DOLK_HUMAN
ID DOLK_HUMAN Reviewed; 538 AA.
AC Q9UPQ8; Q5SRE6;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Dolichol kinase;
DE EC=2.7.1.108 {ECO:0000269|PubMed:12213788, ECO:0000269|PubMed:16923818, ECO:0000269|PubMed:17273964};
DE AltName: Full=Transmembrane protein 15;
GN Name=DOLK; Synonyms=KIAA1094, TMEM15; ORFNames=UNQ2422/PRO4980;
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], CATALYTIC ACTIVITY, AND FUNCTION.
RC TISSUE=Brain;
RX PubMed=12213788; DOI=10.1093/glycob/cwf068;
RA Fernandez F., Shridas P., Jiang S., Aebi M., Waechter C.J.;
RT "Expression and characterization of a human cDNA that complements the
RT temperature-sensitive defect in dolichol kinase activity in the yeast
RT sec59-1 mutant: the enzymatic phosphorylation of dolichol and
RT diacylglycerol are catalyzed by separate CTP-mediated kinase activities in
RT Saccharomyces cerevisiae.";
RL Glycobiology 12:555-562(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=10470851; DOI=10.1093/dnares/6.3.197;
RA Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:197-205(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pancreas, and Spleen;
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 SUBCELLULAR LOCATION, TOPOLOGY, FUNCTION, CATALYTIC ACTIVITY, CTP-BINDING,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF GLY-443; ASP-451;
RP LYS-470; LYS-471; THR-472; GLU-474 AND GLY-475.
RX PubMed=16923818; DOI=10.1074/jbc.m604087200;
RA Shridas P., Waechter C.J.;
RT "Human dolichol kinase, a polytopic endoplasmic reticulum membrane protein
RT with a cytoplasmically oriented CTP-binding site.";
RL J. Biol. Chem. 281:31696-31704(2006).
RN [7]
RP VARIANTS CDG1M SER-99 AND SER-441, CHARACTERIZATION OF VARIANTS CDG1M
RP SER-99 AND SER-441, FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=17273964; DOI=10.1086/512130;
RA Kranz C., Jungeblut C., Denecke J., Erlekotte A., Sohlbach C., Debus V.,
RA Kehl H.G., Harms E., Reith A., Reichel S., Groebe H., Hammersen G.,
RA Schwarzer U., Marquardt T.;
RT "A defect in dolichol phosphate biosynthesis causes a new inherited
RT disorder with death in early infancy.";
RL Am. J. Hum. Genet. 80:433-440(2007).
CC -!- FUNCTION: Catalyzes CTP-mediated phosphorylation of dolichol, the
CC terminal step in de novo dolichyl monophosphate (Dol-P) biosynthesis
CC (PubMed:12213788, PubMed:16923818, PubMed:17273964). Dol-P is a lipid
CC carrier essential for the synthesis of N-linked and O-linked
CC oligosaccharides and for GPI anchors (PubMed:12213788).
CC {ECO:0000269|PubMed:12213788, ECO:0000269|PubMed:16923818,
CC ECO:0000269|PubMed:17273964}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CTP + di-trans,poly-cis-dolichol = a dolichyl phosphate + CDP
CC + H(+); Xref=Rhea:RHEA:13133, Rhea:RHEA-COMP:9517, Rhea:RHEA-
CC COMP:9521, ChEBI:CHEBI:15378, ChEBI:CHEBI:16091, ChEBI:CHEBI:37563,
CC ChEBI:CHEBI:57683, ChEBI:CHEBI:58069; EC=2.7.1.108;
CC Evidence={ECO:0000269|PubMed:12213788, ECO:0000269|PubMed:16923818,
CC ECO:0000269|PubMed:17273964};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13134;
CC Evidence={ECO:0000305|PubMed:16923818};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=22.8 uM for dolichol {ECO:0000269|PubMed:16923818};
CC KM=3.5 uM for CTP {ECO:0000269|PubMed:16923818};
CC -!- INTERACTION:
CC Q9UPQ8; Q92624: APPBP2; NbExp=3; IntAct=EBI-8645574, EBI-743771;
CC Q9UPQ8; P11912: CD79A; NbExp=3; IntAct=EBI-8645574, EBI-7797864;
CC Q9UPQ8; Q9H9P2: CHODL; NbExp=3; IntAct=EBI-8645574, EBI-17447707;
CC Q9UPQ8; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-8645574, EBI-6942903;
CC Q9UPQ8; Q92838: EDA; NbExp=6; IntAct=EBI-8645574, EBI-529425;
CC Q9UPQ8; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-8645574, EBI-18304435;
CC Q9UPQ8; Q8TBE3: FNDC9; NbExp=3; IntAct=EBI-8645574, EBI-12142257;
CC Q9UPQ8; P48165: GJA8; NbExp=3; IntAct=EBI-8645574, EBI-17458373;
CC Q9UPQ8; Q8TED1: GPX8; NbExp=3; IntAct=EBI-8645574, EBI-11721746;
CC Q9UPQ8; Q09470: KCNA1; NbExp=7; IntAct=EBI-8645574, EBI-8286599;
CC Q9UPQ8; Q16322: KCNA10; NbExp=5; IntAct=EBI-8645574, EBI-12265328;
CC Q9UPQ8; P22001: KCNA3; NbExp=6; IntAct=EBI-8645574, EBI-8627664;
CC Q9UPQ8; P17658: KCNA6; NbExp=4; IntAct=EBI-8645574, EBI-6426142;
CC Q9UPQ8; Q9HCJ2: LRRC4C; NbExp=4; IntAct=EBI-8645574, EBI-3925442;
CC Q9UPQ8; Q92536: SLC7A6; NbExp=3; IntAct=EBI-8645574, EBI-2880595;
CC Q9UPQ8; Q8TBG9: SYNPR; NbExp=3; IntAct=EBI-8645574, EBI-10273251;
CC Q9UPQ8; Q96B21: TMEM45B; NbExp=3; IntAct=EBI-8645574, EBI-3923061;
CC Q9UPQ8; Q96HE8: TMEM80; NbExp=3; IntAct=EBI-8645574, EBI-11742770;
CC Q9UPQ8; Q9H7M9: VSIR; NbExp=3; IntAct=EBI-8645574, EBI-744988;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:16923818}; Multi-pass membrane protein
CC {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- DISEASE: Congenital disorder of glycosylation 1M (CDG1M) [MIM:610768]:
CC A form of congenital disorder of glycosylation, a multisystem disorder
CC caused by a defect in glycoprotein biosynthesis and characterized by
CC under-glycosylated serum glycoproteins. Congenital disorders of
CC glycosylation result in a wide variety of clinical features, such as
CC defects in the nervous system development, psychomotor retardation,
CC dysmorphic features, hypotonia, coagulation disorders, and
CC immunodeficiency. The broad spectrum of features reflects the critical
CC role of N-glycoproteins during embryonic development, differentiation,
CC and maintenance of cell functions. CDG1M is a very severe disease with
CC death occurring in early life. {ECO:0000269|PubMed:17273964}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- MISCELLANEOUS: Complements the defects in growth, dolichol kinase
CC activity and protein N-glycosylation at the restrictive temperature in
CC yeast sec59 mutant cells. {ECO:0000269|PubMed:12213788}.
CC -!- SIMILARITY: Belongs to the polyprenol kinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA83046.2; 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; AB029017; BAA83046.2; ALT_INIT; mRNA.
DR EMBL; AY358759; AAQ89119.1; -; mRNA.
DR EMBL; AL672142; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC035556; AAH35556.1; -; mRNA.
DR CCDS; CCDS6915.1; -.
DR RefSeq; NP_055723.1; NM_014908.3.
DR AlphaFoldDB; Q9UPQ8; -.
DR BioGRID; 116517; 52.
DR IntAct; Q9UPQ8; 31.
DR MINT; Q9UPQ8; -.
DR STRING; 9606.ENSP00000361667; -.
DR iPTMnet; Q9UPQ8; -.
DR PhosphoSitePlus; Q9UPQ8; -.
DR BioMuta; DOLK; -.
DR DMDM; 20140913; -.
DR EPD; Q9UPQ8; -.
DR jPOST; Q9UPQ8; -.
DR MassIVE; Q9UPQ8; -.
DR MaxQB; Q9UPQ8; -.
DR PaxDb; Q9UPQ8; -.
DR PeptideAtlas; Q9UPQ8; -.
DR PRIDE; Q9UPQ8; -.
DR ProteomicsDB; 85419; -.
DR Antibodypedia; 53680; 75 antibodies from 18 providers.
DR DNASU; 22845; -.
DR Ensembl; ENST00000372586.4; ENSP00000361667.3; ENSG00000175283.8.
DR GeneID; 22845; -.
DR KEGG; hsa:22845; -.
DR MANE-Select; ENST00000372586.4; ENSP00000361667.3; NM_014908.4; NP_055723.1.
DR UCSC; uc004bwr.4; human.
DR CTD; 22845; -.
DR DisGeNET; 22845; -.
DR GeneCards; DOLK; -.
DR GeneReviews; DOLK; -.
DR HGNC; HGNC:23406; DOLK.
DR HPA; ENSG00000175283; Low tissue specificity.
DR MalaCards; DOLK; -.
DR MIM; 610746; gene.
DR MIM; 610768; phenotype.
DR neXtProt; NX_Q9UPQ8; -.
DR OpenTargets; ENSG00000175283; -.
DR Orphanet; 91131; DK1-CDG.
DR Orphanet; 154; Familial isolated dilated cardiomyopathy.
DR PharmGKB; PA162384054; -.
DR VEuPathDB; HostDB:ENSG00000175283; -.
DR eggNOG; KOG2468; Eukaryota.
DR GeneTree; ENSGT00390000004067; -.
DR HOGENOM; CLU_027611_2_1_1; -.
DR InParanoid; Q9UPQ8; -.
DR OMA; GPGGWLC; -.
DR OrthoDB; 1533260at2759; -.
DR PhylomeDB; Q9UPQ8; -.
DR TreeFam; TF323379; -.
DR BRENDA; 2.7.1.108; 2681.
DR PathwayCommons; Q9UPQ8; -.
DR Reactome; R-HSA-446199; Synthesis of Dolichyl-phosphate.
DR Reactome; R-HSA-4755583; Defective DOLK causes DOLK-CDG.
DR SignaLink; Q9UPQ8; -.
DR SIGNOR; Q9UPQ8; -.
DR BioGRID-ORCS; 22845; 374 hits in 1079 CRISPR screens.
DR GeneWiki; Dolichol_kinase; -.
DR GenomeRNAi; 22845; -.
DR Pharos; Q9UPQ8; Tbio.
DR PRO; PR:Q9UPQ8; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q9UPQ8; protein.
DR Bgee; ENSG00000175283; Expressed in stromal cell of endometrium and 178 other tissues.
DR ExpressionAtlas; Q9UPQ8; baseline and differential.
DR Genevisible; Q9UPQ8; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0004168; F:dolichol kinase activity; IDA:UniProtKB.
DR GO; GO:0006489; P:dolichyl diphosphate biosynthetic process; TAS:Reactome.
DR GO; GO:0043048; P:dolichyl monophosphate biosynthetic process; IDA:UniProtKB.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR InterPro; IPR026566; DOLK.
DR InterPro; IPR032974; Polypren_kinase.
DR PANTHER; PTHR13205; PTHR13205; 1.
DR PANTHER; PTHR13205:SF15; PTHR13205:SF15; 1.
PE 1: Evidence at protein level;
KW Congenital disorder of glycosylation; Disease variant;
KW Endoplasmic reticulum; Kinase; Lipid metabolism; Membrane;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..538
FT /note="Dolichol kinase"
FT /id="PRO_0000072595"
FT TOPO_DOM 1..13
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:16923818"
FT TRANSMEM 14..34
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 35..74
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 75..95
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 96..111
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 112..132
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 133..134
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 135..155
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 156..163
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 164..184
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 185..188
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 189..209
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 210..224
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 225..245
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 246..254
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 255..275
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 276..297
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 298..318
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 319..337
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 338..354
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 355..359
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 360..380
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 381..401
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 402..422
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 423..436
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 437..457
FT /note="Helical; Name=13"
FT /evidence="ECO:0000255"
FT TOPO_DOM 458..472
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:16923818"
FT TRANSMEM 473..493
FT /note="Helical; Name=14"
FT /evidence="ECO:0000255"
FT TOPO_DOM 494..495
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 496..516
FT /note="Helical; Name=15"
FT /evidence="ECO:0000255"
FT TOPO_DOM 517..538
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:16923818"
FT REGION 459..474
FT /note="CTP-binding"
FT /evidence="ECO:0000269|PubMed:16923818"
FT VARIANT 99
FT /note="C -> S (in CDG1M; 2% residual dolichol kinase
FT activity; fails to complement the temperature-sensitive
FT phenotype of DK1-deficient yeast cells; dbSNP:rs137853109)"
FT /evidence="ECO:0000269|PubMed:17273964"
FT /id="VAR_032851"
FT VARIANT 224
FT /note="D -> V (in dbSNP:rs17485436)"
FT /id="VAR_049709"
FT VARIANT 441
FT /note="Y -> S (in CDG1M; 4% residual dolichol kinase
FT activity; fails to complement the temperature-sensitive
FT phenotype of DK1-deficient yeast cells; dbSNP:rs137853110)"
FT /evidence="ECO:0000269|PubMed:17273964"
FT /id="VAR_032852"
FT MUTAGEN 443
FT /note="G->D: Abolishes dolichol kinase activity."
FT /evidence="ECO:0000269|PubMed:16923818"
FT MUTAGEN 451
FT /note="D->A: Reduces dolichol kinase activity."
FT /evidence="ECO:0000269|PubMed:16923818"
FT MUTAGEN 470
FT /note="K->A: Reduces dolichol kinase activity. Significant
FT reduction in binding affinity for CTP; when associated with
FT A-471."
FT /evidence="ECO:0000269|PubMed:16923818"
FT MUTAGEN 471
FT /note="K->A: Reduces dolichol kinase activity. Significant
FT reduction in binding affinity for CTP."
FT /evidence="ECO:0000269|PubMed:16923818"
FT MUTAGEN 472
FT /note="T->A: Reduces dolichol kinase activity. Significant
FT reduction in binding affinity for CTP."
FT /evidence="ECO:0000269|PubMed:16923818"
FT MUTAGEN 474
FT /note="E->A: No effect on dolichol kinase activity."
FT /evidence="ECO:0000269|PubMed:16923818"
FT MUTAGEN 475
FT /note="G->A: No effect on dolichol kinase activity."
FT /evidence="ECO:0000269|PubMed:16923818"
SQ SEQUENCE 538 AA; 59268 MW; EB7D1BABD45362AD CRC64;
MTRECPSPAP GPGAPLSGSV LAEAAVVFAV VLSIHATVWD RYSWCAVALA VQAFYVQYKW
DRLLQQGSAV FQFRMSANSG LLPASMVMPL LGLVMKERCQ TAGNPFFERF GIVVAATGMA
VALFSSVLAL GITRPVPTNT CVILGLAGGV IIYIMKHSLS VGEVIEVLEV LLIFVYLNMI
LLYLLPRCFT PGEALLVLGG ISFVLNQLIK RSLTLVESQG DPVDFFLLVV VVGMVLMGIF
FSTLFVFMDS GTWASSIFFH LMTCVLSLGV VLPWLHRLIR RNPLLWLLQF LFQTDTRIYL
LAYWSLLATL ACLVVLYQNA KRSSSESKKH QAPTIARKYF HLIVVATYIP GIIFDRPLLY
VAATVCLAVF IFLEYVRYFR IKPLGHTLRS FLSLFLDERD SGPLILTHIY LLLGMSLPIW
LIPRPCTQKG SLGGARALVP YAGVLAVGVG DTVASIFGST MGEIRWPGTK KTFEGTMTSI
FAQIISVALI LIFDSGVDLN YSYAWILGSI STVSLLEAYT TQIDNLLLPL YLLILLMA
