ID RN220_HUMAN Reviewed; 566 AA. AC Q5VTB9; B3KPJ3; B4DLZ9; E9PCS1; Q4KMX2; Q9NVP6; DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot. DT 07-DEC-2004, sequence version 1. DT 27-MAR-2024, entry version 166. DE RecName: Full=E3 ubiquitin-protein ligase RNF220; DE EC=2.3.2.27; DE AltName: Full=RING finger protein 220; DE AltName: Full=RING-type E3 ubiquitin transferase RNF220 {ECO:0000305}; GN Name=RNF220; Synonyms=C1orf164; 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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Brain; 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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). 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 [4] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-390, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [5] RP IDENTIFICATION BY MASS 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 [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 INTERACTION WITH CTNNB1 AND USP7, AND FUNCTION. RX PubMed=25266658; DOI=10.1128/mcb.00731-14; RA Ma P., Yang X., Kong Q., Li C., Yang S., Li Y., Mao B.; RT "The ubiquitin ligase RNF220 enhances canonical Wnt signaling through USP7- RT mediated deubiquitination of beta-catenin."; RL Mol. Cell. Biol. 34:4355-4366(2014). RN [8] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-277, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25218447; DOI=10.1038/nsmb.2890; RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., RA Vertegaal A.C.; RT "Uncovering global SUMOylation signaling networks in a site-specific RT manner."; RL Nat. Struct. Mol. Biol. 21:927-936(2014). RN [9] RP VARIANTS HLD23 GLN-363 AND GLN-365, CHARACTERIZATION OF VARIANTS HLD23 RP GLN-363 AND GLN-365, INTERACTION WITH CTNNB1, FUNCTION, SUBCELLULAR RP LOCATION, AND TISSUE SPECIFICITY. RX PubMed=33964137; DOI=10.1093/brain/awab185; RA Sferra A., Fortugno P., Motta M., Aiello C., Petrini S., Ciolfi A., RA Cipressa F., Moroni I., Leuzzi V., Pieroni L., Marini F., RA Boespflug Tanguy O., Eymard-Pierre E., Danti F.R., Compagnucci C., RA Zambruno G., Brusco A., Santorelli F.M., Chiapparini L., Francalanci P., RA Loizzo A.L., Tartaglia M., Cestra G., Bertini E.; RT "Biallelic mutations in RNF220 cause laminopathies featuring RT leukodystrophy, ataxia and deafness."; RL Brain 144:3020-3035(2021). CC -!- FUNCTION: E3 ubiquitin-protein ligase that promotes the ubiquitination CC and proteasomal degradation of SIN3B (By similarity). Independently of CC its E3 ligase activity, acts as a CTNNB1 stabilizer through USP7- CC mediated deubiquitination of CTNNB1 promoting Wnt signaling CC (PubMed:25266658, PubMed:33964137). Plays a critical role in the CC regulation of nuclear lamina (PubMed:33964137). CC {ECO:0000250|UniProtKB:Q6PDX6, ECO:0000269|PubMed:25266658, CC ECO:0000269|PubMed:33964137}. 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 with SIN3B (By similarity). Interacts with CTNNB1 CC (via Armadillo repeats 2-8) (PubMed:25266658, PubMed:33964137). CC Interacts with USP7 (via MATH domain) (PubMed:25266658). CC {ECO:0000250|UniProtKB:Q6PDX6, ECO:0000269|PubMed:25266658, CC ECO:0000269|PubMed:33964137}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:33964137}. Nucleus CC {ECO:0000269|PubMed:33964137}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q5VTB9-1; Sequence=Displayed; CC Name=2; CC IsoId=Q5VTB9-3; Sequence=VSP_055437, VSP_055438; CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Abundant in brain and CC spinal cord, particularly in the cerebellum and cerebral cortex. In CC fetal tissues expressed in the cerebellum, spinal cord and cortex. CC {ECO:0000269|PubMed:33964137}. CC -!- PTM: Auto-ubiquitinated; leads to proteasomal degradation. CC {ECO:0000250}. CC -!- DISEASE: Leukodystrophy, hypomyelinating, 23, with ataxia, deafness, CC liver dysfunction, and dilated cardiomyopathy (HLD23) [MIM:619688]: An CC autosomal recessive neurodegenerative disorder with systemic CC manifestations. Affected individuals show delayed motor development and CC ataxic gait in early childhood that progresses to spastic paraplegia CC with loss of ambulation in the first decades of life. Additional CC features include progressive sensorineural hearing loss, hepatic CC dysfunction, and dilated cardiomyopathy. Death occurs in the first or CC second decades. Brain imaging shows hypomyelination, diffuse white CC matter abnormalities, and thin corpus callosum. CC {ECO:0000269|PubMed:33964137}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SEQUENCE CAUTION: CC Sequence=BAA91704.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={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; AK001459; BAA91704.1; ALT_INIT; mRNA. DR EMBL; AK056424; BAG51705.1; -; mRNA. DR EMBL; AK297228; BAG59711.1; -; mRNA. DR EMBL; AL122004; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL359373; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL596225; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC034221; AAH34221.1; -; mRNA. DR EMBL; BC098266; AAH98266.1; -; mRNA. DR EMBL; BC098300; AAH98300.1; -; mRNA. DR CCDS; CCDS510.1; -. [Q5VTB9-1] DR RefSeq; NP_001306885.1; NM_001319956.1. [Q5VTB9-1] DR RefSeq; NP_001306886.1; NM_001319957.1. [Q5VTB9-3] DR RefSeq; NP_060620.2; NM_018150.3. [Q5VTB9-1] DR RefSeq; XP_016857112.1; XM_017001623.1. DR RefSeq; XP_016857113.1; XM_017001624.1. DR RefSeq; XP_016857114.1; XM_017001625.1. [Q5VTB9-1] DR AlphaFoldDB; Q5VTB9; -. DR BioGRID; 120481; 42. DR IntAct; Q5VTB9; 13. DR MINT; Q5VTB9; -. DR STRING; 9606.ENSP00000347548; -. DR GlyCosmos; Q5VTB9; 1 site, 1 glycan. DR GlyGen; Q5VTB9; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q5VTB9; -. DR PhosphoSitePlus; Q5VTB9; -. DR BioMuta; RNF220; -. DR DMDM; 74756788; -. DR EPD; Q5VTB9; -. DR jPOST; Q5VTB9; -. DR MassIVE; Q5VTB9; -. DR MaxQB; Q5VTB9; -. DR PaxDb; 9606-ENSP00000347548; -. DR PeptideAtlas; Q5VTB9; -. DR ProteomicsDB; 4573; -. DR ProteomicsDB; 65319; -. [Q5VTB9-1] DR Pumba; Q5VTB9; -. DR Antibodypedia; 32475; 68 antibodies from 15 providers. DR DNASU; 55182; -. DR Ensembl; ENST00000355387.6; ENSP00000347548.2; ENSG00000187147.19. [Q5VTB9-1] DR Ensembl; ENST00000361799.7; ENSP00000354872.2; ENSG00000187147.19. [Q5VTB9-1] DR GeneID; 55182; -. DR KEGG; hsa:55182; -. DR MANE-Select; ENST00000361799.7; ENSP00000354872.2; NM_018150.4; NP_060620.2. DR UCSC; uc001clv.2; human. [Q5VTB9-1] DR AGR; HGNC:25552; -. DR CTD; 55182; -. DR DisGeNET; 55182; -. DR GeneCards; RNF220; -. DR HGNC; HGNC:25552; RNF220. DR HPA; ENSG00000187147; Group enriched (brain, skeletal muscle). DR MalaCards; RNF220; -. DR MIM; 616136; gene. DR MIM; 619688; phenotype. DR neXtProt; NX_Q5VTB9; -. DR OpenTargets; ENSG00000187147; -. DR PharmGKB; PA162401886; -. DR VEuPathDB; HostDB:ENSG00000187147; -. DR eggNOG; ENOG502QR1N; Eukaryota. DR GeneTree; ENSGT00390000016573; -. DR HOGENOM; CLU_035321_0_0_1; -. DR InParanoid; Q5VTB9; -. DR OMA; PTCDAKI; -. DR OrthoDB; 12276at2759; -. DR PhylomeDB; Q5VTB9; -. DR TreeFam; TF324716; -. DR PathwayCommons; Q5VTB9; -. DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation. DR SignaLink; Q5VTB9; -. DR SIGNOR; Q5VTB9; -. DR UniPathway; UPA00143; -. DR BioGRID-ORCS; 55182; 17 hits in 1197 CRISPR screens. DR ChiTaRS; RNF220; human. DR GeneWiki; RNF220; -. DR GenomeRNAi; 55182; -. DR Pharos; Q5VTB9; Tbio. DR PRO; PR:Q5VTB9; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q5VTB9; Protein. DR Bgee; ENSG00000187147; Expressed in C1 segment of cervical spinal cord and 206 other cell types or tissues. DR ExpressionAtlas; Q5VTB9; baseline and differential. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0005652; C:nuclear lamina; IMP:UniProtKB. DR GO; GO:0005634; C:nucleus; IMP:UniProtKB. DR GO; GO:0032991; C:protein-containing complex; IDA:GO_Central. DR GO; GO:0008013; F:beta-catenin binding; IMP:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. 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:0021904; P:dorsal/ventral neural tube patterning; IEA:Ensembl. DR GO; GO:0003358; P:noradrenergic neuron development; IEA:Ensembl. DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IMP:UniProtKB. DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IGI:MGI. DR GO; GO:0051865; P:protein autoubiquitination; ISS:UniProtKB. DR GO; GO:0006513; P:protein monoubiquitination; IGI:MGI. DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB. DR GO; GO:2000677; P:regulation of transcription regulatory region DNA binding; IGI:MGI. DR CDD; cd16563; RING-HC_RNF220; 1. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1. DR InterPro; IPR031824; RNF220_mid. DR InterPro; IPR040178; RNF220_RING. DR InterPro; IPR001841; Znf_RING. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR PANTHER; PTHR13459:SF3; E3 UBIQUITIN-PROTEIN LIGASE RNF220; 1. DR PANTHER; PTHR13459; UNCHARACTERIZED; 1. DR Pfam; PF15926; RNF220; 2. DR Pfam; PF13923; zf-C3HC4_2; 1. DR SUPFAM; SSF57850; RING/U-box; 1. DR PROSITE; PS50089; ZF_RING_2; 1. DR Genevisible; Q5VTB9; HS. PE 1: Evidence at protein level; KW Alternative splicing; Cardiomyopathy; Coiled coil; Cytoplasm; Deafness; KW Disease variant; Isopeptide bond; Leukodystrophy; Metal-binding; Nucleus; KW Phosphoprotein; Reference proteome; Transferase; Ubl conjugation; KW Ubl conjugation pathway; Zinc; Zinc-finger. FT CHAIN 1..566 FT /note="E3 ubiquitin-protein ligase RNF220" FT /id="PRO_0000277657" FT ZN_FING 514..553 FT /note="RING-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175" FT REGION 277..297 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 514..522 FT /note="Required for targeting to the cytoplasm" FT /evidence="ECO:0000250" FT COILED 485..513 FT /evidence="ECO:0000255" FT MOD_RES 390 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT CROSSLNK 277 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447" FT VAR_SEQ 1..239 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_055437" FT VAR_SEQ 331 FT /note="Q -> QVCPLCNRPLAGSEQEMSRHVEHCLSK (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_055438" FT VARIANT 363 FT /note="R -> Q (in HLD23; shows decreased beta-catenin FT binding)" FT /evidence="ECO:0000269|PubMed:33964137" FT /id="VAR_086785" FT VARIANT 365 FT /note="R -> Q (in HLD23; shows decreased beta-catenin FT binding)" FT /evidence="ECO:0000269|PubMed:33964137" FT /id="VAR_086786" FT CONFLICT 84 FT /note="A -> V (in Ref. 3; AAH98300)" FT /evidence="ECO:0000305" FT CONFLICT 277 FT /note="K -> E (in Ref. 1; BAG51705)" FT /evidence="ECO:0000305" SQ SEQUENCE 566 AA; 62765 MW; AAE3C723032B062B CRC64; MDLHRAAFKM ENSSYLPNPL ASPALMVLAS TAEASRDASI PCQQPRPFGV PVSVDKDVHI PFTNGSYTFA SMYHRQGGVP GTFANRDFPP SLLHLHPQFA PPNLDCTPIS MLNHSGVGAF RPFASTEDRE SYQSAFTPAK RLKNCHDTES PHLRFSDADG KEYDFGTQLP SSSPGSLKVD DTGKKIFAVS GLISDREASS SPEDRNDRCK KKAAALFDSQ APICPICQVL LRPSELQEHM EQELEQLAQL PSSKNSLLKD AMAPGTPKSL LLSASIKREG ESPTASPHSS ATDDLHHSDR YQTFLRVRAN RQTRLNARIG KMKRRKQDEG QREGSCMAED DAVDIEHENN NRFEEYEWCG QKRIRATTLL EGGFRGSGFI MCSGKENPDS DADLDVDGDD TLEYGKPQYT EADVIPCTGE EPGEAKEREA LRGAVLNGGP PSTRITPEFS KWASDEMPST SNGESSKQEA MQKTCKNSDI EKITEDSAVT TFEALKARVR ELERQLSRGD RYKCLICMDS YSMPLTSIQC WHVHCEECWL RTLGAKKLCP QCNTITAPGD LRRIYL //