LIN41_HUMAN
ID LIN41_HUMAN Reviewed; 868 AA.
AC Q2Q1W2;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=E3 ubiquitin-protein ligase TRIM71 {ECO:0000305};
DE EC=2.3.2.27;
DE AltName: Full=Protein lin-41 homolog;
DE AltName: Full=RING-type E3 ubiquitin transferase TRIM71 {ECO:0000305};
DE AltName: Full=Tripartite motif-containing protein 71;
GN Name=TRIM71 {ECO:0000312|HGNC:HGNC:32669}; Synonyms=LIN41;
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].
RA Lerner M., Corcoran M., Nielsen M., Zubarev R., Uhlen M., Hober S.,
RA Grander D., Sangfelt O.;
RT "The RBCC gene RFP2 (LEU5/TRIM13), frequently deleted in various
RT malignancies, encodes a ring E3 ubiquitin ligase.";
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP IDENTIFICATION.
RX PubMed=16245339; DOI=10.1002/dvdy.20591;
RA Lancman J.J., Caruccio N.C., Harfe B.D., Pasquinelli A.E., Schageman J.J.,
RA Pertsemlidis A., Fallon J.F.;
RT "Analysis of the regulation of lin-41 during chick and mouse limb
RT development.";
RL Dev. Dyn. 234:948-960(2005).
RN [3]
RP IDENTIFICATION.
RX PubMed=16247770; DOI=10.1002/dvdy.20599;
RA Maller Schulman B.R., Esquela-Kerscher A., Slack F.J.;
RT "Reciprocal expression of lin-41 and the microRNAs let-7 and mir-125 during
RT mouse embryogenesis.";
RL Dev. Dyn. 234:1046-1054(2005).
RN [4]
RP TISSUE SPECIFICITY, AND DOWN-REGULATION BY RETINOIC ACID.
RX PubMed=15722555; DOI=10.1074/jbc.m412247200;
RA Lee Y.S., Kim H.K., Chung S., Kim K.-S., Dutta A.;
RT "Depletion of human micro-RNA miR-125b reveals that it is critical for the
RT proliferation of differentiated cells but not for the down-regulation of
RT putative targets during differentiation.";
RL J. Biol. Chem. 280:16635-16641(2005).
RN [5]
RP INDUCTION.
RX PubMed=17890240; DOI=10.1093/molbev/msm195;
RA Lin Y.C., Hsieh L.C., Kuo M.W., Yu J., Kuo H.H., Lo W.L., Lin R.J.,
RA Yu A.L., Li W.H.;
RT "Human TRIM71 and its nematode homologue are targets of let-7 microRNA and
RT its zebrafish orthologue is essential for development.";
RL Mol. Biol. Evol. 24:2525-2534(2007).
RN [6]
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 [7]
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=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH AGO2; HSP90AA1; MOV10;
RP PABPC1; PUM1; PUM2; STAU2; XRN1 AND XRN2, RNA-BINDING, DOMAIN, AND
RP MUTAGENESIS OF GLY-647; HIS-675; TYR-702 AND ARG-751.
RX PubMed=23125361; DOI=10.1093/nar/gks1032;
RA Loedige I., Gaidatzis D., Sack R., Meister G., Filipowicz W.;
RT "The mammalian TRIM-NHL protein TRIM71/LIN-41 is a repressor of mRNA
RT function.";
RL Nucleic Acids Res. 41:518-532(2013).
RN [9]
RP FUNCTION, BIOTECHNOLOGY, SUBCELLULAR LOCATION, AND INDUCTION BY LET-7.
RX PubMed=24239284; DOI=10.1016/j.stem.2013.11.001;
RA Worringer K.A., Rand T.A., Hayashi Y., Sami S., Takahashi K., Tanabe K.,
RA Narita M., Srivastava D., Yamanaka S.;
RT "The let-7/LIN-41 pathway regulates reprogramming to human induced
RT pluripotent stem cells by controlling expression of prodifferentiation
RT genes.";
RL Cell Stem Cell 14:40-52(2014).
RN [10]
RP FUNCTION, AND MIRNA-BINDING.
RX PubMed=28431233; DOI=10.1016/j.molcel.2017.03.014;
RA Treiber T., Treiber N., Plessmann U., Harlander S., Daiss J.L., Eichner N.,
RA Lehmann G., Schall K., Urlaub H., Meister G.;
RT "A Compendium of RNA-Binding Proteins that Regulate MicroRNA Biogenesis.";
RL Mol. Cell 66:270-284(2017).
RN [11]
RP VARIANTS HYDCC1 HIS-608 AND HIS-796.
RX PubMed=29983323; DOI=10.1016/j.neuron.2018.06.019;
RA Furey C.G., Choi J., Jin S.C., Zeng X., Timberlake A.T.,
RA Nelson-Williams C., Mansuri M.S., Lu Q., Duran D., Panchagnula S.,
RA Allocco A., Karimy J.K., Khanna A., Gaillard J.R., DeSpenza T., Antwi P.,
RA Loring E., Butler W.E., Smith E.R., Warf B.C., Strahle J.M., Limbrick D.D.,
RA Storm P.B., Heuer G., Jackson E.M., Iskandar B.J., Johnston J.M.,
RA Tikhonova I., Castaldi C., Lopez-Giraldez F., Bjornson R.D., Knight J.R.,
RA Bilguvar K., Mane S., Alper S.L., Haider S., Guclu B., Bayri Y., Sahin Y.,
RA Apuzzo M.L.J., Duncan C.C., DiLuna M.L., Guenel M., Lifton R.P.,
RA Kahle K.T.;
RT "De Novo Mutation in Genes Regulating Neural Stem Cell Fate in Human
RT Congenital Hydrocephalus.";
RL Neuron 99:302-314.e4(2018).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that cooperates with the
CC microRNAs (miRNAs) machinery and promotes embryonic stem cells
CC proliferation and maintenance (Probable). Binds to miRNAs and
CC associates with AGO2, participating in post-transcriptional repression
CC of transcripts such as CDKN1A (By similarity). In addition,
CC participates in post-transcriptional mRNA repression in a miRNA
CC independent mechanism (PubMed:23125361). Facilitates the G1-S
CC transition to promote rapid embryonic stem cell self-renewal by
CC repressing CDKN1A expression. Required to maintain proliferation and
CC prevent premature differentiation of neural progenitor cells during
CC early neural development: positively regulates FGF signaling by
CC controlling the stability of SHCBP1 (By similarity). Specific regulator
CC of miRNA biogenesis. Binds to miRNA MIR29A hairpin and
CC postranscriptionally modulates MIR29A levels, which indirectly
CC regulates TET proteins expression (PubMed:28431233).
CC {ECO:0000250|UniProtKB:Q1PSW8, ECO:0000269|PubMed:23125361,
CC ECO:0000269|PubMed:28431233, ECO:0000305|PubMed:24239284}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts (via NHL repeats) with AGO2; the interaction
CC increases in presence of RNA (PubMed:23125361). Interacts with
CC HSP90AA1. Interacts (via NHL repeats) with MOV10, PABPC1, PUM1, PUM2,
CC STAU2, XRN1 and XRN2 in an RNA-dependent manner (PubMed:23125361).
CC Interacts with SHCBP1; leading to enhance its stability (By
CC similarity). {ECO:0000250|UniProtKB:Q1PSW8,
CC ECO:0000269|PubMed:23125361}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000269|PubMed:23125361,
CC ECO:0000269|PubMed:24239284}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in testis.
CC {ECO:0000269|PubMed:15722555}.
CC -!- INDUCTION: Negatively regulated by the microRNA (miRNA) let-7 which
CC causes degradation of the mRNA encoding this protein. This requires a
CC let-7 complementary site (LCS) in the 3'-UTR of the mRNA encoding this
CC protein (PubMed:17890240, PubMed:24239284). Down-regulated by retinoic
CC acid in Tera-2 cells (PubMed:15722555). {ECO:0000269|PubMed:15722555,
CC ECO:0000269|PubMed:17890240, ECO:0000269|PubMed:24239284}.
CC -!- DOMAIN: The NHL domain, containing the 6 NHL repeats, is necessary and
CC sufficient to target RNA but not to repress mRNA. The minimal region
CC needed to execute repression consists of the coiled coil domain and the
CC Filamin repeat. The RING-type domain is dispensable for mRNA
CC repression. {ECO:0000269|PubMed:23125361}.
CC -!- PTM: Autoubiquitinated. {ECO:0000250|UniProtKB:Q1PSW8}.
CC -!- DISEASE: Hydrocephalus, congenital communicating, 1 (HYDCC1)
CC [MIM:618667]: A form of congenital hydrocephalus, a disease
CC characterized by onset in utero of enlarged ventricles due to
CC accumulation of ventricular cerebrospinal fluid. Affected individuals
CC may have neurologic impairment. HYDCC1 inheritance is autosomal
CC dominant. {ECO:0000269|PubMed:29983323}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- BIOTECHNOLOGY: Promotes reprogramming of differentiated cells to an
CC embryonic-like state designated iPS (induced pluripotent stem) cells.
CC iPS cells exhibit the morphology and growth properties of ES cells and
CC express ES cell marker genes. Inhibits translation of the
CC prodifferentiation transcription factor EGR1 through binding to its
CC mRNA and regulates a broad array of differentiation genes.
CC {ECO:0000269|PubMed:24239284}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
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DR EMBL; DQ232881; ABB18374.1; -; mRNA.
DR CCDS; CCDS43060.1; -.
DR RefSeq; NP_001034200.1; NM_001039111.2.
DR AlphaFoldDB; Q2Q1W2; -.
DR SMR; Q2Q1W2; -.
DR BioGRID; 126279; 59.
DR IntAct; Q2Q1W2; 17.
DR MINT; Q2Q1W2; -.
DR STRING; 9606.ENSP00000373272; -.
DR iPTMnet; Q2Q1W2; -.
DR PhosphoSitePlus; Q2Q1W2; -.
DR BioMuta; TRIM71; -.
DR DMDM; 121941685; -.
DR EPD; Q2Q1W2; -.
DR jPOST; Q2Q1W2; -.
DR MassIVE; Q2Q1W2; -.
DR MaxQB; Q2Q1W2; -.
DR PaxDb; Q2Q1W2; -.
DR PeptideAtlas; Q2Q1W2; -.
DR PRIDE; Q2Q1W2; -.
DR ProteomicsDB; 61436; -.
DR Antibodypedia; 45336; 190 antibodies from 33 providers.
DR DNASU; 131405; -.
DR Ensembl; ENST00000383763.6; ENSP00000373272.3; ENSG00000206557.6.
DR GeneID; 131405; -.
DR KEGG; hsa:131405; -.
DR MANE-Select; ENST00000383763.6; ENSP00000373272.3; NM_001039111.3; NP_001034200.1.
DR UCSC; uc003cff.4; human.
DR CTD; 131405; -.
DR DisGeNET; 131405; -.
DR GeneCards; TRIM71; -.
DR HGNC; HGNC:32669; TRIM71.
DR HPA; ENSG00000206557; Tissue enriched (testis).
DR MalaCards; TRIM71; -.
DR MIM; 618570; gene.
DR MIM; 618667; phenotype.
DR neXtProt; NX_Q2Q1W2; -.
DR OpenTargets; ENSG00000206557; -.
DR Orphanet; 269505; Congenital communicating hydrocephalus.
DR PharmGKB; PA144596246; -.
DR VEuPathDB; HostDB:ENSG00000206557; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000159099; -.
DR HOGENOM; CLU_008645_4_1_1; -.
DR InParanoid; Q2Q1W2; -.
DR OMA; QGEPRCS; -.
DR OrthoDB; 489543at2759; -.
DR PhylomeDB; Q2Q1W2; -.
DR TreeFam; TF331018; -.
DR PathwayCommons; Q2Q1W2; -.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q2Q1W2; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 131405; 17 hits in 1110 CRISPR screens.
DR ChiTaRS; TRIM71; human.
DR GenomeRNAi; 131405; -.
DR Pharos; Q2Q1W2; Tbio.
DR PRO; PR:Q2Q1W2; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q2Q1W2; protein.
DR Bgee; ENSG00000206557; Expressed in secondary oocyte and 52 other tissues.
DR Genevisible; Q2Q1W2; HS.
DR GO; GO:0000932; C:P-body; IDA:UniProtKB.
DR GO; GO:0035198; F:miRNA binding; IDA:UniProtKB.
DR GO; GO:0030371; F:translation repressor activity; IDA:CACAO.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0061158; P:3'-UTR-mediated mRNA destabilization; IDA:CACAO.
DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0010586; P:miRNA metabolic process; ISS:UniProtKB.
DR GO; GO:0035196; P:miRNA processing; IMP:UniProtKB.
DR GO; GO:0035278; P:miRNA-mediated gene silencing by inhibition of translation; ISS:UniProtKB.
DR GO; GO:0017148; P:negative regulation of translation; IDA:CACAO.
DR GO; GO:0001843; P:neural tube closure; IEA:Ensembl.
DR GO; GO:0021915; P:neural tube development; ISS:UniProtKB.
DR GO; GO:2000637; P:positive regulation of miRNA-mediated gene silencing; IEA:Ensembl.
DR GO; GO:0010608; P:post-transcriptional regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0051865; P:protein autoubiquitination; ISS:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0060964; P:regulation of miRNA-mediated gene silencing; ISS:UniProtKB.
DR GO; GO:2000177; P:regulation of neural precursor cell proliferation; ISS:UniProtKB.
DR GO; GO:0072089; P:stem cell proliferation; ISS:UniProtKB.
DR Gene3D; 2.120.10.30; -; 2.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR017868; Filamin/ABP280_repeat-like.
DR InterPro; IPR001298; Filamin/ABP280_rpt.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR001258; NHL_repeat.
DR InterPro; IPR000315; Znf_B-box.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR Pfam; PF00630; Filamin; 1.
DR Pfam; PF01436; NHL; 6.
DR Pfam; PF00643; zf-B_box; 1.
DR SMART; SM00336; BBOX; 2.
DR SMART; SM00557; IG_FLMN; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS50194; FILAMIN_REPEAT; 1.
DR PROSITE; PS51125; NHL; 6.
DR PROSITE; PS50119; ZF_BBOX; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Coiled coil; Cytoplasm; Developmental protein;
KW Disease variant; Metal-binding; Reference proteome; Repeat; RNA-binding;
KW RNA-mediated gene silencing; Transferase; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:21406692"
FT CHAIN 2..868
FT /note="E3 ubiquitin-protein ligase TRIM71"
FT /id="PRO_0000279511"
FT REPEAT 479..580
FT /note="Filamin"
FT REPEAT 593..636
FT /note="NHL 1"
FT REPEAT 640..683
FT /note="NHL 2"
FT REPEAT 687..730
FT /note="NHL 3"
FT REPEAT 734..777
FT /note="NHL 4"
FT REPEAT 781..824
FT /note="NHL 5"
FT REPEAT 828..868
FT /note="NHL 6"
FT ZN_FING 12..95
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 194..241
FT /note="B box-type 1; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT ZN_FING 273..314
FT /note="B box-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT REGION 26..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 127..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 391..427
FT /evidence="ECO:0000255"
FT COMPBIAS 26..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..181
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 278
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 281
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 301
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 306
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT VARIANT 608
FT /note="R -> H (in HYDCC1; dbSNP:rs1575362216)"
FT /evidence="ECO:0000269|PubMed:29983323"
FT /id="VAR_083426"
FT VARIANT 796
FT /note="R -> H (in HYDCC1; dbSNP:rs1575362492)"
FT /evidence="ECO:0000269|PubMed:29983323"
FT /id="VAR_083427"
FT MUTAGEN 647
FT /note="G->D: Strongly decreases repression on mRNA."
FT /evidence="ECO:0000269|PubMed:23125361"
FT MUTAGEN 675
FT /note="H->L: Abolishes repression on mRNA. Abolishes
FT interaction with AGO2, PABPC1 and PUM2. Increases
FT interaction with HSP90AA1."
FT /evidence="ECO:0000269|PubMed:23125361"
FT MUTAGEN 702
FT /note="Y->A: Decreases repression on mRNA. Decreases
FT interaction with HSP90AA1. Abolishes interaction with
FT PABPC1 and PUM2. Increases interaction with AGO2."
FT /evidence="ECO:0000269|PubMed:23125361"
FT MUTAGEN 751
FT /note="R->A: Decreases repression on mRNA. Abolishes
FT interaction with AGO2, HSP90AA1, PABPC1 and PUM2."
FT /evidence="ECO:0000269|PubMed:23125361"
SQ SEQUENCE 868 AA; 93385 MW; A71A1E5CC019F80D CRC64;
MASFPETDFQ ICLLCKEMCG SPAPLSSNSS ASSSSSQTST SSGGGGGGPG AAARRLHVLP
CLHAFCRPCL EAHRLPAAGG GAAGEPLKLR CPVCDQKVVL AEAAGMDALP SSAFLLSNLL
DAVVATADEP PPKNGRAGAP AGAGGHSNHR HHAHHAHPRA SASAPPLPQA PQPPAPSRSA
PGGPAASPSA LLLRRPHGCS SCDEGNAASS RCLDCQEHLC DNCVRAHQRV RLTKDHYIER
GPPGPGAAAA AQQLGLGPPF PGPPFSILSV FPERLGFCQH HDDEVLHLYC DTCSVPICRE
CTMGRHGGHS FIYLQEALQD SRALTIQLLA DAQQGRQAIQ LSIEQAQTVA EQVEMKAKVV
QSEVKAVTAR HKKALEEREC ELLWKVEKIR QVKAKSLYLQ VEKLRQNLNK LESTISAVQQ
VLEEGRALDI LLARDRMLAQ VQELKTVRSL LQPQEDDRVM FTPPDQALYL AIKSFGFVSS
GAFAPLTKAT GDGLKRALQG KVASFTVIGY DHDGEPRLSG GDLMSAVVLG PDGNLFGAEV
SDQQNGTYVV SYRPQLEGEH LVSVTLCNQH IENSPFKVVV KSGRSYVGIG LPGLSFGSEG
DSDGKLCRPW GVSVDKEGYI IVADRSNNRI QVFKPCGAFH HKFGTLGSRP GQFDRPAGVA
CDASRRIVVA DKDNHRIQIF TFEGQFLLKF GEKGTKNGQF NYPWDVAVNS EGKILVSDTR
NHRIQLFGPD GVFLNKYGFE GALWKHFDSP RGVAFNHEGH LVVTDFNNHR LLVIHPDCQS
ARFLGSEGTG NGQFLRPQGV AVDQEGRIIV ADSRNHRVQM FESNGSFLCK FGAQGSGFGQ
MDRPSGIAIT PDGMIVVVDF GNNRILVF
