ID LARP6_HUMAN Reviewed; 491 AA.
AC Q9BRS8; Q5XKE4; Q8N3N2; Q9NUR0;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 27-MAR-2024, entry version 175.
DE RecName: Full=La-related protein 6;
DE AltName: Full=Acheron;
DE Short=Achn;
DE AltName: Full=La ribonucleoprotein domain family member 6;
GN Name=LARP6;
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=Hippocampus, and Rhabdomyosarcoma;
RX PubMed=17383118; DOI=10.1016/j.gene.2007.01.033;
RA Valavanis C., Wang Z., Sun D., Vaine M., Schwartz L.M.;
RT "Acheron, a novel member of the Lupus antigen family, is induced during the
RT programmed cell death of skeletal muscles in the moth Manduca sexta.";
RL Gene 393:101-109(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 1).
RC TISSUE=Melanoma;
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=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Adrenal cortex, Brain, and Muscle;
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 [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [7]
RP FUNCTION, AND INTERACTION WITH MYH10.
RX PubMed=20603131; DOI=10.1016/j.jmb.2010.06.057;
RA Cai L., Fritz D., Stefanovic L., Stefanovic B.;
RT "Nonmuscle myosin-dependent synthesis of type I collagen.";
RL J. Mol. Biol. 401:564-578(2010).
RN [8]
RP FUNCTION, AND INTERACTION WITH VIM.
RX PubMed=21746880; DOI=10.1128/mcb.05263-11;
RA Challa A.A., Stefanovic B.;
RT "A novel role of vimentin filaments: binding and stabilization of collagen
RT mRNAs.";
RL Mol. Cell. Biol. 31:3773-3789(2011).
RN [9]
RP FUNCTION, AND INTERACTION WITH DHX9.
RX PubMed=22190748; DOI=10.1261/rna.030288.111;
RA Manojlovic Z., Stefanovic B.;
RT "A novel role of RNA helicase A in regulation of translation of type I
RT collagen mRNAs.";
RL RNA 18:321-334(2012).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: Regulates the coordinated translation of type I collagen
CC alpha-1 and alpha-2 mRNAs, CO1A1 and CO1A2. Stabilizes mRNAs through
CC high-affinity binding of a stem-loop structure in their 5' UTR. This
CC regulation requires VIM and MYH10 filaments, and the helicase DHX9.
CC {ECO:0000269|PubMed:20603131, ECO:0000269|PubMed:21746880,
CC ECO:0000269|PubMed:22190748}.
CC -!- SUBUNIT: Interacts (via the HTH domain) with VIM/vimentin. Interacts
CC (via C-terminus) with non-muscle myosin MYH10. Interacts (via C-
CC terminus) with DHX9. {ECO:0000269|PubMed:20603131,
CC ECO:0000269|PubMed:21746880, ECO:0000269|PubMed:22190748}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17383118}. Nucleus
CC {ECO:0000269|PubMed:17383118}. Note=Shuttles between the nucleus and
CC the cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9BRS8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BRS8-2; Sequence=VSP_042565;
CC -!- TISSUE SPECIFICITY: Expressed in numerous tissues.
CC {ECO:0000269|PubMed:17383118}.
CC -!- DOMAIN: The RRM domain mediates the association with collagen mRNAs
CC stem-loops.
CC ---------------------------------------------------------------------------
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DR EMBL; AF443828; AAN76710.1; -; mRNA.
DR EMBL; AF443829; AAN76711.1; -; mRNA.
DR EMBL; AK002058; BAA92061.1; -; mRNA.
DR EMBL; AL833876; CAD38733.2; -; mRNA.
DR EMBL; AC009269; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC090868; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC006082; AAH06082.1; -; mRNA.
DR EMBL; BC009446; AAH09446.1; -; mRNA.
DR EMBL; BC014018; AAH14018.1; -; mRNA.
DR EMBL; BC039153; AAH39153.1; -; mRNA.
DR CCDS; CCDS10236.1; -. [Q9BRS8-2]
DR CCDS; CCDS32281.1; -. [Q9BRS8-1]
DR RefSeq; NP_001273608.1; NM_001286679.1.
DR RefSeq; NP_060827.2; NM_018357.3. [Q9BRS8-1]
DR RefSeq; NP_932062.1; NM_197958.2. [Q9BRS8-2]
DR PDB; 2MTF; NMR; -; A=70-183.
DR PDB; 2MTG; NMR; -; A=178-295.
DR PDBsum; 2MTF; -.
DR PDBsum; 2MTG; -.
DR AlphaFoldDB; Q9BRS8; -.
DR BMRB; Q9BRS8; -.
DR SMR; Q9BRS8; -.
DR BioGRID; 120604; 6.
DR IntAct; Q9BRS8; 2.
DR STRING; 9606.ENSP00000299213; -.
DR ChEMBL; CHEMBL4739702; -.
DR GlyConnect; 1953; 5 N-Linked glycans (1 site).
DR GlyCosmos; Q9BRS8; 1 site, 5 glycans.
DR GlyGen; Q9BRS8; 1 site, 5 N-linked glycans (1 site).
DR iPTMnet; Q9BRS8; -.
DR PhosphoSitePlus; Q9BRS8; -.
DR BioMuta; LARP6; -.
DR DMDM; 74752287; -.
DR EPD; Q9BRS8; -.
DR jPOST; Q9BRS8; -.
DR MassIVE; Q9BRS8; -.
DR MaxQB; Q9BRS8; -.
DR PaxDb; 9606-ENSP00000299213; -.
DR PeptideAtlas; Q9BRS8; -.
DR ProteomicsDB; 78825; -. [Q9BRS8-1]
DR ProteomicsDB; 78826; -. [Q9BRS8-2]
DR Pumba; Q9BRS8; -.
DR Antibodypedia; 14073; 148 antibodies from 19 providers.
DR CPTC; Q9BRS8; Previous GeneCards.
DR DNASU; 55323; -.
DR Ensembl; ENST00000299213.10; ENSP00000299213.7; ENSG00000166173.11. [Q9BRS8-1]
DR Ensembl; ENST00000344870.4; ENSP00000343869.3; ENSG00000166173.11. [Q9BRS8-2]
DR GeneID; 55323; -.
DR KEGG; hsa:55323; -.
DR MANE-Select; ENST00000299213.10; ENSP00000299213.7; NM_018357.4; NP_060827.2.
DR UCSC; uc002ass.5; human. [Q9BRS8-1]
DR AGR; HGNC:24012; -.
DR CTD; 55323; -.
DR DisGeNET; 55323; -.
DR GeneCards; LARP6; -.
DR HGNC; HGNC:24012; LARP6.
DR HPA; ENSG00000166173; Tissue enhanced (brain).
DR MIM; 611300; gene.
DR neXtProt; NX_Q9BRS8; -.
DR OpenTargets; ENSG00000166173; -.
DR PharmGKB; PA142671568; -.
DR VEuPathDB; HostDB:ENSG00000166173; -.
DR eggNOG; KOG1855; Eukaryota.
DR GeneTree; ENSGT00940000159103; -.
DR HOGENOM; CLU_015330_1_0_1; -.
DR InParanoid; Q9BRS8; -.
DR OMA; WIGGLWR; -.
DR OrthoDB; 2913004at2759; -.
DR PhylomeDB; Q9BRS8; -.
DR TreeFam; TF326594; -.
DR PathwayCommons; Q9BRS8; -.
DR SignaLink; Q9BRS8; -.
DR SIGNOR; Q9BRS8; -.
DR BioGRID-ORCS; 55323; 13 hits in 1143 CRISPR screens.
DR ChiTaRS; LARP6; human.
DR GeneWiki; LARP6; -.
DR GenomeRNAi; 55323; -.
DR Pharos; Q9BRS8; Tbio.
DR PRO; PR:Q9BRS8; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q9BRS8; Protein.
DR Bgee; ENSG00000166173; Expressed in lateral globus pallidus and 188 other cell types or tissues.
DR ExpressionAtlas; Q9BRS8; baseline and differential.
DR Genevisible; Q9BRS8; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005844; C:polysome; IBA:GO_Central.
DR GO; GO:0048027; F:mRNA 5'-UTR binding; IDA:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0017022; F:myosin binding; IPI:UniProtKB.
DR GO; GO:0035613; F:RNA stem-loop binding; IDA:UniProtKB.
DR GO; GO:1990825; F:sequence-specific mRNA binding; IDA:UniProtKB.
DR GO; GO:0032967; P:positive regulation of collagen biosynthetic process; IMP:UniProtKB.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR CDD; cd08033; LARP_6; 1.
DR CDD; cd12289; RRM_LARP6; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR045180; La_dom_prot.
DR InterPro; IPR006630; La_HTH.
DR InterPro; IPR034880; LARP6_RRM.
DR InterPro; IPR002344; Lupus_La.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR024642; SUZ-C.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR22792:SF71; LA-RELATED PROTEIN 6; 1.
DR PANTHER; PTHR22792; LUPUS LA PROTEIN-RELATED; 1.
DR Pfam; PF05383; La; 1.
DR Pfam; PF12901; SUZ-C; 1.
DR PRINTS; PR00302; LUPUSLA.
DR SMART; SM00715; LA; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS50961; HTH_LA; 1.
DR PROSITE; PS51938; SUZ_C; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm; Nucleus;
KW Phosphoprotein; Reference proteome; RNA-binding; Translation regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..491
FT /note="La-related protein 6"
FT /id="PRO_0000281141"
FT DOMAIN 86..177
FT /note="HTH La-type RNA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00332"
FT DOMAIN 184..296
FT /note="RRM"
FT DOMAIN 427..485
FT /note="SUZ-C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01287"
FT REGION 1..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 293..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 423..491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 186..193
FT /note="Nuclear export signal"
FT MOTIF 296..302
FT /note="Nuclear localization signal"
FT COMPBIAS 73..87
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..329
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..347
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..390
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 443..457
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..491
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BN59"
FT VAR_SEQ 67..491
FT /note="SGTTASGGENEREDLEQEWKPPDEELIKKLVDQIEFYFSDENLEKDAFLLKH
FT VRRNKLGYVSVKLLTSFKKVKHLTRDWRTTAHALKYSVVLELNEDHRKVRRTTPVPLFP
FT NENLPSKMLLVYDLYLSPKLWALATPQKNGRVQEKVMEHLLKLFGTFGVISSVRILKPG
FT RELPPDIRRISSRYSQVGTQECAIVEFEEVEAAIKAHEFMITESQGKENMKAVLIGMKP
FT PKKKPAKDKNHDEEPTASIHLNKSLNKRVEELQYMGDESSANSSSDPESNPTSPMAGRR
FT HAATNKLSPSGHQNLFLSPNASPCTSPWSSPLAQRKGVSRKSPLAEEGRLNCSTSPEIF
FT RKCMDYSSDSSVTPSGSPWVRRRRQAEMGTQEKSPGTSPLLSRKMQTADGLPVGVLRLP
FT RGPDNTRGFHGHERSRACV -> RNRSSVNSRTMLASFIVSSAPSTAPST (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_042565"
FT CONFLICT 103
FT /note="Y -> C (in Ref. 2; BAA92061)"
FT /evidence="ECO:0000305"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:2MTF"
FT HELIX 90..103
FT /evidence="ECO:0007829|PDB:2MTF"
FT HELIX 106..109
FT /evidence="ECO:0007829|PDB:2MTF"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:2MTF"
FT HELIX 116..119
FT /evidence="ECO:0007829|PDB:2MTF"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:2MTF"
FT HELIX 129..133
FT /evidence="ECO:0007829|PDB:2MTF"
FT TURN 136..140
FT /evidence="ECO:0007829|PDB:2MTF"
FT HELIX 145..153
FT /evidence="ECO:0007829|PDB:2MTF"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:2MTF"
FT TURN 162..165
FT /evidence="ECO:0007829|PDB:2MTF"
FT TURN 177..179
FT /evidence="ECO:0007829|PDB:2MTF"
FT STRAND 185..189
FT /evidence="ECO:0007829|PDB:2MTG"
FT TURN 195..199
FT /evidence="ECO:0007829|PDB:2MTG"
FT HELIX 209..224
FT /evidence="ECO:0007829|PDB:2MTG"
FT STRAND 227..233
FT /evidence="ECO:0007829|PDB:2MTG"
FT TURN 235..237
FT /evidence="ECO:0007829|PDB:2MTG"
FT HELIX 241..246
FT /evidence="ECO:0007829|PDB:2MTG"
FT TURN 247..249
FT /evidence="ECO:0007829|PDB:2MTG"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:2MTG"
FT STRAND 258..264
FT /evidence="ECO:0007829|PDB:2MTG"
FT HELIX 266..279
FT /evidence="ECO:0007829|PDB:2MTG"
FT TURN 280..284
FT /evidence="ECO:0007829|PDB:2MTG"
FT STRAND 287..291
FT /evidence="ECO:0007829|PDB:2MTG"
SQ SEQUENCE 491 AA; 54737 MW; 2CF3AFFFD69BDD07 CRC64;
MAQSGGEARP GPKTAVQIRV AIQEAEDVDE LEDEEEGAET RGAGDPARYL SPGWGSASEE
EPSRGHSGTT ASGGENERED LEQEWKPPDE ELIKKLVDQI EFYFSDENLE KDAFLLKHVR
RNKLGYVSVK LLTSFKKVKH LTRDWRTTAH ALKYSVVLEL NEDHRKVRRT TPVPLFPNEN
LPSKMLLVYD LYLSPKLWAL ATPQKNGRVQ EKVMEHLLKL FGTFGVISSV RILKPGRELP
PDIRRISSRY SQVGTQECAI VEFEEVEAAI KAHEFMITES QGKENMKAVL IGMKPPKKKP
AKDKNHDEEP TASIHLNKSL NKRVEELQYM GDESSANSSS DPESNPTSPM AGRRHAATNK
LSPSGHQNLF LSPNASPCTS PWSSPLAQRK GVSRKSPLAE EGRLNCSTSP EIFRKCMDYS
SDSSVTPSGS PWVRRRRQAE MGTQEKSPGT SPLLSRKMQT ADGLPVGVLR LPRGPDNTRG
FHGHERSRAC V
//
