HHP1_ARATH
ID HHP1_ARATH Reviewed; 332 AA.
AC Q93ZH9;
DT 03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Heptahelical transmembrane protein 1;
DE AltName: Full=PAQR family protein HHP1;
GN Name=HHP1; OrderedLocusNames=At5g20270; ORFNames=F5O24.160;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP GENE FAMILY, NOMENCLATURE, AND TISSUE SPECIFICITY.
RX PubMed=16263907; DOI=10.1093/jxb/eri311;
RA Hsieh M.H., Goodman H.M.;
RT "A novel gene family in Arabidopsis encoding putative heptahelical
RT transmembrane proteins homologous to human adiponectin receptors and
RT progestin receptors.";
RL J. Exp. Bot. 56:3137-3147(2005).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19286917; DOI=10.1093/jxb/erp039;
RA Chen C.C., Liang C.S., Kao A.L., Yang C.C.;
RT "HHP1 is involved in osmotic stress sensitivity in Arabidopsis.";
RL J. Exp. Bot. 60:1589-1604(2009).
RN [8]
RP FUNCTION, INTERACTION WITH ICE1, TISSUE SPECIFICITY, AND INDUCTION BY
RP DROUGHT.
RX PubMed=20566565; DOI=10.1093/jxb/erq162;
RA Chen C.C., Liang C.S., Kao A.L., Yang C.C.;
RT "HHP1, a novel signalling component in the cross-talk between the cold and
RT osmotic signalling pathways in Arabidopsis.";
RL J. Exp. Bot. 61:3305-3320(2010).
CC -!- FUNCTION: May act as a negative regulator of abscisic acid (ABA)-
CC mediated osmotic stress signaling and function in cross-talk between
CC cold and osmotic signaling. {ECO:0000269|PubMed:19286917,
CC ECO:0000269|PubMed:20566565}.
CC -!- SUBUNIT: Interacts (via N-terminus) with SCRM/ICE1.
CC {ECO:0000269|PubMed:20566565}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, hypocotyls, vasculature of
CC cotyledons and leaves, hydathodes and guard cells. In reproductive
CC organs, expressed in trichomes, veins of sepals, stamens and stigmata
CC of pistils. {ECO:0000269|PubMed:16263907, ECO:0000269|PubMed:19286917,
CC ECO:0000269|PubMed:20566565}.
CC -!- INDUCTION: By abscisic acid (ABA), salt, osmotic and drought stresses.
CC {ECO:0000269|PubMed:19286917, ECO:0000269|PubMed:20566565}.
CC -!- DISRUPTION PHENOTYPE: Reduced apical meristem dominance and length of
CC hypocotyl, and increased cotyledon curling. Mutant plants are
CC hypersensitive to ABA and osmotic stress.
CC {ECO:0000269|PubMed:19286917}.
CC -!- SIMILARITY: Belongs to the ADIPOR family. {ECO:0000305}.
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DR EMBL; AF296825; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED92823.1; -; Genomic_DNA.
DR EMBL; AY057524; AAL09764.1; -; mRNA.
DR EMBL; AY143975; AAN28914.1; -; mRNA.
DR EMBL; AK226838; BAE98931.1; -; mRNA.
DR EMBL; AY086377; AAM64444.1; -; mRNA.
DR RefSeq; NP_197527.1; NM_122034.3.
DR AlphaFoldDB; Q93ZH9; -.
DR SMR; Q93ZH9; -.
DR BioGRID; 17425; 19.
DR IntAct; Q93ZH9; 18.
DR STRING; 3702.AT5G20270.1; -.
DR iPTMnet; Q93ZH9; -.
DR PaxDb; Q93ZH9; -.
DR PRIDE; Q93ZH9; -.
DR ProteomicsDB; 230278; -.
DR EnsemblPlants; AT5G20270.1; AT5G20270.1; AT5G20270.
DR GeneID; 832149; -.
DR Gramene; AT5G20270.1; AT5G20270.1; AT5G20270.
DR KEGG; ath:AT5G20270; -.
DR Araport; AT5G20270; -.
DR TAIR; locus:2149319; AT5G20270.
DR eggNOG; KOG0748; Eukaryota.
DR HOGENOM; CLU_023075_4_0_1; -.
DR InParanoid; Q93ZH9; -.
DR OMA; DYCGIAM; -.
DR OrthoDB; 1524940at2759; -.
DR PhylomeDB; Q93ZH9; -.
DR PRO; PR:Q93ZH9; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q93ZH9; baseline and differential.
DR Genevisible; Q93ZH9; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0009788; P:negative regulation of abscisic acid-activated signaling pathway; IMP:UniProtKB.
DR GO; GO:0009725; P:response to hormone; IEP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IEP:TAIR.
DR GO; GO:0009744; P:response to sucrose; IEP:TAIR.
DR InterPro; IPR004254; AdipoR/HlyIII-related.
DR PANTHER; PTHR20855; PTHR20855; 1.
DR Pfam; PF03006; HlyIII; 1.
PE 1: Evidence at protein level;
KW Membrane; Reference proteome; Stress response; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..332
FT /note="Heptahelical transmembrane protein 1"
FT /id="PRO_0000430047"
FT TOPO_DOM 1..98
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 120..138
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 139..159
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 160..172
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 194..199
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 200..220
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 221..233
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 234..254
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 255..262
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 263..283
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 284..303
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 304..324
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 325..332
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..40
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 332 AA; 37877 MW; CC3531FCC1FD1335 CRC64;
MDQNGHNDEA ETVSCGNGNC KSKIVPGDDH GGDESSGTKR RKKRKTQQKT MKRRELMSYC
ELPEYMKDNE YILNYYRADW SIRDAFFSVF SFHNESLNVW THLIGFIFFV ALTVANIIHH
DGFFPVDAKS PGNVTRWPFF VFLGGSMFCL LASSICHLFC CHSKELNVFL LRIDYAGITA
MIITSFFPPI FYIFQCTPRW YFIYLAGITS MGIFTIITLF TPSLSAPKYR AFRALLFASM
GLFGIVPAAH ALVVNWGNPQ RNVTLVYELL MAVFYLVGTG FYVGRVPERL KPGWFDRVGH
SHQIFHVFVL LGALSHYAAA LLFLDWRDHV GC
