K22O_HUMAN
ID K22O_HUMAN Reviewed; 638 AA.
AC Q01546; B4DRR3; Q7Z795;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Keratin, type II cytoskeletal 2 oral;
DE AltName: Full=Cytokeratin-2P;
DE Short=CK-2P;
DE Short=K2P;
DE AltName: Full=Keratin-76;
DE Short=K76;
DE AltName: Full=Type-II keratin Kb9;
GN Name=KRT76; Synonyms=KRT2B, KRT2P;
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 [MRNA], FUNCTION, DEVELOPMENTAL STAGE, AND VARIANT
RP THR-359.
RX PubMed=1282112; DOI=10.1111/j.1432-0436.1992.tb00690.x;
RA Collin C., Ouhayoun J.P., Grund C., Franke W.W.;
RT "Suprabasal marker proteins distinguishing keratinizing squamous epithelia:
RT cytokeratin 2 polypeptides of oral masticatory epithelium and epidermis are
RT different.";
RL Differentiation 51:137-148(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=15737194; DOI=10.1111/j.0022-202x.2004.23530.x;
RA Rogers M.A., Edler L., Winter H., Langbein L., Beckmann I., Schweizer J.;
RT "Characterization of new members of the human type II keratin gene family
RT and a general evaluation of the keratin gene domain on chromosome
RT 12q13.13.";
RL J. Invest. Dermatol. 124:536-544(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Tongue;
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 [4]
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 [5]
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).
RN [6]
RP VARIANT [LARGE SCALE ANALYSIS] VAL-168.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [7]
RP VARIANT [LARGE SCALE ANALYSIS] THR-359, AND IDENTIFICATION BY MASS
RP 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).
CC -!- FUNCTION: Probably contributes to terminal cornification.
CC {ECO:0000269|PubMed:1282112}.
CC -!- SUBUNIT: Heterotetramer of two type I and two type II keratins.
CC -!- INTERACTION:
CC Q01546; Q9NX04: C1orf109; NbExp=3; IntAct=EBI-2952745, EBI-8643161;
CC Q01546; Q8TAB5: C1orf216; NbExp=3; IntAct=EBI-2952745, EBI-747505;
CC Q01546; Q9UQM7: CAMK2A; NbExp=3; IntAct=EBI-2952745, EBI-1383687;
CC Q01546; Q2TAC2-2: CCDC57; NbExp=3; IntAct=EBI-2952745, EBI-10961624;
CC Q01546; Q16543: CDC37; NbExp=3; IntAct=EBI-2952745, EBI-295634;
CC Q01546; Q8IYR0: CFAP206; NbExp=3; IntAct=EBI-2952745, EBI-749051;
CC Q01546; Q6W0C5: DPPA3; NbExp=3; IntAct=EBI-2952745, EBI-12082590;
CC Q01546; Q8IYI6: EXOC8; NbExp=3; IntAct=EBI-2952745, EBI-742102;
CC Q01546; Q6PJQ5: FOXR2; NbExp=3; IntAct=EBI-2952745, EBI-8468543;
CC Q01546; O43559: FRS3; NbExp=3; IntAct=EBI-2952745, EBI-725515;
CC Q01546; O14964: HGS; NbExp=3; IntAct=EBI-2952745, EBI-740220;
CC Q01546; Q9UI26-2: IPO11; NbExp=3; IntAct=EBI-2952745, EBI-12200335;
CC Q01546; Q8NA54: IQUB; NbExp=3; IntAct=EBI-2952745, EBI-10220600;
CC Q01546; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-2952745, EBI-14069005;
CC Q01546; P08779: KRT16; NbExp=3; IntAct=EBI-2952745, EBI-356410;
CC Q01546; P35900: KRT20; NbExp=3; IntAct=EBI-2952745, EBI-742094;
CC Q01546; Q7Z3Z0: KRT25; NbExp=3; IntAct=EBI-2952745, EBI-11980019;
CC Q01546; Q7Z3Y8: KRT27; NbExp=3; IntAct=EBI-2952745, EBI-3044087;
CC Q01546; Q15323: KRT31; NbExp=5; IntAct=EBI-2952745, EBI-948001;
CC Q01546; O76013-2: KRT36; NbExp=3; IntAct=EBI-2952745, EBI-11958506;
CC Q01546; O76014: KRT37; NbExp=3; IntAct=EBI-2952745, EBI-1045716;
CC Q01546; O76015: KRT38; NbExp=3; IntAct=EBI-2952745, EBI-1047263;
CC Q01546; Q6A163: KRT39; NbExp=3; IntAct=EBI-2952745, EBI-11958242;
CC Q01546; Q6A162: KRT40; NbExp=3; IntAct=EBI-2952745, EBI-10171697;
CC Q01546; O95678: KRT75; NbExp=3; IntAct=EBI-2952745, EBI-2949715;
CC Q01546; O43790: KRT86; NbExp=3; IntAct=EBI-2952745, EBI-9996498;
CC Q01546; O95447: LCA5L; NbExp=3; IntAct=EBI-2952745, EBI-8473670;
CC Q01546; P61968: LMO4; NbExp=3; IntAct=EBI-2952745, EBI-2798728;
CC Q01546; Q9GZQ8: MAP1LC3B; NbExp=2; IntAct=EBI-2952745, EBI-373144;
CC Q01546; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-2952745, EBI-10172526;
CC Q01546; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-2952745, EBI-11522433;
CC Q01546; Q8NI38: NFKBID; NbExp=3; IntAct=EBI-2952745, EBI-10271199;
CC Q01546; O15160: POLR1C; NbExp=5; IntAct=EBI-2952745, EBI-1055079;
CC Q01546; Q9UHP6: RSPH14; NbExp=3; IntAct=EBI-2952745, EBI-748350;
CC Q01546; Q63HR2: TNS2; NbExp=3; IntAct=EBI-2952745, EBI-949753;
CC Q01546; P36406: TRIM23; NbExp=3; IntAct=EBI-2952745, EBI-740098;
CC Q01546; P14373: TRIM27; NbExp=3; IntAct=EBI-2952745, EBI-719493;
CC Q01546; Q9BYV2: TRIM54; NbExp=3; IntAct=EBI-2952745, EBI-2130429;
CC Q01546; Q9BZW7: TSGA10; NbExp=3; IntAct=EBI-2952745, EBI-744794;
CC Q01546; Q8N720: ZNF655; NbExp=3; IntAct=EBI-2952745, EBI-625509;
CC -!- DEVELOPMENTAL STAGE: Synthesized during maturation of epidermal
CC keratinocytes. {ECO:0000269|PubMed:1282112}.
CC -!- MISCELLANEOUS: There are two types of cytoskeletal and microfibrillar
CC keratin: I (acidic; 40-55 kDa) and II (neutral to basic; 56-70 kDa).
CC -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000255|PROSITE-ProRule:PRU01188}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAG61375.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Human Intermediate Filament Mutation Database;
CC URL="http://www.interfil.org";
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DR EMBL; M99063; AAA35746.1; -; mRNA.
DR EMBL; AJ564103; CAD91891.1; -; Genomic_DNA.
DR EMBL; AK299390; BAG61375.1; ALT_SEQ; mRNA.
DR EMBL; AC068988; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC139763; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS8838.1; -.
DR PIR; I53169; I53169.
DR RefSeq; NP_056932.2; NM_015848.4.
DR AlphaFoldDB; Q01546; -.
DR SMR; Q01546; -.
DR BioGRID; 119492; 58.
DR IntAct; Q01546; 54.
DR MINT; Q01546; -.
DR STRING; 9606.ENSP00000330101; -.
DR iPTMnet; Q01546; -.
DR PhosphoSitePlus; Q01546; -.
DR SwissPalm; Q01546; -.
DR BioMuta; KRT76; -.
DR DMDM; 317373371; -.
DR jPOST; Q01546; -.
DR MassIVE; Q01546; -.
DR PaxDb; Q01546; -.
DR PeptideAtlas; Q01546; -.
DR PRIDE; Q01546; -.
DR ProteomicsDB; 57971; -.
DR Antibodypedia; 14669; 511 antibodies from 24 providers.
DR DNASU; 51350; -.
DR Ensembl; ENST00000332411.2; ENSP00000330101.2; ENSG00000185069.2.
DR GeneID; 51350; -.
DR KEGG; hsa:51350; -.
DR MANE-Select; ENST00000332411.2; ENSP00000330101.2; NM_015848.4; NP_056932.2.
DR UCSC; uc001sax.3; human.
DR CTD; 51350; -.
DR DisGeNET; 51350; -.
DR GeneCards; KRT76; -.
DR HGNC; HGNC:24430; KRT76.
DR HPA; ENSG00000185069; Group enriched (lymphoid tissue, salivary gland).
DR MIM; 616671; gene.
DR neXtProt; NX_Q01546; -.
DR OpenTargets; ENSG00000185069; -.
DR PharmGKB; PA147357785; -.
DR VEuPathDB; HostDB:ENSG00000185069; -.
DR eggNOG; ENOG502QURK; Eukaryota.
DR GeneTree; ENSGT00940000162365; -.
DR HOGENOM; CLU_012560_6_0_1; -.
DR InParanoid; Q01546; -.
DR OMA; MSHSGMG; -.
DR OrthoDB; 824246at2759; -.
DR PhylomeDB; Q01546; -.
DR TreeFam; TF317854; -.
DR PathwayCommons; Q01546; -.
DR Reactome; R-HSA-6805567; Keratinization.
DR Reactome; R-HSA-6809371; Formation of the cornified envelope.
DR SignaLink; Q01546; -.
DR BioGRID-ORCS; 51350; 10 hits in 1067 CRISPR screens.
DR GenomeRNAi; 51350; -.
DR Pharos; Q01546; Tdark.
DR PRO; PR:Q01546; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q01546; protein.
DR Bgee; ENSG00000185069; Expressed in gingiva and 17 other tissues.
DR Genevisible; Q01546; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005882; C:intermediate filament; NAS:UniProtKB.
DR GO; GO:0045095; C:keratin filament; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0030280; F:structural constituent of skin epidermis; IBA:GO_Central.
DR GO; GO:0007010; P:cytoskeleton organization; NAS:UniProtKB.
DR GO; GO:0045109; P:intermediate filament organization; IBA:GO_Central.
DR GO; GO:0031424; P:keratinization; IBA:GO_Central.
DR GO; GO:0043473; P:pigmentation; IEA:Ensembl.
DR GO; GO:0048733; P:sebaceous gland development; IEA:Ensembl.
DR InterPro; IPR018039; IF_conserved.
DR InterPro; IPR039008; IF_rod_dom.
DR InterPro; IPR032444; Keratin_2_head.
DR InterPro; IPR003054; Keratin_II.
DR Pfam; PF00038; Filament; 1.
DR Pfam; PF16208; Keratin_2_head; 1.
DR PRINTS; PR01276; TYPE2KERATIN.
DR SMART; SM01391; Filament; 1.
DR PROSITE; PS00226; IF_ROD_1; 1.
DR PROSITE; PS51842; IF_ROD_2; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Intermediate filament; Keratin; Methylation;
KW Reference proteome.
FT CHAIN 1..638
FT /note="Keratin, type II cytoskeletal 2 oral"
FT /id="PRO_0000063714"
FT DOMAIN 183..496
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..182
FT /note="Head"
FT REGION 183..218
FT /note="Coil 1A"
FT REGION 219..237
FT /note="Linker 1"
FT REGION 238..329
FT /note="Coil 1B"
FT REGION 330..353
FT /note="Linker 12"
FT REGION 354..492
FT /note="Coil 2"
FT REGION 493..638
FT /note="Tail"
FT REGION 532..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..638
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 85
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q6IFZ6"
FT MOD_RES 110
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q6IFZ6"
FT MOD_RES 584
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q6IFZ6"
FT VARIANT 168
FT /note="L -> V (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036368"
FT VARIANT 283
FT /note="A -> T (in dbSNP:rs11170271)"
FT /id="VAR_028425"
FT VARIANT 359
FT /note="A -> T (in dbSNP:rs6580904)"
FT /evidence="ECO:0000269|PubMed:1282112,
FT ECO:0007744|PubMed:21269460"
FT /id="VAR_028426"
FT VARIANT 629
FT /note="T -> M (in dbSNP:rs2280480)"
FT /id="VAR_028427"
FT CONFLICT 356
FT /note="E -> K (in Ref. 3; BAG61375)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 638 AA; 65841 MW; 6A312B8260BE06A9 CRC64;
MNRQVCKKSF SGRSQGFSGR SAVVSGSSRM SCVARSGGAG GGACGFRSGA GSFGSRSLYN
LGSNKSISIS VAAGSSRAGG FGGGRSSCGF AGGYGGGFGG SYGGGFGGGR GVGSGFGGAG
GFGGAGGFGG PGVFGGPGSF GGPGGFGPGG FPGGIQEVIV NQSLLQPLNV EIDPQIGQVK
AQEREQIKTL NNKFASFIDK VRFLEQQNKV LETKWELLQQ QTTGSGPSSL EPCFESYISF
LCKQLDSLLG ERGNLEGELK SMQDLVEDFK KKYEDEINKR TAAENEFVGL KKDVDAAFMN
KVELQAKVDS LTDEVSFLRT LYEMELSQMQ SHASDTSVVL SMDNNRCLDL GSIIAEVRAQ
YEEIAQRSKS EAEALYQTKL GELQTTAGRH GDDLRNTKSE IMELNRMIQR LRAEIENVKK
QNANLQTAIA EAEQRGEMAL KDANAKLQDL QTALQKAKDD LARLLRDYQE LMNVKLALDV
EIATYRKLLE GEECRMSGEC QSAVCISVVS NVTSTSGSSG SSRGVFGGVS GSGSGGYKGG
SSSSSSSGYG VSGGSGSGYG GVSSGSTGGR GSSGSYQSSS SGSRLGGAGS ISVSHSGMGS
SSGSIQTSGG SGYKSGGGGS TSIRFSQTTS SSQHSSTK
