ID   TYRP2_HUMAN             Reviewed;         519 AA.
AC   P40126; Q09GT4;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   24-JAN-2024, entry version 199.
DE   RecName: Full=L-dopachrome tautomerase {ECO:0000305};
DE            Short=DCT;
DE            Short=DT;
DE            EC=5.3.3.12 {ECO:0000250|UniProtKB:P29812};
DE   AltName: Full=L-dopachrome Delta-isomerase;
DE   AltName: Full=Tyrosinase-related protein 2;
DE            Short=TRP-2;
DE            Short=TRP2;
DE   Flags: Precursor;
GN   Name=DCT {ECO:0000312|HGNC:HGNC:2709}; Synonyms=TYRP2;
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] (ISOFORM 1).
RX   PubMed=8148378; DOI=10.1016/0167-4781(94)90292-5;
RA   Yokoyama K., Suzuki H., Yasumoto K.I., Tomita Y., Shibahara S.;
RT   "Molecular cloning and functional analysis of a cDNA coding for human
RT   DOPAchrome tautomerase/tyrosinase-related protein-2.";
RL   Biochim. Biophys. Acta 1217:317-321(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=8206391; DOI=10.1016/0378-1119(94)90114-7;
RA   Cassady J.L., Sturm R.A.;
RT   "Sequence of the human dopachrome tautomerase-encoding TRP-2 cDNA.";
RL   Gene 143:295-298(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
RX   PubMed=8306979; DOI=10.1111/j.1432-1033.1994.tb19922.x;
RA   Bouchard B., del Marmol V., Jackson I.J., Cherif D., Dubertret L.;
RT   "Molecular characterization of a human tyrosinase-related-protein-2 cDNA.
RT   Patterns of expression in melanocytic cells.";
RL   Eur. J. Biochem. 219:127-134(1994).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND ALTERNATIVE SPLICING.
RC   TISSUE=Melanoma;
RX   PubMed=11777994; DOI=10.4049/jimmunol.168.2.951;
RA   Khong H.T., Rosenberg S.A.;
RT   "Pre-existing immunity to tyrosinase-related protein (TRP)-2, a new TRP-2
RT   isoform, and the NY-ESO-1 melanoma antigen in a patient with a dramatic
RT   response to immunotherapy.";
RL   J. Immunol. 168:951-956(2002).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15057823; DOI=10.1038/nature02379;
RA   Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA   Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA   Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA   Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA   Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA   Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA   Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA   Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA   Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA   Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA   Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA   Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA   Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA   Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA   Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA   Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA   Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA   Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA   Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA   Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA   Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA   Rogers J., Ross M.T.;
RT   "The DNA sequence and analysis of human chromosome 13.";
RL   Nature 428:522-528(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Mammary gland;
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   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-98.
RC   TISSUE=Liver;
RX   PubMed=8530077; DOI=10.1006/geno.1995.1211;
RA   Sturm R.A., O'Sullivan B.J., Box N.F., Smith A.G., Smit S.E.,
RA   Puttick E.R.J., Parsons P.G., Dunn I.S.;
RT   "Chromosomal structure of the human TYRP1 and TYRP2 loci and comparison of
RT   the tyrosinase-related protein gene family.";
RL   Genomics 29:24-34(1995).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-98.
RC   TISSUE=Liver;
RX   PubMed=7929451; DOI=10.1016/s0021-9258(18)47128-1;
RA   Yokoyama K., Yasumoto K.I., Suzuki H., Shibahara S.;
RT   "Cloning of the human DOPAchrome tautomerase/tyrosinase-related protein 2
RT   gene and identification of two regulatory regions required for its pigment
RT   cell-specific expression.";
RL   J. Biol. Chem. 269:27080-27087(1994).
RN   [9]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC   TISSUE=Melanoma;
RX   PubMed=12643545; DOI=10.1021/pr025562r;
RA   Basrur V., Yang F., Kushimoto T., Higashimoto Y., Yasumoto K., Valencia J.,
RA   Muller J., Vieira W.D., Watabe H., Shabanowitz J., Hearing V.J., Hunt D.F.,
RA   Appella E.;
RT   "Proteomic analysis of early melanosomes: identification of novel
RT   melanosomal proteins.";
RL   J. Proteome Res. 2:69-79(2003).
RN   [10]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC   TISSUE=Melanoma;
RX   PubMed=17081065; DOI=10.1021/pr060363j;
RA   Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J.,
RA   Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S.,
RA   Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.;
RT   "Proteomic and bioinformatic characterization of the biogenesis and
RT   function of melanosomes.";
RL   J. Proteome Res. 5:3135-3144(2006).
RN   [11]
RP   INTERACTION WITH TYR, AND INDUCTION BY BLUE LIGHT.
RX   PubMed=28842328; DOI=10.1016/j.jid.2017.07.833;
RA   Regazzetti C., Sormani L., Debayle D., Bernerd F., Tulic M.K.,
RA   De Donatis G.M., Chignon-Sicard B., Rocchi S., Passeron T.;
RT   "Melanocytes Sense Blue Light and Regulate Pigmentation through Opsin-3.";
RL   J. Invest. Dermatol. 138:171-178(2018).
RN   [12]
RP   VARIANTS OCA8 SER-40 AND TRP-61, AND FUNCTION.
RX   PubMed=33100333; DOI=10.1038/s41436-020-00997-8;
RA   Pennamen P., Tingaud-Sequeira A., Gazova I., Keighren M., McKie L.,
RA   Marlin S., Gherbi Halem S., Kaplan J., Delevoye C., Lacombe D.,
RA   Plaisant C., Michaud V., Lasseaux E., Javerzat S., Jackson I., Arveiler B.;
RT   "Dopachrome tautomerase variants in patients with oculocutaneous
RT   albinism.";
RL   Genet. Med. 23:479-487(2021).
CC   -!- FUNCTION: Plays a role in melanin biosynthesis (PubMed:33100333).
CC       Catalyzes the conversion of L-dopachrome into 5,6-dihydroxyindole-2-
CC       carboxylic acid (DHICA). {ECO:0000269|PubMed:33100333,
CC       ECO:0000269|PubMed:8306979}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-dopachrome = 5,6-dihydroxyindole-2-carboxylate;
CC         Xref=Rhea:RHEA:13041, ChEBI:CHEBI:16875, ChEBI:CHEBI:57509;
CC         EC=5.3.3.12; Evidence={ECO:0000250|UniProtKB:P29812};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P29812};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:P29812};
CC   -!- PATHWAY: Pigment biosynthesis; melanin biosynthesis.
CC       {ECO:0000269|PubMed:33100333}.
CC   -!- SUBUNIT: Forms an OPN3-dependent complex with TYR in response to blue
CC       light in melanocytes. {ECO:0000269|PubMed:28842328}.
CC   -!- INTERACTION:
CC       P40126; P60201-2: PLP1; NbExp=3; IntAct=EBI-18640065, EBI-12188331;
CC   -!- SUBCELLULAR LOCATION: Melanosome membrane {ECO:0000269|PubMed:12643545,
CC       ECO:0000269|PubMed:17081065}; Single-pass type I membrane protein
CC       {ECO:0000269|PubMed:12643545, ECO:0000269|PubMed:17081065}. Melanosome
CC       {ECO:0000250|UniProtKB:P29812}. Note=Proper trafficking to melanosome
CC       is regulated by SGSM2, ANKRD27, RAB9A, RAB32 and RAB38.
CC       {ECO:0000250|UniProtKB:P29812}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P40126-1; Sequence=Displayed;
CC       Name=2; Synonyms=TRP-2-6b;
CC         IsoId=P40126-2; Sequence=VSP_043581;
CC   -!- INDUCTION: Induced by blue light (415nm).
CC       {ECO:0000269|PubMed:28842328}.
CC   -!- PTM: Glycosylated. {ECO:0000250|UniProtKB:P29812}.
CC   -!- DISEASE: Albinism, oculocutaneous, 8 (OCA8) [MIM:619165]: A form of
CC       oculocutaneous albinism, a disorder of pigmentation characterized by
CC       reduced biosynthesis of melanin in the skin, hair and eyes. OCA8 is an
CC       autosomal recessive form characterized by mild hair and skin
CC       hypopigmentation, associated with ocular features including nystagmus,
CC       reduced visual acuity, iris transillumination, and hypopigmentation of
CC       the retina. {ECO:0000269|PubMed:33100333}. Note=The disease is caused
CC       by variants affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the tyrosinase family. {ECO:0000305}.
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DR   EMBL; D17547; BAA04484.1; -; mRNA.
DR   EMBL; L18967; AAA20870.1; -; mRNA.
DR   EMBL; S69231; AAC60627.1; -; mRNA.
DR   EMBL; DQ902581; ABI73976.1; -; mRNA.
DR   EMBL; AL139318; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC028311; AAH28311.1; -; mRNA.
DR   EMBL; L38953; AAC41925.1; -; Genomic_DNA.
DR   EMBL; D28767; BAA05956.1; -; Genomic_DNA.
DR   CCDS; CCDS45060.1; -. [P40126-2]
DR   CCDS; CCDS9470.1; -. [P40126-1]
DR   PIR; S43510; YRHUR2.
DR   RefSeq; NP_001123361.1; NM_001129889.2. [P40126-2]
DR   RefSeq; NP_001913.2; NM_001922.4. [P40126-1]
DR   PDB; 4HX1; X-ray; 1.80 A; C=180-188.
DR   PDBsum; 4HX1; -.
DR   AlphaFoldDB; P40126; -.
DR   SMR; P40126; -.
DR   BioGRID; 108006; 29.
DR   IntAct; P40126; 8.
DR   STRING; 9606.ENSP00000392762; -.
DR   TCDB; 9.B.423.1.3; the tysrosinase (tyr) family.
DR   GlyCosmos; P40126; 6 sites, No reported glycans.
DR   GlyGen; P40126; 7 sites, 1 O-linked glycan (1 site).
DR   iPTMnet; P40126; -.
DR   PhosphoSitePlus; P40126; -.
DR   BioMuta; DCT; -.
DR   DMDM; 731026; -.
DR   EPD; P40126; -.
DR   jPOST; P40126; -.
DR   MassIVE; P40126; -.
DR   PaxDb; 9606-ENSP00000392762; -.
DR   PeptideAtlas; P40126; -.
DR   ProteomicsDB; 55335; -. [P40126-1]
DR   ProteomicsDB; 55336; -. [P40126-2]
DR   Antibodypedia; 2252; 475 antibodies from 33 providers.
DR   DNASU; 1638; -.
DR   Ensembl; ENST00000377028.10; ENSP00000366227.4; ENSG00000080166.16. [P40126-1]
DR   Ensembl; ENST00000446125.1; ENSP00000392762.1; ENSG00000080166.16. [P40126-2]
DR   GeneID; 1638; -.
DR   KEGG; hsa:1638; -.
DR   MANE-Select; ENST00000377028.10; ENSP00000366227.4; NM_001922.5; NP_001913.2.
DR   UCSC; uc001vlv.6; human. [P40126-1]
DR   AGR; HGNC:2709; -.
DR   CTD; 1638; -.
DR   DisGeNET; 1638; -.
DR   GeneCards; DCT; -.
DR   HGNC; HGNC:2709; DCT.
DR   HPA; ENSG00000080166; Tissue enriched (skin).
DR   MalaCards; DCT; -.
DR   MIM; 191275; gene.
DR   MIM; 619165; phenotype.
DR   neXtProt; NX_P40126; -.
DR   OpenTargets; ENSG00000080166; -.
DR   Orphanet; 597733; Oculocutaneous albinism type 8.
DR   PharmGKB; PA27179; -.
DR   VEuPathDB; HostDB:ENSG00000080166; -.
DR   eggNOG; ENOG502QRNA; Eukaryota.
DR   GeneTree; ENSGT00940000156856; -.
DR   HOGENOM; CLU_038693_1_0_1; -.
DR   InParanoid; P40126; -.
DR   OMA; FFNRTCK; -.
DR   OrthoDB; 70287at2759; -.
DR   PhylomeDB; P40126; -.
DR   TreeFam; TF315865; -.
DR   PathwayCommons; P40126; -.
DR   Reactome; R-HSA-5662702; Melanin biosynthesis.
DR   SignaLink; P40126; -.
DR   SIGNOR; P40126; -.
DR   UniPathway; UPA00785; -.
DR   BioGRID-ORCS; 1638; 12 hits in 1152 CRISPR screens.
DR   ChiTaRS; DCT; human.
DR   GeneWiki; Dopachrome_tautomerase; -.
DR   GenomeRNAi; 1638; -.
DR   Pharos; P40126; Tbio.
DR   PRO; PR:P40126; -.
DR   Proteomes; UP000005640; Chromosome 13.
DR   RNAct; P40126; Protein.
DR   Bgee; ENSG00000080166; Expressed in upper leg skin and 126 other cell types or tissues.
DR   ExpressionAtlas; P40126; baseline and differential.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR   GO; GO:0042470; C:melanosome; ISS:UniProtKB.
DR   GO; GO:0033162; C:melanosome membrane; TAS:Reactome.
DR   GO; GO:0016020; C:membrane; TAS:ProtInc.
DR   GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR   GO; GO:0005507; F:copper ion binding; TAS:ProtInc.
DR   GO; GO:0004167; F:dopachrome isomerase activity; ISS:UniProtKB.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0048468; P:cell development; IEA:Ensembl.
DR   GO; GO:0048066; P:developmental pigmentation; IBA:GO_Central.
DR   GO; GO:0008544; P:epidermis development; TAS:ProtInc.
DR   GO; GO:0006583; P:melanin biosynthetic process from tyrosine; ISS:UniProtKB.
DR   GO; GO:0002052; P:positive regulation of neuroblast proliferation; IBA:GO_Central.
DR   GO; GO:0009637; P:response to blue light; IDA:UniProtKB.
DR   GO; GO:0021847; P:ventricular zone neuroblast division; IBA:GO_Central.
DR   Gene3D; 1.10.1280.10; Di-copper center containing domain from catechol oxidase; 1.
DR   InterPro; IPR008922; Di-copper_centre_dom_sf.
DR   InterPro; IPR002227; Tyrosinase_Cu-bd.
DR   PANTHER; PTHR11474:SF4; L-DOPACHROME TAUTOMERASE; 1.
DR   PANTHER; PTHR11474; TYROSINASE FAMILY MEMBER; 1.
DR   Pfam; PF00264; Tyrosinase; 1.
DR   PRINTS; PR00092; TYROSINASE.
DR   SUPFAM; SSF48056; Di-copper centre-containing domain; 1.
DR   PROSITE; PS00497; TYROSINASE_1; 1.
DR   PROSITE; PS00498; TYROSINASE_2; 1.
DR   Genevisible; P40126; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Albinism; Alternative splicing; Disease variant;
KW   Glycoprotein; Isomerase; Melanin biosynthesis; Membrane; Metal-binding;
KW   Reference proteome; Signal; Transmembrane; Transmembrane helix; Zinc.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..519
FT                   /note="L-dopachrome tautomerase"
FT                   /id="PRO_0000035892"
FT   TOPO_DOM        24..472
FT                   /note="Lumenal, melanosome"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        473..493
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        494..519
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   BINDING         189
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000250"
FT   BINDING         211
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000250"
FT   BINDING         220
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000250"
FT   BINDING         369
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250"
FT   BINDING         373
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250"
FT   BINDING         396
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        170
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        178
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        237
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        300
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        342
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        377
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         393
FT                   /note="V -> VVISNRLLYNATTNILEHVRKEKATKELPSLHVL (in isoform
FT                   2)"
FT                   /evidence="ECO:0000303|PubMed:11777994"
FT                   /id="VSP_043581"
FT   VARIANT         40
FT                   /note="C -> S (in OCA8; dbSNP:rs370729240)"
FT                   /evidence="ECO:0000269|PubMed:33100333"
FT                   /id="VAR_085343"
FT   VARIANT         61
FT                   /note="C -> W (in OCA8; dbSNP:rs1885297366)"
FT                   /evidence="ECO:0000269|PubMed:33100333"
FT                   /id="VAR_085344"
SQ   SEQUENCE   519 AA;  59145 MW;  AFDDF21768002A89 CRC64;
     MSPLWWGFLL SCLGCKILPG AQGQFPRVCM TVDSLVNKEC CPRLGAESAN VCGSQQGRGQ
     CTEVRADTRP WSGPYILRNQ DDRELWPRKF FHRTCKCTGN FAGYNCGDCK FGWTGPNCER
     KKPPVIRQNI HSLSPQEREQ FLGALDLAKK RVHPDYVITT QHWLGLLGPN GTQPQFANCS
     VYDFFVWLHY YSVRDTLLGP GRPYRAIDFS HQGPAFVTWH RYHLLCLERD LQRLIGNESF
     ALPYWNFATG RNECDVCTDQ LFGAARPDDP TLISRNSRFS SWETVCDSLD DYNHLVTLCN
     GTYEGLLRRN QMGRNSMKLP TLKDIRDCLS LQKFDNPPFF QNSTFSFRNA LEGFDKADGT
     LDSQVMSLHN LVHSFLNGTN ALPHSAANDP IFVVLHSFTD AIFDEWMKRF NPPADAWPQE
     LAPIGHNRMY NMVPFFPPVT NEELFLTSDQ LGYSYAIDLP VSVEETPGWP TTLLVVMGTL
     VALVGLFVLL AFLQYRRLRK GYTPLMETHL SSKRYTEEA
//