ID   ARV1_HUMAN              Reviewed;         271 AA.
AC   Q9H2C2; A8KAI4; Q5VSN7; Q5VSN8; Q5VSN9; Q5VSP0; Q5VSP2; Q9H2H2; Q9H5V6;
AC   Q9UFF5;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   27-MAR-2024, entry version 162.
DE   RecName: Full=Protein ARV1;
DE            Short=hARV1;
GN   Name=ARV1; ORFNames=HT035;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND POSSIBLE FUNCTION.
RX   PubMed=11063737; DOI=10.1074/jbc.c000710200;
RA   Tinkelenberg A.H., Liu Y., Alcantara F., Khan S., Guo Z., Bard M.,
RA   Sturley S.L.;
RT   "Mutations in yeast ARV1 alter intracellular sterol distribution and are
RT   complemented by human ARV1.";
RL   J. Biol. Chem. 275:40667-40670(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   He Y., Tan D., Lai J., Xie Y., Qian W., Yu M., He J.;
RT   "Cloning and analysis of a G1/S and G2/M phase transition related
RT   protein.";
RL   Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Hypothalamus;
RA   Xu X., Yang Y., Gao G., Xiao H., Chen Z., Han Z.;
RL   Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Uterus;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
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., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., 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., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., 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., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., 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., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Bone marrow;
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 project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 192-271.
RC   TISSUE=Testis;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [9]
RP   POSSIBLE FUNCTION.
RX   PubMed=12145310; DOI=10.1074/jbc.m206624200;
RA   Swain E., Stukey J., McDonough V., Germann M., Liu Y., Sturley S.L.,
RA   Nickels J.T. Jr.;
RT   "Yeast cells lacking the ARV1 gene harbor defects in sphingolipid
RT   metabolism. Complementation by human ARV1.";
RL   J. Biol. Chem. 277:36152-36160(2002).
RN   [10]
RP   FUNCTION, SUBCELLULAR LOCATION, 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   [11]
RP   VARIANT DEE38 ARG-189, AND INVOLVEMENT IN DEE38.
RX   PubMed=25558065; DOI=10.1016/j.celrep.2014.12.015;
RA   Alazami A.M., Patel N., Shamseldin H.E., Anazi S., Al-Dosari M.S.,
RA   Alzahrani F., Hijazi H., Alshammari M., Aldahmesh M.A., Salih M.A.,
RA   Faqeih E., Alhashem A., Bashiri F.A., Al-Owain M., Kentab A.Y., Sogaty S.,
RA   Al Tala S., Temsah M.H., Tulbah M., Aljelaify R.F., Alshahwan S.A.,
RA   Seidahmed M.Z., Alhadid A.A., Aldhalaan H., Alqallaf F., Kurdi W.,
RA   Alfadhel M., Babay Z., Alsogheer M., Kaya N., Al-Hassnan Z.N.,
RA   Abdel-Salam G.M., Al-Sannaa N., Al Mutairi F., El Khashab H.Y., Bohlega S.,
RA   Jia X., Nguyen H.C., Hammami R., Adly N., Mohamed J.Y., Abdulwahab F.,
RA   Ibrahim N., Naim E.A., Al-Younes B., Meyer B.F., Hashem M., Shaheen R.,
RA   Xiong Y., Abouelhoda M., Aldeeri A.A., Monies D.M., Alkuraya F.S.;
RT   "Accelerating novel candidate gene discovery in neurogenetic disorders via
RT   whole-exome sequencing of prescreened multiplex consanguineous families.";
RL   Cell Rep. 10:148-161(2015).
RN   [12]
RP   VARIANTS DEE38 59-LYS--ASN-98 DEL AND ARG-189, AND CHARACTERIZATION OF
RP   VARIANTS DEE38 59-LYS--ASN-98 AND ARG-189.
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:11063737,
CC       PubMed:12145310, PubMed:20663892). Participates in sterol transport out
CC       of the ER and distribution into plasma membranes (PubMed:20663892).
CC       {ECO:0000269|PubMed:11063737, ECO:0000269|PubMed:12145310,
CC       ECO:0000269|PubMed:20663892}.
CC   -!- INTERACTION:
CC       Q9H2C2; Q13520: AQP6; NbExp=3; IntAct=EBI-11724186, EBI-13059134;
CC       Q9H2C2; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-11724186, EBI-6942903;
CC       Q9H2C2; Q15125: EBP; NbExp=3; IntAct=EBI-11724186, EBI-3915253;
CC       Q9H2C2; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-11724186, EBI-18304435;
CC       Q9H2C2; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-11724186, EBI-13345167;
CC       Q9H2C2; P15941-11: MUC1; NbExp=3; IntAct=EBI-11724186, EBI-17263240;
CC       Q9H2C2; Q6P5S7: RNASEK; NbExp=3; IntAct=EBI-11724186, EBI-18397230;
CC       Q9H2C2; Q9NY72: SCN3B; NbExp=4; IntAct=EBI-11724186, EBI-17247926;
CC       Q9H2C2; Q3KNW5: SLC10A6; NbExp=3; IntAct=EBI-11724186, EBI-18159983;
CC       Q9H2C2; Q96MV1: TLCD4; NbExp=3; IntAct=EBI-11724186, EBI-12947623;
CC       Q9H2C2; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-11724186, EBI-8638294;
CC       Q9H2C2; Q9Y320: TMX2; NbExp=3; IntAct=EBI-11724186, EBI-6447886;
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:20663892}; Multi-pass membrane protein
CC       {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in liver and adipose.
CC       {ECO:0000269|PubMed:20663892}.
CC   -!- DISEASE: Developmental and epileptic encephalopathy 38 (DEE38)
CC       [MIM:617020]: A form of epileptic encephalopathy, a heterogeneous group
CC       of severe early-onset epilepsies characterized by refractory seizures,
CC       neurodevelopmental impairment, and poor prognosis. Development is
CC       normal prior to seizure onset, after which cognitive and motor delays
CC       become apparent. DEE38 inheritance is autosomal recessive.
CC       {ECO:0000269|PubMed:25558065, ECO:0000269|PubMed:27270415}. Note=The
CC       disease is caused by variants affecting the gene represented in this
CC       entry.
CC   -!- MISCELLANEOUS: When transfected in S.cerevisiae, it can complement the
CC       absence of yeast of ARV1 protein, suggesting a conserved role in
CC       sphingolipid metabolism. {ECO:0000269|PubMed:11063737,
CC       ECO:0000269|PubMed:12145310}.
CC   -!- SIMILARITY: Belongs to the ARV1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB15513.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR   EMBL; AF290878; AAG47671.1; -; mRNA.
DR   EMBL; AF321442; AAK11180.1; -; mRNA.
DR   EMBL; AF271780; AAG44791.1; -; mRNA.
DR   EMBL; AK026629; BAB15513.1; ALT_SEQ; mRNA.
DR   EMBL; AK293049; BAF85738.1; -; mRNA.
DR   EMBL; AL732414; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL844165; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471098; EAW69935.1; -; Genomic_DNA.
DR   EMBL; BC016309; AAH16309.1; -; mRNA.
DR   EMBL; AL122047; CAB59183.3; -; mRNA.
DR   CCDS; CCDS1589.1; -.
DR   PIR; T34534; T34534.
DR   RefSeq; NP_001333921.1; NM_001346992.1.
DR   RefSeq; NP_073623.1; NM_022786.2.
DR   AlphaFoldDB; Q9H2C2; -.
DR   BioGRID; 122307; 63.
DR   IntAct; Q9H2C2; 31.
DR   MINT; Q9H2C2; -.
DR   STRING; 9606.ENSP00000312458; -.
DR   TCDB; 9.A.19.1.2; the lipid intermediate transporter (arv1) family.
DR   iPTMnet; Q9H2C2; -.
DR   PhosphoSitePlus; Q9H2C2; -.
DR   BioMuta; ARV1; -.
DR   DMDM; 74752603; -.
DR   EPD; Q9H2C2; -.
DR   jPOST; Q9H2C2; -.
DR   MassIVE; Q9H2C2; -.
DR   MaxQB; Q9H2C2; -.
DR   PaxDb; 9606-ENSP00000312458; -.
DR   PeptideAtlas; Q9H2C2; -.
DR   ProteomicsDB; 80527; -.
DR   Pumba; Q9H2C2; -.
DR   Antibodypedia; 34681; 104 antibodies from 21 providers.
DR   DNASU; 64801; -.
DR   Ensembl; ENST00000310256.7; ENSP00000312458.2; ENSG00000173409.14.
DR   GeneID; 64801; -.
DR   KEGG; hsa:64801; -.
DR   MANE-Select; ENST00000310256.7; ENSP00000312458.2; NM_022786.3; NP_073623.1.
DR   UCSC; uc001huh.4; human.
DR   AGR; HGNC:29561; -.
DR   CTD; 64801; -.
DR   DisGeNET; 64801; -.
DR   GeneCards; ARV1; -.
DR   HGNC; HGNC:29561; ARV1.
DR   HPA; ENSG00000173409; Low tissue specificity.
DR   MalaCards; ARV1; -.
DR   MIM; 611647; gene.
DR   MIM; 617020; phenotype.
DR   neXtProt; NX_Q9H2C2; -.
DR   OpenTargets; ENSG00000173409; -.
DR   Orphanet; 442835; Non-specific early-onset epileptic encephalopathy.
DR   PharmGKB; PA134935092; -.
DR   VEuPathDB; HostDB:ENSG00000173409; -.
DR   eggNOG; KOG3134; Eukaryota.
DR   GeneTree; ENSGT00390000002675; -.
DR   InParanoid; Q9H2C2; -.
DR   OMA; IHGKLCV; -.
DR   OrthoDB; 1204580at2759; -.
DR   PhylomeDB; Q9H2C2; -.
DR   TreeFam; TF105845; -.
DR   PathwayCommons; Q9H2C2; -.
DR   Reactome; R-HSA-191273; Cholesterol biosynthesis.
DR   SignaLink; Q9H2C2; -.
DR   BioGRID-ORCS; 64801; 15 hits in 1154 CRISPR screens.
DR   ChiTaRS; ARV1; human.
DR   GenomeRNAi; 64801; -.
DR   Pharos; Q9H2C2; Tbio.
DR   PRO; PR:Q9H2C2; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q9H2C2; Protein.
DR   Bgee; ENSG00000173409; Expressed in cardiac muscle of right atrium and 192 other cell types or tissues.
DR   ExpressionAtlas; Q9H2C2; baseline and differential.
DR   GO; GO:0032541; C:cortical endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR   GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR   GO; GO:0015248; F:sterol transporter activity; TAS:Reactome.
DR   GO; GO:0008206; P:bile acid metabolic process; IEA:Ensembl.
DR   GO; GO:0006695; P:cholesterol biosynthetic process; TAS:Reactome.
DR   GO; GO:0030301; P:cholesterol transport; IEA:Ensembl.
DR   GO; GO:0032366; P:intracellular sterol transport; IBA:GO_Central.
DR   GO; GO:0090181; P:regulation of cholesterol metabolic process; IMP:UniProtKB.
DR   GO; GO:0032383; P:regulation of intracellular cholesterol transport; IMP: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; ARV1; 1.
DR   PANTHER; PTHR14467:SF0; PROTEIN ARV1; 1.
DR   Pfam; PF04161; Arv1; 1.
DR   Genevisible; Q9H2C2; HS.
PE   1: Evidence at protein level;
KW   Cholesterol metabolism; Disease variant; Endoplasmic reticulum; Epilepsy;
KW   Lipid metabolism; Lipid transport; Membrane; Reference proteome;
KW   Steroid metabolism; Sterol metabolism; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..271
FT                   /note="Protein ARV1"
FT                   /id="PRO_0000228659"
FT   TRANSMEM        144..164
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        176..196
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        233..253
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   VARIANT         59..98
FT                   /note="Missing (in DEE38; loss of protein stability; yeast
FT                   complementation assays show that the variant does not
FT                   rescue cell growth)"
FT                   /evidence="ECO:0000269|PubMed:27270415"
FT                   /id="VAR_077050"
FT   VARIANT         101
FT                   /note="G -> E (in dbSNP:rs35764859)"
FT                   /id="VAR_033525"
FT   VARIANT         189
FT                   /note="G -> R (in DEE38; loss of protein stability; yeast
FT                   complementation assays show that the variant does partially
FT                   rescue cell growth; dbSNP:rs730882241)"
FT                   /evidence="ECO:0000269|PubMed:25558065,
FT                   ECO:0000269|PubMed:27270415"
FT                   /id="VAR_077051"
FT   CONFLICT        135..136
FT                   /note="AK -> VR (in Ref. 4; BAB15513)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        182
FT                   /note="A -> D (in Ref. 2; AAG44791)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   271 AA;  31052 MW;  35C065EB00FD4671 CRC64;
     MGNGGRSGLQ QGKGNVDGVA ATPTAASASC QYRCIECNQE AKELYRDYNH GVLKITICKS
     CQKPVDKYIE YDPVIILINA ILCKAQAYRH ILFNTQINIH GKLCIFCLLC EAYLRWWQLQ
     DSNQNTAPDD LIRYAKEWDF YRMFAIAALE QTAYFIGIFT FLWVERPMTA KKKPNFILLL
     KALLLSSYGK LLLIPAVIWE HDYTSVCLKL IKVFVLTSNF QAIRVTLNIN RKLSFLAVLS
     GLLLESIMVY FFQSMEWDVG SDYAIFKSQD F
//