ARV2_ARATH
ID ARV2_ARATH Reviewed; 228 AA.
AC Q5MK23; Q9M127;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Protein ARV 2 {ECO:0000303|PubMed:16725371};
DE Short=AtArv2p {ECO:0000303|PubMed:16725371};
GN Name=ARV2 {ECO:0000303|PubMed:16725371};
GN OrderedLocusNames=At4g01510 {ECO:0000312|Araport:AT4G01510};
GN ORFNames=F11O4.16 {ECO:0000312|EMBL:CAB77721.1};
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 [MRNA], FUNCTION, MUTAGENESIS OF 1-MET--ASN-68,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Col-3;
RX PubMed=16725371; DOI=10.1016/j.bbalip.2006.03.025;
RA Fores O., Arro M., Pahissa A., Ferrero S., Germann M., Stukey J.,
RA McDonough V., Nickels J.T. Jr., Campos N., Ferrer A.;
RT "Arabidopsis thaliana expresses two functional isoforms of Arvp, a protein
RT involved in the regulation of cellular lipid homeostasis.";
RL Biochim. Biophys. Acta 1761:725-735(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
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).
CC -!- FUNCTION: Mediator of sterol homeostasis involved in sterol uptake,
CC trafficking and distribution into membranes. Regulates also the
CC sphingolipid metabolism. {ECO:0000269|PubMed:16725371}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:16725371}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q9H2C2}.
CC -!- TISSUE SPECIFICITY: Restricted to tissues in which cells are actively
CC dividing or expanding. Mostly expressed in roots and flowers, and, to a
CC lower extent, in stems and leaves. {ECO:0000269|PubMed:16725371}.
CC -!- DEVELOPMENTAL STAGE: In floral tissues, expressed in pollen grains and
CC fertilized ovules until they develop into seeds, and, at low levels, in
CC the styles. Observed in germinating seedlings, and later confined to
CC shoot and root apical meristems. {ECO:0000269|PubMed:16725371}.
CC -!- SIMILARITY: Belongs to the ARV1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB77721.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY758071; AAV92716.1; -; mRNA.
DR EMBL; AL161492; CAB77721.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002687; AEE82034.1; -; Genomic_DNA.
DR PIR; F85019; F85019.
DR RefSeq; NP_192060.2; NM_116381.4.
DR AlphaFoldDB; Q5MK23; -.
DR STRING; 3702.AT4G01510.1; -.
DR PaxDb; Q5MK23; -.
DR PRIDE; Q5MK23; -.
DR EnsemblPlants; AT4G01510.1; AT4G01510.1; AT4G01510.
DR GeneID; 826763; -.
DR Gramene; AT4G01510.1; AT4G01510.1; AT4G01510.
DR KEGG; ath:AT4G01510; -.
DR Araport; AT4G01510; -.
DR TAIR; locus:2117012; AT4G01510.
DR eggNOG; KOG3134; Eukaryota.
DR HOGENOM; CLU_057366_1_0_1; -.
DR InParanoid; Q5MK23; -.
DR OMA; KITICDS; -.
DR PRO; PR:Q5MK23; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q5MK23; baseline and differential.
DR GO; GO:0032541; C:cortical endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0032366; P:intracellular sterol transport; IBA:GO_Central.
DR GO; GO:0097036; P:regulation of plasma membrane sterol distribution; IBA:GO_Central.
DR GO; GO:0006665; P:sphingolipid metabolic process; IMP:TAIR.
DR GO; GO:0016125; P:sterol metabolic process; IMP:TAIR.
DR InterPro; IPR007290; Arv1.
DR PANTHER; PTHR14467; PTHR14467; 1.
DR Pfam; PF04161; Arv1; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycoprotein; Lipid metabolism; Lipid transport;
KW Membrane; Reference proteome; Sphingolipid metabolism; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..228
FT /note="Protein ARV 2"
FT /id="PRO_0000446892"
FT TRANSMEM 37..57
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 123..143
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 1..68
FT /note="Missing: Impaired ability to complement arv1-
FT disrupted yeast."
FT /evidence="ECO:0000269|PubMed:16725371"
FT MUTAGEN 1..56
FT /note="Missing: Impaired ability to complement arv1-
FT disrupted yeast."
FT /evidence="ECO:0000269|PubMed:16725371"
FT MUTAGEN 1..46
FT /note="Missing: Impaired ability to complement arv1-
FT disrupted yeast."
FT /evidence="ECO:0000269|PubMed:16725371"
FT MUTAGEN 1..35
FT /note="Missing: Normal ability to complement arv1-disrupted
FT yeast."
FT /evidence="ECO:0000269|PubMed:16725371"
SQ SEQUENCE 228 AA; 25950 MW; 0B25DF55325C319E CRC64;
MAREKKTCVE CGHKVKSLFI QYSPGNFRLM KCENCEEVAD EYVECELLII FIDLILHKTK
AYRHLLYNVV NQESANVQHL LWKLVLAYLL LDTYRSLLLR RTNDGSNVSM SFLFESLEVL
VNVLSANFAF VFSFAFAAKL MLVMPRGKEI LLTILISSYV KIFLFAMPVW EFPVSVIFIV
DMLVLTSNAV ALKVMTESAT SRCLAVCFIA HSIRFLVDQI SGHLGSVM
