ID KCTD9_HUMAN Reviewed; 389 AA. AC Q7L273; Q6NUM8; Q9NXV4; DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 27-MAR-2024, entry version 157. DE RecName: Full=BTB/POZ domain-containing protein KCTD9; GN Name=KCTD9; 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]. RC TISSUE=Testis, and Uterus; 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 151-389. RC TISSUE=Colon; 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=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 [4] RP X-RAY CRYSTALLOGRAPHY (2.76 ANGSTROMS) OF 89-191, PENTAMERIZATION, RP INTERACTION WITH CUL3, AND MUTAGENESIS OF VAL-125. RX PubMed=26334369; DOI=10.1016/j.jmb.2015.08.019; RA Ji A.X., Chu A., Nielsen T.K., Benlekbir S., Rubinstein J.L., Prive G.G.; RT "Structural insights into KCTD protein assembly and CULLIN3 recognition."; RL J. Mol. Biol. 428:92-107(2016). CC -!- FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 CC ubiquitin-protein ligase complex, which mediates the ubiquitination of CC target proteins, leading to their degradation by the proteasome. CC {ECO:0000305}. CC -!- PATHWAY: Protein modification; protein ubiquitination. {ECO:0000305}. CC -!- SUBUNIT: Forms pentamers. Component of a complex composed of 5 subunits CC of KCTD9 and 5 CUL3. {ECO:0000269|PubMed:26334369}. CC -!- INTERACTION: CC Q7L273; Q5BKX5-3: ACTMAP; NbExp=3; IntAct=EBI-4397613, EBI-11976299; CC Q7L273; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-4397613, EBI-10173507; CC Q7L273; Q49AR9: ANKS1A; NbExp=3; IntAct=EBI-4397613, EBI-11954519; CC Q7L273; P29972: AQP1; NbExp=3; IntAct=EBI-4397613, EBI-745213; CC Q7L273; Q03989: ARID5A; NbExp=3; IntAct=EBI-4397613, EBI-948603; CC Q7L273; Q8N9N5-2: BANP; NbExp=3; IntAct=EBI-4397613, EBI-11524452; CC Q7L273; Q9H2G9: BLZF1; NbExp=3; IntAct=EBI-4397613, EBI-2548012; CC Q7L273; Q9H257: CARD9; NbExp=3; IntAct=EBI-4397613, EBI-751319; CC Q7L273; Q9HC52: CBX8; NbExp=6; IntAct=EBI-4397613, EBI-712912; CC Q7L273; Q16543: CDC37; NbExp=3; IntAct=EBI-4397613, EBI-295634; CC Q7L273; Q6NVV7: CDPF1; NbExp=3; IntAct=EBI-4397613, EBI-2802782; CC Q7L273; P27918: CFP; NbExp=3; IntAct=EBI-4397613, EBI-9038570; CC Q7L273; P78560: CRADD; NbExp=3; IntAct=EBI-4397613, EBI-520375; CC Q7L273; Q13618: CUL3; NbExp=10; IntAct=EBI-4397613, EBI-456129; CC Q7L273; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-4397613, EBI-742054; CC Q7L273; Q05D60: DEUP1; NbExp=3; IntAct=EBI-4397613, EBI-748597; CC Q7L273; Q08426: EHHADH; NbExp=4; IntAct=EBI-4397613, EBI-2339219; CC Q7L273; Q7L775: EPM2AIP1; NbExp=3; IntAct=EBI-4397613, EBI-6255981; CC Q7L273; Q9H5Z6: FAM124B; NbExp=3; IntAct=EBI-4397613, EBI-741626; CC Q7L273; P55040: GEM; NbExp=6; IntAct=EBI-4397613, EBI-744104; CC Q7L273; Q9NYA3: GOLGA6A; NbExp=3; IntAct=EBI-4397613, EBI-11163335; CC Q7L273; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-4397613, EBI-5916454; CC Q7L273; Q9H8Y8: GORASP2; NbExp=7; IntAct=EBI-4397613, EBI-739467; CC Q7L273; O95872: GPANK1; NbExp=3; IntAct=EBI-4397613, EBI-751540; CC Q7L273; P49639: HOXA1; NbExp=5; IntAct=EBI-4397613, EBI-740785; CC Q7L273; P31273: HOXC8; NbExp=3; IntAct=EBI-4397613, EBI-1752118; CC Q7L273; Q86VF2-5: IGFN1; NbExp=3; IntAct=EBI-4397613, EBI-11955401; CC Q7L273; Q14005-2: IL16; NbExp=3; IntAct=EBI-4397613, EBI-17178971; CC Q7L273; Q0VD86: INCA1; NbExp=3; IntAct=EBI-4397613, EBI-6509505; CC Q7L273; Q7L273: KCTD9; NbExp=4; IntAct=EBI-4397613, EBI-4397613; CC Q7L273; Q9HAQ2: KIF9; NbExp=3; IntAct=EBI-4397613, EBI-8472129; CC Q7L273; Q53HC5: KLHL26; NbExp=3; IntAct=EBI-4397613, EBI-724915; CC Q7L273; Q15323: KRT31; NbExp=3; IntAct=EBI-4397613, EBI-948001; CC Q7L273; O76011: KRT34; NbExp=3; IntAct=EBI-4397613, EBI-1047093; CC Q7L273; Q92764: KRT35; NbExp=3; IntAct=EBI-4397613, EBI-1058674; CC Q7L273; Q6A162: KRT40; NbExp=3; IntAct=EBI-4397613, EBI-10171697; CC Q7L273; Q52LG2: KRTAP13-2; NbExp=3; IntAct=EBI-4397613, EBI-11953846; CC Q7L273; Q3SY46: KRTAP13-3; NbExp=3; IntAct=EBI-4397613, EBI-10241252; CC Q7L273; Q8TBB1: LNX1; NbExp=6; IntAct=EBI-4397613, EBI-739832; CC Q7L273; Q17RB8: LONRF1; NbExp=6; IntAct=EBI-4397613, EBI-2341787; CC Q7L273; Q9UI95: MAD2L2; NbExp=3; IntAct=EBI-4397613, EBI-77889; CC Q7L273; Q8WWY6: MBD3L1; NbExp=3; IntAct=EBI-4397613, EBI-12516603; CC Q7L273; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-4397613, EBI-16439278; CC Q7L273; Q5JXC2: MIIP; NbExp=3; IntAct=EBI-4397613, EBI-2801965; CC Q7L273; O14561: NDUFAB1; NbExp=3; IntAct=EBI-4397613, EBI-1246261; CC Q7L273; Q9GZT8: NIF3L1; NbExp=3; IntAct=EBI-4397613, EBI-740897; CC Q7L273; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-4397613, EBI-741158; CC Q7L273; Q8NFH5: NUP35; NbExp=7; IntAct=EBI-4397613, EBI-9050429; CC Q7L273; Q17RL8: PDZD4; NbExp=3; IntAct=EBI-4397613, EBI-10239064; CC Q7L273; Q99471: PFDN5; NbExp=3; IntAct=EBI-4397613, EBI-357275; CC Q7L273; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-4397613, EBI-79165; CC Q7L273; O60568: PLOD3; NbExp=3; IntAct=EBI-4397613, EBI-741582; CC Q7L273; Q8N490: PNKD; NbExp=3; IntAct=EBI-4397613, EBI-746368; CC Q7L273; Q8WVV4-1: POF1B; NbExp=3; IntAct=EBI-4397613, EBI-11986735; CC Q7L273; Q96T49: PPP1R16B; NbExp=3; IntAct=EBI-4397613, EBI-10293968; CC Q7L273; Q6NYC8: PPP1R18; NbExp=3; IntAct=EBI-4397613, EBI-2557469; CC Q7L273; Q9NQX0: PRDM6; NbExp=3; IntAct=EBI-4397613, EBI-11320284; CC Q7L273; P54646: PRKAA2; NbExp=3; IntAct=EBI-4397613, EBI-1383852; CC Q7L273; P25786: PSMA1; NbExp=6; IntAct=EBI-4397613, EBI-359352; CC Q7L273; P49721: PSMB2; NbExp=3; IntAct=EBI-4397613, EBI-359335; CC Q7L273; Q93062: RBPMS; NbExp=3; IntAct=EBI-4397613, EBI-740322; CC Q7L273; Q8HWS3: RFX6; NbExp=3; IntAct=EBI-4397613, EBI-746118; CC Q7L273; Q9BVN2: RUSC1; NbExp=3; IntAct=EBI-4397613, EBI-6257312; CC Q7L273; Q7Z5V6-2: SAXO4; NbExp=3; IntAct=EBI-4397613, EBI-12000762; CC Q7L273; O00560: SDCBP; NbExp=6; IntAct=EBI-4397613, EBI-727004; CC Q7L273; P63208: SKP1; NbExp=3; IntAct=EBI-4397613, EBI-307486; CC Q7L273; Q8ND83: SLAIN1; NbExp=3; IntAct=EBI-4397613, EBI-10269374; CC Q7L273; Q53HV7-2: SMUG1; NbExp=3; IntAct=EBI-4397613, EBI-12275818; CC Q7L273; Q496A3: SPATS1; NbExp=3; IntAct=EBI-4397613, EBI-3923692; CC Q7L273; Q9NZD8: SPG21; NbExp=3; IntAct=EBI-4397613, EBI-742688; CC Q7L273; Q8N865: SPMIP4; NbExp=3; IntAct=EBI-4397613, EBI-10174456; CC Q7L273; Q8NCR6: SPMIP6; NbExp=3; IntAct=EBI-4397613, EBI-10269322; CC Q7L273; Q96LM6: SPMIP9; NbExp=3; IntAct=EBI-4397613, EBI-743976; CC Q7L273; O75558: STX11; NbExp=3; IntAct=EBI-4397613, EBI-714135; CC Q7L273; Q5T7P8-2: SYT6; NbExp=6; IntAct=EBI-4397613, EBI-10246152; CC Q7L273; Q5VWN6: TASOR2; NbExp=3; IntAct=EBI-4397613, EBI-745958; CC Q7L273; Q5VWN6-2: TASOR2; NbExp=3; IntAct=EBI-4397613, EBI-10172380; CC Q7L273; Q96N21: TEPSIN; NbExp=3; IntAct=EBI-4397613, EBI-11139477; CC Q7L273; Q63HR2: TNS2; NbExp=3; IntAct=EBI-4397613, EBI-949753; CC Q7L273; P14373: TRIM27; NbExp=6; IntAct=EBI-4397613, EBI-719493; CC Q7L273; Q13049: TRIM32; NbExp=6; IntAct=EBI-4397613, EBI-742790; CC Q7L273; Q8IWZ5: TRIM42; NbExp=6; IntAct=EBI-4397613, EBI-5235829; CC Q7L273; Q15654: TRIP6; NbExp=3; IntAct=EBI-4397613, EBI-742327; CC Q7L273; Q9H9P5-5: UNKL; NbExp=3; IntAct=EBI-4397613, EBI-12817837; CC Q7L273; Q9UK80: USP21; NbExp=3; IntAct=EBI-4397613, EBI-373242; CC Q7L273; Q70EL1-9: USP54; NbExp=3; IntAct=EBI-4397613, EBI-11975223; CC Q7L273; Q9BRX9: WDR83; NbExp=3; IntAct=EBI-4397613, EBI-7705033; CC Q7L273; P24278: ZBTB25; NbExp=3; IntAct=EBI-4397613, EBI-739899; CC Q7L273; B2RXF5: ZBTB42; NbExp=3; IntAct=EBI-4397613, EBI-12287587; CC Q7L273; Q9H9D4: ZNF408; NbExp=3; IntAct=EBI-4397613, EBI-347633; CC Q7L273; Q9BUY5: ZNF426; NbExp=3; IntAct=EBI-4397613, EBI-743265; CC Q7L273; Q6ZNG0: ZNF620; NbExp=3; IntAct=EBI-4397613, EBI-4395669; CC Q7L273; P36508: ZNF76; NbExp=3; IntAct=EBI-4397613, EBI-7254550; CC -!- SEQUENCE CAUTION: CC Sequence=BAA90904.1; 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; BC021216; AAH21216.2; -; mRNA. DR EMBL; BC068518; AAH68518.1; -; mRNA. DR EMBL; AK000045; BAA90904.1; ALT_INIT; mRNA. DR CCDS; CCDS6048.1; -. DR RefSeq; NP_060104.2; NM_017634.3. DR PDB; 5BXH; X-ray; 2.76 A; A/B/C/D/E=89-191. DR PDBsum; 5BXH; -. DR AlphaFoldDB; Q7L273; -. DR SMR; Q7L273; -. DR BioGRID; 120153; 231. DR IntAct; Q7L273; 100. DR MINT; Q7L273; -. DR STRING; 9606.ENSP00000221200; -. DR GlyGen; Q7L273; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q7L273; -. DR PhosphoSitePlus; Q7L273; -. DR BioMuta; KCTD9; -. DR DMDM; 50400921; -. DR EPD; Q7L273; -. DR jPOST; Q7L273; -. DR MassIVE; Q7L273; -. DR MaxQB; Q7L273; -. DR PaxDb; 9606-ENSP00000221200; -. DR PeptideAtlas; Q7L273; -. DR ProteomicsDB; 68757; -. DR Pumba; Q7L273; -. DR Antibodypedia; 22883; 289 antibodies from 22 providers. DR DNASU; 54793; -. DR Ensembl; ENST00000221200.9; ENSP00000221200.4; ENSG00000104756.17. DR GeneID; 54793; -. DR KEGG; hsa:54793; -. DR MANE-Select; ENST00000221200.9; ENSP00000221200.4; NM_017634.4; NP_060104.2. DR UCSC; uc003xeo.4; human. DR AGR; HGNC:22401; -. DR CTD; 54793; -. DR DisGeNET; 54793; -. DR GeneCards; KCTD9; -. DR HGNC; HGNC:22401; KCTD9. DR HPA; ENSG00000104756; Low tissue specificity. DR neXtProt; NX_Q7L273; -. DR OpenTargets; ENSG00000104756; -. DR PharmGKB; PA134869993; -. DR VEuPathDB; HostDB:ENSG00000104756; -. DR eggNOG; KOG1665; Eukaryota. DR GeneTree; ENSGT00940000154314; -. DR HOGENOM; CLU_043894_0_0_1; -. DR InParanoid; Q7L273; -. DR OMA; YACIKNA; -. DR OrthoDB; 54069at2759; -. DR PhylomeDB; Q7L273; -. DR TreeFam; TF313754; -. DR PathwayCommons; Q7L273; -. DR SignaLink; Q7L273; -. DR UniPathway; UPA00143; -. DR BioGRID-ORCS; 54793; 73 hits in 1123 CRISPR screens. DR ChiTaRS; KCTD9; human. DR GenomeRNAi; 54793; -. DR Pharos; Q7L273; Tbio. DR PRO; PR:Q7L273; -. DR Proteomes; UP000005640; Chromosome 8. DR RNAct; Q7L273; Protein. DR Bgee; ENSG00000104756; Expressed in blood vessel layer and 194 other cell types or tissues. DR ExpressionAtlas; Q7L273; baseline and differential. DR GO; GO:0097602; F:cullin family protein binding; IDA:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0043621; F:protein self-association; IDA:UniProtKB. DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro. DR GO; GO:0051260; P:protein homooligomerization; IEA:InterPro. DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway. DR CDD; cd18368; BTB_POZ_KCTD9; 1. DR CDD; cd17073; KHA; 1. DR Gene3D; 2.160.20.80; E3 ubiquitin-protein ligase SopA; 1. DR InterPro; IPR001646; 5peptide_repeat. DR InterPro; IPR000210; BTB/POZ_dom. DR InterPro; IPR036572; Doublecortin_dom_sf. DR InterPro; IPR021789; KHA_dom. DR InterPro; IPR011333; SKP1/BTB/POZ_sf. DR InterPro; IPR003131; T1-type_BTB. DR PANTHER; PTHR14136:SF17; BTB_POZ DOMAIN-CONTAINING PROTEIN KCTD9; 1. DR PANTHER; PTHR14136; UNCHARACTERIZED; 1. DR Pfam; PF02214; BTB_2; 1. DR Pfam; PF11834; KHA; 1. DR Pfam; PF00805; Pentapeptide; 2. DR SMART; SM00225; BTB; 1. DR SUPFAM; SSF89837; Doublecortin (DC); 1. DR SUPFAM; SSF141571; Pentapeptide repeat-like; 1. DR SUPFAM; SSF54695; POZ domain; 1. DR PROSITE; PS50097; BTB; 1. DR PROSITE; PS51490; KHA; 1. DR Genevisible; Q7L273; HS. PE 1: Evidence at protein level; KW 3D-structure; Phosphoprotein; Reference proteome; Repeat; KW Ubl conjugation pathway. FT CHAIN 1..389 FT /note="BTB/POZ domain-containing protein KCTD9" FT /id="PRO_0000191293" FT DOMAIN 3..82 FT /note="KHA" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00823" FT DOMAIN 89..161 FT /note="BTB" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037" FT DOMAIN 224..256 FT /note="Pentapeptide repeat 1" FT /evidence="ECO:0000255" FT DOMAIN 258..297 FT /note="Pentapeptide repeat 2" FT /evidence="ECO:0000255" FT DOMAIN 338..376 FT /note="Pentapeptide repeat 3" FT /evidence="ECO:0000255" FT MOD_RES 11 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MUTAGEN 125 FT /note="V->A: Impaired interaction with CUL3." FT /evidence="ECO:0000269|PubMed:26334369" FT CONFLICT 12 FT /note="P -> R (in Ref. 1; AAH68518)" FT /evidence="ECO:0000305" FT STRAND 90..95 FT /evidence="ECO:0007829|PDB:5BXH" FT STRAND 98..103 FT /evidence="ECO:0007829|PDB:5BXH" FT HELIX 104..108 FT /evidence="ECO:0007829|PDB:5BXH" FT HELIX 115..119 FT /evidence="ECO:0007829|PDB:5BXH" FT STRAND 136..138 FT /evidence="ECO:0007829|PDB:5BXH" FT TURN 143..145 FT /evidence="ECO:0007829|PDB:5BXH" FT HELIX 146..154 FT /evidence="ECO:0007829|PDB:5BXH" FT HELIX 165..175 FT /evidence="ECO:0007829|PDB:5BXH" FT HELIX 178..188 FT /evidence="ECO:0007829|PDB:5BXH" SQ SEQUENCE 389 AA; 42567 MW; 43D4AE36F3B9618F CRC64; MRRVTLFLNG SPKNGKVVAV YGTLSDLLSV ASSKLGIKAT SVYNGKGGLI DDIALIRDDD VLFVCEGEPF IDPQTDSKPP EGLLGFHTDW LTLNVGGRYF TTTRSTLVNK EPDSMLAHMF KDKGVWGNKQ DHRGAFLIDR SPEYFEPILN YLRHGQLIVN DGINLLGVLE EARFFGIDSL IEHLEVAIKN SQPPEDHSPI SRKEFVRFLL ATPTKSELRC QGLNFSGADL SRLDLRYINF KMANLSRCNL AHANLCCANL ERADLSGSVL DCANLQGVKM LCSNAEGASL KLCNFEDPSG LKANLEGANL KGVDMEGSQM TGINLRVATL KNAKLKNCNL RGATLAGTDL ENCDLSGCDL QEANLRGSNV KGAIFEEMLT PLHMSQSVR //