ID   ACOT9_HUMAN             Reviewed;         439 AA.
AC   Q9Y305; B3KNC9; B7ZM94;
DT   08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 2.
DT   27-MAR-2024, entry version 172.
DE   RecName: Full=Acyl-coenzyme A thioesterase 9, mitochondrial;
DE            Short=Acyl-CoA thioesterase 9;
DE            EC=3.1.2.-;
DE   AltName: Full=Acyl-CoA thioester hydrolase 9;
DE   Flags: Precursor;
GN   Name=ACOT9; ORFNames=CGI-16;
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 [LARGE SCALE MRNA] (ISOFORM 2).
RX   PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA   Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT   "Identification of novel human genes evolutionarily conserved in
RT   Caenorhabditis elegans by comparative proteomics.";
RL   Genome Res. 10:703-713(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Placenta;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15772651; DOI=10.1038/nature03440;
RA   Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA   Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA   Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA   Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA   Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA   Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA   Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA   Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA   Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA   Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA   Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA   Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA   Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA   Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA   Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA   Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA   Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA   Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA   Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA   Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA   Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA   Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA   Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA   Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA   Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA   Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA   Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA   Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA   Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA   Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA   McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA   Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA   Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA   Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA   Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA   Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA   Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA   Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA   Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA   Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA   d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA   Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA   Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA   Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA   Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA   Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA   Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA   Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA   Rogers J., Bentley D.R.;
RT   "The DNA sequence of the human X chromosome.";
RL   Nature 434:325-337(2005).
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] (ISOFORM 1).
RC   TISSUE=Brain, and Testis;
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   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-103, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [10]
RP   VARIANT [LARGE SCALE ANALYSIS] HIS-305.
RX   PubMed=18772397; DOI=10.1126/science.1164368;
RA   Jones S., Zhang X., Parsons D.W., Lin J.C., Leary R.J., Angenendt P.,
RA   Mankoo P., Carter H., Kamiyama H., Jimeno A., Hong S.M., Fu B., Lin M.T.,
RA   Calhoun E.S., Kamiyama M., Walter K., Nikolskaya T., Nikolsky Y.,
RA   Hartigan J., Smith D.R., Hidalgo M., Leach S.D., Klein A.P., Jaffee E.M.,
RA   Goggins M., Maitra A., Iacobuzio-Donahue C., Eshleman J.R., Kern S.E.,
RA   Hruban R.H., Karchin R., Papadopoulos N., Parmigiani G., Vogelstein B.,
RA   Velculescu V.E., Kinzler K.W.;
RT   "Core signaling pathways in human pancreatic cancers revealed by global
RT   genomic analyses.";
RL   Science 321:1801-1806(2008).
CC   -!- FUNCTION: Acyl-CoA thioesterases are a group of enzymes that catalyze
CC       the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A
CC       (CoASH), providing the potential to regulate intracellular levels of
CC       acyl-CoAs, free fatty acids and CoASH. Active on long chain acyl-CoAs.
CC   -!- SUBUNIT: Interacts with NYAP1, NYAP2 and MYO16. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q9Y305-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9Y305-2; Sequence=VSP_036419;
CC       Name=3;
CC         IsoId=Q9Y305-3; Sequence=VSP_036420;
CC       Name=4;
CC         IsoId=Q9Y305-4; Sequence=VSP_041093;
CC   -!- SIMILARITY: Belongs to the acyl coenzyme A hydrolase family.
CC       {ECO:0000305}.
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DR   EMBL; AF132950; AAD27725.1; -; mRNA.
DR   EMBL; AK024337; BAG51291.1; -; mRNA.
DR   EMBL; BX648512; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AC093011; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC131011; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471074; EAW98998.1; -; Genomic_DNA.
DR   EMBL; BC136671; AAI36672.1; -; mRNA.
DR   EMBL; BC144360; AAI44361.1; -; mRNA.
DR   CCDS; CCDS35216.1; -. [Q9Y305-1]
DR   CCDS; CCDS43924.1; -. [Q9Y305-4]
DR   CCDS; CCDS83460.1; -. [Q9Y305-3]
DR   RefSeq; NP_001028755.2; NM_001033583.2. [Q9Y305-1]
DR   RefSeq; NP_001032248.1; NM_001037171.1. [Q9Y305-4]
DR   RefSeq; NP_001317188.1; NM_001330259.1. [Q9Y305-3]
DR   AlphaFoldDB; Q9Y305; -.
DR   SMR; Q9Y305; -.
DR   BioGRID; 117132; 174.
DR   IntAct; Q9Y305; 56.
DR   MINT; Q9Y305; -.
DR   STRING; 9606.ENSP00000368605; -.
DR   ChEMBL; CHEMBL4295987; -.
DR   GlyGen; Q9Y305; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9Y305; -.
DR   PhosphoSitePlus; Q9Y305; -.
DR   SwissPalm; Q9Y305; -.
DR   BioMuta; ACOT9; -.
DR   DMDM; 224471815; -.
DR   EPD; Q9Y305; -.
DR   jPOST; Q9Y305; -.
DR   MassIVE; Q9Y305; -.
DR   MaxQB; Q9Y305; -.
DR   PaxDb; 9606-ENSP00000368605; -.
DR   PeptideAtlas; Q9Y305; -.
DR   ProteomicsDB; 85953; -. [Q9Y305-1]
DR   ProteomicsDB; 85954; -. [Q9Y305-2]
DR   ProteomicsDB; 85955; -. [Q9Y305-3]
DR   ProteomicsDB; 85956; -. [Q9Y305-4]
DR   Pumba; Q9Y305; -.
DR   Antibodypedia; 24512; 280 antibodies from 31 providers.
DR   DNASU; 23597; -.
DR   Ensembl; ENST00000336430.11; ENSP00000336580.7; ENSG00000123130.17. [Q9Y305-1]
DR   Ensembl; ENST00000379295.5; ENSP00000368597.1; ENSG00000123130.17. [Q9Y305-3]
DR   Ensembl; ENST00000379303.10; ENSP00000368605.5; ENSG00000123130.17. [Q9Y305-4]
DR   GeneID; 23597; -.
DR   KEGG; hsa:23597; -.
DR   MANE-Select; ENST00000379303.10; ENSP00000368605.5; NM_001037171.2; NP_001032248.1. [Q9Y305-4]
DR   UCSC; uc004dao.4; human. [Q9Y305-1]
DR   AGR; HGNC:17152; -.
DR   CTD; 23597; -.
DR   DisGeNET; 23597; -.
DR   GeneCards; ACOT9; -.
DR   HGNC; HGNC:17152; ACOT9.
DR   HPA; ENSG00000123130; Low tissue specificity.
DR   MIM; 300862; gene.
DR   neXtProt; NX_Q9Y305; -.
DR   OpenTargets; ENSG00000123130; -.
DR   PharmGKB; PA142672656; -.
DR   VEuPathDB; HostDB:ENSG00000123130; -.
DR   eggNOG; KOG2763; Eukaryota.
DR   GeneTree; ENSGT00390000005330; -.
DR   InParanoid; Q9Y305; -.
DR   OMA; QFNYTFL; -.
DR   OrthoDB; 778282at2759; -.
DR   PhylomeDB; Q9Y305; -.
DR   TreeFam; TF313352; -.
DR   BioCyc; MetaCyc:HS04631-MONOMER; -.
DR   PathwayCommons; Q9Y305; -.
DR   Reactome; R-HSA-77289; Mitochondrial Fatty Acid Beta-Oxidation.
DR   SignaLink; Q9Y305; -.
DR   BioGRID-ORCS; 23597; 12 hits in 783 CRISPR screens.
DR   ChiTaRS; ACOT9; human.
DR   GenomeRNAi; 23597; -.
DR   Pharos; Q9Y305; Tbio.
DR   PRO; PR:Q9Y305; -.
DR   Proteomes; UP000005640; Chromosome X.
DR   RNAct; Q9Y305; Protein.
DR   Bgee; ENSG00000123130; Expressed in secondary oocyte and 193 other cell types or tissues.
DR   ExpressionAtlas; Q9Y305; baseline and differential.
DR   GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; ISS:HGNC-UCL.
DR   GO; GO:0003986; F:acetyl-CoA hydrolase activity; ISS:HGNC-UCL.
DR   GO; GO:0047617; F:acyl-CoA hydrolase activity; ISS:UniProtKB.
DR   GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016290; F:palmitoyl-CoA hydrolase activity; ISS:UniProtKB.
DR   GO; GO:0006637; P:acyl-CoA metabolic process; ISS:HGNC-UCL.
DR   CDD; cd03442; BFIT_BACH; 2.
DR   Gene3D; 3.10.129.10; Hotdog Thioesterase; 2.
DR   InterPro; IPR033120; HOTDOG_ACOT.
DR   InterPro; IPR029069; HotDog_dom_sf.
DR   PANTHER; PTHR12655; ACYL-COA THIOESTERASE; 1.
DR   PANTHER; PTHR12655:SF0; ACYL-COENZYME A THIOESTERASE 9, MITOCHONDRIAL; 1.
DR   SUPFAM; SSF54637; Thioesterase/thiol ester dehydrase-isomerase; 2.
DR   PROSITE; PS51770; HOTDOG_ACOT; 2.
DR   Genevisible; Q9Y305; HS.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Hydrolase; Mitochondrion;
KW   Reference proteome; Repeat; Serine esterase; Transit peptide.
FT   TRANSIT         1..21
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250"
FT   CHAIN           22..439
FT                   /note="Acyl-coenzyme A thioesterase 9, mitochondrial"
FT                   /id="PRO_0000053812"
FT   DOMAIN          84..209
FT                   /note="HotDog ACOT-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01106"
FT   DOMAIN          289..401
FT                   /note="HotDog ACOT-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01106"
FT   MOD_RES         103
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   VAR_SEQ         1..60
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_036420"
FT   VAR_SEQ         5..39
FT                   /note="ALRLCALGKGQLTPGRGLTQGPQNPKKQGIFHIHE -> PC (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:10810093"
FT                   /id="VSP_036419"
FT   VAR_SEQ         39
FT                   /note="E -> EACSSIHVNH (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:17974005"
FT                   /id="VSP_041093"
FT   VARIANT         305
FT                   /note="N -> H (in a pancreatic ductal adenocarcinoma
FT                   sample; somatic mutation)"
FT                   /evidence="ECO:0000269|PubMed:18772397"
FT                   /id="VAR_062668"
FT   CONFLICT        188
FT                   /note="L -> S (in Ref. 2; BAG51291)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   439 AA;  49902 MW;  1CE2158D4F83D4D6 CRC64;
     MRRAALRLCA LGKGQLTPGR GLTQGPQNPK KQGIFHIHEV RDKLREIVGA STNWRDHVKA
     MEERKLLHSF LAKSQDGLPP RRMKDSYIEV LLPLGSEPEL REKYLTVQNT VRFGRILEDL
     DSLGVLICYM HNKIHSAKMS PLSIVTALVD KIDMCKKSLS PEQDIKFSGH VSWVGKTSME
     VKMQMFQLHG DEFCPVLDAT FVMVARDSEN KGPAFVNPLI PESPEEEELF RQGELNKGRR
     IAFSSTSLLK MAPSAEERTT IHEMFLSTLD PKTISFRSRV LPSNAVWMEN SKLKSLEICH
     PQERNIFNRI FGGFLMRKAY ELAWATACSF GGSRPFVVAV DDIMFQKPVE VGSLLFLSSQ
     VCFTQNNYIQ VRVHSEVASL QEKQHTTTNV FHFTFMSEKE VPLVFPKTYG ESMLYLDGQR
     HFNSMSGPAT LRKDYLVEP
//