KCTD9_HUMAN
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 03-AUG-2022, entry version 148.
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; 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; Q5BKX5-3: C19orf54; NbExp=3; IntAct=EBI-4397613, EBI-11976299;
CC Q7L273; Q8N865: C7orf31; NbExp=3; IntAct=EBI-4397613, EBI-10174456;
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; Q7Z5V6-2: PPP1R32; NbExp=3; IntAct=EBI-4397613, EBI-12000762;
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; 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; Q8NCR6: SMRP1; NbExp=3; IntAct=EBI-4397613, EBI-10269322;
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; 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; Q96LM6: TEX37; NbExp=3; IntAct=EBI-4397613, EBI-743976;
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};
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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; 124.
DR IntAct; Q7L273; 99.
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; Q7L273; -.
DR PeptideAtlas; Q7L273; -.
DR PRIDE; Q7L273; -.
DR ProteomicsDB; 68757; -.
DR Antibodypedia; 22883; 243 antibodies from 22 providers.
DR DNASU; 54793; -.
DR Ensembl; ENST00000221200.9; ENSP00000221200.4; ENSG00000104756.16.
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 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; 1041330at2759; -.
DR PhylomeDB; Q7L273; -.
DR TreeFam; TF313754; -.
DR PathwayCommons; Q7L273; -.
DR SignaLink; Q7L273; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 54793; 71 hits in 1048 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 192 other tissues.
DR ExpressionAtlas; Q7L273; baseline and differential.
DR Genevisible; Q7L273; HS.
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 Gene3D; 3.30.710.10; -; 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 Pfam; PF02214; BTB_2; 1.
DR Pfam; PF11834; KHA; 1.
DR Pfam; PF00805; Pentapeptide; 3.
DR SMART; SM00225; BTB; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
DR SUPFAM; SSF89837; SSF89837; 1.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS51490; KHA; 1.
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
