ACOX2_HUMAN
ID ACOX2_HUMAN Reviewed; 681 AA.
AC Q99424; A6NF16; B2R8U5;
DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Peroxisomal acyl-coenzyme A oxidase 2 {ECO:0000303|PubMed:14702039};
DE EC=1.17.99.3 {ECO:0000269|PubMed:27884763};
DE AltName: Full=3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl-CoA 24-hydroxylase;
DE AltName: Full=3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl-CoA oxidase {ECO:0000250|UniProtKB:O02767};
DE AltName: Full=Trihydroxycoprostanoyl-CoA oxidase {ECO:0000250|UniProtKB:P97562};
DE Short=THCA-CoA oxidase {ECO:0000250|UniProtKB:O02767};
DE Short=THCCox;
GN Name=ACOX2 {ECO:0000312|HGNC:HGNC:120};
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], PROTEIN SEQUENCE OF 8-14; 271-282; 337-346;
RP 450-468 AND 656-664, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=8943006; DOI=10.1073/pnas.93.24.13748;
RA Baumgart E., Vanhooren J.C.T., Fransen M., Marynen P., Puype M.,
RA Vandekerckhove J., Leunissen J.A.M., Fahimi H.D., Mannaerts G.P.,
RA Van Veldhoven P.P.;
RT "Molecular characterization of the human peroxisomal branched-chain acyl-
RT CoA oxidase: cDNA cloning, chromosomal assignment, tissue distribution, and
RT evidence for the absence of the protein in Zellweger's syndrome.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:13748-13753(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Fournier B., Baumgart E., Fahimi D., Mannaerts G.P., Van Veldhoven P.P.;
RT "Genomic sequence of peroxisomal human branched chain acyl-CoA oxidase.";
RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon;
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9 AND THR-13, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [8]
RP INVOLVEMENT IN CBAS6, VARIANT CBAS6 69-TYR--LEU-682 DEL, AND
RP CHARACTERIZATION OF VARIANT CBAS6 69-TYR--LEU-682 DEL.
RX PubMed=27647924; DOI=10.1073/pnas.1613228113;
RA Vilarinho S., Sari S., Mazzacuva F., Bilguevar K., Esendagli-Yilmaz G.,
RA Jain D., Akyol G., Dalgic B., Guenel M., Clayton P.T., Lifton R.P.;
RT "ACOX2 deficiency: A disorder of bile acid synthesis with transaminase
RT elevation, liver fibrosis, ataxia, and cognitive impairment.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:11289-11293(2016).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INVOLVEMENT IN CBAS6,
RP VARIANT CBAS6 TRP-225, AND CHARACTERIZATION OF VARIANT CBAS6 TRP-225.
RX PubMed=27884763; DOI=10.1016/j.jhep.2016.11.005;
RA Monte M.J., Alonso-Pena M., Briz O., Herraez E., Berasain C., Argemi J.,
RA Prieto J., Marin J.J.;
RT "ACOX2 deficiency: An inborn error of bile acid synthesis identified in an
RT adolescent with persistent hypertransaminasemia.";
RL J. Hepatol. 66:581-588(2017).
CC -!- FUNCTION: Oxidizes the CoA esters of the bile acid intermediates
CC di- and tri-hydroxycholestanoic acids (PubMed:27884763). Capable of
CC oxidizing short as well as long chain 2-methyl branched fatty acids (By
CC similarity). {ECO:0000250|UniProtKB:P07872,
CC ECO:0000269|PubMed:27884763}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oyl-
CC CoA + A + H2O = (24R,25R)-3alpha,7alpha,12alpha,24-tetrahydroxy-
CC 5beta-cholestan-26-oyl-CoA + AH2; Xref=Rhea:RHEA:15733,
CC ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:58677, ChEBI:CHEBI:59807; EC=1.17.99.3;
CC Evidence={ECO:0000269|PubMed:27884763};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15734;
CC Evidence={ECO:0000305|PubMed:27884763};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(25S)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oyl-
CC CoA + O2 = (24E)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholest-24-
CC en-26-oyl-CoA + H2O2; Xref=Rhea:RHEA:46728, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:59879, ChEBI:CHEBI:77251;
CC Evidence={ECO:0000250|UniProtKB:O02767};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46729;
CC Evidence={ECO:0000250|UniProtKB:O02767};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P07872};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P07872}.
CC -!- INTERACTION:
CC Q99424; P63172: DYNLT1; NbExp=3; IntAct=EBI-12026476, EBI-1176455;
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:27884763,
CC ECO:0000269|PubMed:8943006}.
CC -!- TISSUE SPECIFICITY: Present in all tissues tested: heart, brain,
CC placenta, lung, liver, skeletal muscle, kidney and pancreas. Most
CC abundant in heart, liver and kidney. {ECO:0000269|PubMed:8943006}.
CC -!- DISEASE: Congenital bile acid synthesis defect 6 (CBAS6) [MIM:617308]:
CC An inborn error of bile acid synthesis characterized by abnormally
CC increased liver enzymes, hypolipidemia and low cholesterol, vitamin D
CC deficiency, elevated plasma and urinary levels of C27 intermediate bile
CC acids 3alpha,7alpha-dihydroxy-5beta-cholestanoic acid (DHCA) and
CC 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoic acid (THCA). Serum
CC levels of phytanic and pristanic acids are normal. Clinical features
CC include liver fibrosis, mild ataxia, delayed development, and cognitive
CC impairment. Liver histology shows many thin fibrous septa, swollen
CC hepatocytes, glycogenated nuclei, and focal acinar transformation,
CC consistent with hepatocellular injury and regeneration, without signs
CC of obvious cholestasis, cholate stasis, or steatosis. CBAS6
CC transmission pattern is consistent with autosomal recessive
CC inheritance. {ECO:0000269|PubMed:27647924,
CC ECO:0000269|PubMed:27884763}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the acyl-CoA oxidase family. {ECO:0000305}.
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DR EMBL; X95190; CAA64489.1; -; mRNA.
DR EMBL; AJ001541; CAB65596.1; -; Genomic_DNA.
DR EMBL; AJ001542; CAB65596.1; JOINED; Genomic_DNA.
DR EMBL; AJ001543; CAB65596.1; JOINED; Genomic_DNA.
DR EMBL; AJ001544; CAB65596.1; JOINED; Genomic_DNA.
DR EMBL; AJ001545; CAB65596.1; JOINED; Genomic_DNA.
DR EMBL; AJ001546; CAB65596.1; JOINED; Genomic_DNA.
DR EMBL; AJ001547; CAB65596.1; JOINED; Genomic_DNA.
DR EMBL; AJ001548; CAB65596.1; JOINED; Genomic_DNA.
DR EMBL; AK313512; BAG36292.1; -; mRNA.
DR EMBL; AC116036; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471055; EAW65375.1; -; Genomic_DNA.
DR EMBL; BC047700; AAH47700.1; -; mRNA.
DR CCDS; CCDS33775.1; -.
DR RefSeq; NP_003491.1; NM_003500.3.
DR RefSeq; XP_005265562.1; XM_005265505.1.
DR AlphaFoldDB; Q99424; -.
DR SMR; Q99424; -.
DR BioGRID; 113906; 6.
DR IntAct; Q99424; 3.
DR STRING; 9606.ENSP00000307697; -.
DR iPTMnet; Q99424; -.
DR PhosphoSitePlus; Q99424; -.
DR BioMuta; ACOX2; -.
DR DMDM; 17366636; -.
DR jPOST; Q99424; -.
DR MassIVE; Q99424; -.
DR MaxQB; Q99424; -.
DR PaxDb; Q99424; -.
DR PeptideAtlas; Q99424; -.
DR PRIDE; Q99424; -.
DR ProteomicsDB; 78260; -.
DR Antibodypedia; 31666; 323 antibodies from 33 providers.
DR DNASU; 8309; -.
DR Ensembl; ENST00000302819.10; ENSP00000307697.5; ENSG00000168306.13.
DR GeneID; 8309; -.
DR KEGG; hsa:8309; -.
DR MANE-Select; ENST00000302819.10; ENSP00000307697.5; NM_003500.4; NP_003491.1.
DR UCSC; uc003dkl.4; human.
DR CTD; 8309; -.
DR DisGeNET; 8309; -.
DR GeneCards; ACOX2; -.
DR HGNC; HGNC:120; ACOX2.
DR HPA; ENSG00000168306; Tissue enriched (liver).
DR MalaCards; ACOX2; -.
DR MIM; 601641; gene.
DR MIM; 617308; phenotype.
DR neXtProt; NX_Q99424; -.
DR OpenTargets; ENSG00000168306; -.
DR PharmGKB; PA24444; -.
DR VEuPathDB; HostDB:ENSG00000168306; -.
DR eggNOG; KOG0136; Eukaryota.
DR GeneTree; ENSGT00940000160985; -.
DR HOGENOM; CLU_014629_3_1_1; -.
DR InParanoid; Q99424; -.
DR OMA; PMMRGKL; -.
DR OrthoDB; 416859at2759; -.
DR PhylomeDB; Q99424; -.
DR TreeFam; TF300672; -.
DR BioCyc; MetaCyc:HS09732-MON; -.
DR PathwayCommons; Q99424; -.
DR Reactome; R-HSA-193368; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
DR Reactome; R-HSA-389887; Beta-oxidation of pristanoyl-CoA.
DR Reactome; R-HSA-9033241; Peroxisomal protein import.
DR SignaLink; Q99424; -.
DR BioGRID-ORCS; 8309; 5 hits in 1067 CRISPR screens.
DR ChiTaRS; ACOX2; human.
DR GenomeRNAi; 8309; -.
DR Pharos; Q99424; Tbio.
DR PRO; PR:Q99424; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q99424; protein.
DR Bgee; ENSG00000168306; Expressed in right lobe of liver and 134 other tissues.
DR ExpressionAtlas; Q99424; baseline and differential.
DR Genevisible; Q99424; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005782; C:peroxisomal matrix; TAS:Reactome.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR GO; GO:0033791; F:3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl-CoA 24-hydroxylase activity; IDA:UniProtKB.
DR GO; GO:0003997; F:acyl-CoA oxidase activity; IBA:GO_Central.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0005504; F:fatty acid binding; IBA:GO_Central.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; ISS:UniProtKB.
DR GO; GO:0016401; F:palmitoyl-CoA oxidase activity; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0033540; P:fatty acid beta-oxidation using acyl-CoA oxidase; IDA:UniProtKB.
DR GO; GO:0055088; P:lipid homeostasis; IBA:GO_Central.
DR GO; GO:0010942; P:positive regulation of cell death; IDA:UniProtKB.
DR GO; GO:1902884; P:positive regulation of response to oxidative stress; IDA:UniProtKB.
DR GO; GO:0000038; P:very long-chain fatty acid metabolic process; IBA:GO_Central.
DR Gene3D; 1.10.540.10; -; 1.
DR Gene3D; 2.40.110.10; -; 1.
DR InterPro; IPR029320; Acyl-CoA_ox_N.
DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
DR InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR InterPro; IPR012258; Acyl-CoA_oxidase.
DR InterPro; IPR002655; Acyl-CoA_oxidase_C.
DR InterPro; IPR036250; AcylCo_DH-like_C.
DR InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom.
DR PANTHER; PTHR10909; PTHR10909; 1.
DR Pfam; PF01756; ACOX; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF14749; Acyl-CoA_ox_N; 1.
DR PIRSF; PIRSF000168; Acyl-CoA_oxidase; 1.
DR SUPFAM; SSF47203; SSF47203; 2.
DR SUPFAM; SSF56645; SSF56645; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disease variant; FAD; Fatty acid metabolism;
KW Flavoprotein; Lipid metabolism; Oxidoreductase; Peroxisome; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..681
FT /note="Peroxisomal acyl-coenzyme A oxidase 2"
FT /id="PRO_0000204681"
FT MOTIF 679..681
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97562"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 13
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 66
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXD1"
FT MOD_RES 137
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXD1"
FT MOD_RES 453
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXD1"
FT MOD_RES 561
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXD1"
FT VARIANT 69..681
FT /note="Missing (in CBAS6; patient liver samples show
FT absence of the protein; complete loss of fatty acid beta-
FT oxidation activity)"
FT /evidence="ECO:0000269|PubMed:27647924"
FT /id="VAR_078764"
FT VARIANT 225
FT /note="R -> W (in CBAS6; reduces fatty acid beta-oxidation
FT activity; does not alter subcellular location;
FT dbSNP:rs150832314)"
FT /evidence="ECO:0000269|PubMed:27884763"
FT /id="VAR_078765"
SQ SEQUENCE 681 AA; 76827 MW; 7FAE9236FCBE6D4D CRC64;
MGSPVHRVSL GDTWSRQMHP DIESERYMQS FDVERLTNIL DGGAQNTALR RKVESIIHSY
PEFSCKDNYF MTQNERYKAA MRRAFHIRLI ARRLGWLEDG RELGYAYRAL SGDVALNIHR
VFVRALRSLG SEEQIAKWDP LCKNIQIIAT YAQTELGHGT YLQGLETEAT YDAATQEFVI
HSPTLTATKW WPGDLGRSAT HALVQAQLIC SGARRGMHAF IVPIRSLQDH TPLPGIIIGD
IGPKMDFDQT DNGFLQLNHV RVPRENMLSR FAQVLPDGTY VKLGTAQSNY LPMVVVRVEL
LSGEILPILQ KACVIAMRYS VIRRQSRLRP SDPEAKVLDY QTQQQKLFPQ LAISYAFHFL
AVSLLEFFQH SYTAILNQDF SFLPELHALS TGMKAMMSEF CTQGAEMCRR ACGGHGYSKL
SGLPSLVTKL SASCTYEGEN TVLYLQVARF LVKSYLQTQM SPGSTPQRSL SPSVAYLTAP
DLARCPAQRA ADFLCPELYT TAWAHVAVRL IKDSVQHLQT LTQSGADQHE AWNQTTVIHL
QAAKVHCYYV TVKGFTEALE KLENEPAIQQ VLKRLCDLHA IHGILTNSGD FLHDAFLSGA
QVDMARTAYL DLLRLIRKDA ILLTDAFDFT DQCLNSALGC YDGNVYERLF QWAQKSPTNT
QENPAYEEYI RPLLQSWRSK L
