ID AT7L3_HUMAN Reviewed; 347 AA. AC Q14CW9; Q8IY68; Q96N40; Q9NPU5; DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot. DT 22-AUG-2006, sequence version 1. DT 27-MAR-2024, entry version 136. DE RecName: Full=Ataxin-7-like protein 3 {ECO:0000255|HAMAP-Rule:MF_03047}; DE AltName: Full=SAGA-associated factor 11 homolog {ECO:0000255|HAMAP-Rule:MF_03047}; GN Name=ATXN7L3 {ECO:0000255|HAMAP-Rule:MF_03047}; 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] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 5-347 (ISOFORM 2). RC TISSUE=Lymph; 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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 123-347 (ISOFORM 1). RC TISSUE=Teratocarcinoma; 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] OF 161-347. RC TISSUE=Amygdala; 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 FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SAGA RP COMPLEX, INTERACTION WITH ENY2 AND USP22, AND DOMAIN. RX PubMed=18206972; DOI=10.1016/j.molcel.2007.12.011; RA Zhao Y., Lang G., Ito S., Bonnet J., Metzger E., Sawatsubashi S., RA Suzuki E., Le Guezennec X., Stunnenberg H.G., Krasnov A., Georgieva S.G., RA Schuele R., Takeyama K., Kato S., Tora L., Devys D.; RT "A TFTC/STAGA module mediates histone H2A and H2B deubiquitination, RT coactivates nuclear receptors, and counteracts heterochromatin silencing."; RL Mol. Cell 29:92-101(2008). RN [5] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-281, 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 [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-278 AND SER-281, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-281 AND SER-326, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [9] RP FUNCTION, AND IDENTIFICATION IN THE SAGA COMPLEX. RX PubMed=21746879; DOI=10.1128/mcb.05231-11; RA Lang G., Bonnet J., Umlauf D., Karmodiya K., Koffler J., Stierle M., RA Devys D., Tora L.; RT "The tightly controlled deubiquitination activity of the human SAGA complex RT differentially modifies distinct gene regulatory elements."; RL Mol. Cell. Biol. 31:3734-3744(2011). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129; SER-131 AND SER-281, AND RP IDENTIFICATION BY MASS SPECTROMETRY [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 [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131; SER-281 AND SER-326, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-281, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [13] RP FUNCTION, IDENTIFICATION IN THE SAGA COMPLEX, INTERACTION WITH ENY2 AND RP USP22, AND SUBCELLULAR LOCATION. RX PubMed=27601583; DOI=10.1128/mcb.00193-16; RA Li W., Atanassov B.S., Lan X., Mohan R.D., Swanson S.K., Farria A.T., RA Florens L., Washburn M.P., Workman J.L., Dent S.Y.; RT "Cytoplasmic ATXN7L3B interferes with nuclear functions of the SAGA RT deubiquitinase module."; RL Mol. Cell. Biol. 36:2855-2866(2016). RN [14] RP STRUCTURE BY NMR OF 197-276 IN COMPLEX WITH ZINC. RX PubMed=20634802; DOI=10.1038/embor.2010.98; RA Bonnet J., Wang Y.H., Spedale G., Atkinson R.A., Romier C., Hamiche A., RA Pijnappel W.W., Timmers H.T., Tora L., Devys D., Kieffer B.; RT "The structural plasticity of SCA7 domains defines their differential RT nucleosome-binding properties."; RL EMBO Rep. 11:612-618(2010). CC -!- FUNCTION: Component of the transcription regulatory histone acetylation CC (HAT) complex SAGA, a multiprotein complex that activates transcription CC by remodeling chromatin and mediating histone acetylation and CC deubiquitination. Within the SAGA complex, participates in a subcomplex CC that specifically deubiquitinates both histones H2A and H2B CC (PubMed:18206972, PubMed:21746879). The SAGA complex is recruited to CC specific gene promoters by activators such as MYC, where it is required CC for transcription. Required for nuclear receptor-mediated CC transactivation. Within the complex, it is required to recruit USP22 CC and ENY2 into the SAGA complex (PubMed:18206972). Regulates H2B CC monoubiquitination (H2Bub1) levels. Affects subcellular distribution of CC ENY2, USP22 and ATXN7L3B (PubMed:27601583). {ECO:0000255|HAMAP- CC Rule:MF_03047, ECO:0000269|PubMed:18206972, CC ECO:0000269|PubMed:21746879, ECO:0000269|PubMed:27601583}. CC -!- SUBUNIT: Component of some SAGA transcription coactivator-HAT CC complexes, at least composed of ATXN7, ATXN7L3, ENY2, GCN5L2, SUPT3H, CC TAF10, TRRAP and USP22. Within the SAGA complex, ENY2, ATXN7, ATXN7L3, CC and USP22 form an additional subcomplex of SAGA called the DUB module CC (deubiquitination module) (PubMed:18206972, PubMed:21746879, CC PubMed:27601583). Interacts directly with ENY2 and USP22 CC (PubMed:18206972). {ECO:0000255|HAMAP-Rule:MF_03047, CC ECO:0000269|PubMed:18206972, ECO:0000269|PubMed:21746879, CC ECO:0000269|PubMed:27601583}. CC -!- INTERACTION: CC Q14CW9; Q9NPA8: ENY2; NbExp=6; IntAct=EBI-949215, EBI-719226; CC Q14CW9; Q9UPT9-2: USP22; NbExp=3; IntAct=EBI-949215, EBI-12074414; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03047, CC ECO:0000269|PubMed:27601583}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q14CW9-1; Sequence=Displayed; CC Name=2; CC IsoId=Q14CW9-2; Sequence=VSP_036721; CC -!- DOMAIN: The long N-terminal helix forms part of the 'assembly lobe' of CC the SAGA deubiquitination module. {ECO:0000255|HAMAP-Rule:MF_03047, CC ECO:0000269|PubMed:18206972}. CC -!- DOMAIN: The C-terminal SGF11-type zinc-finger domain together with the CC C-terminal catalytic domain of USP22 forms the 'catalytic lobe' of the CC SAGA deubiquitination module. {ECO:0000255|HAMAP-Rule:MF_03047}. CC -!- SIMILARITY: Belongs to the SGF11 family. {ECO:0000255|HAMAP- CC Rule:MF_03047}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH37418.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=BAB71070.1; Type=Erroneous initiation; 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; BC037418; AAH37418.1; ALT_INIT; mRNA. DR EMBL; BC113595; AAI13596.1; -; mRNA. DR EMBL; BC126113; AAI26114.1; -; mRNA. DR EMBL; AK056002; BAB71070.1; ALT_INIT; mRNA. DR EMBL; AL390158; CAB99093.1; -; mRNA. DR CCDS; CCDS42345.1; -. [Q14CW9-1] DR CCDS; CCDS45697.1; -. [Q14CW9-2] DR RefSeq; NP_001092303.1; NM_001098833.1. DR RefSeq; NP_064603.1; NM_020218.1. DR RefSeq; XP_016880374.1; XM_017024885.1. DR RefSeq; XP_016880375.1; XM_017024886.1. DR PDB; 2KKT; NMR; -; A=197-276. DR PDBsum; 2KKT; -. DR AlphaFoldDB; Q14CW9; -. DR BMRB; Q14CW9; -. DR SMR; Q14CW9; -. DR BioGRID; 121289; 51. DR ComplexPortal; CPX-6802; SAGA complex, KAT2B variant. DR ComplexPortal; CPX-900; SAGA complex, KAT2A variant. DR ComplexPortal; CPX-903; TFTC histone acetylation complex. DR CORUM; Q14CW9; -. DR IntAct; Q14CW9; 37. DR MINT; Q14CW9; -. DR STRING; 9606.ENSP00000397259; -. DR iPTMnet; Q14CW9; -. DR PhosphoSitePlus; Q14CW9; -. DR BioMuta; ATXN7L3; -. DR DMDM; 121948758; -. DR EPD; Q14CW9; -. DR jPOST; Q14CW9; -. DR MassIVE; Q14CW9; -. DR MaxQB; Q14CW9; -. DR PaxDb; 9606-ENSP00000397259; -. DR PeptideAtlas; Q14CW9; -. DR ProteomicsDB; 60332; -. [Q14CW9-1] DR ProteomicsDB; 60333; -. [Q14CW9-2] DR Pumba; Q14CW9; -. DR Antibodypedia; 54391; 99 antibodies from 24 providers. DR DNASU; 56970; -. DR Ensembl; ENST00000389384.8; ENSP00000374035.3; ENSG00000087152.16. [Q14CW9-1] DR Ensembl; ENST00000454077.6; ENSP00000397259.1; ENSG00000087152.16. [Q14CW9-2] DR Ensembl; ENST00000587097.6; ENSP00000465614.2; ENSG00000087152.16. [Q14CW9-1] DR MANE-Select; ENST00000587097.6; ENSP00000465614.2; NM_001382309.1; NP_001369238.1. DR UCSC; uc002ifz.4; human. [Q14CW9-1] DR AGR; HGNC:25416; -. DR DisGeNET; 56970; -. DR GeneCards; ATXN7L3; -. DR HGNC; HGNC:25416; ATXN7L3. DR HPA; ENSG00000087152; Low tissue specificity. DR MIM; 619010; gene. DR neXtProt; NX_Q14CW9; -. DR OpenTargets; ENSG00000087152; -. DR PharmGKB; PA134991793; -. DR VEuPathDB; HostDB:ENSG00000087152; -. DR eggNOG; KOG2612; Eukaryota. DR GeneTree; ENSGT00940000158253; -. DR InParanoid; Q14CW9; -. DR OMA; PSNYENM; -. DR OrthoDB; 5404108at2759; -. DR PhylomeDB; Q14CW9; -. DR TreeFam; TF324580; -. DR PathwayCommons; Q14CW9; -. DR Reactome; R-HSA-3214847; HATs acetylate histones. DR SignaLink; Q14CW9; -. DR SIGNOR; Q14CW9; -. DR BioGRID-ORCS; 56970; 242 hits in 1173 CRISPR screens. DR ChiTaRS; ATXN7L3; human. DR EvolutionaryTrace; Q14CW9; -. DR GenomeRNAi; 56970; -. DR Pharos; Q14CW9; Tbio. DR PRO; PR:Q14CW9; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; Q14CW9; Protein. DR Bgee; ENSG00000087152; Expressed in prefrontal cortex and 178 other cell types or tissues. DR ExpressionAtlas; Q14CW9; baseline and differential. DR GO; GO:0071819; C:DUBm complex; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0000124; C:SAGA complex; IDA:UniProtKB. DR GO; GO:0033276; C:transcription factor TFTC complex; NAS:ComplexPortal. DR GO; GO:0030374; F:nuclear receptor coactivator activity; IDA:UniProtKB. DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW. DR GO; GO:0016578; P:histone deubiquitination; IBA:GO_Central. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:0006282; P:regulation of DNA repair; NAS:ComplexPortal. DR GO; GO:0043484; P:regulation of RNA splicing; NAS:ComplexPortal. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:ComplexPortal. DR Gene3D; 6.10.140.1270; -; 1. DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1. DR HAMAP; MF_03047; Sgf11; 1. DR InterPro; IPR013246; SAGA_su_Sgf11. DR InterPro; IPR013243; SCA7_dom. DR PANTHER; PTHR46367; ATAXIN-7-LIKE PROTEIN 3; 1. DR PANTHER; PTHR46367:SF1; ATAXIN-7-LIKE PROTEIN 3; 1. DR Pfam; PF08313; SCA7; 1. DR Pfam; PF08209; Sgf11; 1. DR PROSITE; PS51505; SCA7; 1. DR Genevisible; Q14CW9; HS. PE 1: Evidence at protein level; KW 3D-structure; Activator; Alternative splicing; Chromatin regulator; KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Transcription; KW Transcription regulation; Zinc; Zinc-finger. FT CHAIN 1..347 FT /note="Ataxin-7-like protein 3" FT /id="PRO_0000278301" FT DOMAIN 196..263 FT /note="SCA7" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03047" FT ZN_FING 84..105 FT /note="SGF11-type" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03047" FT REGION 116..184 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 275..347 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 143..178 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 275..303 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 129 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 131 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 278 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 281 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 326 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT VAR_SEQ 159 FT /note="K -> KLWYLPFQ (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_036721" FT HELIX 199..204 FT /evidence="ECO:0007829|PDB:2KKT" FT TURN 205..207 FT /evidence="ECO:0007829|PDB:2KKT" FT TURN 214..217 FT /evidence="ECO:0007829|PDB:2KKT" FT STRAND 226..228 FT /evidence="ECO:0007829|PDB:2KKT" FT HELIX 231..241 FT /evidence="ECO:0007829|PDB:2KKT" SQ SEQUENCE 347 AA; 38651 MW; 742D85BFF4ADD0C0 CRC64; MKMEEMSLSG LDNSKLEAIA QEIYADLVED SCLGFCFEVH RAVKCGYFFL DDTDPDSMKD FEIVDQPGLD IFGQVFNQWK SKECVCPNCS RSIAASRFAP HLEKCLGMGR NSSRIANRRI ANSNNMNKSE SDQEDNDDIN DNDWSYGSEK KAKKRKSDKN PNSPRRSKSL KHKNGELSNS DPFKYNNSTG ISYETLGPEE LRSLLTTQCG VISEHTKKMC TRSLRCPQHT DEQRRTVRIY FLGPSAVLPE VESSLDNDSF DMTDSQALIS RLQWDGSSDL SPSDSGSSKT SENQGWGLGT NSSESRKTKK KKSHLSLVGT ASGLGSNKKK KPKPPAPPTP SIYDDIN //