MBNL3_HUMAN
ID MBNL3_HUMAN Reviewed; 354 AA.
AC Q9NUK0; Q5JXN8; Q5JXN9; Q5JXP4; Q6UDQ1; Q8IUR4; Q8TAD9; Q8TAF4; Q9H0Z7;
AC Q9UF37;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2002, sequence version 2.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Muscleblind-like protein 3;
DE AltName: Full=Cys3His CCG1-required protein;
DE AltName: Full=Muscleblind-like X-linked protein;
DE AltName: Full=Protein HCHCR;
GN Name=MBNL3; Synonyms=CHCR, MBLX39, MBXL;
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] (ISOFORMS 1 AND 2), AND FUNCTION.
RC TISSUE=Embryonic kidney;
RX PubMed=12297108; DOI=10.1006/dbio.2002.0798;
RA Squillace R.M., Chenault D.M., Wang E.H.;
RT "Inhibition of muscle differentiation by the novel muscleblind-related
RT protein CHCR.";
RL Dev. Biol. 250:218-230(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Urbinati C.R., Swanson M.S.;
RT "MBLX39 sequence.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RA Li H., Yu R., Zheng G., Ke R., Zhou G., Shen C., Li M., Xiao W., Lin L.,
RA Yang S.;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 5).
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5).
RC TISSUE=Lung;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 60-354.
RC TISSUE=Testis;
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 [8]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND ALTERNATIVE SPLICING.
RX PubMed=11929853; DOI=10.1093/hmg/11.7.805;
RA Fardaei M., Rogers M.T., Thorpe H.M., Larkin K., Hamshere M.G.,
RA Harper P.S., Brook J.D.;
RT "Three proteins, MBNL, MBLL and MBXL, co-localize in vivo with nuclear foci
RT of expanded-repeat transcripts in DM1 and DM2 cells.";
RL Hum. Mol. Genet. 11:805-814(2002).
RN [9]
RP FUNCTION.
RX PubMed=15257297; DOI=10.1038/sj.emboj.7600300;
RA Ho T.H., Charlet-B N., Poulos M.G., Singh G., Swanson M.S., Cooper T.A.;
RT "Muscleblind proteins regulate alternative splicing.";
RL EMBO J. 23:3103-3112(2004).
CC -!- FUNCTION: Mediates pre-mRNA alternative splicing regulation. Acts
CC either as activator or repressor of splicing on specific pre-mRNA
CC targets. Inhibits cardiac troponin-T (TNNT2) pre-mRNA exon inclusion
CC but induces insulin receptor (IR) pre-mRNA exon inclusion in muscle.
CC Antagonizes the alternative splicing activity pattern of CELF proteins.
CC May play a role in myotonic dystrophy pathophysiology (DM). Could
CC inhibit terminal muscle differentiation, acting at approximately the
CC time of myogenin induction. {ECO:0000269|PubMed:12297108,
CC ECO:0000269|PubMed:15257297}.
CC -!- INTERACTION:
CC Q9NUK0; O75553: DAB1; NbExp=3; IntAct=EBI-6661142, EBI-7875264;
CC Q9NUK0-3; P86480: PRR20D; NbExp=3; IntAct=EBI-12049233, EBI-12754095;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11929853}. Cytoplasm
CC {ECO:0000269|PubMed:11929853}. Note=Greater concentration in the
CC nucleus. In both DM1 and DM2 patients, colocalizes with nuclear foci of
CC retained expanded-repeat transcripts.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=HCHCR-G, G;
CC IsoId=Q9NUK0-1; Sequence=Displayed;
CC Name=2; Synonyms=HCHCR-R, R;
CC IsoId=Q9NUK0-2; Sequence=VSP_006433, VSP_006434;
CC Name=3;
CC IsoId=Q9NUK0-3; Sequence=VSP_006431, VSP_006432;
CC Name=4;
CC IsoId=Q9NUK0-4; Sequence=VSP_006431, VSP_006432, VSP_015935;
CC Name=5;
CC IsoId=Q9NUK0-5; Sequence=VSP_044309;
CC -!- TISSUE SPECIFICITY: Highly expressed in the placenta.
CC {ECO:0000269|PubMed:11929853}.
CC -!- SIMILARITY: Belongs to the muscleblind family. {ECO:0000305}.
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DR EMBL; AY072692; AAL65661.1; -; mRNA.
DR EMBL; AF467070; AAL87670.1; -; mRNA.
DR EMBL; AB077698; BAB85648.1; -; mRNA.
DR EMBL; AB077699; BAB85649.1; -; mRNA.
DR EMBL; AJ427918; CAD20869.1; -; mRNA.
DR EMBL; AJ427919; CAD20870.1; -; mRNA.
DR EMBL; AF491305; AAM09533.1; -; mRNA.
DR EMBL; AY372211; AAQ75759.1; -; mRNA.
DR EMBL; AK002178; BAA92124.1; -; mRNA.
DR EMBL; AK300248; BAG62014.1; -; mRNA.
DR EMBL; AL161442; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL050310; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC042090; AAH42090.1; -; mRNA.
DR EMBL; BC074775; AAH74775.1; -; mRNA.
DR EMBL; BC074776; AAH74776.1; -; mRNA.
DR EMBL; AL133625; CAB63751.1; -; mRNA.
DR CCDS; CCDS14633.1; -. [Q9NUK0-1]
DR CCDS; CCDS14634.1; -. [Q9NUK0-2]
DR CCDS; CCDS55492.1; -. [Q9NUK0-5]
DR CCDS; CCDS55494.1; -. [Q9NUK0-5]
DR PIR; T43463; T43463.
DR RefSeq; NP_001164172.1; NM_001170701.1. [Q9NUK0-3]
DR RefSeq; NP_001164173.1; NM_001170702.1. [Q9NUK0-4]
DR RefSeq; NP_001164174.1; NM_001170703.1. [Q9NUK0-5]
DR RefSeq; NP_001164175.1; NM_001170704.1. [Q9NUK0-5]
DR RefSeq; NP_060858.2; NM_018388.3. [Q9NUK0-1]
DR RefSeq; NP_597846.1; NM_133486.2. [Q9NUK0-2]
DR RefSeq; XP_005262491.1; XM_005262434.3. [Q9NUK0-1]
DR RefSeq; XP_016885124.1; XM_017029635.1.
DR RefSeq; XP_016885125.1; XM_017029636.1. [Q9NUK0-1]
DR RefSeq; XP_016885128.1; XM_017029639.1. [Q9NUK0-5]
DR AlphaFoldDB; Q9NUK0; -.
DR SMR; Q9NUK0; -.
DR BioGRID; 120909; 13.
DR IntAct; Q9NUK0; 6.
DR STRING; 9606.ENSP00000359890; -.
DR GlyGen; Q9NUK0; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NUK0; -.
DR PhosphoSitePlus; Q9NUK0; -.
DR BioMuta; MBNL3; -.
DR DMDM; 26396510; -.
DR EPD; Q9NUK0; -.
DR jPOST; Q9NUK0; -.
DR MassIVE; Q9NUK0; -.
DR MaxQB; Q9NUK0; -.
DR PaxDb; Q9NUK0; -.
DR PeptideAtlas; Q9NUK0; -.
DR PRIDE; Q9NUK0; -.
DR ProteomicsDB; 70598; -.
DR ProteomicsDB; 82679; -. [Q9NUK0-1]
DR ProteomicsDB; 82680; -. [Q9NUK0-2]
DR ProteomicsDB; 82681; -. [Q9NUK0-3]
DR ProteomicsDB; 82682; -. [Q9NUK0-4]
DR Antibodypedia; 446; 157 antibodies from 25 providers.
DR DNASU; 55796; -.
DR Ensembl; ENST00000370839.7; ENSP00000359876.3; ENSG00000076770.15. [Q9NUK0-2]
DR Ensembl; ENST00000370844.5; ENSP00000359881.1; ENSG00000076770.15. [Q9NUK0-5]
DR Ensembl; ENST00000370849.7; ENSP00000359886.3; ENSG00000076770.15. [Q9NUK0-3]
DR Ensembl; ENST00000370853.8; ENSP00000359890.3; ENSG00000076770.15. [Q9NUK0-1]
DR Ensembl; ENST00000394311.6; ENSP00000377848.2; ENSG00000076770.15. [Q9NUK0-5]
DR Ensembl; ENST00000538204.5; ENSP00000439618.1; ENSG00000076770.15. [Q9NUK0-4]
DR GeneID; 55796; -.
DR KEGG; hsa:55796; -.
DR MANE-Select; ENST00000370853.8; ENSP00000359890.3; NM_001386889.1; NP_001373818.1.
DR UCSC; uc004ewt.4; human. [Q9NUK0-1]
DR CTD; 55796; -.
DR DisGeNET; 55796; -.
DR GeneCards; MBNL3; -.
DR HGNC; HGNC:20564; MBNL3.
DR HPA; ENSG00000076770; Tissue enhanced (liver, placenta).
DR MIM; 300413; gene.
DR neXtProt; NX_Q9NUK0; -.
DR OpenTargets; ENSG00000076770; -.
DR PharmGKB; PA134992936; -.
DR VEuPathDB; HostDB:ENSG00000076770; -.
DR eggNOG; KOG2494; Eukaryota.
DR GeneTree; ENSGT00950000182897; -.
DR HOGENOM; CLU_053536_0_0_1; -.
DR InParanoid; Q9NUK0; -.
DR OMA; IECKYAH; -.
DR OrthoDB; 1543798at2759; -.
DR PhylomeDB; Q9NUK0; -.
DR TreeFam; TF321931; -.
DR PathwayCommons; Q9NUK0; -.
DR SignaLink; Q9NUK0; -.
DR BioGRID-ORCS; 55796; 8 hits in 697 CRISPR screens.
DR ChiTaRS; MBNL3; human.
DR GeneWiki; MBNL3; -.
DR GenomeRNAi; 55796; -.
DR Pharos; Q9NUK0; Tbio.
DR PRO; PR:Q9NUK0; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q9NUK0; protein.
DR Bgee; ENSG00000076770; Expressed in cauda epididymis and 171 other tissues.
DR ExpressionAtlas; Q9NUK0; baseline and differential.
DR Genevisible; Q9NUK0; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0045662; P:negative regulation of myoblast differentiation; IEA:Ensembl.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0043484; P:regulation of RNA splicing; IDA:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR InterPro; IPR000571; Znf_CCCH.
DR Pfam; PF00642; zf-CCCH; 1.
DR SMART; SM00356; ZnF_C3H1; 4.
DR PROSITE; PS50103; ZF_C3H1; 4.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Developmental protein; Metal-binding;
KW mRNA processing; mRNA splicing; Nucleus; Reference proteome; Repeat; Zinc;
KW Zinc-finger.
FT CHAIN 1..354
FT /note="Muscleblind-like protein 3"
FT /id="PRO_0000089180"
FT ZN_FING 14..42
FT /note="C3H1-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 48..74
FT /note="C3H1-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 174..202
FT /note="C3H1-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 210..236
FT /note="C3H1-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT VAR_SEQ 1..96
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_044309"
FT VAR_SEQ 1..50
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.3"
FT /id="VSP_006431"
FT VAR_SEQ 51..57
FT /note="VVACFDS -> MERASKN (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.3"
FT /id="VSP_006432"
FT VAR_SEQ 258..292
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12297108"
FT /id="VSP_006433"
FT VAR_SEQ 308..319
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_015935"
FT VAR_SEQ 352..354
FT /note="LKF -> IPQLSIDELNSSMFVSQM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12297108"
FT /id="VSP_006434"
FT CONFLICT 113
FT /note="S -> P (in Ref. 3; AAQ75759)"
FT /evidence="ECO:0000305"
FT CONFLICT 187
FT /note="N -> I (in Ref. 3; AAQ75759)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 354 AA; 38532 MW; 145E1AF8CB3BEE27 CRC64;
MTAVNVALIR DTKWLTLEVC REFQRGTCSR ADADCKFAHP PRVCHVENGR VVACFDSLKG
RCTRENCKYL HPPPHLKTQL EINGRNNLIQ QKTAAAMFAQ QMQLMLQNAQ MSSLGSFPMT
PSIPANPPMA FNPYIPHPGM GLVPAELVPN TPVLIPGNPP LAMPGAVGPK LMRSDKLEVC
REFQRGNCTR GENDCRYAHP TDASMIEASD NTVTICMDYI KGRCSREKCK YFHPPAHLQA
RLKAAHHQMN HSAASAMALQ PGTLQLIPKR SALEKPNGAT PVFNPTVFHC QQALTNLQLP
QPAFIPAGPI LCMAPASNIV PMMHGATPTT VSAATTPATS VPFAAPTTGN QLKF
