FTId=VSP_014839.
FT VARIANT 143 143 A -> V (in dbSNP:rs17875960).
FT /FTId=VAR_023075.
FT CONFLICT 158 158 G -> R (in Ref. 2; AAF89547).
FT CONFLICT 159 159 Y -> S (in Ref. 1; AAL26806).
SQ SEQUENCE 159 AA; 17419 MW; 7E1D5C7E79AE6BC5 CRC64;
MELPAVNLKV ILLGHWLLTT WGCIVFSGSY AWANFTILAL GVWAVAQRDS IDAISMFLGG
LLATIFLDIV HISIFYPRVS LTDTGRFGVG MAILSLLLKP LSCCFVYHMY RERGGELLVH
TGFLGSSQDR SAYQTIDSAE APADPFAVPE GRSQDARGY
//
MIM
608729
*RECORD*
*FIELD* NO
608729
*FIELD* TI
*608729 ANGIOTENSIN II RECEPTOR-ASSOCIATED PROTEIN; AGTRAP
;;ATRAP
*FIELD* TX
CLONING
read more
Using the C-terminal domain of murine At2r1a (106165) as bait in a yeast
2-hybrid screen, Daviet et al. (1999) cloned mouse Agtrap from a kidney
cDNA library. The deduced 161-amino acid protein has a calculated
molecular mass of 17.8 kD. It contains several extensive N-terminal
hydrophobic domains, as well as potential sites for phosphorylation and
N-glycosylation. Northern blot analysis detected transcripts of 1.2 and
0.8 kb in all mouse tissues examined, with relatively high levels in
kidney, testis, and heart. PCR also detected Agtrap expression in mouse
aortic tissue and vascular smooth muscle cells (VSMCs).
By sequencing clones obtained from a fetal brain cDNA library, followed
by EST database analysis, Wang et al. (2002) cloned human AGTRAP. The
deduced 159-amino acid protein has a calculated molecular mass of 17.3
kD. AGTRAP has a 21-amino acid N-terminal transmembrane region that is
followed by a conserved cysteine, which is potentially palmitoylated.
Mouse and human AGTRAP share 74% amino acid homology. Northern blot
analysis detected a 1.2-kb transcript in almost all tissues examined,
with highest abundance in kidney, heart, pancreas, and thyroid.
GENE FUNCTION
By affinity chromatography and coimmunoprecipitation experiments, Daviet
et al. (1999) confirmed association between mouse Agtrap and At2r1a.
Agtrap interacted specifically with the C-terminal domain of At2r1a, but
not with the C-terminal domains of several other hormone receptors,
including AT2R2 (300034), CHRM3 (118494), BDKRB2 (113503), EDNRB
(131244), and ADRB2 (109690). Overexpression of Agtrap in COS-7 cells
inhibited At2r1a activation of phospholipase C (see 607120). It did not
affect Chrm3 activation.
Cui et al. (2000) determined that transfection of mouse Agtrap into
adult rat VSMCs potentiated At2r1 internalization upon angiotensin II
(see 106150) stimulation. Receptor-induced DNA synthesis was inhibited
in Agtrap-transfected VSMCs, and this was associated with inhibition of
Stat3 (102582) and Akt (see 164730) phosphorylation. Cui et al. (2000)
concluded that AGTRAP is a negative regulator of AT2R1-mediated cell
proliferation in VSMCs.
Using several assays of protein interaction, Wang et al. (2002) showed
that AGTRAP interacted with RACK1 (176981). They suggested that the
AGTRAP-RACK1 interaction may help recruit the signaling complex to AT2R1
and affect receptor signaling.
Using a yeast 2-hybrid assay, Guo et al. (2005) demonstrated that mouse
Caml (CAMLG; 601118) interacted with Atrap. The N-terminal hydrophilic
domain of Caml mediated the interaction, and the proteins colocalized in
the endoplasmic reticulum. Atrap knockdown increased NFAT (see NFATC2;
600490) activity, and overexpression of Atrap decreased angiotensin II-
or Caml-induced NFAT transcriptional activation. Overexpression of the
N-terminal ATRAP-interacting domain of Caml increased angiotensin
II-induced NFAT promoter activity, whereas overexpression of the
C-terminal end of Caml disrupted the effect of angiotensin II on NFAT
signaling.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the AGTRAP
gene to chromosome 1 (TMAP SHGC-32094).
*FIELD* RF
1. Cui, T.-X.; Nakagami, H.; Iwai, M.; Takeda, Y.; Shiuchi, T.; Tamura,
K.; Daviet, L.; Horiuchi, M.: ATRAP, novel AT1 receptor associated
protein, enhances internalization of AT1 receptor and inhibits vascular
smooth muscle cell growth. Biochem. Biophys. Res. Commun. 279: 938-941,
2000.
2. Daviet, L.; Lehtonen, J. Y. A.; Tamura, K.; Griese, D. P.; Horiuchi,
M.; Dzau, V. J.: Cloning and characterization of ATRAP, a novel protein
that interacts with the angiotensin II type 1 receptor. J. Biol.
Chem. 274: 17058-17062, 1999.
3. Guo, S.; Lopez-Ilasaca, M.; Dzau, V. J.: Identification of calcium-modulating
cyclophilin ligand (CAML) as transducer of angiotensin II-mediated
nuclear factor of activated T cells (NFAT) activation. J. Biol. Chem. 280:
12536-12541, 2005.
4. Wang, W.; Huang, Y.; Zhou, Z.; Tang, R.; Zhao, W.; Zeng, L.; Xu,
M.; Cheng, C.; Gu, S.; Ying, K.; Xie, Y.; Mao, Y.: Identification
and characterization of AGTRAP, a human homolog of murine angiotensin
II receptor-associated protein (Agtrap). Int. J. Biochem. Cell Biol. 34:
93-102, 2002.
*FIELD* CN
Patricia A. Hartz - updated: 9/16/2005
*FIELD* CD
Patricia A. Hartz: 6/14/2004
*FIELD* ED
wwang: 10/14/2008
mgross: 9/16/2005
mgross: 6/14/2004
*RECORD*
*FIELD* NO
608729
*FIELD* TI
*608729 ANGIOTENSIN II RECEPTOR-ASSOCIATED PROTEIN; AGTRAP
;;ATRAP
*FIELD* TX
CLONING
read more
Using the C-terminal domain of murine At2r1a (106165) as bait in a yeast
2-hybrid screen, Daviet et al. (1999) cloned mouse Agtrap from a kidney
cDNA library. The deduced 161-amino acid protein has a calculated
molecular mass of 17.8 kD. It contains several extensive N-terminal
hydrophobic domains, as well as potential sites for phosphorylation and
N-glycosylation. Northern blot analysis detected transcripts of 1.2 and
0.8 kb in all mouse tissues examined, with relatively high levels in
kidney, testis, and heart. PCR also detected Agtrap expression in mouse
aortic tissue and vascular smooth muscle cells (VSMCs).
By sequencing clones obtained from a fetal brain cDNA library, followed
by EST database analysis, Wang et al. (2002) cloned human AGTRAP. The
deduced 159-amino acid protein has a calculated molecular mass of 17.3
kD. AGTRAP has a 21-amino acid N-terminal transmembrane region that is
followed by a conserved cysteine, which is potentially palmitoylated.
Mouse and human AGTRAP share 74% amino acid homology. Northern blot
analysis detected a 1.2-kb transcript in almost all tissues examined,
with highest abundance in kidney, heart, pancreas, and thyroid.
GENE FUNCTION
By affinity chromatography and coimmunoprecipitation experiments, Daviet
et al. (1999) confirmed association between mouse Agtrap and At2r1a.
Agtrap interacted specifically with the C-terminal domain of At2r1a, but
not with the C-terminal domains of several other hormone receptors,
including AT2R2 (300034), CHRM3 (118494), BDKRB2 (113503), EDNRB
(131244), and ADRB2 (109690). Overexpression of Agtrap in COS-7 cells
inhibited At2r1a activation of phospholipase C (see 607120). It did not
affect Chrm3 activation.
Cui et al. (2000) determined that transfection of mouse Agtrap into
adult rat VSMCs potentiated At2r1 internalization upon angiotensin II
(see 106150) stimulation. Receptor-induced DNA synthesis was inhibited
in Agtrap-transfected VSMCs, and this was associated with inhibition of
Stat3 (102582) and Akt (see 164730) phosphorylation. Cui et al. (2000)
concluded that AGTRAP is a negative regulator of AT2R1-mediated cell
proliferation in VSMCs.
Using several assays of protein interaction, Wang et al. (2002) showed
that AGTRAP interacted with RACK1 (176981). They suggested that the
AGTRAP-RACK1 interaction may help recruit the signaling complex to AT2R1
and affect receptor signaling.
Using a yeast 2-hybrid assay, Guo et al. (2005) demonstrated that mouse
Caml (CAMLG; 601118) interacted with Atrap. The N-terminal hydrophilic
domain of Caml mediated the interaction, and the proteins colocalized in
the endoplasmic reticulum. Atrap knockdown increased NFAT (see NFATC2;
600490) activity, and overexpression of Atrap decreased angiotensin II-
or Caml-induced NFAT transcriptional activation. Overexpression of the
N-terminal ATRAP-interacting domain of Caml increased angiotensin
II-induced NFAT promoter activity, whereas overexpression of the
C-terminal end of Caml disrupted the effect of angiotensin II on NFAT
signaling.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the AGTRAP
gene to chromosome 1 (TMAP SHGC-32094).
*FIELD* RF
1. Cui, T.-X.; Nakagami, H.; Iwai, M.; Takeda, Y.; Shiuchi, T.; Tamura,
K.; Daviet, L.; Horiuchi, M.: ATRAP, novel AT1 receptor associated
protein, enhances internalization of AT1 receptor and inhibits vascular
smooth muscle cell growth. Biochem. Biophys. Res. Commun. 279: 938-941,
2000.
2. Daviet, L.; Lehtonen, J. Y. A.; Tamura, K.; Griese, D. P.; Horiuchi,
M.; Dzau, V. J.: Cloning and characterization of ATRAP, a novel protein
that interacts with the angiotensin II type 1 receptor. J. Biol.
Chem. 274: 17058-17062, 1999.
3. Guo, S.; Lopez-Ilasaca, M.; Dzau, V. J.: Identification of calcium-modulating
cyclophilin ligand (CAML) as transducer of angiotensin II-mediated
nuclear factor of activated T cells (NFAT) activation. J. Biol. Chem. 280:
12536-12541, 2005.
4. Wang, W.; Huang, Y.; Zhou, Z.; Tang, R.; Zhao, W.; Zeng, L.; Xu,
M.; Cheng, C.; Gu, S.; Ying, K.; Xie, Y.; Mao, Y.: Identification
and characterization of AGTRAP, a human homolog of murine angiotensin
II receptor-associated protein (Agtrap). Int. J. Biochem. Cell Biol. 34:
93-102, 2002.
*FIELD* CN
Patricia A. Hartz - updated: 9/16/2005
*FIELD* CD
Patricia A. Hartz: 6/14/2004
*FIELD* ED
wwang: 10/14/2008
mgross: 9/16/2005
mgross: 6/14/2004