ID CNO10_HUMAN Reviewed; 744 AA. AC Q9H9A5; B7Z7L1; F8WAF2; Q9BU30; Q9H5J7; Q9H8X1; Q9H9W0; Q9HAH3; Q9UFJ2; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 23-FEB-2022, entry version 179. DE RecName: Full=CCR4-NOT transcription complex subunit 10; GN Name=CNOT10; 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; 2; 5 AND 6), NUCLEOTIDE RP SEQUENCE [LARGE SCALE MRNA] OF 85-744 (ISOFORM 4), AND VARIANT SER-348. RC TISSUE=Embryo, 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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16641997; DOI=10.1038/nature04728; RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.; RT "The DNA sequence, annotation and analysis of human chromosome 3."; RL Nature 440:1194-1198(2006). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT RP SER-736. RC TISSUE=Skin; 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 482-744 (ISOFORM 1). RC TISSUE=Testis; 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 [6] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [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 [7] RP IDENTIFICATION IN THE CCR4-NOT COMPLEX, AND COMPOSITION OF THE CCR4-NOT RP COMPLEX. RX PubMed=19558367; DOI=10.1042/bj20090500; RA Lau N.C., Kolkman A., van Schaik F.M., Mulder K.W., Pijnappel W.W., RA Heck A.J., Timmers H.T.; RT "Human Ccr4-Not complexes contain variable deadenylase subunits."; RL Biochem. J. 422:443-453(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 IDENTIFICATION IN THE CCR4-NOT COMPLEX. RX PubMed=23232451; DOI=10.4161/rna.23065; RA Mauxion F., Preve B., Seraphin B.; RT "C2ORF29/CNOT11 and CNOT10 form a new module of the CCR4-NOT complex."; RL RNA Biol. 10:267-276(2013). RN [10] RP FUNCTION. RX PubMed=23221646; DOI=10.1093/nar/gks1133; RA Farber V., Erben E., Sharma S., Stoecklin G., Clayton C.; RT "Trypanosome CNOT10 is essential for the integrity of the NOT deadenylase RT complex and for degradation of many mRNAs."; RL Nucleic Acids Res. 41:1211-1222(2013). RN [11] RP INTERACTION WITH CNOT11. RX PubMed=23303381; DOI=10.4161/rna.23018; RA Bawankar P., Loh B., Wohlbold L., Schmidt S., Izaurralde E.; RT "NOT10 and C2orf29/NOT11 form a conserved module of the CCR4-NOT complex RT that docks onto the NOT1 N-terminal domain."; RL RNA Biol. 10:228-244(2013). RN [12] RP IDENTIFICATION BY 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). CC -!- FUNCTION: Component of the CCR4-NOT complex which is one of the major CC cellular mRNA deadenylases and is linked to various cellular processes CC including bulk mRNA degradation, miRNA-mediated repression, CC translational repression during translational initiation and general CC transcription regulation. Additional complex functions may be a CC consequence of its influence on mRNA expression. Is not required for CC association of CNOT7 to the CCR4-NOT complex. CC {ECO:0000269|PubMed:23221646}. CC -!- SUBUNIT: Component of the CCR4-NOT complex; distinct complexes seem to CC exist that differ in the participation of probably mutually exclusive CC catalytic subunits. CNOT10 and CNOT11 form a subcomplex docked to the CC CNOT1 scaffold. {ECO:0000269|PubMed:19558367, CC ECO:0000269|PubMed:23232451}. CC -!- INTERACTION: CC Q9H9A5; Q9UKZ1: CNOT11; NbExp=4; IntAct=EBI-1054261, EBI-2562014; CC Q9H9A5; P42858: HTT; NbExp=4; IntAct=EBI-1054261, EBI-466029; CC Q9H9A5; Q9HCJ0: TNRC6C; NbExp=10; IntAct=EBI-1054261, EBI-6507625; CC Q9H9A5-3; P42858: HTT; NbExp=3; IntAct=EBI-25957177, EBI-466029; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000305}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=6; CC Name=1; CC IsoId=Q9H9A5-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9H9A5-2; Sequence=VSP_030312; CC Name=3; CC IsoId=Q9H9A5-3; Sequence=VSP_030313; CC Name=4; CC IsoId=Q9H9A5-4; Sequence=VSP_030313, VSP_030314; CC Name=5; CC IsoId=Q9H9A5-5; Sequence=VSP_030311; CC Name=6; CC IsoId=Q9H9A5-6; Sequence=VSP_045557; CC -!- SIMILARITY: Belongs to the CNOT10 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAB13876.1; 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; AK021695; BAB13876.1; ALT_INIT; mRNA. DR EMBL; AK022576; BAB14108.1; -; mRNA. DR EMBL; AK022952; BAB14327.1; -; mRNA. DR EMBL; AK023227; BAB14478.1; -; mRNA. DR EMBL; AK027026; BAB15629.1; -; mRNA. DR EMBL; AK302196; BAH13647.1; -; mRNA. DR EMBL; AC138972; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC139452; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471055; EAW64435.1; -; Genomic_DNA. DR EMBL; BC002928; AAH02928.1; -; mRNA. DR EMBL; BC002931; AAH02931.1; -; mRNA. DR EMBL; AL117639; CAB56027.2; -; mRNA. DR CCDS; CCDS2655.1; -. [Q9H9A5-1] DR CCDS; CCDS58821.1; -. [Q9H9A5-3] DR CCDS; CCDS58822.1; -. [Q9H9A5-6] DR RefSeq; NP_001243670.1; NM_001256741.1. [Q9H9A5-3] DR RefSeq; NP_001243671.1; NM_001256742.1. [Q9H9A5-6] DR RefSeq; NP_056257.1; NM_015442.2. [Q9H9A5-1] DR BioGRID; 117411; 119. DR ComplexPortal; CPX-2522; CCR4-NOT mRNA deadenylase complex, CNOT6L-CNOT7 variant. DR ComplexPortal; CPX-2535; CCR4-NOT mRNA deadenylase complex, CNOT6L-CNOT8 variant. DR ComplexPortal; CPX-2849; CCR4-NOT mRNA deadenylase complex, CNOT6-CNOT8 variant. DR ComplexPortal; CPX-707; CCR4-NOT mRNA deadenylase complex, CNOT6-CNOT7 variant. DR CORUM; Q9H9A5; -. DR DIP; DIP-46839N; -. DR IntAct; Q9H9A5; 42. DR MINT; Q9H9A5; -. DR STRING; 9606.ENSP00000399862; -. DR ChEMBL; CHEMBL4105878; -. DR GlyGen; Q9H9A5; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9H9A5; -. DR PhosphoSitePlus; Q9H9A5; -. DR BioMuta; CNOT10; -. DR DMDM; 74733982; -. DR EPD; Q9H9A5; -. DR jPOST; Q9H9A5; -. DR MassIVE; Q9H9A5; -. DR MaxQB; Q9H9A5; -. DR PaxDb; Q9H9A5; -. DR PeptideAtlas; Q9H9A5; -. DR PRIDE; Q9H9A5; -. DR ProteomicsDB; 30485; -. DR ProteomicsDB; 81300; -. [Q9H9A5-1] DR ProteomicsDB; 81301; -. [Q9H9A5-2] DR ProteomicsDB; 81302; -. [Q9H9A5-3] DR ProteomicsDB; 81303; -. [Q9H9A5-4] DR ProteomicsDB; 81304; -. [Q9H9A5-5] DR Antibodypedia; 27780; 84 antibodies from 22 providers. DR DNASU; 25904; -. DR Ensembl; ENST00000328834; ENSP00000330060; ENSG00000182973. DR Ensembl; ENST00000331889; ENSP00000329376; ENSG00000182973. [Q9H9A5-3] DR Ensembl; ENST00000454516; ENSP00000399862; ENSG00000182973. [Q9H9A5-6] DR GeneID; 25904; -. DR KEGG; hsa:25904; -. DR MANE-Select; ENST00000328834.10; ENSP00000330060.5; NM_015442.3; NP_056257.1. DR UCSC; uc003cfc.2; human. [Q9H9A5-1] DR CTD; 25904; -. DR GeneCards; CNOT10; -. DR HGNC; HGNC:23817; CNOT10. DR HPA; ENSG00000182973; Low tissue specificity. DR neXtProt; NX_Q9H9A5; -. DR PharmGKB; PA134862503; -. DR VEuPathDB; HostDB:ENSG00000182973; -. DR eggNOG; KOG2471; Eukaryota. DR GeneTree; ENSGT00390000001827; -. DR HOGENOM; CLU_013100_0_0_1; -. DR InParanoid; Q9H9A5; -. DR OMA; WRHLVIN; -. DR OrthoDB; 249353at2759; -. DR PhylomeDB; Q9H9A5; -. DR TreeFam; TF323368; -. DR PathwayCommons; Q9H9A5; -. DR Reactome; R-HSA-429947; Deadenylation of mRNA. DR Reactome; R-HSA-6804115; TP53 regulates transcription of additional cell cycle genes whose exact role in the p53 pathway remain uncertain. DR SignaLink; Q9H9A5; -. DR BioGRID-ORCS; 25904; 38 hits in 1058 CRISPR screens. DR ChiTaRS; CNOT10; human. DR GenomeRNAi; 25904; -. DR Pharos; Q9H9A5; Tdark. DR PRO; PR:Q9H9A5; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; Q9H9A5; protein. DR Bgee; ENSG00000182973; Expressed in testis and 164 other tissues. DR ExpressionAtlas; Q9H9A5; baseline and differential. DR Genevisible; Q9H9A5; HS. DR GO; GO:0030014; C:CCR4-NOT complex; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW. DR GO; GO:0006402; P:mRNA catabolic process; IBA:GO_Central. DR GO; GO:0017148; P:negative regulation of translation; IBA:GO_Central. DR Gene3D; 1.25.40.10; -; 2. DR InterPro; IPR039740; CNOT10. DR InterPro; IPR011990; TPR-like_helical_dom_sf. DR InterPro; IPR019734; TPR_repeat. DR PANTHER; PTHR12979; PTHR12979; 1. DR SMART; SM00028; TPR; 4. DR SUPFAM; SSF48452; SSF48452; 3. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Coiled coil; Cytoplasm; Nucleus; KW Reference proteome; RNA-mediated gene silencing; Transcription; KW Transcription regulation; Translation regulation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:19413330" FT CHAIN 2..744 FT /note="CCR4-NOT transcription complex subunit 10" FT /id="PRO_0000314579" FT REGION 1..25 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 183..204 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 477..521 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 602..634 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 74..107 FT /evidence="ECO:0000255" FT COMPBIAS 183..203 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 482..502 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0007744|PubMed:19413330" FT VAR_SEQ 1..293 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_030311" FT VAR_SEQ 1..7 FT /note="MAADKPA -> MKSIGVKTVKVCGSKSSVRIEGQPCSLGQSRRKVKLMGERS FT YTLSIGNGDYFWANKEMLWDYVQTLS (in isoform 6)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_045557" FT VAR_SEQ 144 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_030312" FT VAR_SEQ 505..532 FT /note="SSKSHDGDKFIPAPPSSPLRKQELENLK -> R (in isoform 3 and FT isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334" FT /id="VSP_030313" FT VAR_SEQ 556..577 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_030314" FT VARIANT 348 FT /note="T -> S (in dbSNP:rs11558687)" FT /evidence="ECO:0000269|PubMed:14702039" FT /id="VAR_053982" FT VARIANT 736 FT /note="P -> S (in dbSNP:rs17849684)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_037957" FT CONFLICT 5 FT /note="K -> R (in Ref. 1; BAB14108)" FT /evidence="ECO:0000305" FT CONFLICT 52 FT /note="C -> R (in Ref. 1; BAB14478)" FT /evidence="ECO:0000305" FT CONFLICT 270 FT /note="V -> M (in Ref. 1; BAB13876)" FT /evidence="ECO:0000305" FT CONFLICT 478 FT /note="D -> G (in Ref. 1; BAB14108)" FT /evidence="ECO:0000305" FT CONFLICT 509 FT /note="H -> Y (in Ref. 1; BAB14108)" FT /evidence="ECO:0000305" FT CONFLICT 518 FT /note="P -> L (in Ref. 1; BAH13647)" FT /evidence="ECO:0000305" FT CONFLICT 622 FT /note="A -> T (in Ref. 1; BAB14478)" FT /evidence="ECO:0000305" SQ SEQUENCE 744 AA; 82310 MW; BA1984B71F0A1E7A CRC64; MAADKPADQG AEKHEGTGQS SGITDQEKEL STNAFQAFTS GNYDACLQHL ACLQDINKDD YKIILNTAVA EFFKSNQTTT DNLRQTLNQL KNQVHSAVEE MDGLDDVENS MLYYNQAVIL YHLRQYTEAI SVGEKLYQFI EPFEEKFAQA VCFLLVDLYI LTYQAEKALH LLAVLEKMIS QGNNNKNGKN ETGNNNNKDG SNHKAESGAL IEAAKSKIHQ YKVRAYIQMK SLKACKREIK SVMNTAGNSA PSLFLKSNFE YLRGNYRKAV KLLNSSNIAE HPGFMKTGEC LRCMFWNNLG CIHFAMSKHN LGIFYFKKAL QENDNVCAQL SAGSTDPGKK FSGRPMCTLL TNKRYELLYN CGIQLLHIGR PLAAFECLIE AVQVYHANPR LWLRLAECCI AANKGTSEQE TKGLPSKKGI VQSIVGQGYH RKIVLASQSI QNTVYNDGQS SAIPVASMEF AAICLRNALL LLPEEQQDPK QENGAKNSNQ LGGNTESSES SETCSSKSHD GDKFIPAPPS SPLRKQELEN LKCSILACSA YVALALGDNL MALNHADKLL QQPKLSGSLK FLGHLYAAEA LISLDRISDA ITHLNPENVT DVSLGISSNE QDQGSDKGEN EAMESSGKRA PQCYPSSVNS ARTVMLFNLG SAYCLRSEYD KARKCLHQAA SMIHPKEVPP EAILLAVYLE LQNGNTQLAL QIIKRNQLLP AVKTHSEVRK KPVFQPVHPI QPIQMPAFTT VQRK //