ARV1_MOUSE
ID ARV1_MOUSE Reviewed; 266 AA.
AC Q9D0U9; Q8BY08;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Protein ARV1;
GN Name=Arv1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=20663892; DOI=10.1074/jbc.m110.165761;
RA Tong F., Billheimer J., Shechtman C.F., Liu Y., Crooke R., Graham M.,
RA Cohen D.E., Sturley S.L., Rader D.J.;
RT "Decreased expression of ARV1 results in cholesterol retention in the
RT endoplasmic reticulum and abnormal bile acid metabolism.";
RL J. Biol. Chem. 285:33632-33641(2010).
RN [3]
RP DISRUPTION PHENOTYPE.
RX PubMed=27270415; DOI=10.1093/hmg/ddw157;
RA Palmer E.E., Jarrett K.E., Sachdev R.K., Al Zahrani F., Hashem M.O.,
RA Ibrahim N., Sampaio H., Kandula T., Macintosh R., Gupta R., Conlon D.M.,
RA Billheimer J.T., Rader D.J., Funato K., Walkey C.J., Lee C.S., Loo C.,
RA Brammah S., Elakis G., Zhu Y., Buckley M., Kirk E.P., Bye A.,
RA Alkuraya F.S., Roscioli T., Lagor W.R.;
RT "Neuronal deficiency of ARV1 causes an autosomal recessive epileptic
RT encephalopathy.";
RL Hum. Mol. Genet. 25:3042-3054(2016).
CC -!- FUNCTION: Plays a role as a mediator in the endoplasmic reticulum (ER)
CC cholesterol and bile acid homeostasis (PubMed:20663892). Participates
CC in sterol transport out of the ER and distribution into plasma
CC membranes (PubMed:20663892). {ECO:0000269|PubMed:20663892}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9H2C2}; Multi-pass membrane protein
CC {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in lung.
CC {ECO:0000269|PubMed:20663892}.
CC -!- DISRUPTION PHENOTYPE: Mice show an increase in the abundance of type 1
CC oxidative muscle fibers in the diaphragm. Female mice show also an
CC increase in the abundance of type 1 muscle fibers in the extensor
CC digitorum longus. Conditional knockout in neurons leads to decreased
CC body mass; male show reduced white adipose tissue mass while female
CC show reduced perigonadal fat mass. Show also abnormal circling behavior
CC and severe seizures. {ECO:0000269|PubMed:27270415}.
CC -!- SIMILARITY: Belongs to the ARV1 family. {ECO:0000305}.
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DR EMBL; AK004398; BAB23288.1; -; mRNA.
DR EMBL; AK042561; BAC31293.1; -; mRNA.
DR CCDS; CCDS22774.1; -.
DR RefSeq; NP_081131.1; NM_026855.4.
DR RefSeq; XP_006531400.1; XM_006531337.3.
DR RefSeq; XP_006531401.1; XM_006531338.2.
DR RefSeq; XP_011246798.1; XM_011248496.2.
DR AlphaFoldDB; Q9D0U9; -.
DR STRING; 10090.ENSMUSP00000034463; -.
DR PhosphoSitePlus; Q9D0U9; -.
DR EPD; Q9D0U9; -.
DR MaxQB; Q9D0U9; -.
DR PaxDb; Q9D0U9; -.
DR PRIDE; Q9D0U9; -.
DR ProteomicsDB; 277240; -.
DR Antibodypedia; 34681; 100 antibodies from 21 providers.
DR DNASU; 68865; -.
DR Ensembl; ENSMUST00000034463; ENSMUSP00000034463; ENSMUSG00000031982.
DR GeneID; 68865; -.
DR KEGG; mmu:68865; -.
DR UCSC; uc009nxn.1; mouse.
DR CTD; 64801; -.
DR MGI; MGI:1916115; Arv1.
DR VEuPathDB; HostDB:ENSMUSG00000031982; -.
DR eggNOG; KOG3134; Eukaryota.
DR GeneTree; ENSGT00390000002675; -.
DR HOGENOM; CLU_076722_0_0_1; -.
DR InParanoid; Q9D0U9; -.
DR OMA; KITICDS; -.
DR OrthoDB; 1466379at2759; -.
DR PhylomeDB; Q9D0U9; -.
DR TreeFam; TF105845; -.
DR Reactome; R-MMU-191273; Cholesterol biosynthesis.
DR BioGRID-ORCS; 68865; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Arv1; mouse.
DR PRO; PR:Q9D0U9; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q9D0U9; protein.
DR Bgee; ENSMUSG00000031982; Expressed in yolk sac and 139 other tissues.
DR ExpressionAtlas; Q9D0U9; baseline and differential.
DR Genevisible; Q9D0U9; MM.
DR GO; GO:0032541; C:cortical endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
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:0008206; P:bile acid metabolic process; IMP:MGI.
DR GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0030301; P:cholesterol transport; IDA:MGI.
DR GO; GO:0032366; P:intracellular sterol transport; IBA:GO_Central.
DR GO; GO:0090181; P:regulation of cholesterol metabolic process; IMP:MGI.
DR GO; GO:0032383; P:regulation of intracellular cholesterol transport; ISS:UniProtKB.
DR GO; GO:0097036; P:regulation of plasma membrane sterol distribution; IBA:GO_Central.
DR GO; GO:0006665; P:sphingolipid metabolic process; IBA:GO_Central.
DR GO; GO:0016125; P:sterol metabolic process; IBA:GO_Central.
DR InterPro; IPR007290; Arv1.
DR PANTHER; PTHR14467; PTHR14467; 1.
DR Pfam; PF04161; Arv1; 1.
PE 2: Evidence at transcript level;
KW Cholesterol metabolism; Endoplasmic reticulum; Lipid metabolism;
KW Lipid transport; Membrane; Reference proteome; Steroid metabolism;
KW Sterol metabolism; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..266
FT /note="Protein ARV1"
FT /id="PRO_0000228660"
FT TRANSMEM 139..159
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 228..248
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 266 AA; 30535 MW; 8A7C7C1078F4BC76 CRC64;
MGTGGRRGTR SGKGTEGAAA TSSSCLYRCI ECNREAQELY RDYSHGVLKI TICKSCQKPV
DKYIEYDPVI ILINAILCKT QAYRHILFNT KINIHGKLCM FCLLCEAYLR WWQLQDSSQS
PAPDDVIRYA KEWDFYRMFV IASFEQAAFL TGIFAFLWVQ QPMTAKRAPD FVLLLKALLL
SSYGKLLLIP AVIWEHDYTP LCLRLIKVFV LTSNFQAVRV TLNTNRRLSL LVVLSGLLLE
SIVVFFFQRM EWDVSSDCAL YKSQDF
