PHYD1_HUMAN
ID PHYD1_HUMAN Reviewed; 291 AA.
AC Q5SRE7; A6PWN9; A6PWP0; B3KT57; B4E3X8; Q5SRE9; Q5SRF0; Q7Z623; Q7Z7P9;
AC Q96GM4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Phytanoyl-CoA dioxygenase domain-containing protein 1 {ECO:0000303|PubMed:21530488};
DE Short=Protein PHYHD1 {ECO:0000303|PubMed:21530488};
DE EC=1.14.11.- {ECO:0000269|PubMed:21530488};
GN Name=PHYHD1 {ECO:0000312|HGNC:HGNC:23396};
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=Hippocampus;
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 [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Lung, and Muscle;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-55, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [6]
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 [7]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH IRON IONS AND
RP ALPHA-KETOGLUTARATE, FUNCTION, ACTIVITY REGULATION, AND COFACTOR.
RX PubMed=21530488; DOI=10.1016/j.bbrc.2011.04.059;
RA Zhang Z., Kochan G.T., Ng S.S., Kavanagh K.L., Oppermann U.,
RA Schofield C.J., McDonough M.A.;
RT "Crystal structure of PHYHD1A, a 2OG oxygenase related to phytanoyl-CoA
RT hydroxylase.";
RL Biochem. Biophys. Res. Commun. 408:553-558(2011).
CC -!- FUNCTION: 2-oxoglutarate(2OG)-dependent dioxygenase that catalyzes the
CC conversion of 2-oxoglutarate to succinate and CO(2) in an iron-
CC dependent manner (PubMed:21530488). However, does not couple 2OG
CC turnover to the hydroxylation of acyl-coenzyme A derivatives, implying
CC that it is not directly involved in phytanoyl coenzyme-A metabolism
CC (PubMed:21530488). Does not show detectable activity towards fatty acid
CC CoA thioesters (PubMed:21530488). {ECO:0000269|PubMed:21530488}.
CC -!- FUNCTION: [Isoform 2]: Isoform 2 probably lacks enzyme activity.
CC {ECO:0000269|PubMed:21530488}.
CC -!- FUNCTION: [Isoform 3]: Isoform 3 probably lacks enzyme activity.
CC {ECO:0000269|PubMed:21530488}.
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000269|PubMed:21530488};
CC -!- ACTIVITY REGULATION: Activity is increased by ascorbate. Inhibited by
CC myristoyl-CoA. {ECO:0000269|PubMed:21530488}.
CC -!- INTERACTION:
CC Q5SRE7; Q9NUX5: POT1; NbExp=2; IntAct=EBI-2623130, EBI-752420;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=A, PHYHD1A;
CC IsoId=Q5SRE7-1; Sequence=Displayed;
CC Name=2; Synonyms=C, PHYHD1C;
CC IsoId=Q5SRE7-2; Sequence=VSP_030077;
CC Name=3; Synonyms=B, PHYHD1B;
CC IsoId=Q5SRE7-3; Sequence=VSP_030078;
CC -!- SIMILARITY: Belongs to the PhyH family. PHYHD1 subfamily.
CC {ECO:0000305}.
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DR EMBL; AK095000; BAG52969.1; -; mRNA.
DR EMBL; AL672142; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471090; EAW87844.1; -; Genomic_DNA.
DR EMBL; CH471090; EAW87845.1; -; Genomic_DNA.
DR EMBL; CH471090; EAW87847.1; -; Genomic_DNA.
DR EMBL; BC009373; AAH09373.1; -; mRNA.
DR EMBL; BC051300; AAH51300.1; -; mRNA.
DR EMBL; BC053853; AAH53853.1; -; mRNA.
DR CCDS; CCDS43885.1; -. [Q5SRE7-1]
DR CCDS; CCDS43886.1; -. [Q5SRE7-2]
DR CCDS; CCDS6914.1; -. [Q5SRE7-3]
DR RefSeq; NP_001094346.1; NM_001100876.1. [Q5SRE7-1]
DR RefSeq; NP_001094347.1; NM_001100877.1. [Q5SRE7-2]
DR RefSeq; NP_777593.2; NM_174933.3. [Q5SRE7-3]
DR PDB; 2OPW; X-ray; 1.90 A; A=1-291.
DR PDB; 3OBZ; X-ray; 2.15 A; A=1-291.
DR PDBsum; 2OPW; -.
DR PDBsum; 3OBZ; -.
DR AlphaFoldDB; Q5SRE7; -.
DR SMR; Q5SRE7; -.
DR BioGRID; 129029; 7.
DR IntAct; Q5SRE7; 3.
DR STRING; 9606.ENSP00000309515; -.
DR GlyGen; Q5SRE7; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q5SRE7; -.
DR PhosphoSitePlus; Q5SRE7; -.
DR BioMuta; PHYHD1; -.
DR DMDM; 166220781; -.
DR EPD; Q5SRE7; -.
DR jPOST; Q5SRE7; -.
DR MassIVE; Q5SRE7; -.
DR MaxQB; Q5SRE7; -.
DR PaxDb; Q5SRE7; -.
DR PeptideAtlas; Q5SRE7; -.
DR PRIDE; Q5SRE7; -.
DR ProteomicsDB; 63846; -. [Q5SRE7-1]
DR ProteomicsDB; 63847; -. [Q5SRE7-2]
DR ProteomicsDB; 63848; -. [Q5SRE7-3]
DR Antibodypedia; 2006; 142 antibodies from 25 providers.
DR DNASU; 254295; -.
DR Ensembl; ENST00000308941.9; ENSP00000309515.5; ENSG00000175287.19. [Q5SRE7-3]
DR Ensembl; ENST00000353176.9; ENSP00000340945.5; ENSG00000175287.19. [Q5SRE7-2]
DR Ensembl; ENST00000372592.8; ENSP00000361673.3; ENSG00000175287.19. [Q5SRE7-1]
DR Ensembl; ENST00000421063.6; ENSP00000409928.2; ENSG00000175287.19. [Q5SRE7-2]
DR GeneID; 254295; -.
DR KEGG; hsa:254295; -.
DR MANE-Select; ENST00000372592.8; ENSP00000361673.3; NM_001100876.2; NP_001094346.1.
DR UCSC; uc004bwn.3; human. [Q5SRE7-1]
DR CTD; 254295; -.
DR DisGeNET; 254295; -.
DR GeneCards; PHYHD1; -.
DR HGNC; HGNC:23396; PHYHD1.
DR HPA; ENSG00000175287; Low tissue specificity.
DR neXtProt; NX_Q5SRE7; -.
DR OpenTargets; ENSG00000175287; -.
DR PharmGKB; PA134959674; -.
DR VEuPathDB; HostDB:ENSG00000175287; -.
DR eggNOG; KOG3290; Eukaryota.
DR GeneTree; ENSGT00390000006287; -.
DR HOGENOM; CLU_048953_0_0_1; -.
DR InParanoid; Q5SRE7; -.
DR OMA; KYSEDNW; -.
DR PhylomeDB; Q5SRE7; -.
DR TreeFam; TF300011; -.
DR PathwayCommons; Q5SRE7; -.
DR SignaLink; Q5SRE7; -.
DR BioGRID-ORCS; 254295; 10 hits in 1069 CRISPR screens.
DR ChiTaRS; PHYHD1; human.
DR EvolutionaryTrace; Q5SRE7; -.
DR GenomeRNAi; 254295; -.
DR Pharos; Q5SRE7; Tdark.
DR PRO; PR:Q5SRE7; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q5SRE7; protein.
DR Bgee; ENSG00000175287; Expressed in body of pancreas and 154 other tissues.
DR ExpressionAtlas; Q5SRE7; baseline and differential.
DR Genevisible; Q5SRE7; HS.
DR GO; GO:0016706; F:2-oxoglutarate-dependent dioxygenase activity; IDA:FlyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR008775; Phytyl_CoA_dOase.
DR Pfam; PF05721; PhyH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Dioxygenase; Iron; Metal-binding;
KW Oxidoreductase; Phosphoprotein; Reference proteome.
FT CHAIN 1..291
FT /note="Phytanoyl-CoA dioxygenase domain-containing protein
FT 1"
FT /id="PRO_0000313633"
FT BINDING 102
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:O14832"
FT BINDING 141
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:O14832"
FT BINDING 156..158
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:O14832"
FT BINDING 156
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:O14832"
FT BINDING 158
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:O14832"
FT BINDING 174
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:O14832"
FT BINDING 246
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:O14832"
FT BINDING 248
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:O14832"
FT BINDING 257
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:O14832"
FT MOD_RES 55
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT VAR_SEQ 125..145
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030077"
FT VAR_SEQ 146..291
FT /note="QPHFGGEVSPHQDASFLYTEPLGRVLGVWIAVEDATLENGCLWFIPGSHTSG
FT VSRRMVRAPVGSAPGTSFLGSEPARDNSLFVPTPVQRGALVLIHGEVVHKSKQNLSDRS
FT RQAYTFHLMEASGTTWSPENWLQPTAELPFPQLYT -> SPLIRTPPSCTRSPWAGCWA
FT CGSQWRMPRWRTAVSGSSLAPTPVVCQEGWSGPLLAQRLVPASLGQSQPGITASLCPPQ
FT CREGPWSSSMEKWYTRASRTSLTARARPTLSTSWRPLAPPGARRTGSSQQLNCPFPNCT
FT PKGSRRAGALAPPG (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030078"
FT VARIANT 222
FT /note="R -> W (in dbSNP:rs10988159)"
FT /id="VAR_050529"
FT HELIX 6..15
FT /evidence="ECO:0007829|PDB:2OPW"
FT STRAND 16..20
FT /evidence="ECO:0007829|PDB:2OPW"
FT HELIX 26..41
FT /evidence="ECO:0007829|PDB:2OPW"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:2OPW"
FT HELIX 56..71
FT /evidence="ECO:0007829|PDB:2OPW"
FT TURN 72..75
FT /evidence="ECO:0007829|PDB:2OPW"
FT STRAND 76..81
FT /evidence="ECO:0007829|PDB:2OPW"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:3OBZ"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:3OBZ"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:2OPW"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:2OPW"
FT STRAND 99..105
FT /evidence="ECO:0007829|PDB:2OPW"
FT HELIX 107..110
FT /evidence="ECO:0007829|PDB:2OPW"
FT HELIX 112..118
FT /evidence="ECO:0007829|PDB:2OPW"
FT HELIX 121..130
FT /evidence="ECO:0007829|PDB:2OPW"
FT STRAND 133..143
FT /evidence="ECO:0007829|PDB:2OPW"
FT TURN 147..149
FT /evidence="ECO:0007829|PDB:2OPW"
FT STRAND 153..156
FT /evidence="ECO:0007829|PDB:2OPW"
FT HELIX 158..160
FT /evidence="ECO:0007829|PDB:2OPW"
FT STRAND 164..168
FT /evidence="ECO:0007829|PDB:2OPW"
FT STRAND 170..178
FT /evidence="ECO:0007829|PDB:2OPW"
FT TURN 182..185
FT /evidence="ECO:0007829|PDB:2OPW"
FT STRAND 187..190
FT /evidence="ECO:0007829|PDB:2OPW"
FT STRAND 194..196
FT /evidence="ECO:0007829|PDB:2OPW"
FT STRAND 199..204
FT /evidence="ECO:0007829|PDB:2OPW"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:3OBZ"
FT STRAND 213..217
FT /evidence="ECO:0007829|PDB:2OPW"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:2OPW"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:2OPW"
FT STRAND 237..241
FT /evidence="ECO:0007829|PDB:2OPW"
FT STRAND 245..248
FT /evidence="ECO:0007829|PDB:2OPW"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:2OPW"
FT STRAND 259..266
FT /evidence="ECO:0007829|PDB:2OPW"
FT CONFLICT Q5SRE7-3:193
FT /note="E -> G (in Ref. 4; AAH09373)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 291 AA; 32411 MW; 7796A6C35A2E97DD CRC64;
MACLSPSQLQ KFQQDGFLVL EGFLSAEECV AMQQRIGEIV AEMDVPLHCR TEFSTQEEEQ
LRAQGSTDYF LSSGDKIRFF FEKGVFDEKG NFLVPPEKSI NKIGHALHAH DPVFKSITHS
FKVQTLARSL GLQMPVVVQS MYIFKQPHFG GEVSPHQDAS FLYTEPLGRV LGVWIAVEDA
TLENGCLWFI PGSHTSGVSR RMVRAPVGSA PGTSFLGSEP ARDNSLFVPT PVQRGALVLI
HGEVVHKSKQ NLSDRSRQAY TFHLMEASGT TWSPENWLQP TAELPFPQLY T
