ZC3HD_MOUSE
ID ZC3HD_MOUSE Reviewed; 1729 AA.
AC E9Q784; B9EHN9;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Zinc finger CCCH domain-containing protein 13 {ECO:0000305};
GN Name=Zc3h13 {ECO:0000303|PubMed:29535189, ECO:0000303|PubMed:29547716,
GN ECO:0000312|MGI:MGI:1914552};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-242; THR-263 AND SER-265, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-198; SER-207; SER-242;
RP THR-263; SER-907; SER-909; SER-913; SER-953; SER-1069; SER-1086; SER-1090
RP AND SER-1093, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP FUNCTION, AND IDENTIFICATION IN THE WMM COMPLEX.
RX PubMed=29535189; DOI=10.1101/gad.309146.117;
RA Knuckles P., Lence T., Haussmann I.U., Jacob D., Kreim N., Carl S.H.,
RA Masiello I., Hares T., Villasenor R., Hess D., Andrade-Navarro M.A.,
RA Biggiogera M., Helm M., Soller M., Buehler M., Roignant J.Y.;
RT "Zc3h13/Flacc is required for adenosine methylation by bridging the mRNA-
RT binding factor Rbm15/Spenito to the m6A machinery component Wtap/Fl(2)d.";
RL Genes Dev. 32:415-429(2018).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION IN THE WMM COMPLEX.
RX PubMed=29547716; DOI=10.1016/j.molcel.2018.02.015;
RA Wen J., Lv R., Ma H., Shen H., He C., Wang J., Jiao F., Liu H., Yang P.,
RA Tan L., Lan F., Shi Y.G., He C., Shi Y., Diao J.;
RT "Zc3h13 regulates nuclear RNA m6A methylation and mouse embryonic stem cell
RT self-renewal.";
RL Mol. Cell 69:1028-1038(2018).
CC -!- FUNCTION: Associated component of the WMM complex, a complex that
CC mediates N6-methyladenosine (m6A) methylation of RNAs, a modification
CC that plays a role in the efficiency of mRNA splicing and RNA processing
CC (PubMed:29535189, PubMed:29547716). Acts as a key regulator of m6A
CC methylation by promoting m6A methylation of mRNAs at the 3'-UTR
CC (PubMed:29547716). Controls embryonic stem cells (ESCs) pluripotency
CC via its role in m6A methylation (PubMed:29547716). In the WMM complex,
CC anchors component of the MACOM subcomplex in the nucleus
CC (PubMed:29547716). Also required for bridging WTAP to the RNA-binding
CC component RBM15 (RBM15 or RBM15B) (PubMed:29535189).
CC {ECO:0000269|PubMed:29535189, ECO:0000269|PubMed:29547716}.
CC -!- SUBUNIT: Component of the WMM complex, a N6-methyltransferase complex
CC composed of a catalytic subcomplex, named MAC, and of an associated
CC subcomplex, named MACOM (PubMed:29535189, PubMed:29547716). The MAC
CC subcomplex is composed of METTL3 and METTL14 (PubMed:29535189,
CC PubMed:29547716). The MACOM subcomplex is composed of WTAP, ZC3H13,
CC CBLL1/HAKAI, VIRMA, and, in some cases of RBM15 (RBM15 or RBM15B)
CC (PubMed:29535189, PubMed:29547716). Also a component of a MACOM-like
CC complex, named WTAP complex, composed of WTAP, ZC3H13, CBLL1/HAKAI,
CC VIRMA, RBM15, BCLAF1 and THRAP3 (By similarity).
CC {ECO:0000250|UniProtKB:Q5T200, ECO:0000269|PubMed:29535189,
CC ECO:0000269|PubMed:29547716}.
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250|UniProtKB:Q5T200}.
CC Nucleus, nucleoplasm {ECO:0000269|PubMed:29547716}.
CC -!- SIMILARITY: Belongs to the ZC3H13 family. {ECO:0000305}.
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DR EMBL; AC161877; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC138264; AAI38265.1; -; mRNA.
DR CCDS; CCDS27278.1; -.
DR RefSeq; NP_080359.2; NM_026083.2.
DR RefSeq; XP_006519508.1; XM_006519445.3.
DR RefSeq; XP_006519509.1; XM_006519446.3.
DR RefSeq; XP_006519510.1; XM_006519447.3.
DR AlphaFoldDB; E9Q784; -.
DR ComplexPortal; CPX-1609; WMM N6-adenosine-methyltransferase complex.
DR DIP; DIP-58951N; -.
DR IntAct; E9Q784; 1.
DR STRING; 10090.ENSMUSP00000022577; -.
DR iPTMnet; E9Q784; -.
DR PhosphoSitePlus; E9Q784; -.
DR EPD; E9Q784; -.
DR jPOST; E9Q784; -.
DR MaxQB; E9Q784; -.
DR PaxDb; E9Q784; -.
DR PRIDE; E9Q784; -.
DR ProteomicsDB; 275270; -.
DR Antibodypedia; 23654; 112 antibodies from 22 providers.
DR DNASU; 67302; -.
DR Ensembl; ENSMUST00000022577; ENSMUSP00000022577; ENSMUSG00000022000.
DR GeneID; 67302; -.
DR KEGG; mmu:67302; -.
DR UCSC; uc007uqs.1; mouse.
DR UCSC; uc007uqt.2; mouse.
DR CTD; 23091; -.
DR MGI; MGI:1914552; Zc3h13.
DR VEuPathDB; HostDB:ENSMUSG00000022000; -.
DR eggNOG; KOG1874; Eukaryota.
DR GeneTree; ENSGT00730000111163; -.
DR HOGENOM; CLU_003683_0_0_1; -.
DR InParanoid; E9Q784; -.
DR OrthoDB; 248688at2759; -.
DR TreeFam; TF332670; -.
DR BioGRID-ORCS; 67302; 10 hits in 71 CRISPR screens.
DR ChiTaRS; Zc3h13; mouse.
DR PRO; PR:E9Q784; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; E9Q784; protein.
DR Bgee; ENSMUSG00000022000; Expressed in rostral migratory stream and 227 other tissues.
DR ExpressionAtlas; E9Q784; baseline and differential.
DR Genevisible; E9Q784; MM.
DR GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR GO; GO:0036396; C:RNA N6-methyladenosine methyltransferase complex; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0080009; P:mRNA methylation; IDA:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:2000036; P:regulation of stem cell population maintenance; IMP:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR Pfam; PF00642; zf-CCCH; 1.
DR SMART; SM00356; ZnF_C3H1; 1.
DR SUPFAM; SSF90229; SSF90229; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Developmental protein; Isopeptide bond; Metal-binding;
KW mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..1729
FT /note="Zinc finger CCCH domain-containing protein 13"
FT /id="PRO_0000434521"
FT ZN_FING 36..64
FT /note="C3H1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 57..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 182..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 581..1527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 162..196
FT /evidence="ECO:0000255"
FT COILED 706..865
FT /evidence="ECO:0000255"
FT COMPBIAS 13..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..156
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..196
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..318
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..344
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..387
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 389..528
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 581..634
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 639..658
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 659..943
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 954..1037
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1044..1074
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1084..1103
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1118..1157
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1189..1218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1219..1252
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1253..1276
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1277..1511
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T200"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T200"
FT MOD_RES 198
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 207
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 209
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T200"
FT MOD_RES 211
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T200"
FT MOD_RES 242
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 263
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 265
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326"
FT MOD_RES 316
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T200"
FT MOD_RES 318
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T200"
FT MOD_RES 324
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T200"
FT MOD_RES 327
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T200"
FT MOD_RES 353
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5T200"
FT MOD_RES 363
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5T200"
FT MOD_RES 369
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T200"
FT MOD_RES 371
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T200"
FT MOD_RES 380
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T200"
FT MOD_RES 704
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T200"
FT MOD_RES 907
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 909
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 913
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 921
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T200"
FT MOD_RES 924
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T200"
FT MOD_RES 929
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T200"
FT MOD_RES 949
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T200"
FT MOD_RES 951
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T200"
FT MOD_RES 953
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 958
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5T200"
FT MOD_RES 1069
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1086
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1090
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1093
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1109
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5T200"
FT MOD_RES 1256
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T200"
FT MOD_RES 1259
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T200"
FT MOD_RES 1273
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T200"
FT MOD_RES 1275
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T200"
FT MOD_RES 1295
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T200"
FT MOD_RES 1427
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T200"
FT MOD_RES 1443
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T200"
FT MOD_RES 1447
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T200"
FT MOD_RES 1467
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T200"
FT MOD_RES 1470
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T200"
FT MOD_RES 1499
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T200"
FT MOD_RES 1526
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T200"
FT CROSSLNK 179
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5T200"
FT CONFLICT 1501
FT /note="E -> EA (in Ref. 2; AAI38265)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1729 AA; 203755 MW; 3769C505A180454B CRC64;
MSKIRRKVTV ENTKTISEST SRRPSVFERL GPSTGSTTET QCRNWLKTGS CLYGNTCRFI
HGPSPRGKGY SSNYRRSPER PTGDLRERMK NKRQDVDSES QKRNTEEPSS PVRKESSRGR
HRDKEDIKIV KERTPESEEE NVEWETNRDD SDNGDINYDY VHELSLEMKR QKIQRELMKL
EQENMDKREE IIIQKEVSPE VVRSKLSPSP SLRKSSKSPK RKSSPKASSA GKKERKAAVV
ASPLLDQQRN SKGNQSKKKG PRTPSPPPPI LEDIILGKKY KEKYKVKDRI EEKPRDGKDR
GRDFEKQREK RDKPRSSSPG QHHSPLSSRH HSSSSQSGSS IQRHSPSPRR KRTPSPSYQR
TLTPSLRRSA SPYPTHCLSS PQRKQSPPRH RSPMREKGRH DHERTSQSHD RRHERREETR
GKRDREKDTR EERESEHDHR DDREPRDSRD RRDTRDRREL RDSRDMRDSR EMRDYSRDAK
ESRDPRDSRS ARDVHDYRDR EARDAHARDV RDARDARDAR DARDIRDVRD VRDVRDVRDV
RDVRDVRDVR DVRDARDVRD VRDARDVRDV RDVRDGHRKE DVYQEEARSY GRNHLREESS
RVELRNDSRN ESRSEIRNDR MGRSRGRGPE LPEKGSRGTR GSQMDSHSSG SNYHDSWETR
SSYPERDRYP ERDTRDPARD SSFERRHGER DRRDNRERDQ RPSSPIRHQG RSEELERDER
REERRIDRVD ERRDDRVRDR DRDRERERER EREREREREK ERERELERER AREREREREK
ERERERERER DQRDRDHDRE RERERERERE KEREREREER ERERERERER ERERERERER
ERERERERER AREREKERER QREWEDKDKG RDDRREKRED IHVREDRIPR DSHEERKSKK
RYRNEGSPSP RQSPKRRREH SPDSDTYHSG DDKNEKHRLL SQVVRPQESR SLSPSHLTED
RQGRWKEEDR KSERKESSRR YEEQELKEKL SCGDRQREQA ESVDSSRVRA QDLLSHRQAE
DRDRDGSDRA HDEKKKAKAP KKPVKKKKEE DVGVERGNLE THEDSQVFSP KKGQKKKNIE
KKRKRSKGDS DVSDEEAAPQ NKKKRGPRTP PLAIKEELAD ISTDKDGVLE DPLKKENTAF
SDWSDEDVPD RTEGLEAEHT AATATPGSTP SPLSSLLPPP PPVAAASTAA TALASSAVSA
TTSATSSSSA ATSNTNGSED SHRKCHRARG EKVEVSHVTL EDTPHRKLVD QKRSSSLGSN
RSHRSHTSGR LRSPSNDSAH RSGDDQGSRK RVLHSGSRDR EKTKSLEITG ERKSRIDQLK
RGEPSRSTSS DRQDSRSHSS RRSSPESDRQ VHSRSGSFDS RDRLQERDRY EHDRERERDR
RDPRQREWDR EAEKEWPRTR DRDRLRERDR DRDRRRDLDR ERERLISDPM ERDRERERTF
ETSQLESGKR SEVKLESEHE RDLEGSSRDS VALDKERMDR DLGSVQGFED VSKAERTESL
EGDDESKLDD AHSLGSGAGE GYEPISDDEL DEILAGDAEK REDQQEEEKM PDPLDVIDVD
WSGLMPKHPK EPREPGAALL KFTPGAVLLR VGISKKLAGS ELFTKVKETC QQLVEKPKDA
DSLFEHELGA LNMAALLRKE ERASLLSDLG PCCKALCFRR DSAIRKQLVK NEKGTVKQAY
TNTPMVDNEL LRLSLRLFKK KATCHAPGQE KTEDGKLGPC SIQQELCVS
