ID   CP2U1_HUMAN             Reviewed;         544 AA.
AC   Q7Z449; B2RMV7; Q96EQ6;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   27-MAR-2024, entry version 176.
DE   RecName: Full=Cytochrome P450 2U1 {ECO:0000303|PubMed:24563460};
DE   AltName: Full=Long-chain fatty acid omega-monooxygenase {ECO:0000305|PubMed:24563460};
DE            EC=1.14.14.80 {ECO:0000269|PubMed:14660610, ECO:0000269|PubMed:24563460};
GN   Name=CYP2U1 {ECO:0000303|PubMed:14660610,
GN   ECO:0000312|HGNC:HGNC:20582};
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), FUNCTION, SUBCELLULAR LOCATION,
RP   TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, CATALYTIC ACTIVITY, AND PATHWAY.
RC   TISSUE=Thymus;
RX   PubMed=14660610; DOI=10.1074/jbc.m311830200;
RA   Chuang S.S., Helvig C., Taimi M., Ramshaw H.A., Collop A.H., Amad M.,
RA   White J.A., Petkovich M., Jones G., Korczak B.;
RT   "CYP2U1, a novel human thymus- and brain-specific cytochrome P450,
RT   catalyzes omega- and (omega-1)-hydroxylation of fatty acids.";
RL   J. Biol. Chem. 279:6305-6314(2004).
RN   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Brain, and 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   [4]
RP   TISSUE SPECIFICITY.
RX   PubMed=14975754; DOI=10.1016/j.bbrc.2004.01.110;
RA   Karlgren M., Backlund M., Johansson I., Oscarson M., Ingelman-Sundberg M.;
RT   "Characterization and tissue distribution of a novel human cytochrome P450-
RT   CYP2U1.";
RL   Biochem. Biophys. Res. Commun. 315:679-685(2004).
RN   [5]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=15752708; DOI=10.1016/j.abb.2005.02.001;
RA   Choudhary D., Jansson I., Stoilov I., Sarfarazi M., Schenkman J.B.;
RT   "Expression patterns of mouse and human CYP orthologs (families 1-4) during
RT   development and in different adult tissues.";
RL   Arch. Biochem. Biophys. 436:50-61(2005).
RN   [6]
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP   PROTEIN SEQUENCE OF 60-544, AND PATHWAY.
RX   PubMed=24563460; DOI=10.1074/jbc.m114.550004;
RA   Siller M., Goyal S., Yoshimoto F.K., Xiao Y., Wei S., Guengerich F.P.;
RT   "Oxidation of endogenous N-arachidonoylserotonin by human cytochrome P450
RT   2U1.";
RL   J. Biol. Chem. 289:10476-10487(2014).
RN   [7]
RP   VARIANTS SPG56 ARG-262; VAL-316; GLY-380 AND TRP-488, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=23176821; DOI=10.1016/j.ajhg.2012.11.001;
RA   Tesson C., Nawara M., Salih M.A., Rossignol R., Zaki M.S., Al Balwi M.,
RA   Schule R., Mignot C., Obre E., Bouhouche A., Santorelli F.M., Durand C.M.,
RA   Oteyza A.C., El-Hachimi K.H., Al Drees A., Bouslam N., Lamari F.,
RA   Elmalik S.A., Kabiraj M.M., Seidahmed M.Z., Esteves T., Gaussen M.,
RA   Monin M.L., Gyapay G., Lechner D., Gonzalez M., Depienne C., Mochel F.,
RA   Lavie J., Schols L., Lacombe D., Yahyaoui M., Al Abdulkareem I.,
RA   Zuchner S., Yamashita A., Benomar A., Goizet C., Durr A., Gleeson J.G.,
RA   Darios F., Brice A., Stevanin G.;
RT   "Alteration of fatty-acid-metabolizing enzymes affects mitochondrial form
RT   and function in hereditary spastic paraplegia.";
RL   Am. J. Hum. Genet. 91:1051-1064(2012).
CC   -!- FUNCTION: A cytochrome P450 monooxygenase involved in the metabolism of
CC       arachidonic acid and its conjugates (PubMed:14660610, PubMed:24563460).
CC       Mechanistically, uses molecular oxygen inserting one oxygen atom into a
CC       substrate, and reducing the second into a water molecule, with two
CC       electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-
CC       ferrihemoprotein reductase) (PubMed:14660610, PubMed:24563460). Acts as
CC       an omega and omega-1 hydroxylase for arachidonic acid and possibly for
CC       other long chain fatty acids. May modulate the arachidonic acid
CC       signaling pathway and play a role in other fatty acid signaling
CC       processes (PubMed:14660610, PubMed:24563460). May down-regulate the
CC       biological activities of N-arachidonoyl-serotonin, an endocannabinoid
CC       that has anti-nociceptive effects through inhibition of fatty acid
CC       amide hydrolase FAAH, TRPV1 receptor and T-type calcium channels.
CC       Catalyzes C-2 oxidation of the indole ring of N-arachidonoyl-serotonin
CC       forming a less active product 2-oxo-N-arachidonoyl-serotonin
CC       (PubMed:24563460). {ECO:0000269|PubMed:14660610,
CC       ECO:0000269|PubMed:24563460}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an omega-methyl-long-chain fatty acid + O2 + reduced
CC         [NADPH--hemoprotein reductase] = an omega-hydroxy-long-chain fatty
CC         acid + H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC         Xref=Rhea:RHEA:56748, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:140991,
CC         ChEBI:CHEBI:140992; EC=1.14.14.80;
CC         Evidence={ECO:0000269|PubMed:14660610, ECO:0000269|PubMed:24563460};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56749;
CC         Evidence={ECO:0000305|PubMed:14660610, ECO:0000305|PubMed:24563460};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced
CC         [NADPH--hemoprotein reductase] = 19-hydroxy-(5Z,8Z,11Z,14Z)-
CC         eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC         reductase]; Xref=Rhea:RHEA:39759, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC         COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:32395, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC         ChEBI:CHEBI:76627; Evidence={ECO:0000269|PubMed:14660610,
CC         ECO:0000269|PubMed:24563460};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39760;
CC         Evidence={ECO:0000305|PubMed:14660610, ECO:0000305|PubMed:24563460};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced
CC         [NADPH--hemoprotein reductase] = 20-hydroxy-(5Z,8Z,11Z,14Z)-
CC         eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC         reductase]; Xref=Rhea:RHEA:39755, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC         COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:32395, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC         ChEBI:CHEBI:76624; Evidence={ECO:0000269|PubMed:14660610,
CC         ECO:0000269|PubMed:24563460};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39756;
CC         Evidence={ECO:0000305|PubMed:14660610, ECO:0000305|PubMed:24563460};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N-[(5Z,8Z,11Z,14Z)-eicosatetraenoyl]-serotonin + O2 + reduced
CC         [NADPH--hemoprotein reductase] = 2-oxo-N-[(5Z,8Z,11Z,14Z)-
CC         eicosatetraenoyl]-serotonin + H(+) + H2O + oxidized
CC         [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:50296, Rhea:RHEA-
CC         COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618,
CC         ChEBI:CHEBI:58210, ChEBI:CHEBI:132255, ChEBI:CHEBI:132256;
CC         Evidence={ECO:0000269|PubMed:24563460};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50297;
CC         Evidence={ECO:0000305|PubMed:24563460};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000269|PubMed:24563460};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=2.7 uM for arachidonic acid;
CC         KM=82 uM for N-arachidonoylserotonin {ECO:0000269|PubMed:24563460};
CC   -!- PATHWAY: Lipid metabolism; arachidonate metabolism.
CC       {ECO:0000305|PubMed:14660610, ECO:0000305|PubMed:24563460}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:14660610}; Multi-pass membrane protein
CC       {ECO:0000255}. Microsome membrane {ECO:0000269|PubMed:14660610}; Multi-
CC       pass membrane protein {ECO:0000255}. Mitochondrion inner membrane
CC       {ECO:0000269|PubMed:23176821}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q7Z449-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q7Z449-2; Sequence=VSP_026222, VSP_026223;
CC   -!- TISSUE SPECIFICITY: Widely expressed with stronger expression in
CC       thymus, heart and cerebellum. {ECO:0000269|PubMed:14660610,
CC       ECO:0000269|PubMed:14975754, ECO:0000269|PubMed:15752708}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in fetal thymus.
CC       {ECO:0000269|PubMed:14660610, ECO:0000269|PubMed:15752708}.
CC   -!- DISEASE: Spastic paraplegia 56, autosomal recessive, with or without
CC       pseudoxanthoma elasticum (SPG56) [MIM:615030]: A form of spastic
CC       paraplegia, a neurodegenerative disorder characterized by a slow,
CC       gradual, progressive weakness and spasticity of the lower limbs. Rate
CC       of progression and the severity of symptoms are quite variable. Initial
CC       symptoms may include difficulty with balance, weakness and stiffness in
CC       the legs, muscle spasms, and dragging the toes when walking.
CC       Complicated forms are recognized by additional variable features
CC       including spastic quadriparesis, seizures, dementia, amyotrophy,
CC       extrapyramidal disturbance, cerebral or cerebellar atrophy, optic
CC       atrophy, and peripheral neuropathy, as well as by extra neurological
CC       manifestations. In SPG56, upper limbs are often also affected. Some
CC       SPG56 patients may have a subclinical axonal neuropathy; others also
CC       have pseudoxanthoma elasticum. {ECO:0000269|PubMed:23176821}. Note=The
CC       disease is caused by variants affecting the gene represented in this
CC       entry.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AY343323; AAQ21380.1; -; mRNA.
DR   EMBL; CH471057; EAX06216.1; -; Genomic_DNA.
DR   EMBL; BC012027; AAH12027.1; -; mRNA.
DR   EMBL; BC132767; AAI32768.1; -; mRNA.
DR   EMBL; BC136483; AAI36484.1; -; mRNA.
DR   CCDS; CCDS34047.1; -. [Q7Z449-1]
DR   RefSeq; NP_898898.1; NM_183075.2. [Q7Z449-1]
DR   AlphaFoldDB; Q7Z449; -.
DR   SMR; Q7Z449; -.
DR   BioGRID; 125252; 6.
DR   IntAct; Q7Z449; 2.
DR   STRING; 9606.ENSP00000333212; -.
DR   BindingDB; Q7Z449; -.
DR   ChEMBL; CHEMBL4523986; -.
DR   SwissLipids; SLP:000001048; -.
DR   iPTMnet; Q7Z449; -.
DR   PhosphoSitePlus; Q7Z449; -.
DR   BioMuta; CYP2U1; -.
DR   DMDM; 74762432; -.
DR   EPD; Q7Z449; -.
DR   jPOST; Q7Z449; -.
DR   MassIVE; Q7Z449; -.
DR   MaxQB; Q7Z449; -.
DR   PaxDb; 9606-ENSP00000333212; -.
DR   PeptideAtlas; Q7Z449; -.
DR   ProteomicsDB; 69149; -. [Q7Z449-1]
DR   ProteomicsDB; 69150; -. [Q7Z449-2]
DR   Pumba; Q7Z449; -.
DR   Antibodypedia; 26251; 171 antibodies from 25 providers.
DR   DNASU; 113612; -.
DR   Ensembl; ENST00000332884.11; ENSP00000333212.6; ENSG00000155016.18. [Q7Z449-1]
DR   GeneID; 113612; -.
DR   KEGG; hsa:113612; -.
DR   MANE-Select; ENST00000332884.11; ENSP00000333212.6; NM_183075.3; NP_898898.1.
DR   UCSC; uc003hyp.4; human. [Q7Z449-1]
DR   AGR; HGNC:20582; -.
DR   CTD; 113612; -.
DR   DisGeNET; 113612; -.
DR   GeneCards; CYP2U1; -.
DR   HGNC; HGNC:20582; CYP2U1.
DR   HPA; ENSG00000155016; Tissue enriched (lymphoid).
DR   MalaCards; CYP2U1; -.
DR   MIM; 610670; gene.
DR   MIM; 615030; phenotype.
DR   neXtProt; NX_Q7Z449; -.
DR   OpenTargets; ENSG00000155016; -.
DR   Orphanet; 320411; Autosomal recessive spastic paraplegia type 56.
DR   PharmGKB; PA134924269; -.
DR   VEuPathDB; HostDB:ENSG00000155016; -.
DR   eggNOG; KOG0156; Eukaryota.
DR   GeneTree; ENSGT00940000157714; -.
DR   HOGENOM; CLU_001570_22_3_1; -.
DR   InParanoid; Q7Z449; -.
DR   OMA; EPCIQQG; -.
DR   OrthoDB; 2900138at2759; -.
DR   PhylomeDB; Q7Z449; -.
DR   TreeFam; TF352043; -.
DR   PathwayCommons; Q7Z449; -.
DR   Reactome; R-HSA-211958; Miscellaneous substrates.
DR   Reactome; R-HSA-2142816; Synthesis of (16-20)-hydroxyeicosatetraenoic acids (HETE).
DR   Reactome; R-HSA-5579011; Defective CYP2U1 causes SPG56.
DR   SABIO-RK; Q7Z449; -.
DR   SignaLink; Q7Z449; -.
DR   UniPathway; UPA00383; -.
DR   BioGRID-ORCS; 113612; 13 hits in 1153 CRISPR screens.
DR   ChiTaRS; CYP2U1; human.
DR   GeneWiki; CYP2U1; -.
DR   GenomeRNAi; 113612; -.
DR   Pharos; Q7Z449; Tbio.
DR   PRO; PR:Q7Z449; -.
DR   Proteomes; UP000005640; Chromosome 4.
DR   RNAct; Q7Z449; Protein.
DR   Bgee; ENSG00000155016; Expressed in thymus and 181 other cell types or tissues.
DR   ExpressionAtlas; Q7Z449; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0052869; F:arachidonic acid omega-hydroxylase activity; IDA:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0102033; F:long-chain fatty acid omega-hydroxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004497; F:monooxygenase activity; TAS:Reactome.
DR   GO; GO:0016712; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen; IBA:GO_Central.
DR   GO; GO:0008395; F:steroid hydroxylase activity; IBA:GO_Central.
DR   GO; GO:1903604; P:cytochrome metabolic process; TAS:Reactome.
DR   GO; GO:0097267; P:omega-hydroxylase P450 pathway; IDA:UniProtKB.
DR   GO; GO:0006082; P:organic acid metabolic process; IBA:GO_Central.
DR   GO; GO:0006805; P:xenobiotic metabolic process; IBA:GO_Central.
DR   CDD; cd20666; CYP2U1; 1.
DR   Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002401; Cyt_P450_E_grp-I.
DR   InterPro; IPR008069; Cyt_P450_E_grp-I_CYP2D-like.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   PANTHER; PTHR24300:SF281; CYTOCHROME P450 2U1; 1.
DR   PANTHER; PTHR24300; CYTOCHROME P450 508A4-RELATED; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR01686; EP450ICYP2D.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; Cytochrome P450; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
DR   Genevisible; Q7Z449; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Direct protein sequencing; Disease variant;
KW   Endoplasmic reticulum; Heme; Hereditary spastic paraplegia; Iron;
KW   Lipid metabolism; Membrane; Metal-binding; Microsome; Mitochondrion;
KW   Mitochondrion inner membrane; Monooxygenase; Neurodegeneration;
KW   Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..544
FT                   /note="Cytochrome P450 2U1"
FT                   /id="PRO_0000291756"
FT   TRANSMEM        30..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        113..133
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        261..281
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        342..362
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        495..515
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         490
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         164..168
FT                   /note="GVVFA -> ELFQE (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_026222"
FT   VAR_SEQ         169..544
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_026223"
FT   VARIANT         262
FT                   /note="C -> R (in SPG56; dbSNP:rs397514515)"
FT                   /evidence="ECO:0000269|PubMed:23176821"
FT                   /id="VAR_069575"
FT   VARIANT         316
FT                   /note="D -> V (in SPG56; dbSNP:rs397514513)"
FT                   /evidence="ECO:0000269|PubMed:23176821"
FT                   /id="VAR_069576"
FT   VARIANT         380
FT                   /note="E -> G (in SPG56; dbSNP:rs397514514)"
FT                   /evidence="ECO:0000269|PubMed:23176821"
FT                   /id="VAR_069577"
FT   VARIANT         488
FT                   /note="R -> W (in SPG56; dbSNP:rs141431913)"
FT                   /evidence="ECO:0000269|PubMed:23176821"
FT                   /id="VAR_069578"
SQ   SEQUENCE   544 AA;  61987 MW;  01A0729318605770 CRC64;
     MSSPGPSQPP AEDPPWPARL LRAPLGLLRL DPSGGALLLC GLVALLGWSW LRRRRARGIP
     PGPTPWPLVG NFGHVLLPPF LRRRSWLSSR TRAAGIDPSV IGPQVLLAHL ARVYGSIFSF
     FIGHYLVVVL SDFHSVREAL VQQAEVFSDR PRVPLISIVT KEKGVVFAHY GPVWRQQRKF
     SHSTLRHFGL GKLSLEPKII EEFKYVKAEM QKHGEDPFCP FSIISNAVSN IICSLCFGQR
     FDYTNSEFKK MLGFMSRGLE ICLNSQVLLV NICPWLYYLP FGPFKELRQI EKDITSFLKK
     IIKDHQESLD RENPQDFIDM YLLHMEEERK NNSNSSFDEE YLFYIIGDLF IAGTDTTTNS
     LLWCLLYMSL NPDVQEKVHE EIERVIGANR APSLTDKAQM PYTEATIMEV QRLTVVVPLA
     IPHMTSENTV LQGYTIPKGT LILPNLWSVH RDPAIWEKPE DFYPNRFLDD QGQLIKKETF
     IPFGIGKRVC MGEQLAKMEL FLMFVSLMQS FAFALPEDSK KPLLTGRFGL TLAPHPFNIT
     ISRR
//