ZN346_HUMAN
ID ZN346_HUMAN Reviewed; 294 AA.
AC Q9UL40; B7Z367; Q68CV9; Q6ZMW1;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Zinc finger protein 346;
DE AltName: Full=Just another zinc finger protein;
GN Name=ZNF346; Synonyms=JAZ;
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).
RC TISSUE=Placenta;
RX PubMed=10488071; DOI=10.1074/jbc.274.39.27399;
RA Yang M., May W.S., Ito T.;
RT "JAZ requires the double-stranded RNA-binding zinc finger motifs for
RT nuclear localization.";
RL J. Biol. Chem. 274:27399-27406(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Hippocampus, and Testis;
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=Brain;
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=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Uterus;
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 IDENTIFICATION IN A NUCLEAR EXPORT RECEPTOR COMPLEX WITH XPO5; RAN; ILF3
RP AND DOUBLE-STRANDED RNA, SUBCELLULAR LOCATION, AND INTERACTION WITH XPO5
RP AND ILF3.
RX PubMed=15254228; DOI=10.1128/mcb.24.15.6608-6619.2004;
RA Chen T., Brownawell A.M., Macara I.G.;
RT "Nucleocytoplasmic shuttling of JAZ, a new cargo protein for exportin-5.";
RL Mol. Cell. Biol. 24:6608-6619(2004).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [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 [8]
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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
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 SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-114 AND LYS-170, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [12]
RP STRUCTURE BY NMR OF 168-227, AND FUNCTION.
RX PubMed=24521053; DOI=10.1021/bi401675h;
RA Burge R.G., Martinez-Yamout M.A., Dyson H.J., Wright P.E.;
RT "Structural characterization of interactions between the double-stranded
RT RNA-binding zinc finger protein JAZ and nucleic acids.";
RL Biochemistry 53:1495-1510(2014).
CC -!- FUNCTION: Binds with low affinity to dsDNA and ssRNA, and with high
CC affinity to dsRNA, with no detectable sequence specificity
CC (PubMed:24521053). May bind to specific miRNA hairpins
CC (PubMed:28431233). {ECO:0000269|PubMed:24521053,
CC ECO:0000269|PubMed:28431233}.
CC -!- SUBUNIT: Forms a heteromeric complex with XPO5 and ILF3. Found in a
CC nuclear export complex with XPO5, RAN, ILF3, ZNF346 and double-stranded
CC RNA. Interacts with XPO5. Interacts with ILF3 in an RNA-independent
CC manner. {ECO:0000269|PubMed:15254228}.
CC -!- INTERACTION:
CC Q9UL40; P78563-4: ADARB1; NbExp=3; IntAct=EBI-2462313, EBI-12002366;
CC Q9UL40; P46379-2: BAG6; NbExp=3; IntAct=EBI-2462313, EBI-10988864;
CC Q9UL40; P19525: EIF2AK2; NbExp=3; IntAct=EBI-2462313, EBI-640775;
CC Q9UL40; Q92993: KAT5; NbExp=3; IntAct=EBI-2462313, EBI-399080;
CC Q9UL40; O14901: KLF11; NbExp=3; IntAct=EBI-2462313, EBI-948266;
CC Q9UL40; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-2462313, EBI-11742507;
CC Q9UL40; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-2462313, EBI-739832;
CC Q9UL40; O15226: NKRF; NbExp=3; IntAct=EBI-2462313, EBI-766011;
CC Q9UL40; O76064: RNF8; NbExp=3; IntAct=EBI-2462313, EBI-373337;
CC Q9UL40; Q15047-2: SETDB1; NbExp=3; IntAct=EBI-2462313, EBI-9090795;
CC Q9UL40; Q96SI9: STRBP; NbExp=3; IntAct=EBI-2462313, EBI-740355;
CC Q9UL40; Q15633: TARBP2; NbExp=6; IntAct=EBI-2462313, EBI-978581;
CC Q9UL40; P61981: YWHAG; NbExp=3; IntAct=EBI-2462313, EBI-359832;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:15254228}.
CC Cytoplasm {ECO:0000269|PubMed:15254228}. Note=Nuclear at steady state,
CC primarily in the nucleolus. Shuttles between the nucleus and cytoplasm
CC when associated with XPO5.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9UL40-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UL40-2; Sequence=VSP_015971;
CC Name=3;
CC IsoId=Q9UL40-3; Sequence=VSP_055098;
CC -!- DOMAIN: The zinc-finger domains are required for binding to dsRNA, and
CC also for nuclear localization. {ECO:0000250}.
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DR EMBL; AF083340; AAD52018.1; -; mRNA.
DR EMBL; AK131469; BAD18614.1; -; mRNA.
DR EMBL; AK295549; BAH12103.1; -; mRNA.
DR EMBL; CR749692; CAH18475.1; -; mRNA.
DR EMBL; AC027314; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC027317; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC007775; AAH07775.1; -; mRNA.
DR CCDS; CCDS4409.1; -. [Q9UL40-1]
DR CCDS; CCDS78094.1; -. [Q9UL40-2]
DR CCDS; CCDS83052.1; -. [Q9UL40-3]
DR RefSeq; NP_001295142.1; NM_001308213.1. [Q9UL40-2]
DR RefSeq; NP_001295143.1; NM_001308214.1. [Q9UL40-3]
DR RefSeq; NP_001295148.1; NM_001308219.1.
DR RefSeq; NP_001295152.1; NM_001308223.1.
DR RefSeq; NP_036411.1; NM_012279.3. [Q9UL40-1]
DR RefSeq; XP_016864784.1; XM_017009295.1. [Q9UL40-1]
DR RefSeq; XP_016864785.1; XM_017009296.1. [Q9UL40-1]
DR PDB; 2MKD; NMR; -; A=168-227.
DR PDB; 2MKN; NMR; -; A=168-227.
DR PDBsum; 2MKD; -.
DR PDBsum; 2MKN; -.
DR AlphaFoldDB; Q9UL40; -.
DR BMRB; Q9UL40; -.
DR SMR; Q9UL40; -.
DR BioGRID; 117109; 383.
DR IntAct; Q9UL40; 42.
DR STRING; 9606.ENSP00000350869; -.
DR GlyGen; Q9UL40; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UL40; -.
DR MetOSite; Q9UL40; -.
DR PhosphoSitePlus; Q9UL40; -.
DR BioMuta; ZNF346; -.
DR DMDM; 74735051; -.
DR EPD; Q9UL40; -.
DR jPOST; Q9UL40; -.
DR MassIVE; Q9UL40; -.
DR MaxQB; Q9UL40; -.
DR PaxDb; Q9UL40; -.
DR PeptideAtlas; Q9UL40; -.
DR PRIDE; Q9UL40; -.
DR ProteomicsDB; 6494; -.
DR ProteomicsDB; 84940; -. [Q9UL40-1]
DR ProteomicsDB; 84941; -. [Q9UL40-2]
DR Antibodypedia; 17273; 313 antibodies from 32 providers.
DR DNASU; 23567; -.
DR Ensembl; ENST00000358149.8; ENSP00000350869.3; ENSG00000113761.12. [Q9UL40-1]
DR Ensembl; ENST00000503039.1; ENSP00000424495.1; ENSG00000113761.12. [Q9UL40-2]
DR Ensembl; ENST00000503425.5; ENSP00000421212.1; ENSG00000113761.12. [Q9UL40-3]
DR GeneID; 23567; -.
DR KEGG; hsa:23567; -.
DR MANE-Select; ENST00000358149.8; ENSP00000350869.3; NM_012279.4; NP_036411.1.
DR UCSC; uc003mfi.4; human. [Q9UL40-1]
DR CTD; 23567; -.
DR DisGeNET; 23567; -.
DR GeneCards; ZNF346; -.
DR HGNC; HGNC:16403; ZNF346.
DR HPA; ENSG00000113761; Low tissue specificity.
DR MIM; 605308; gene.
DR neXtProt; NX_Q9UL40; -.
DR OpenTargets; ENSG00000113761; -.
DR PharmGKB; PA134898181; -.
DR VEuPathDB; HostDB:ENSG00000113761; -.
DR eggNOG; ENOG502RVNK; Eukaryota.
DR GeneTree; ENSGT00940000159101; -.
DR HOGENOM; CLU_056875_0_1_1; -.
DR InParanoid; Q9UL40; -.
DR OrthoDB; 1565630at2759; -.
DR PhylomeDB; Q9UL40; -.
DR TreeFam; TF350019; -.
DR PathwayCommons; Q9UL40; -.
DR SignaLink; Q9UL40; -.
DR BioGRID-ORCS; 23567; 11 hits in 1081 CRISPR screens.
DR ChiTaRS; ZNF346; human.
DR GeneWiki; ZNF346; -.
DR GenomeRNAi; 23567; -.
DR Pharos; Q9UL40; Tbio.
DR PRO; PR:Q9UL40; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q9UL40; protein.
DR Bgee; ENSG00000113761; Expressed in pancreatic ductal cell and 151 other tissues.
DR ExpressionAtlas; Q9UL40; baseline and differential.
DR Genevisible; Q9UL40; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003725; F:double-stranded RNA binding; IDA:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0035198; F:miRNA binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR IDEAL; IID00685; -.
DR InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR SMART; SM00355; ZnF_C2H2; 4.
DR SMART; SM00451; ZnF_U1; 4.
DR SUPFAM; SSF57667; SSF57667; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Isopeptide bond; Metal-binding; Nucleus; Reference proteome; Repeat;
KW RNA-binding; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..294
FT /note="Zinc finger protein 346"
FT /id="PRO_0000191809"
FT ZN_FING 70..104
FT /note="Matrin-type 1"
FT ZN_FING 131..165
FT /note="Matrin-type 2"
FT ZN_FING 182..216
FT /note="Matrin-type 3"
FT ZN_FING 236..270
FT /note="Matrin-type 4"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 75
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 78
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 91
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 136
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 139
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 152
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 158
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT CROSSLNK 114
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 170
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 58
FT /note="E -> EAQFFPHSRTVIPILVLSETYSLCHP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_015971"
FT VAR_SEQ 94..125
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055098"
FT CONFLICT 152
FT /note="H -> Y (in Ref. 3; CAH18475)"
FT /evidence="ECO:0000305"
FT TURN 176..178
FT /evidence="ECO:0007829|PDB:2MKD"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:2MKD"
FT TURN 188..191
FT /evidence="ECO:0007829|PDB:2MKD"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:2MKD"
FT HELIX 197..203
FT /evidence="ECO:0007829|PDB:2MKD"
FT HELIX 207..222
FT /evidence="ECO:0007829|PDB:2MKD"
SQ SEQUENCE 294 AA; 32933 MW; 095F02E19FBCFBE0 CRC64;
MEYPAPATVQ AADGGAAGPY SSSELLEGQE PDGVRFDRER ARRLWEAVSG AQPVGREEVE
HMIQKNQCLF TNTQCKVCCA LLISESQKLA HYQSKKHANK VKRYLAIHGM ETLKGETKKL
DSDQKSSRSK DKNQCCPICN MTFSSPVVAQ SHYLGKTHAK NLKLKQQSTK VEALHQNREM
IDPDKFCSLC HATFNDPVMA QQHYVGKKHR KQETKLKLMA RYGRLADPAV TDFPAGKGYP
CKTCKIVLNS IEQYQAHVSG FKHKNQSPKT VASSLGQIPM QRQPIQKDST TLED
