KNTC1_HUMAN
ID KNTC1_HUMAN Reviewed; 2209 AA.
AC P50748; A7E2C4; B3KSG2;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Kinetochore-associated protein 1;
DE AltName: Full=Rough deal homolog;
DE Short=HsROD;
DE Short=Rod;
DE Short=hRod;
GN Name=KNTC1; Synonyms=KIAA0166;
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).
RC TISSUE=Bone marrow;
RX PubMed=8724849; DOI=10.1093/dnares/3.1.17;
RA Nagase T., Seki N., Ishikawa K., Tanaka A., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. V. The
RT coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by analysis of
RT cDNA clones from human cell line KG-1.";
RL DNA Res. 3:17-24(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11146660; DOI=10.1038/35046598;
RA Chan G.K.T., Jablonski S.A., Starr D.A., Goldberg M.L., Yen T.J.;
RT "Human Zw10 and ROD are mitotic checkpoint proteins that bind to
RT kinetochores.";
RL Nat. Cell Biol. 2:944-947(2000).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11590237; DOI=10.1242/jcs.114.17.3103;
RA Scaeerou F., Starr D.A., Piano F., Papoulas O., Karess R.E., Goldberg M.L.;
RT "The ZW10 and Rough Deal checkpoint proteins function together in a large,
RT evolutionarily conserved complex targeted to the kinetochore.";
RL J. Cell Sci. 114:3103-3114(2001).
RN [8]
RP INTERACTION WITH ZWILCH AND ZW10.
RX PubMed=12686595; DOI=10.1091/mbc.e02-09-0624;
RA Williams B.C., Li Z., Liu S., Williams E.V., Leung G., Yen T.J.,
RA Goldberg M.L.;
RT "Zwilch, a new component of the ZW10/ROD complex required for kinetochore
RT functions.";
RL Mol. Biol. Cell 14:1379-1391(2003).
RN [9]
RP FUNCTION, AND IDENTIFICATION IN THE RZZ COMPLEX.
RX PubMed=15824131; DOI=10.1083/jcb.200411118;
RA Kops G.J.P.L., Kim Y., Weaver B.A.A., Mao Y., McLeod I., Yates J.R. III,
RA Tagaya M., Cleveland D.W.;
RT "ZW10 links mitotic checkpoint signaling to the structural kinetochore.";
RL J. Cell Biol. 169:49-60(2005).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [11]
RP INTERACTION WITH ZWILCH, AND IDENTIFICATION IN THE RRZ COMPLEX.
RX PubMed=20462495; DOI=10.1016/j.str.2010.02.014;
RA Civril F., Wehenkel A., Giorgi F.M., Santaguida S., Di Fonzo A.,
RA Grigorean G., Ciccarelli F.D., Musacchio A.;
RT "Structural analysis of the RZZ complex reveals common ancestry with
RT multisubunit vesicle tethering machinery.";
RL Structure 18:616-626(2010).
RN [12]
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1035 AND SER-1045, 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).
CC -!- FUNCTION: Essential component of the mitotic checkpoint, which prevents
CC cells from prematurely exiting mitosis. Required for the assembly of
CC the dynein-dynactin and MAD1-MAD2 complexes onto kinetochores
CC (PubMed:11146660, PubMed:11590237, PubMed:15824131). Its function
CC related to the spindle assembly machinery is proposed to depend on its
CC association in the mitotic RZZ complex. {ECO:0000269|PubMed:11146660,
CC ECO:0000269|PubMed:11590237, ECO:0000269|PubMed:15824131, ECO:0000305}.
CC -!- SUBUNIT: Interacts with ZW10; the interaction is required for stable
CC association with the kinetochore. Component of the RZZ complex composed
CC of KNTC1/ROD, ZW10 and ZWILCH; in the complex interacts directly with
CC ZWILCH. {ECO:0000269|PubMed:12686595, ECO:0000269|PubMed:15824131,
CC ECO:0000269|PubMed:20462495}.
CC -!- INTERACTION:
CC P50748; Q9H900: ZWILCH; NbExp=2; IntAct=EBI-1001245, EBI-1001239;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Chromosome, centromere,
CC kinetochore. Cytoplasm, cytoskeleton, spindle. Note=Dynamic pattern of
CC localization during the cell cycle. At interphase, uniformly
CC distributed throughout the cytoplasm and nucleus. By prophase and until
CC late stages of prometaphase, a fraction of the total pool is
CC concentrated at kinetochores. By metaphase, detected at kinetochores,
CC along spindle fibers and most prominently at the poles. By late
CC anaphase until the end of telophase, no longer detectable on
CC kinetochores or along spindle fibers, but still present at the spindle
CC poles.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P50748-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P50748-2; Sequence=VSP_057013, VSP_057014, VSP_057015;
CC -!- TISSUE SPECIFICITY: High expression in testis.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA11483.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; D79988; BAA11483.2; ALT_INIT; mRNA.
DR EMBL; AK093470; BAG52724.1; -; mRNA.
DR EMBL; AC026333; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC127002; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471054; EAW98334.1; -; Genomic_DNA.
DR EMBL; BC150278; AAI50279.1; -; mRNA.
DR CCDS; CCDS45002.1; -. [P50748-1]
DR RefSeq; NP_055523.1; NM_014708.4. [P50748-1]
DR RefSeq; XP_006719769.1; XM_006719706.2. [P50748-1]
DR PDB; 7QPG; EM; 3.90 A; R/S=2-2209.
DR PDBsum; 7QPG; -.
DR AlphaFoldDB; P50748; -.
DR BioGRID; 115084; 80.
DR ComplexPortal; CPX-6017; RZZ complex.
DR CORUM; P50748; -.
DR DIP; DIP-36479N; -.
DR IntAct; P50748; 25.
DR STRING; 9606.ENSP00000328236; -.
DR iPTMnet; P50748; -.
DR PhosphoSitePlus; P50748; -.
DR BioMuta; KNTC1; -.
DR DMDM; 1723117; -.
DR EPD; P50748; -.
DR jPOST; P50748; -.
DR MassIVE; P50748; -.
DR MaxQB; P50748; -.
DR PaxDb; P50748; -.
DR PeptideAtlas; P50748; -.
DR PRIDE; P50748; -.
DR ProteomicsDB; 3637; -.
DR ProteomicsDB; 56261; -. [P50748-1]
DR Antibodypedia; 9885; 125 antibodies from 19 providers.
DR DNASU; 9735; -.
DR Ensembl; ENST00000333479.12; ENSP00000328236.6; ENSG00000184445.12. [P50748-1]
DR GeneID; 9735; -.
DR KEGG; hsa:9735; -.
DR MANE-Select; ENST00000333479.12; ENSP00000328236.6; NM_014708.6; NP_055523.1.
DR UCSC; uc001ucv.4; human. [P50748-1]
DR CTD; 9735; -.
DR DisGeNET; 9735; -.
DR GeneCards; KNTC1; -.
DR HGNC; HGNC:17255; KNTC1.
DR HPA; ENSG00000184445; Tissue enhanced (bone).
DR MIM; 607363; gene.
DR neXtProt; NX_P50748; -.
DR OpenTargets; ENSG00000184445; -.
DR PharmGKB; PA30184; -.
DR VEuPathDB; HostDB:ENSG00000184445; -.
DR eggNOG; KOG4256; Eukaryota.
DR GeneTree; ENSGT00390000007883; -.
DR HOGENOM; CLU_231522_0_0_1; -.
DR InParanoid; P50748; -.
DR OMA; QIEMAYE; -.
DR OrthoDB; 122381at2759; -.
DR PhylomeDB; P50748; -.
DR TreeFam; TF101176; -.
DR PathwayCommons; P50748; -.
DR Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
DR Reactome; R-HSA-68877; Mitotic Prometaphase.
DR Reactome; R-HSA-9648025; EML4 and NUDC in mitotic spindle formation.
DR SignaLink; P50748; -.
DR SIGNOR; P50748; -.
DR BioGRID-ORCS; 9735; 186 hits in 1089 CRISPR screens.
DR ChiTaRS; KNTC1; human.
DR GenomeRNAi; 9735; -.
DR Pharos; P50748; Tbio.
DR PRO; PR:P50748; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P50748; protein.
DR Bgee; ENSG00000184445; Expressed in ventricular zone and 144 other tissues.
DR ExpressionAtlas; P50748; baseline and differential.
DR Genevisible; P50748; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:HPA.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005828; C:kinetochore microtubule; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; NAS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:1990423; C:RZZ complex; IDA:UniProtKB.
DR GO; GO:0000922; C:spindle pole; IDA:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IBA:GO_Central.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IDA:UniProtKB.
DR GO; GO:1903394; P:protein localization to kinetochore involved in kinetochore assembly; IBA:GO_Central.
DR GO; GO:0065003; P:protein-containing complex assembly; NAS:UniProtKB.
DR GO; GO:0007096; P:regulation of exit from mitosis; NAS:UniProtKB.
DR InterPro; IPR019527; RZZ-complex_KNTC1/ROD_C.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF10493; Rod_C; 2.
DR SUPFAM; SSF50978; SSF50978; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell cycle; Cell division; Centromere;
KW Chromosome; Cytoplasm; Cytoskeleton; Kinetochore; Mitosis; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..2209
FT /note="Kinetochore-associated protein 1"
FT /id="PRO_0000084312"
FT MOD_RES 1035
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1045
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..1575
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_057013"
FT VAR_SEQ 2011..2018
FT /note="VPYFSKAW -> RWRSCYVA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_057014"
FT VAR_SEQ 2019..2209
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_057015"
FT VARIANT 245
FT /note="K -> N (in dbSNP:rs7968222)"
FT /id="VAR_051082"
FT VARIANT 738
FT /note="E -> D (in dbSNP:rs17883249)"
FT /id="VAR_051083"
FT VARIANT 1506
FT /note="T -> M (in dbSNP:rs35315099)"
FT /id="VAR_051084"
FT VARIANT 1830
FT /note="P -> L (in dbSNP:rs7310898)"
FT /id="VAR_051085"
FT VARIANT 2021
FT /note="V -> G (in dbSNP:rs11837038)"
FT /id="VAR_051086"
SQ SEQUENCE 2209 AA; 250749 MW; 514C948733CBFDAC CRC64;
MWNDIELLTN DDTGSGYLSV GSRKEHGTAL YQVDLLVKIS SEKASLNPKI QACSLSDGFI
IVADQSVILL DSICRSLQLH LVFDTEVDVV GLCQEGKFLL VGERSGNLHL IHVTSKQTLL
TNAFVQKAND ENRRTYQNLV IEKDGSNEGT YYMLLLTYSG FFCITNLQLL KIQQAIENVD
FSTAKKLQGQ IKSSFISTEN YHTLGCLSLV AGDLASEVPV IIGGTGNCAF SKWEPDSSKK
GMTVKNLIDA EIIKGAKKFQ LIDNLLFVLD TDNVLSLWDI YTLTPVWNWP SLHVEEFLLT
TEADSPSSVT WQGITNLKLI ALTASANKKM KNLMVYSLPT MEILYSLEVS SVSSLVQTGI
STDTIYLLEG VCKNDPKLSE DSVSVLVLRC LTEALPENRL SRLLHKHRFA EAESFAIQFG
LDVELVYKVK SNHILEKLAL SSVDASEQTE WQQLVDDAKE NLHKIQDDEF VVNYCLKAQW
ITYETTQEML NYAKTRLLKK EDKTALIYSD GLKEVLRAHA KLTTFYGAFG PEKFSGSSWI
EFLNNEDDLK DIFLQLKEGN LVCAQYLWLR HRANFESRFD VKMLESLLNS MSASVSLQKL
CPWFKNDVIP FVRRTVPEGQ IILAKWLEQA ARNLELTDKA NWPENGLQLA EIFFTAEKTD
ELGLASSWHW ISLKDYQNTE EVCQLRTLVN NLRELITLHR KYNCKLALSD FEKENTTTIV
FRMFDKVLAP ELIPSILEKF IRVYMREHDL QEEELLLLYI EDLLNRCSSK STSLFETAWE
AKAMAVIACL SDTDLIFDAV LKIMYAAVVP WSAAVEQLVK QHLEMDHPKV KLLQESYKLM
EMKKLLRGYG IREVNLLNKE IMRVVRYILK QDVPSSLEDA LKVAQAFMLS DDEIYSLRII
DLIDREQGED CLLLLKSLPP AEAEKTAERV IIWARLALQE EPDHSKEGKA WRMSVAKTSV
DILKILCDIQ KDNLQKKDEC EEMLKLFKEV ASLQENFEVF LSFEDYSNSS LVADLREQHI
KAHEVAQAKH KPGSTPEPIA AEVRSPSMES KLHRQALALQ MSKQELEAEL TLRALKDGNI
KTALKKCSDL FKYHCNADTG KLLFLTCQKL CQMLADNVPV TVPVGLNLPS MIHDLASQAA
TICSPDFLLD ALELCKHTLM AVELSRQCQM DDCGILMKAS FGTHKDPYEE WSYSDFFSED
GIVLESQMVL PVIYELISSL VPLAESKRYP LESTSLPYCS LNEGDGLVLP VINSISALLQ
NLQESSQWEL ALRFVVGSFG TCLQHSVSNF MNATLSEKLF GETTLVKSRH VVMELKEKAV
IFIRENATTL LHKVFNCRLV DLDLALGYCT LLPQKDVFEN LWKLIDKAWQ NYDKILAISL
VGSELASLYQ EIEMGLKFRE LSTDAQWGIR LGKLGISFQP VFRQHFLTKK DLIKALVENI
DMDTSLILEY CSTFQLDCDA VLQLFIETLL HNTNAGQGQG DASMDSAKRR HPKLLAKALE
MVPLLTSTKD LVISLSGILH KLDPYDYEMI EVVLKVIERA DEKITNININ QALSILKHLK
SYRRISPPVD LEYQYMLEHV ITLPSAAQTR LPFHLIFFGT AQNFWKILST ELSEESFPTL
LLISKLMKFS LDTLYVSTAK HVFEKKLKPK LLKLTQAKSS TLINKEITKI TQTIESCLLS
IVNPEWAVAI AISLAQDIPE GSFKISALKF CLYLAERWLQ NIPSQDEKRE KAEALLKKLH
IQYRRSGTEA VLIAHKLNTE EYLRVIGKPA HLIVSLYEHP SINQRIQNSS GTDYPDIHAA
AKEIAEVNEI NLEKVWDMLL EKWLCPSTKP GEKPSELFEL QEDEALRRVQ YLLLSRPIDY
SSRMLFVFAT STTTTLGMHQ LTFAHRTRAL QCLFYLADKE TIESLFKKPI EEVKSYLRCI
TFLASFETLN IPITYELFCS SPKEGMIKGL WKNHSHESMA VRLVTELCLE YKIYDLQLWN
GLLQKLLGFN MIPYLRKVLK AISSIHSLWQ VPYFSKAWQR VIQIPLLSAS CPLSPDQLSD
CSESLIAVLE CPVSGDLDLI GVARQYIQLE LPAFALACLM LMPHSEKRHQ QIKNFLGSCD
PQVILKQLEE HMNTGQLAGF SHQIRSLILN NIINKKEFGI LAKTKYFQML KMHAMNTNNI
TELVNYLAND LSLDEASVLI TEYSKHCGKP VPPDTAPCEI LKMFLSGLS
