ID MYOZ3_HUMAN Reviewed; 251 AA. AC Q8TDC0; B2R9Q4; D3DQG9; Q8IVM1; Q8IVN1; DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 18-MAY-2010, sequence version 2. DT 24-JAN-2024, entry version 147. DE RecName: Full=Myozenin-3; DE AltName: Full=Calsarcin-3; DE AltName: Full=FATZ-related protein 3; GN Name=MYOZ3 {ECO:0000312|HGNC:HGNC:18565}; GN Synonyms=FRP3 {ECO:0000312|EMBL:CAC83076.1}; 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] {ECO:0000305, ECO:0000312|EMBL:AAL79336.1} RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT PRO-161, INTERACTION WITH RP ACTN2; FLNC; LDB3; PPP3CA AND TCAP, AND TISSUE SPECIFICITY. RX PubMed=11842093; DOI=10.1074/jbc.m200712200; RA Frey N., Olson E.N.; RT "Calsarcin-3, a novel skeletal muscle-specific member of the calsarcin RT family, interacts with multiple Z-disc proteins."; RL J. Biol. Chem. 277:13998-14004(2002). RN [2] {ECO:0000305, ECO:0000312|EMBL:CAC83076.1} RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), AND VARIANT PRO-161. RC TISSUE=Skeletal muscle {ECO:0000312|EMBL:CAC83076.1}; RA Scannapieco P., Greggio E., Bortoletto G., Ievolella C., Lanfranchi G.; RT "New muscular proteins."; RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT PRO-161. RC TISSUE=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 [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] {ECO:0000305, ECO:0000312|EMBL:CAC83076.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT PRO-161. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [6] {ECO:0000305, ECO:0000312|EMBL:AAH69380.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT PRO-161. RC TISSUE=Lung {ECO:0000312|EMBL:AAH74871.1}; 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). CC -!- FUNCTION: Myozenins may serve as intracellular binding proteins CC involved in linking Z line proteins such as alpha-actinin, gamma- CC filamin, TCAP/telethonin, LDB3/ZASP and localizing calcineurin CC signaling to the sarcomere. Plays an important role in the modulation CC of calcineurin signaling. May play a role in myofibrillogenesis. CC -!- SUBUNIT: Interacts with ACTN2, LDB3, FLNC, PPP3CA and TCAP. CC {ECO:0000269|PubMed:11842093}. CC -!- INTERACTION: CC Q8TDC0; Q9NYB9-2: ABI2; NbExp=3; IntAct=EBI-5662487, EBI-11096309; CC Q8TDC0; Q53H80: AKIRIN2; NbExp=3; IntAct=EBI-5662487, EBI-742928; CC Q8TDC0; Q86U10: ASPG; NbExp=3; IntAct=EBI-5662487, EBI-19946665; CC Q8TDC0; Q7L5A3: ATOSB; NbExp=3; IntAct=EBI-5662487, EBI-745689; CC Q8TDC0; P0C7T5: ATXN1L; NbExp=3; IntAct=EBI-5662487, EBI-8624731; CC Q8TDC0; O95429: BAG4; NbExp=3; IntAct=EBI-5662487, EBI-2949658; CC Q8TDC0; O75934: BCAS2; NbExp=3; IntAct=EBI-5662487, EBI-1050106; CC Q8TDC0; Q5SWW7: C10orf55; NbExp=3; IntAct=EBI-5662487, EBI-12809220; CC Q8TDC0; Q2TAC2-2: CCDC57; NbExp=3; IntAct=EBI-5662487, EBI-10961624; CC Q8TDC0; A8MTA8-2: CIMIP2B; NbExp=3; IntAct=EBI-5662487, EBI-12160437; CC Q8TDC0; Q03060-25: CREM; NbExp=3; IntAct=EBI-5662487, EBI-12884642; CC Q8TDC0; Q8IUI8: CRLF3; NbExp=3; IntAct=EBI-5662487, EBI-2872414; CC Q8TDC0; Q15038: DAZAP2; NbExp=3; IntAct=EBI-5662487, EBI-724310; CC Q8TDC0; Q9NQL9: DMRT3; NbExp=3; IntAct=EBI-5662487, EBI-9679045; CC Q8TDC0; O43281-2: EFS; NbExp=3; IntAct=EBI-5662487, EBI-11525448; CC Q8TDC0; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-5662487, EBI-744099; CC Q8TDC0; Q8IYI6: EXOC8; NbExp=3; IntAct=EBI-5662487, EBI-742102; CC Q8TDC0; A1KXE4-2: FAM168B; NbExp=3; IntAct=EBI-5662487, EBI-12193763; CC Q8TDC0; Q13643: FHL3; NbExp=3; IntAct=EBI-5662487, EBI-741101; CC Q8TDC0; Q5TD97: FHL5; NbExp=3; IntAct=EBI-5662487, EBI-750641; CC Q8TDC0; O75603: GCM2; NbExp=3; IntAct=EBI-5662487, EBI-10188645; CC Q8TDC0; Q9NYA3: GOLGA6A; NbExp=3; IntAct=EBI-5662487, EBI-11163335; CC Q8TDC0; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-5662487, EBI-5916454; CC Q8TDC0; A0A024R8L2: hCG_1987119; NbExp=3; IntAct=EBI-5662487, EBI-14103818; CC Q8TDC0; O75031: HSF2BP; NbExp=3; IntAct=EBI-5662487, EBI-7116203; CC Q8TDC0; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-5662487, EBI-2556193; CC Q8TDC0; O76011: KRT34; NbExp=3; IntAct=EBI-5662487, EBI-1047093; CC Q8TDC0; O76013-2: KRT36; NbExp=3; IntAct=EBI-5662487, EBI-11958506; CC Q8TDC0; O95678: KRT75; NbExp=3; IntAct=EBI-5662487, EBI-2949715; CC Q8TDC0; Q3LI72: KRTAP19-5; NbExp=3; IntAct=EBI-5662487, EBI-1048945; CC Q8TDC0; Q3LI70: KRTAP19-6; NbExp=3; IntAct=EBI-5662487, EBI-12805508; CC Q8TDC0; Q3LI64: KRTAP6-1; NbExp=3; IntAct=EBI-5662487, EBI-12111050; CC Q8TDC0; Q8IUC3: KRTAP7-1; NbExp=3; IntAct=EBI-5662487, EBI-18394498; CC Q8TDC0; Q8IUC2: KRTAP8-1; NbExp=5; IntAct=EBI-5662487, EBI-10261141; CC Q8TDC0; Q16719-2: KYNU; NbExp=3; IntAct=EBI-5662487, EBI-12351611; CC Q8TDC0; Q96PV6: LENG8; NbExp=3; IntAct=EBI-5662487, EBI-739546; CC Q8TDC0; P25791-3: LMO2; NbExp=3; IntAct=EBI-5662487, EBI-11959475; CC Q8TDC0; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-5662487, EBI-11742507; CC Q8TDC0; P61968: LMO4; NbExp=3; IntAct=EBI-5662487, EBI-2798728; CC Q8TDC0; Q17RB8: LONRF1; NbExp=3; IntAct=EBI-5662487, EBI-2341787; CC Q8TDC0; Q6PF18: MORN3; NbExp=3; IntAct=EBI-5662487, EBI-9675802; CC Q8TDC0; Q96DV4: MRPL38; NbExp=3; IntAct=EBI-5662487, EBI-720441; CC Q8TDC0; Q9HC98-4: NEK6; NbExp=3; IntAct=EBI-5662487, EBI-11750983; CC Q8TDC0; P61970: NUTF2; NbExp=3; IntAct=EBI-5662487, EBI-591778; CC Q8TDC0; P78337: PITX1; NbExp=3; IntAct=EBI-5662487, EBI-748265; CC Q8TDC0; Q8IYS1: PM20D2; NbExp=3; IntAct=EBI-5662487, EBI-11339910; CC Q8TDC0; Q9NQX0: PRDM6; NbExp=3; IntAct=EBI-5662487, EBI-11320284; CC Q8TDC0; P28070: PSMB4; NbExp=3; IntAct=EBI-5662487, EBI-603350; CC Q8TDC0; Q13882: PTK6; NbExp=3; IntAct=EBI-5662487, EBI-1383632; CC Q8TDC0; Q6NUQ1: RINT1; NbExp=3; IntAct=EBI-5662487, EBI-726876; CC Q8TDC0; Q9BVN2: RUSC1; NbExp=3; IntAct=EBI-5662487, EBI-6257312; CC Q8TDC0; Q8WW14-2: SPMIP5; NbExp=3; IntAct=EBI-5662487, EBI-12831628; CC Q8TDC0; Q96SF7: TBX15; NbExp=3; IntAct=EBI-5662487, EBI-10191361; CC Q8TDC0; Q8WW24: TEKT4; NbExp=3; IntAct=EBI-5662487, EBI-750487; CC Q8TDC0; O75865-2: TRAPPC6A; NbExp=3; IntAct=EBI-5662487, EBI-8451480; CC Q8TDC0; Q86WV8: TSC1; NbExp=3; IntAct=EBI-5662487, EBI-12806590; CC Q8TDC0; Q96PN8: TSSK3; NbExp=3; IntAct=EBI-5662487, EBI-3918381; CC Q8TDC0; Q6NVU6: UFSP1; NbExp=3; IntAct=EBI-5662487, EBI-12068150; CC Q8TDC0; Q6ZNG0: ZNF620; NbExp=3; IntAct=EBI-5662487, EBI-4395669; CC Q8TDC0; P0C7X2: ZNF688; NbExp=3; IntAct=EBI-5662487, EBI-4395732; CC -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, Z line CC {ECO:0000250}. Note=Localized at the Z-line of skeletal muscle. CC {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1 {ECO:0000269|PubMed:11842093}; CC IsoId=Q8TDC0-1; Sequence=Displayed; CC Name=2 {ECO:0000269|Ref.2}; CC IsoId=Q8TDC0-2; Sequence=VSP_051879; CC Name=3 {ECO:0000269|Ref.2}; CC IsoId=Q8TDC0-3; Sequence=VSP_051876, VSP_051877, VSP_051878; CC -!- TISSUE SPECIFICITY: Expressed specifically in skeletal muscle. Not CC detected in heart. {ECO:0000269|PubMed:11842093}. CC -!- SIMILARITY: Belongs to the myozenin family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF480443; AAL79336.1; -; mRNA. DR EMBL; AJ277961; CAC81912.1; -; mRNA. DR EMBL; AJ300586; CAC83076.1; -; mRNA. DR EMBL; AJ300587; CAC83077.1; -; mRNA. DR EMBL; AK313873; BAG36601.1; -; mRNA. DR EMBL; AC008453; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471062; EAW61713.1; -; Genomic_DNA. DR EMBL; CH471062; EAW61714.1; -; Genomic_DNA. DR EMBL; BC069380; AAH69380.1; -; mRNA. DR EMBL; BC069553; AAH69553.1; -; mRNA. DR EMBL; BC074870; AAH74870.1; -; mRNA. DR EMBL; BC074871; AAH74871.1; -; mRNA. DR CCDS; CCDS4309.1; -. [Q8TDC0-1] DR RefSeq; NP_001116325.1; NM_001122853.2. [Q8TDC0-1] DR RefSeq; NP_588612.2; NM_133371.4. [Q8TDC0-1] DR AlphaFoldDB; Q8TDC0; -. DR BioGRID; 124899; 66. DR IntAct; Q8TDC0; 62. DR MINT; Q8TDC0; -. DR STRING; 9606.ENSP00000297130; -. DR iPTMnet; Q8TDC0; -. DR PhosphoSitePlus; Q8TDC0; -. DR BioMuta; MYOZ3; -. DR DMDM; 296439236; -. DR MassIVE; Q8TDC0; -. DR PaxDb; 9606-ENSP00000297130; -. DR PeptideAtlas; Q8TDC0; -. DR ProteomicsDB; 74261; -. [Q8TDC0-1] DR ProteomicsDB; 74262; -. [Q8TDC0-2] DR ProteomicsDB; 74263; -. [Q8TDC0-3] DR Antibodypedia; 50777; 30 antibodies from 13 providers. DR DNASU; 91977; -. DR Ensembl; ENST00000297130.4; ENSP00000297130.4; ENSG00000164591.14. [Q8TDC0-1] DR Ensembl; ENST00000517768.6; ENSP00000428815.1; ENSG00000164591.14. [Q8TDC0-1] DR Ensembl; ENST00000615557.1; ENSP00000478375.1; ENSG00000164591.14. [Q8TDC0-3] DR GeneID; 91977; -. DR KEGG; hsa:91977; -. DR MANE-Select; ENST00000517768.6; ENSP00000428815.1; NM_001122853.3; NP_001116325.1. DR UCSC; uc003lsr.4; human. [Q8TDC0-1] DR AGR; HGNC:18565; -. DR CTD; 91977; -. DR DisGeNET; 91977; -. DR GeneCards; MYOZ3; -. DR HGNC; HGNC:18565; MYOZ3. DR HPA; ENSG00000164591; Group enriched (skeletal muscle, tongue). DR MIM; 610735; gene. DR neXtProt; NX_Q8TDC0; -. DR OpenTargets; ENSG00000164591; -. DR PharmGKB; PA38577; -. DR VEuPathDB; HostDB:ENSG00000164591; -. DR eggNOG; ENOG502S22C; Eukaryota. DR GeneTree; ENSGT00950000183027; -. DR HOGENOM; CLU_071316_1_0_1; -. DR InParanoid; Q8TDC0; -. DR OMA; IMRPGPE; -. DR OrthoDB; 4320129at2759; -. DR PhylomeDB; Q8TDC0; -. DR TreeFam; TF331748; -. DR PathwayCommons; Q8TDC0; -. DR SignaLink; Q8TDC0; -. DR BioGRID-ORCS; 91977; 13 hits in 1158 CRISPR screens. DR GenomeRNAi; 91977; -. DR Pharos; Q8TDC0; Tdark. DR PRO; PR:Q8TDC0; -. DR Proteomes; UP000005640; Chromosome 5. DR RNAct; Q8TDC0; Protein. DR Bgee; ENSG00000164591; Expressed in skeletal muscle tissue of rectus abdominis and 150 other cell types or tissues. DR ExpressionAtlas; Q8TDC0; baseline and differential. DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central. DR GO; GO:0030018; C:Z disc; IBA:GO_Central. DR GO; GO:0003779; F:actin binding; IBA:GO_Central. DR GO; GO:0051373; F:FATZ binding; IBA:GO_Central. DR GO; GO:0031433; F:telethonin binding; IBA:GO_Central. DR InterPro; IPR008438; MYOZ. DR PANTHER; PTHR15941; MYOZENIN; 1. DR PANTHER; PTHR15941:SF15; MYOZENIN-3; 1. DR Pfam; PF05556; Calsarcin; 1. DR Genevisible; Q8TDC0; HS. PE 1: Evidence at protein level; KW Alternative splicing; Cytoplasm; Phosphoprotein; Reference proteome. FT CHAIN 1..251 FT /note="Myozenin-3" FT /id="PRO_0000111102" FT REGION 50..67 FT /note="Binding to ACTN2, PPP3CA and TCAP" FT /evidence="ECO:0000269|PubMed:11842093" FT REGION 67..110 FT /note="Binding to FLNC" FT /evidence="ECO:0000269|PubMed:11842093" FT REGION 79..102 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 186..207 FT /note="Binding to ACTN2" FT /evidence="ECO:0000269|PubMed:11842093" FT COMPBIAS 83..97 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 31 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8R4E4" FT VAR_SEQ 1..20 FT /note="MIPKEQKGPVMAAMGDLTEP -> MLREVGPGVYGGWGGESPLWPFLA (in FT isoform 3)" FT /evidence="ECO:0000303|Ref.2" FT /id="VSP_051876" FT VAR_SEQ 73..83 FT /note="MLAGSARRKVT -> VSKPPLCSWGK (in isoform 3)" FT /evidence="ECO:0000303|Ref.2" FT /id="VSP_051877" FT VAR_SEQ 84..251 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|Ref.2" FT /id="VSP_051878" FT VAR_SEQ 186..231 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|Ref.2" FT /id="VSP_051879" FT VARIANT 161 FT /note="S -> P (in dbSNP:rs194134)" FT /evidence="ECO:0000269|PubMed:11842093, FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334, FT ECO:0000269|Ref.2, ECO:0000269|Ref.5" FT /id="VAR_067718" FT VARIANT 209 FT /note="T -> N (in dbSNP:rs7737542)" FT /id="VAR_056203" SQ SEQUENCE 251 AA; 27157 MW; AF1C09E49CD31D94 CRC64; MIPKEQKGPV MAAMGDLTEP VPTLDLGKKL SVPQDLMMEE LSLRNNRGSL LFQKRQRRVQ KFTFELAASQ RAMLAGSARR KVTGTAESGT VANANGPEGP NYRSELHIFP ASPGASLGGP EGAHPAAAPA GCVPSPSALA PGYAEPLKGV PPEKFNHTAI SKGYRCPWQE FVSYRDYQSD GRSHTPSPND YRNFNKTPVP FGGPLVGGTF PRPGTPFIPE PLSGLELLRL RPSFNRVAQG WVRNLPESEE L //