LAGE3_HUMAN
ID LAGE3_HUMAN Reviewed; 143 AA.
AC Q14657; Q5HY39; Q8IZ78;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=EKC/KEOPS complex subunit LAGE3 {ECO:0000305};
DE AltName: Full=L antigen family member 3 {ECO:0000303|PubMed:12384295};
DE AltName: Full=Protein ESO-3 {ECO:0000303|PubMed:12384295};
DE AltName: Full=Protein ITBA2 {ECO:0000303|PubMed:8786131};
GN Name=LAGE3 {ECO:0000312|HGNC:HGNC:26058};
GN Synonyms=DXS9879E, ESO3 {ECO:0000303|PubMed:12384295},
GN ITBA2 {ECO:0000303|PubMed:8786131};
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 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Blood, and Pancreas;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2-143, AND TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=8786131; DOI=10.1006/geno.1996.0293;
RA Faranda S., Frattini A., Zucchi I., Patrosso C., Milanesi L., Montagna C.,
RA Vezzoni P.;
RT "Characterization and fine localization of two new genes in Xq28 using the
RT genomic sequence/EST database screening approach.";
RL Genomics 34:323-327(1996).
RN [4]
RP IDENTIFICATION, AND TISSUE SPECIFICITY.
RX PubMed=12384295; DOI=10.1016/s0378-1119(02)00879-x;
RA Alpen B., Guere A.O., Scanlan M.J., Old L.J., Chen Y.-T.;
RT "A new member of the NY-ESO-1 gene family is ubiquitously expressed in
RT somatic tissues and evolutionarily conserved.";
RL Gene 297:141-149(2002).
RN [5]
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 [6]
RP IDENTIFICATION IN THE EKC/KEOPS COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=22912744; DOI=10.1371/journal.pone.0042822;
RA Costessi A., Mahrour N., Sharma V., Stunnenberg R., Stoel M.A., Tijchon E.,
RA Conaway J.W., Conaway R.C., Stunnenberg H.G.;
RT "The human EKC/KEOPS complex is recruited to Cullin2 ubiquitin ligases by
RT the human tumour antigen PRAME.";
RL PLoS ONE 7:E42822-E42822(2012).
RN [7]
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 IDENTIFICATION IN THE EKC/KEOPS COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=27903914; DOI=10.1093/nar/gkw1181;
RA Wan L.C., Maisonneuve P., Szilard R.K., Lambert J.P., Ng T.F., Manczyk N.,
RA Huang H., Laister R., Caudy A.A., Gingras A.C., Durocher D., Sicheri F.;
RT "Proteomic analysis of the human KEOPS complex identifies C14ORF142 as a
RT core subunit homologous to yeast Gon7.";
RL Nucleic Acids Res. 45:805-817(2017).
RN [9] {ECO:0007744|PDB:6GWJ}
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH GON7 AND OSGEP, AND
RP IDENTIFICATION IN THE EKC/KEOPS COMPLEX.
RX PubMed=31481669; DOI=10.1038/s41467-019-11951-x;
RA Arrondel C., Missoury S., Snoek R., Patat J., Menara G., Collinet B.,
RA Liger D., Durand D., Gribouval O., Boyer O., Buscara L., Martin G.,
RA Machuca E., Nevo F., Lescop E., Braun D.A., Boschat A.C., Sanquer S.,
RA Guerrera I.C., Revy P., Parisot M., Masson C., Boddaert N., Charbit M.,
RA Decramer S., Novo R., Macher M.A., Ranchin B., Bacchetta J., Laurent A.,
RA Collardeau-Frachon S., van Eerde A.M., Hildebrandt F., Magen D.,
RA Antignac C., van Tilbeurgh H., Mollet G.;
RT "Defects in t6A tRNA modification due to GON7 and YRDC mutations lead to
RT Galloway-Mowat syndrome.";
RL Nat. Commun. 10:3967-3967(2019).
RN [10]
RP INVOLVEMENT IN GAMOS2, VARIANTS GAMOS2 PHE-106 AND SER-137, IDENTIFICATION
RP IN THE EKC/KEOPS COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=28805828; DOI=10.1038/ng.3933;
RA Braun D.A., Rao J., Mollet G., Schapiro D., Daugeron M.C., Tan W.,
RA Gribouval O., Boyer O., Revy P., Jobst-Schwan T., Schmidt J.M.,
RA Lawson J.A., Schanze D., Ashraf S., Ullmann J.F.P., Hoogstraten C.A.,
RA Boddaert N., Collinet B., Martin G., Liger D., Lovric S., Furlano M.,
RA Guerrera I.C., Sanchez-Ferras O., Hu J.F., Boschat A.C., Sanquer S.,
RA Menten B., Vergult S., De Rocker N., Airik M., Hermle T., Shril S.,
RA Widmeier E., Gee H.Y., Choi W.I., Sadowski C.E., Pabst W.L., Warejko J.K.,
RA Daga A., Basta T., Matejas V., Scharmann K., Kienast S.D., Behnam B.,
RA Beeson B., Begtrup A., Bruce M., Ch'ng G.S., Lin S.P., Chang J.H.,
RA Chen C.H., Cho M.T., Gaffney P.M., Gipson P.E., Hsu C.H., Kari J.A.,
RA Ke Y.Y., Kiraly-Borri C., Lai W.M., Lemyre E., Littlejohn R.O., Masri A.,
RA Moghtaderi M., Nakamura K., Ozaltin F., Praet M., Prasad C., Prytula A.,
RA Roeder E.R., Rump P., Schnur R.E., Shiihara T., Sinha M.D., Soliman N.A.,
RA Soulami K., Sweetser D.A., Tsai W.H., Tsai J.D., Topaloglu R., Vester U.,
RA Viskochil D.H., Vatanavicharn N., Waxler J.L., Wierenga K.J., Wolf M.T.F.,
RA Wong S.N., Leidel S.A., Truglio G., Dedon P.C., Poduri A., Mane S.,
RA Lifton R.P., Bouchard M., Kannu P., Chitayat D., Magen D., Callewaert B.,
RA van Tilbeurgh H., Zenker M., Antignac C., Hildebrandt F.;
RT "Mutations in KEOPS-complex genes cause nephrotic syndrome with primary
RT microcephaly.";
RL Nat. Genet. 49:1529-1538(2017).
CC -!- FUNCTION: Component of the EKC/KEOPS complex that is required for the
CC formation of a threonylcarbamoyl group on adenosine at position 37
CC (t(6)A37) in tRNAs that read codons beginning with adenine
CC (PubMed:22912744, PubMed:27903914). The complex is probably involved in
CC the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP
CC (TC-AMP) to the N6 group of A37 (PubMed:22912744, PubMed:27903914).
CC LAGE3 functions as a dimerization module for the complex
CC (PubMed:22912744, PubMed:27903914). {ECO:0000305|PubMed:22912744,
CC ECO:0000305|PubMed:27903914}.
CC -!- SUBUNIT: Component of the EKC/KEOPS complex composed of at least GON7,
CC TP53RK, TPRKB, OSGEP and LAGE3; the whole complex dimerizes.
CC {ECO:0000269|PubMed:22912744, ECO:0000269|PubMed:27903914,
CC ECO:0000269|PubMed:28805828, ECO:0000269|PubMed:31481669}.
CC -!- INTERACTION:
CC Q14657; Q9ULX6: AKAP8L; NbExp=3; IntAct=EBI-1052105, EBI-357530;
CC Q14657; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-1052105, EBI-3867333;
CC Q14657; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-1052105, EBI-5916454;
CC Q14657; Q9BXV9: GON7; NbExp=15; IntAct=EBI-1052105, EBI-6256593;
CC Q14657; O75031: HSF2BP; NbExp=3; IntAct=EBI-1052105, EBI-7116203;
CC Q14657; A0A0C4DGM4: HYKK; NbExp=3; IntAct=EBI-1052105, EBI-10236738;
CC Q14657; Q6A162: KRT40; NbExp=6; IntAct=EBI-1052105, EBI-10171697;
CC Q14657; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-1052105, EBI-10171774;
CC Q14657; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-1052105, EBI-10172526;
CC Q14657; Q8TD10: MIPOL1; NbExp=3; IntAct=EBI-1052105, EBI-2548751;
CC Q14657; Q13064: MKRN3; NbExp=3; IntAct=EBI-1052105, EBI-2340269;
CC Q14657; Q9NPF4: OSGEP; NbExp=4; IntAct=EBI-1052105, EBI-1056510;
CC Q14657; O76083: PDE9A; NbExp=3; IntAct=EBI-1052105, EBI-742764;
CC Q14657; O76083-2: PDE9A; NbExp=3; IntAct=EBI-1052105, EBI-11524542;
CC Q14657; Q9NW61: PLEKHJ1; NbExp=3; IntAct=EBI-1052105, EBI-1057560;
CC Q14657; Q8ND90: PNMA1; NbExp=3; IntAct=EBI-1052105, EBI-302345;
CC Q14657; O75817: POP7; NbExp=3; IntAct=EBI-1052105, EBI-366574;
CC Q14657; P28065: PSMB9; NbExp=4; IntAct=EBI-1052105, EBI-603300;
CC Q14657; P36406: TRIM23; NbExp=3; IntAct=EBI-1052105, EBI-740098;
CC Q14657; P14373: TRIM27; NbExp=3; IntAct=EBI-1052105, EBI-719493;
CC Q14657; A5D8V6: VPS37C; NbExp=3; IntAct=EBI-1052105, EBI-2559305;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:28805828}. Nucleus
CC {ECO:0000269|PubMed:22912744, ECO:0000269|PubMed:27903914,
CC ECO:0000269|PubMed:28805828}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12384295,
CC ECO:0000269|PubMed:8786131}.
CC -!- DISEASE: Galloway-Mowat syndrome 2, X-linked (GAMOS2) [MIM:301006]: A
CC form of Galloway-Mowat syndrome, a severe renal-neurological disease
CC characterized by early-onset nephrotic syndrome associated with
CC microcephaly, central nervous system abnormalities, developmental
CC delays, and a propensity for seizures. Brain anomalies include gyration
CC defects ranging from lissencephaly to pachygyria and polymicrogyria,
CC and cerebellar hypoplasia. Most patients show facial dysmorphism
CC characterized by a small, narrow forehead, large/floppy ears, deep-set
CC eyes, hypertelorism and micrognathia. Additional variable features are
CC visual impairment and arachnodactyly. Most patients die in early
CC childhood. {ECO:0000269|PubMed:28805828}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the CTAG/PCC1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA63489.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; BX936365; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC015744; AAH15744.2; -; mRNA.
DR EMBL; BC062330; AAH62330.1; -; mRNA.
DR EMBL; X92896; CAA63489.1; ALT_FRAME; mRNA.
DR CCDS; CCDS14753.1; -.
DR RefSeq; NP_006005.2; NM_006014.4.
DR PDB; 6GWJ; X-ray; 1.95 A; B=1-143.
DR PDBsum; 6GWJ; -.
DR AlphaFoldDB; Q14657; -.
DR SASBDB; Q14657; -.
DR SMR; Q14657; -.
DR BioGRID; 113888; 107.
DR CORUM; Q14657; -.
DR IntAct; Q14657; 32.
DR MINT; Q14657; -.
DR STRING; 9606.ENSP00000349923; -.
DR GlyGen; Q14657; 1 site, 2 O-linked glycans (1 site).
DR iPTMnet; Q14657; -.
DR PhosphoSitePlus; Q14657; -.
DR BioMuta; LAGE3; -.
DR DMDM; 54041570; -.
DR EPD; Q14657; -.
DR jPOST; Q14657; -.
DR MassIVE; Q14657; -.
DR MaxQB; Q14657; -.
DR PaxDb; Q14657; -.
DR PeptideAtlas; Q14657; -.
DR PRIDE; Q14657; -.
DR ProteomicsDB; 60095; -.
DR Antibodypedia; 31283; 30 antibodies from 16 providers.
DR DNASU; 8270; -.
DR Ensembl; ENST00000357360.5; ENSP00000349923.4; ENSG00000196976.8.
DR GeneID; 8270; -.
DR KEGG; hsa:8270; -.
DR MANE-Select; ENST00000357360.5; ENSP00000349923.4; NM_006014.5; NP_006005.2.
DR UCSC; uc033fbs.1; human.
DR CTD; 8270; -.
DR DisGeNET; 8270; -.
DR GeneCards; LAGE3; -.
DR HGNC; HGNC:26058; LAGE3.
DR HPA; ENSG00000196976; Low tissue specificity.
DR MalaCards; LAGE3; -.
DR MIM; 300060; gene.
DR MIM; 301006; phenotype.
DR neXtProt; NX_Q14657; -.
DR OpenTargets; ENSG00000196976; -.
DR Orphanet; 2065; Galloway-Mowat syndrome.
DR PharmGKB; PA128394540; -.
DR VEuPathDB; HostDB:ENSG00000196976; -.
DR eggNOG; ENOG502SBSA; Eukaryota.
DR GeneTree; ENSGT00410000025802; -.
DR HOGENOM; CLU_113770_2_2_1; -.
DR InParanoid; Q14657; -.
DR OMA; HQRVIGK; -.
DR OrthoDB; 1540775at2759; -.
DR PhylomeDB; Q14657; -.
DR TreeFam; TF337064; -.
DR PathwayCommons; Q14657; -.
DR Reactome; R-HSA-6782315; tRNA modification in the nucleus and cytosol.
DR SignaLink; Q14657; -.
DR BioGRID-ORCS; 8270; 191 hits in 696 CRISPR screens.
DR ChiTaRS; LAGE3; human.
DR GenomeRNAi; 8270; -.
DR Pharos; Q14657; Tdark.
DR PRO; PR:Q14657; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q14657; protein.
DR Bgee; ENSG00000196976; Expressed in oocyte and 184 other tissues.
DR Genevisible; Q14657; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0000408; C:EKC/KEOPS complex; IDA:UniProtKB.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0070525; P:tRNA threonylcarbamoyladenosine metabolic process; IBA:GO_Central.
DR InterPro; IPR015419; CTAG/Pcc1.
DR PANTHER; PTHR31283; PTHR31283; 1.
DR Pfam; PF09341; Pcc1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Disease variant; Epilepsy;
KW Intellectual disability; Nucleus; Reference proteome; tRNA processing.
FT CHAIN 1..143
FT /note="EKC/KEOPS complex subunit LAGE3"
FT /id="PRO_0000218924"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 106
FT /note="V -> F (in GAMOS2; dbSNP:rs1557211306)"
FT /evidence="ECO:0000269|PubMed:28805828"
FT /id="VAR_080374"
FT VARIANT 137
FT /note="F -> S (in GAMOS2; dbSNP:rs1557211209)"
FT /evidence="ECO:0000269|PubMed:28805828"
FT /id="VAR_080375"
FT STRAND 61..68
FT /evidence="ECO:0007829|PDB:6GWJ"
FT HELIX 72..82
FT /evidence="ECO:0007829|PDB:6GWJ"
FT TURN 88..92
FT /evidence="ECO:0007829|PDB:6GWJ"
FT STRAND 93..100
FT /evidence="ECO:0007829|PDB:6GWJ"
FT STRAND 103..111
FT /evidence="ECO:0007829|PDB:6GWJ"
FT HELIX 113..137
FT /evidence="ECO:0007829|PDB:6GWJ"
SQ SEQUENCE 143 AA; 14804 MW; AD164559371449F8 CRC64;
MRDADADAGG GADGGDGRGG HSCRGGVDTA AAPAGGAPPA HAPGPGRDAA SAARGSRMRP
HIFTLSVPFP TPLEAEIAHG SLAPDAEPHQ RVVGKDLTVS GRILVVRWKA EDCRLLRISV
INFLDQLSLV VRTMQRFGPP VSR
