ID PURA1_HUMAN Reviewed; 457 AA.
AC Q8N142; Q86TT6; Q8N714;
DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 24-JAN-2024, entry version 183.
DE RecName: Full=Adenylosuccinate synthetase isozyme 1 {ECO:0000255|HAMAP-Rule:MF_03126};
DE Short=AMPSase 1 {ECO:0000255|HAMAP-Rule:MF_03126};
DE Short=AdSS 1 {ECO:0000255|HAMAP-Rule:MF_03126};
DE EC=6.3.4.4 {ECO:0000255|HAMAP-Rule:MF_03126, ECO:0000269|PubMed:26506222};
DE AltName: Full=Adenylosuccinate synthetase, basic isozyme {ECO:0000255|HAMAP-Rule:MF_03126};
DE AltName: Full=Adenylosuccinate synthetase, muscle isozyme {ECO:0000255|HAMAP-Rule:MF_03126};
DE Short=M-type adenylosuccinate synthetase {ECO:0000255|HAMAP-Rule:MF_03126};
DE AltName: Full=Adenylosuccinate synthetase-like 1 {ECO:0000303|PubMed:15786719};
DE Short=AdSSL1 {ECO:0000303|PubMed:15786719};
DE AltName: Full=IMP--aspartate ligase 1 {ECO:0000255|HAMAP-Rule:MF_03126};
GN Name=ADSS1 {ECO:0000312|HGNC:HGNC:20093};
GN Synonyms=ADSSL1 {ECO:0000255|HAMAP-Rule:MF_03126};
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] (ISOFORM 1), SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Bone marrow stroma;
RX PubMed=15786719; DOI=10.1007/s11010-005-2539-9;
RA Sun H., Li N., Wang X., Chen T., Shi L., Zhang L., Wang J., Wan T., Cao X.;
RT "Molecular cloning and characterization of a novel muscle adenylosuccinate
RT synthetase, AdSSL1, from human bone marrow stromal cells.";
RL Mol. Cell. Biochem. 269:85-94(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Heart;
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 1).
RC TISSUE=Placenta;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=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 [5]
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 [6]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, INVOLVEMENT IN MPD5, VARIANT MPD5
RP ASN-261, AND CHARACTERIZATION OF VARIANT MPD5 ASN-261.
RX PubMed=26506222; DOI=10.1002/ana.24550;
RA Park H.J., Hong Y.B., Choi Y.C., Lee J., Kim E.J., Lee J.S., Mo W.M.,
RA Ki S.M., Kim H.I., Kim H.J., Hyun Y.S., Hong H.D., Nam K., Jung S.C.,
RA Kim S.B., Kim S.H., Kim D.H., Oh K.W., Kim S.H., Yoo J.H., Lee J.E.,
RA Chung K.W., Choi B.O.;
RT "ADSSL1 mutation relevant to autosomal recessive adolescent onset distal
RT myopathy.";
RL Ann. Neurol. 79:231-243(2016).
CC -!- FUNCTION: Component of the purine nucleotide cycle (PNC), which
CC interconverts IMP and AMP to regulate the nucleotide levels in various
CC tissues, and which contributes to glycolysis and ammoniagenesis.
CC Catalyzes the first committed step in the biosynthesis of AMP from IMP.
CC {ECO:0000269|PubMed:26506222}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-
CC dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053,
CC ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03126, ECO:0000269|PubMed:26506222};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03126};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_03126};
CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via de novo pathway; AMP
CC from IMP: step 1/2. {ECO:0000255|HAMAP-Rule:MF_03126,
CC ECO:0000269|PubMed:26506222}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_03126}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03126,
CC ECO:0000269|PubMed:15786719}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8N142-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8N142-2; Sequence=VSP_008421;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in skeletal muscle and
CC heart, as well as in several hematopoietic cell lines and solid tumors.
CC {ECO:0000269|PubMed:15786719}.
CC -!- DISEASE: Myopathy, distal, 5 (MPD5) [MIM:617030]: A form of distal
CC myopathy, a group of muscular disorders characterized by progressive
CC muscular weakness and muscle atrophy beginning in the hands, the legs
CC or the feet. MPD5 is an autosomal recessive form, predominantly
CC affecting the lower limbs. {ECO:0000269|PubMed:26506222}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the adenylosuccinate synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_03126}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH32039.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAD62614.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY037159; AAK67646.1; -; mRNA.
DR EMBL; AK095921; BAC04649.1; -; mRNA.
DR EMBL; BX248286; CAD62614.1; ALT_INIT; mRNA.
DR EMBL; BC032039; AAH32039.1; ALT_FRAME; mRNA.
DR EMBL; BC047904; AAH47904.1; -; mRNA.
DR CCDS; CCDS9990.1; -. [Q8N142-1]
DR CCDS; CCDS9991.1; -. [Q8N142-2]
DR RefSeq; NP_001307353.1; NM_001320424.1.
DR RefSeq; NP_689541.1; NM_152328.4. [Q8N142-1]
DR RefSeq; NP_954634.1; NM_199165.2. [Q8N142-2]
DR AlphaFoldDB; Q8N142; -.
DR SMR; Q8N142; -.
DR BioGRID; 125783; 10.
DR IntAct; Q8N142; 5.
DR MINT; Q8N142; -.
DR STRING; 9606.ENSP00000333019; -.
DR DrugBank; DB03510; 6-O-Phosphoryl Inosine Monophosphate.
DR DrugBank; DB00787; Acyclovir.
DR DrugBank; DB04418; Adenylosuccinic acid.
DR DrugBank; DB05540; Alanosine.
DR DrugBank; DB00128; Aspartic acid.
DR DrugBank; DB04315; Guanosine-5'-Diphosphate.
DR DrugBank; DB04137; Guanosine-5'-Triphosphate.
DR DrugBank; DB02109; Hadacidin.
DR DrugBank; DB04566; Inosinic Acid.
DR iPTMnet; Q8N142; -.
DR PhosphoSitePlus; Q8N142; -.
DR SwissPalm; Q8N142; -.
DR BioMuta; ADSSL1; -.
DR DMDM; 37537958; -.
DR EPD; Q8N142; -.
DR jPOST; Q8N142; -.
DR MassIVE; Q8N142; -.
DR MaxQB; Q8N142; -.
DR PaxDb; 9606-ENSP00000333019; -.
DR PeptideAtlas; Q8N142; -.
DR ProteomicsDB; 71550; -. [Q8N142-1]
DR ProteomicsDB; 71551; -. [Q8N142-2]
DR Pumba; Q8N142; -.
DR Antibodypedia; 28209; 103 antibodies from 18 providers.
DR DNASU; 122622; -.
DR Ensembl; ENST00000330877.7; ENSP00000331260.2; ENSG00000185100.12. [Q8N142-1]
DR Ensembl; ENST00000332972.9; ENSP00000333019.5; ENSG00000185100.12. [Q8N142-2]
DR Ensembl; ENST00000710323.1; ENSP00000518203.1; ENSG00000185100.12. [Q8N142-1]
DR GeneID; 122622; -.
DR KEGG; hsa:122622; -.
DR MANE-Select; ENST00000330877.7; ENSP00000331260.2; NM_152328.5; NP_689541.1.
DR UCSC; uc001ypd.5; human. [Q8N142-1]
DR AGR; HGNC:20093; -.
DR CTD; 122622; -.
DR DisGeNET; 122622; -.
DR GeneCards; ADSS1; -.
DR HGNC; HGNC:20093; ADSS1.
DR HPA; ENSG00000185100; Group enriched (skeletal muscle, tongue).
DR MalaCards; ADSS1; -.
DR MIM; 612498; gene.
DR MIM; 617030; phenotype.
DR neXtProt; NX_Q8N142; -.
DR OpenTargets; ENSG00000185100; -.
DR Orphanet; 482601; Adenylosuccinate synthetase-like 1-related distal myopathy.
DR PharmGKB; PA134974111; -.
DR VEuPathDB; HostDB:ENSG00000185100; -.
DR eggNOG; KOG1355; Eukaryota.
DR GeneTree; ENSGT00390000015553; -.
DR HOGENOM; CLU_029848_0_0_1; -.
DR InParanoid; Q8N142; -.
DR OMA; TNARKWE; -.
DR OrthoDB; 122722at2759; -.
DR PhylomeDB; Q8N142; -.
DR TreeFam; TF300486; -.
DR BRENDA; 6.3.4.4; 2681.
DR PathwayCommons; Q8N142; -.
DR Reactome; R-HSA-73817; Purine ribonucleoside monophosphate biosynthesis.
DR SignaLink; Q8N142; -.
DR SIGNOR; Q8N142; -.
DR UniPathway; UPA00075; UER00335.
DR BioGRID-ORCS; 122622; 9 hits in 1153 CRISPR screens.
DR ChiTaRS; ADSSL1; human.
DR GenomeRNAi; 122622; -.
DR Pharos; Q8N142; Tbio.
DR PRO; PR:Q8N142; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q8N142; Protein.
DR Bgee; ENSG00000185100; Expressed in vastus lateralis and 170 other cell types or tissues.
DR ExpressionAtlas; Q8N142; baseline and differential.
DR Genevisible; Q8N142; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0051015; F:actin filament binding; IEA:Ensembl.
DR GO; GO:0004019; F:adenylosuccinate synthase activity; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; NAS:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0042301; F:phosphate ion binding; NAS:UniProtKB.
DR GO; GO:0044208; P:'de novo' AMP biosynthetic process; IBA:GO_Central.
DR GO; GO:0006167; P:AMP biosynthetic process; IDA:UniProtKB.
DR GO; GO:0006531; P:aspartate metabolic process; IEA:Ensembl.
DR GO; GO:0071257; P:cellular response to electrical stimulus; IEA:Ensembl.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:Ensembl.
DR GO; GO:0002376; P:immune system process; NAS:UniProtKB.
DR GO; GO:0046040; P:IMP metabolic process; IBA:GO_Central.
DR GO; GO:0014850; P:response to muscle activity; IEA:Ensembl.
DR GO; GO:0042594; P:response to starvation; IEA:Ensembl.
DR CDD; cd03108; AdSS; 1.
DR Gene3D; 3.40.440.10; Adenylosuccinate Synthetase, subunit A, domain 1; 1.
DR Gene3D; 1.10.300.10; Adenylosuccinate Synthetase, subunit A, domain 2; 1.
DR Gene3D; 3.90.170.10; Adenylosuccinate Synthetase, subunit A, domain 3; 1.
DR HAMAP; MF_00011; Adenylosucc_synth; 1.
DR HAMAP; MF_03126; Adenylosucc_synth_vert_basic; 1.
DR InterPro; IPR018220; Adenylosuccin_syn_GTP-bd.
DR InterPro; IPR033128; Adenylosuccin_syn_Lys_AS.
DR InterPro; IPR042109; Adenylosuccinate_synth_dom1.
DR InterPro; IPR042110; Adenylosuccinate_synth_dom2.
DR InterPro; IPR042111; Adenylosuccinate_synth_dom3.
DR InterPro; IPR001114; Adenylosuccinate_synthetase.
DR InterPro; IPR027509; AdSS_1_vert.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR00184; purA; 1.
DR PANTHER; PTHR11846; ADENYLOSUCCINATE SYNTHETASE; 1.
DR PANTHER; PTHR11846:SF2; ADENYLOSUCCINATE SYNTHETASE ISOZYME 1; 1.
DR Pfam; PF00709; Adenylsucc_synt; 1.
DR SMART; SM00788; Adenylsucc_synt; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS01266; ADENYLOSUCCIN_SYN_1; 1.
DR PROSITE; PS00513; ADENYLOSUCCIN_SYN_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Disease variant; GTP-binding; Ligase;
KW Magnesium; Metal-binding; Nucleotide-binding; Purine biosynthesis;
KW Reference proteome.
FT CHAIN 1..457
FT /note="Adenylosuccinate synthetase isozyme 1"
FT /id="PRO_0000095132"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 43
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03126"
FT ACT_SITE 71
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03126"
FT BINDING 42..48
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03126"
FT BINDING 43..46
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03126"
FT BINDING 43
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03126"
FT BINDING 43
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03126"
FT BINDING 68..71
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03126"
FT BINDING 70..72
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03126"
FT BINDING 70
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03126"
FT BINDING 163
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03126"
FT BINDING 177
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03126"
FT BINDING 256
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03126"
FT BINDING 271
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03126"
FT BINDING 331..337
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03126"
FT BINDING 335
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03126"
FT BINDING 337
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03126"
FT BINDING 363..365
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03126"
FT BINDING 445..448
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03126"
FT VAR_SEQ 1..64
FT /note="MSGTRASNDRPPGAGGVKRGRLQQEAAATGSRVTVVLGAQWGDEGKGKVVDL
FT LATDADIISRCQ -> MVGRSCGVATQRQGGGQRPTNLALTLSSSPAHSTALPWLPPRS
FT LQLLSGHSVPAQPTPHLPSACGGPTRVTLGEERAWRSHGSNAGGHTCLPRRTAGAGSLT
FT PGGER (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_008421"
FT VARIANT 261
FT /note="D -> N (in MPD5; decreased protein abundance;
FT decreased stability; decreased adenylosuccinate synthase
FT activity; dbSNP:rs140614802)"
FT /evidence="ECO:0000269|PubMed:26506222"
FT /id="VAR_076998"
SQ SEQUENCE 457 AA; 50208 MW; 387341D49721B2EF CRC64;
MSGTRASNDR PPGAGGVKRG RLQQEAAATG SRVTVVLGAQ WGDEGKGKVV DLLATDADII
SRCQGGNNAG HTVVVDGKEY DFHLLPSGII NTKAVSFIGN GVVIHLPGLF EEAEKNEKKG
LKDWEKRLII SDRAHLVFDF HQAVDGLQEV QRQAQEGKNI GTTKKGIGPT YSSKAARTGL
RICDLLSDFD EFSSRFKNLA HQHQSMFPTL EIDIEGQLKR LKGFAERIRP MVRDGVYFMY
EALHGPPKKI LVEGANAALL DIDFGTYPFV TSSNCTVGGV CTGLGIPPQN IGDVYGVVKA
YTTRVGIGAF PTEQINEIGG LLQTRGHEWG VTTGRKRRCG WLDLMILRYA HMVNGFTALA
LTKLDILDVL GEVKVGVSYK LNGKRIPYFP ANQEMLQKVE VEYETLPGWK ADTTGARRWE
DLPPQAQNYI RFVENHVGVA VKWVGVGKSR ESMIQLF
//
