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Cytosolic acyl coenzyme A thioester hydrolase (EC 3.1.2.2) (Acyl-CoA thioesterase 7) (Brain acyl-CoA hydrolase) (BACH) (CTE-IIa) (CTE-II) (Long chain acyl-CoA thioester hydrolase)

 BACH_HUMAN              Reviewed;         380 AA.
O00154; A8K0K7; A8K232; A8K6B8; A8K837; B3KQ12; O43703; Q53Y78;
Q5JYL2; Q5JYL3; Q5JYL4; Q5JYL5; Q5JYL6; Q5TGR4; Q9UJM9; Q9Y539;
Q9Y540;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
12-FEB-2003, sequence version 3.
27-SEP-2017, entry version 167.
RecName: Full=Cytosolic acyl coenzyme A thioester hydrolase;
EC=3.1.2.2;
AltName: Full=Acyl-CoA thioesterase 7;
AltName: Full=Brain acyl-CoA hydrolase;
Short=BACH;
AltName: Full=CTE-IIa;
Short=CTE-II;
AltName: Full=Long chain acyl-CoA thioester hydrolase;
Name=ACOT7; Synonyms=BACH;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), AND CHARACTERIZATION.
TISSUE=Brain;
PubMed=10578051; DOI=10.1093/oxfordjournals.jbchem.a022544;
Yamada J., Kurata A., Hirata M., Taniguchi T., Takama H., Furihata T.,
Shiratori K., Iida N., Takagi-Sakuma M., Watanabe T., Kurosaki K.,
Endo T., Suga T.;
"Purification, molecular cloning, and genomic organization of human
brain long-chain acyl-CoA hydrolase.";
J. Biochem. 126:1013-1019(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 5 AND 6), SUBCELLULAR
LOCATION, AND TISSUE SPECIFICITY.
TISSUE=Brain;
PubMed=12435388; DOI=10.1016/S0006-291X(02)02587-1;
Yamada J., Kuramochi Y., Takagi M., Watanabe T., Suga T.;
"Human brain acyl-CoA hydrolase isoforms encoded by a single gene.";
Biochem. Biophys. Res. Commun. 299:49-56(2002).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
TISSUE=Hippocampus;
Hajra A.K., Uhler M.D., Larkins L.K.;
Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 4; 5; 6 AND 7).
TISSUE=Cerebellum, Colon, Placenta, Stomach, and Subthalamic nucleus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
PROTEIN SEQUENCE OF 79-90, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Fetal brain;
Lubec G., Chen W.-Q.;
Submitted (JAN-2009) to UniProtKB.
[10]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-168; LYS-198 AND LYS-283,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[12]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 209-378.
Structural genomics consortium (SGC);
"Human acyl-CoA thioesterase 7.";
Submitted (AUG-2007) to the PDB data bank.
-!- FUNCTION: Acyl-CoA thioesterases are a group of enzymes that
catalyze the hydrolysis of acyl-CoAs to the free fatty acid and
coenzyme A (CoASH), providing the potential to regulate
intracellular levels of acyl-CoAs, free fatty acids and CoASH. May
play an important physiological function in brain. May play a
regulatory role by modulating the cellular levels of fatty acyl-
CoA ligands for certain transcription factors as well as the
substrates for fatty acid metabolizing enzymes, contributing to
lipid homeostasis. Has broad specificity, active towards fatty
acyl-CoAs with chain-lengths of C8-C18. Has a maximal activity
toward palmitoyl-CoA.
-!- CATALYTIC ACTIVITY: Palmitoyl-CoA + H(2)O = CoA + palmitate.
-!- SUBUNIT: Homohexamer. {ECO:0000250}.
-!- INTERACTION:
Q13554:CAMK2B; NbExp=3; IntAct=EBI-948905, EBI-1058722;
Q15038:DAZAP2; NbExp=4; IntAct=EBI-12007918, EBI-724310;
V9HW27:HEL-S-101; NbExp=3; IntAct=EBI-948905, EBI-10178933;
P43360:MAGEA6; NbExp=3; IntAct=EBI-948905, EBI-1045155;
Q9NVV9:THAP1; NbExp=3; IntAct=EBI-948905, EBI-741515;
Q9UMX0:UBQLN1; NbExp=3; IntAct=EBI-948905, EBI-741480;
Q9UMX0-2:UBQLN1; NbExp=3; IntAct=EBI-948905, EBI-10173939;
-!- SUBCELLULAR LOCATION: Isoform 4: Cytoplasm.
-!- SUBCELLULAR LOCATION: Isoform 6: Cytoplasm.
-!- SUBCELLULAR LOCATION: Isoform 1: Mitochondrion.
-!- SUBCELLULAR LOCATION: Isoform 5: Mitochondrion.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=7;
Name=1; Synonyms=B, HBACHb;
IsoId=O00154-1; Sequence=Displayed;
Name=2; Synonyms=A-X, hBACHa-X;
IsoId=O00154-2; Sequence=VSP_000152, VSP_000155, VSP_000156;
Name=3; Synonyms=A-Xi, hBACHa-Xi;
IsoId=O00154-3; Sequence=VSP_000152, VSP_000154;
Name=4; Synonyms=A, hBACHa;
IsoId=O00154-4; Sequence=VSP_000152;
Note=Major isoform.;
Name=5; Synonyms=C, hBACHc;
IsoId=O00154-5; Sequence=VSP_000151;
Name=6; Synonyms=D, hBACHd;
IsoId=O00154-6; Sequence=VSP_000153;
Name=7;
IsoId=O00154-7; Sequence=VSP_047094;
-!- TISSUE SPECIFICITY: Isoform 4 is expressed exclusively in brain.
{ECO:0000269|PubMed:12435388}.
-!- DOMAIN: Both HotDog ACOT-type hydrolase domains are required for
efficient activity. {ECO:0000250}.
-!- SEQUENCE CAUTION:
Sequence=AAB61211.1; Type=Frameshift; Positions=371; Evidence={ECO:0000305};
Sequence=AAH17365.2; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=CAI19435.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=CAI19774.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; D88894; BAA24350.1; -; mRNA.
EMBL; AB074415; BAC20174.1; -; mRNA.
EMBL; AB074416; BAC20175.1; -; mRNA.
EMBL; AB074417; BAC20176.1; -; mRNA.
EMBL; AB074418; BAC20177.1; -; mRNA.
EMBL; AB074419; BAC20178.1; -; mRNA.
EMBL; U91316; AAB61211.1; ALT_FRAME; mRNA.
EMBL; BT006888; AAP35534.1; -; mRNA.
EMBL; AK289572; BAF82261.1; -; mRNA.
EMBL; AK290097; BAF82786.1; -; mRNA.
EMBL; AK291583; BAF84272.1; -; mRNA.
EMBL; AK292202; BAF84891.1; -; mRNA.
EMBL; AK057168; BAG51874.1; -; mRNA.
EMBL; AL031847; CAI19440.1; -; Genomic_DNA.
EMBL; AL031848; CAI19440.1; JOINED; Genomic_DNA.
EMBL; AL031847; CAI19435.1; ALT_INIT; Genomic_DNA.
EMBL; AL031848; CAI19435.1; JOINED; Genomic_DNA.
EMBL; AL031847; CAI19442.1; -; Genomic_DNA.
EMBL; AL031848; CAI19442.1; JOINED; Genomic_DNA.
EMBL; AL031847; CAI19443.1; -; Genomic_DNA.
EMBL; AL031848; CAI19443.1; JOINED; Genomic_DNA.
EMBL; AL031848; CAI19774.1; ALT_INIT; Genomic_DNA.
EMBL; AL031847; CAI19774.1; JOINED; Genomic_DNA.
EMBL; AL031848; CAI19777.1; -; Genomic_DNA.
EMBL; AL031847; CAI19777.1; JOINED; Genomic_DNA.
EMBL; AL031848; CAI19778.1; -; Genomic_DNA.
EMBL; AL031847; CAI19778.1; JOINED; Genomic_DNA.
EMBL; AL031848; CAI19779.1; -; Genomic_DNA.
EMBL; AL031847; CAI19779.1; JOINED; Genomic_DNA.
EMBL; CH471130; EAW71528.1; -; Genomic_DNA.
EMBL; CH471130; EAW71529.1; -; Genomic_DNA.
EMBL; CH471130; EAW71530.1; -; Genomic_DNA.
EMBL; BC017365; AAH17365.2; ALT_INIT; mRNA.
CCDS; CCDS30573.1; -. [O00154-7]
CCDS; CCDS65.1; -. [O00154-1]
CCDS; CCDS66.1; -. [O00154-5]
CCDS; CCDS67.1; -. [O00154-6]
PIR; JC7161; JC7161.
RefSeq; NP_009205.3; NM_007274.3. [O00154-7]
RefSeq; NP_863654.1; NM_181864.2. [O00154-1]
RefSeq; NP_863655.1; NM_181865.2. [O00154-5]
RefSeq; NP_863656.1; NM_181866.2. [O00154-6]
UniGene; Hs.126137; -.
PDB; 2QQ2; X-ray; 2.80 A; A/B/C/D/E/F/G/H/I/J/K/L=209-378.
PDBsum; 2QQ2; -.
ProteinModelPortal; O00154; -.
SMR; O00154; -.
BioGrid; 116460; 38.
IntAct; O00154; 22.
MINT; MINT-2869715; -.
STRING; 9606.ENSP00000367086; -.
iPTMnet; O00154; -.
PhosphoSitePlus; O00154; -.
SwissPalm; O00154; -.
BioMuta; ACOT7; -.
UCD-2DPAGE; O00154; -.
EPD; O00154; -.
MaxQB; O00154; -.
PaxDb; O00154; -.
PeptideAtlas; O00154; -.
PRIDE; O00154; -.
TopDownProteomics; O00154-1; -. [O00154-1]
DNASU; 11332; -.
Ensembl; ENST00000361521; ENSP00000354615; ENSG00000097021. [O00154-7]
Ensembl; ENST00000377842; ENSP00000367073; ENSG00000097021. [O00154-6]
Ensembl; ENST00000377845; ENSP00000367076; ENSG00000097021. [O00154-5]
Ensembl; ENST00000377855; ENSP00000367086; ENSG00000097021. [O00154-1]
Ensembl; ENST00000377860; ENSP00000367091; ENSG00000097021. [O00154-3]
Ensembl; ENST00000418124; ENSP00000402532; ENSG00000097021. [O00154-2]
Ensembl; ENST00000545482; ENSP00000439218; ENSG00000097021. [O00154-7]
Ensembl; ENST00000608083; ENSP00000476610; ENSG00000097021. [O00154-4]
GeneID; 11332; -.
KEGG; hsa:11332; -.
UCSC; uc001amq.4; human. [O00154-1]
CTD; 11332; -.
DisGeNET; 11332; -.
EuPathDB; HostDB:ENSG00000097021.19; -.
GeneCards; ACOT7; -.
HGNC; HGNC:24157; ACOT7.
HPA; HPA025735; -.
HPA; HPA025762; -.
MIM; 602587; gene.
neXtProt; NX_O00154; -.
OpenTargets; ENSG00000097021; -.
PharmGKB; PA142672655; -.
eggNOG; KOG2763; Eukaryota.
eggNOG; COG1607; LUCA.
GeneTree; ENSGT00760000119297; -.
HOGENOM; HOG000007663; -.
HOVERGEN; HBG036928; -.
InParanoid; O00154; -.
KO; K17360; -.
OMA; PTDVNWG; -.
OrthoDB; EOG091G0CG4; -.
PhylomeDB; O00154; -.
TreeFam; TF329579; -.
BRENDA; 3.1.2.2; 2681.
BRENDA; 3.1.2.20; 2681.
Reactome; R-HSA-77289; Mitochondrial Fatty Acid Beta-Oxidation.
SABIO-RK; O00154; -.
ChiTaRS; ACOT7; human.
EvolutionaryTrace; O00154; -.
GeneWiki; ACOT7; -.
GenomeRNAi; 11332; -.
PRO; PR:O00154; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000097021; -.
ExpressionAtlas; O00154; baseline and differential.
Genevisible; O00154; HS.
GO; GO:0005829; C:cytosol; IDA:BHF-UCL.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0047617; F:acyl-CoA hydrolase activity; TAS:Reactome.
GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW.
GO; GO:0000062; F:fatty-acyl-CoA binding; IDA:BHF-UCL.
GO; GO:0036042; F:long-chain fatty acyl-CoA binding; IDA:BHF-UCL.
GO; GO:0102991; F:myristoyl-CoA hydrolase activity; IEA:UniProtKB-EC.
GO; GO:0016290; F:palmitoyl-CoA hydrolase activity; IDA:BHF-UCL.
GO; GO:0042803; F:protein homodimerization activity; IPI:BHF-UCL.
GO; GO:0006637; P:acyl-CoA metabolic process; TAS:Reactome.
GO; GO:0015937; P:coenzyme A biosynthetic process; IDA:BHF-UCL.
GO; GO:0036116; P:long-chain fatty-acyl-CoA catabolic process; IDA:BHF-UCL.
GO; GO:0051792; P:medium-chain fatty acid biosynthetic process; IDA:BHF-UCL.
GO; GO:0036114; P:medium-chain fatty-acyl-CoA catabolic process; IDA:BHF-UCL.
GO; GO:1900535; P:palmitic acid biosynthetic process; IDA:BHF-UCL.
InterPro; IPR033120; HOTDOG_ACOT.
InterPro; IPR029069; HotDog_dom.
InterPro; IPR006683; Thioestr_dom.
Pfam; PF03061; 4HBT; 2.
SUPFAM; SSF54637; SSF54637; 2.
PROSITE; PS51770; HOTDOG_ACOT; 2.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Cytoplasm; Direct protein sequencing; Hydrolase; Mitochondrion;
Reference proteome; Repeat; Serine esterase.
CHAIN 1 380 Cytosolic acyl coenzyme A thioester
hydrolase.
/FTId=PRO_0000053806.
DOMAIN 50 168 HotDog ACOT-type 1. {ECO:0000255|PROSITE-
ProRule:PRU01106}.
DOMAIN 224 338 HotDog ACOT-type 2. {ECO:0000255|PROSITE-
ProRule:PRU01106}.
ACT_SITE 66 66 {ECO:0000250}.
ACT_SITE 255 255 {ECO:0000250}.
MOD_RES 168 168 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 198 198 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 283 283 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
VAR_SEQ 1 58 MKLLARALRLCEFGRQASSRRLVAGQGCVGPRRGCCAPVQV
VGPRADLPPCGACITGR -> MLLLRRSLSLNVLRKEVDRA
CFGEKAKQ (in isoform 5).
{ECO:0000303|PubMed:12435388,
ECO:0000303|PubMed:14702039}.
/FTId=VSP_000151.
VAR_SEQ 1 57 MKLLARALRLCEFGRQASSRRLVAGQGCVGPRRGCCAPVQV
VGPRADLPPCGACITG -> MSGPDVETPSAIQIC (in
isoform 2, isoform 3 and isoform 4).
{ECO:0000303|PubMed:10578051,
ECO:0000303|PubMed:12435388,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.3, ECO:0000303|Ref.4}.
/FTId=VSP_000152.
VAR_SEQ 1 57 MKLLARALRLCEFGRQASSRRLVAGQGCVGPRRGCCAPVQV
VGPRADLPPCGACITG -> MAFQLS (in isoform
6). {ECO:0000303|PubMed:12435388,
ECO:0000303|PubMed:14702039}.
/FTId=VSP_000153.
VAR_SEQ 1 57 MKLLARALRLCEFGRQASSRRLVAGQGCVGPRRGCCAPVQV
VGPRADLPPCGACITG -> MARPGLIHSAPGLPDTCALLQ
PPAASAAAAPSMSGPDVETPSAIQIC (in isoform
7). {ECO:0000303|PubMed:14702039}.
/FTId=VSP_047094.
VAR_SEQ 287 380 GCVITISGRMTFTSNKSMEIEVLVDADPVVDSSQKRYRAAS
AFFTYVSLSQEGRSLPVPQLVPETEDEKKRFEEGKGRYLQM
KAKRQGHAEPQP -> AHVMPAGADHTAPSSSPSTGTKCSL
LRHHHLGTHDLHEQ (in isoform 3).
{ECO:0000303|PubMed:12435388}.
/FTId=VSP_000154.
VAR_SEQ 287 288 GC -> AP (in isoform 2).
{ECO:0000303|PubMed:12435388}.
/FTId=VSP_000155.
VAR_SEQ 289 380 Missing (in isoform 2).
{ECO:0000303|PubMed:12435388}.
/FTId=VSP_000156.
CONFLICT 82 82 E -> G (in Ref. 5; BAG51874).
{ECO:0000305}.
CONFLICT 371 372 KR -> DD (in Ref. 3; AAB61211).
{ECO:0000305}.
CONFLICT 377 378 EP -> DA (in Ref. 3; AAB61211).
{ECO:0000305}.
HELIX 223 226 {ECO:0000244|PDB:2QQ2}.
STRAND 228 233 {ECO:0000244|PDB:2QQ2}.
HELIX 236 238 {ECO:0000244|PDB:2QQ2}.
STRAND 241 245 {ECO:0000244|PDB:2QQ2}.
HELIX 247 266 {ECO:0000244|PDB:2QQ2}.
STRAND 267 280 {ECO:0000244|PDB:2QQ2}.
STRAND 288 299 {ECO:0000244|PDB:2QQ2}.
STRAND 301 314 {ECO:0000244|PDB:2QQ2}.
STRAND 323 335 {ECO:0000244|PDB:2QQ2}.
HELIX 352 371 {ECO:0000244|PDB:2QQ2}.
SEQUENCE 380 AA; 41796 MW; BDD75D62A60095BC CRC64;
MKLLARALRL CEFGRQASSR RLVAGQGCVG PRRGCCAPVQ VVGPRADLPP CGACITGRIM
RPDDANVAGN VHGGTILKMI EEAGAIISTR HCNSQNGERC VAALARVERT DFLSPMCIGE
VAHVSAEITY TSKHSVEVQV NVMSENILTG AKKLTNKATL WYVPLSLKNV DKVLEVPPVV
YSRQEQEEEG RKRYEAQKLE RMETKWRNGD IVQPVLNPEP NTVSYSQSSL IHLVGPSDCT
LHGFVHGGVT MKLMDEVAGI VAARHCKTNI VTASVDAINF HDKIRKGCVI TISGRMTFTS
NKSMEIEVLV DADPVVDSSQ KRYRAASAFF TYVSLSQEGR SLPVPQLVPE TEDEKKRFEE
GKGRYLQMKA KRQGHAEPQP


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