ID   CP4F3_HUMAN             Reviewed;         520 AA.
AC   Q08477; B7Z8Z3; O60634; Q5U740;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 2.
DT   11-NOV-2015, entry version 156.
DE   RecName: Full=Docosahexaenoic acid omega-hydroxylase CYP4F3 {ECO:0000305};
DE            EC=1.14.13.199 {ECO:0000269|PubMed:16820285};
DE   AltName: Full=20-hydroxyeicosatetraenoic acid synthase {ECO:0000303|PubMed:11461919};
DE            Short=20-HETE synthase {ECO:0000303|PubMed:11461919};
DE            EC=1.14.13.- {ECO:0000269|PubMed:11461919, ECO:0000269|PubMed:16820285};
DE   AltName: Full=CYPIVF3;
DE   AltName: Full=Cytochrome P450 4F3;
DE   AltName: Full=Cytochrome P450-LTB-omega;
DE   AltName: Full=Leukotriene-B(4) 20-monooxygenase 2;
DE   AltName: Full=Leukotriene-B(4) omega-hydroxylase 2;
DE            EC=1.14.13.30 {ECO:0000269|PubMed:8486631};
GN   Name=CYP4F3; Synonyms=LTB4H;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CYP4F3A), VARIANT ASP-269,
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RC   TISSUE=Leukocyte;
RX   PubMed=8486631;
RA   Kikuta Y., Kusunose E., Endo K., Yamamoto S., Sogawa K.,
RA   Fujii-Kuriyama Y., Kusunose M.;
RT   "A novel form of cytochrome P-450 family 4 in human polymorphonuclear
RT   leukocytes. cDNA cloning and expression of leukotriene B4 omega-
RT   hydroxylase.";
RL   J. Biol. Chem. 268:9376-9380(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM CYP4F3A), AND
RP   VARIANT ASP-269.
RX   PubMed=9539102; DOI=10.1089/dna.1998.17.221;
RA   Kikuta Y., Kato M., Yamashita Y., Miyauchi Y., Tanaka K., Kamada N.,
RA   Kusunose M.;
RT   "Human leukotriene B4 omega-hydroxylase (CYP4F3) gene: molecular
RT   cloning and chromosomal localization.";
RL   DNA Cell Biol. 17:221-230(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CYP4F3B).
RC   TISSUE=Fetal liver;
RA   Peng X., Morgan K., Morgan T.R.;
RT   "A novel form of cytochrome P-450 family 4 in human fetal liver.";
RL   Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM CYP4F3B).
RC   TISSUE=Tongue, and Trachea;
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.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   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.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., 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   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ASP-269; ILE-270 AND
RP   THR-271.
RG   SeattleSNPs variation discovery resource;
RL   Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15057824; DOI=10.1038/nature02399;
RA   Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
RA   Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA   Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA   Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA   Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA   Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA   Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA   Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA   Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA   Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA   Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA   Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA   Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA   Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA   Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA   Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA   Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA   Rubin E.M., Lucas S.M.;
RT   "The DNA sequence and biology of human chromosome 19.";
RL   Nature 428:529-535(2004).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM CYP4F3B).
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [9]
RP   ALTERNATIVE SPLICING, AND ALTERNATIVE PROMOTER USAGE.
RX   PubMed=10409674; DOI=10.1074/jbc.274.30.21191;
RA   Christmas P., Ursino S.R., Fox J.W., Soberman R.J.;
RT   "Expression of the CYP4F3 gene. tissue-specific splicing and
RT   alternative promoters generate high and low K(m) forms of leukotriene
RT   B(4) omega-hydroxylase.";
RL   J. Biol. Chem. 274:21191-21199(1999).
RN   [10]
RP   ALTERNATIVE SPLICING, FUNCTION, SUBSTRATE SPECIFICITY, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=11461919; DOI=10.1074/jbc.M104818200;
RA   Christmas P., Jones J.P., Patten C.J., Rock D.A., Zheng Y.,
RA   Cheng S.M., Weber B.M., Carlesso N., Scadden D.T., Rettie A.E.,
RA   Soberman R.J.;
RT   "Alternative splicing determines the function of CYP4F3 by switching
RT   substrate specificity.";
RL   J. Biol. Chem. 276:38166-38172(2001).
RN   [11]
RP   FUNCTION (ISOFORM CYP4F3B), AND CATALYTIC ACTIVITY (ISOFORM CYP4F3B).
RX   PubMed=16820285; DOI=10.1016/j.plefa.2006.05.005;
RA   Harmon S.D., Fang X., Kaduce T.L., Hu S., Raj Gopal V., Falck J.R.,
RA   Spector A.A.;
RT   "Oxygenation of omega-3 fatty acids by human cytochrome P450 4F3B:
RT   effect on 20-hydroxyeicosatetraenoic acid production.";
RL   Prostaglandins Leukot. Essent. Fatty Acids 75:169-177(2006).
RN   [12]
RP   FUNCTION.
RX   PubMed=18577768; DOI=10.1194/jlr.M800199-JLR200;
RA   Fer M., Corcos L., Dreano Y., Plee-Gautier E., Salaun J.P.,
RA   Berthou F., Amet Y.;
RT   "Cytochromes P450 from family 4 are the main omega hydroxylating
RT   enzymes in humans: CYP4F3B is the prominent player in PUFA
RT   metabolism.";
RL   J. Lipid Res. 49:2379-2389(2008).
CC   -!- FUNCTION: Isoform CYP4F3A: Catalyzes the omega-hydroxylation of
CC       leukotriene-B(4), a potent chemoattractant for polymorphonuclear
CC       leukocytes, it has low activity for arachidonic acid.
CC       {ECO:0000269|PubMed:11461919, ECO:0000269|PubMed:8486631}.
CC   -!- FUNCTION: Isoform CYP4F3B: Shows arachidonic acid omega-
CC       hydroxylase activity by mediating conversion of arachidonic acid
CC       to 20-hydroxyeicosatetraenoic acid (20-HETE) (PubMed:11461919,
CC       PubMed:16820285). Has a 30-fold higher Km for leukotriene-B(4)
CC       compared with CYP4F3A (PubMed:11461919). Also converts
CC       eicosapentaenoate (EPA) to 20-hydroxyeicosapentaenoate (20-OH-EPA)
CC       (PubMed:16820285). Acts as a polyunsaturated omega-3 fatty acids
CC       hydroxylase: mediates conversion of docosahexaenoate (DHA) to 22-
CC       hydroxydocosahexaenoate (PubMed:16820285).
CC       {ECO:0000269|PubMed:11461919, ECO:0000269|PubMed:16820285,
CC       ECO:0000269|PubMed:18577768}.
CC   -!- CATALYTIC ACTIVITY: Docosahexaenoate + NADPH + O(2) = 22-
CC       hydroxydocosahexaenoate + NADP(+) + H(2)O.
CC       {ECO:0000269|PubMed:16820285}.
CC   -!- CATALYTIC ACTIVITY: (5Z,8Z,11Z,14Z)-icosatetraenoate + NADPH +
CC       O(2) = (5Z,8Z,11Z,14Z)-20-hydroxyicosa-5,8,11,14-tetraenoate +
CC       NADP(+) + H(2)O. {ECO:0000269|PubMed:11461919,
CC       ECO:0000269|PubMed:16820285}.
CC   -!- CATALYTIC ACTIVITY: (6Z,8E,10E,14Z)-(5S,12R)-5,12-dihydroxyicosa-
CC       6,8,10,14-tetraenoate + NADPH + O(2) = (6Z,8E,10E,14Z)-(5S,12R)-
CC       5,12,20-trihydroxyicosa-6,8,10,14-tetraenoate + NADP(+) + H(2)O.
CC       {ECO:0000269|PubMed:8486631}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:P51869};
CC   -!- ENZYME REGULATION: Inhibited by carbon monoxide (CO).
CC   -!- PATHWAY: Lipid metabolism; leukotriene B4 degradation.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
CC       Microsome membrane {ECO:0000250}; Single-pass membrane protein
CC       {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative promoter usage, Alternative splicing; Named isoforms=2;
CC       Name=CYP4F3A;
CC         IsoId=Q08477-1; Sequence=Displayed;
CC       Name=CYP4F3B;
CC         IsoId=Q08477-2; Sequence=VSP_047193;
CC   -!- TISSUE SPECIFICITY: Isoform CYP4F3A is expressed in the
CC       polymorphonuclear leukocytes as well as leukocytes and bone
CC       marrow. Isoform CYP4F3B is selectively expressed in liver and
CC       kidney and is also the predominant CYP4F isoform in trachea and
CC       tissues of the gastrointestinal tract.
CC       {ECO:0000269|PubMed:11461919}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=SeattleSNPs;
CC       URL="http://pga.gs.washington.edu/data/cyp4f3/";
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DR   EMBL; D12620; BAA02144.1; -; mRNA.
DR   EMBL; D12621; BAA02145.1; -; mRNA.
DR   EMBL; AB002454; BAA25990.1; -; mRNA.
DR   EMBL; AB002461; BAA25991.1; -; Genomic_DNA.
DR   EMBL; AF054821; AAC08589.1; -; mRNA.
DR   EMBL; AK304200; BAH14129.1; -; mRNA.
DR   EMBL; AK316136; BAH14507.1; -; mRNA.
DR   EMBL; AY792513; AAV40834.1; -; Genomic_DNA.
DR   EMBL; AD000685; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471106; EAW84489.1; -; Genomic_DNA.
DR   EMBL; BC136299; AAI36300.1; -; mRNA.
DR   CCDS; CCDS12332.1; -. [Q08477-1]
DR   CCDS; CCDS59362.1; -. [Q08477-2]
DR   PIR; A46661; A46661.
DR   RefSeq; NP_000887.2; NM_000896.2. [Q08477-1]
DR   RefSeq; NP_001186137.1; NM_001199208.1. [Q08477-2]
DR   RefSeq; NP_001186138.1; NM_001199209.1. [Q08477-2]
DR   UniGene; Hs.106242; -.
DR   ProteinModelPortal; Q08477; -.
DR   SMR; Q08477; 98-510.
DR   IntAct; Q08477; 2.
DR   STRING; 9606.ENSP00000221307; -.
DR   PhosphoSite; Q08477; -.
DR   BioMuta; CYP4F3; -.
DR   DMDM; 56757430; -.
DR   PaxDb; Q08477; -.
DR   PRIDE; Q08477; -.
DR   Ensembl; ENST00000221307; ENSP00000221307; ENSG00000186529. [Q08477-1]
DR   Ensembl; ENST00000585846; ENSP00000468105; ENSG00000186529. [Q08477-2]
DR   Ensembl; ENST00000586182; ENSP00000466395; ENSG00000186529. [Q08477-2]
DR   Ensembl; ENST00000591058; ENSP00000466988; ENSG00000186529. [Q08477-2]
DR   GeneID; 4051; -.
DR   KEGG; hsa:4051; -.
DR   UCSC; uc002nbj.3; human. [Q08477-1]
DR   UCSC; uc002nbk.3; human.
DR   CTD; 4051; -.
DR   GeneCards; CYP4F3; -.
DR   H-InvDB; HIX0039919; -.
DR   H-InvDB; HIX0169080; -.
DR   H-InvDB; HIX0169326; -.
DR   HGNC; HGNC:2646; CYP4F3.
DR   HPA; HPA058960; -.
DR   MIM; 601270; gene.
DR   neXtProt; NX_Q08477; -.
DR   PharmGKB; PA234; -.
DR   eggNOG; KOG0157; Eukaryota.
DR   eggNOG; COG2124; LUCA.
DR   GeneTree; ENSGT00760000118816; -.
DR   HOGENOM; HOG000233833; -.
DR   HOVERGEN; HBG000182; -.
DR   InParanoid; Q08477; -.
DR   KO; K17726; -.
DR   OMA; RFCHPNI; -.
DR   OrthoDB; EOG7CNZFK; -.
DR   PhylomeDB; Q08477; -.
DR   TreeFam; TF105088; -.
DR   Reactome; R-HSA-211935; Fatty acids.
DR   Reactome; R-HSA-211958; Miscellaneous substrates.
DR   Reactome; R-HSA-211979; Eicosanoids.
DR   Reactome; R-HSA-2142691; Synthesis of Leukotrienes (LT) and Eoxins (EX).
DR   SABIO-RK; Q08477; -.
DR   UniPathway; UPA00883; -.
DR   GeneWiki; CYP4F3; -.
DR   GenomeRNAi; 4051; -.
DR   NextBio; 15870; -.
DR   PRO; PR:Q08477; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   Bgee; Q08477; -.
DR   CleanEx; HS_CYP4F3; -.
DR   ExpressionAtlas; Q08477; baseline and differential.
DR   Genevisible; Q08477; HS.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0052871; F:alpha-tocopherol omega-hydroxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0050051; F:leukotriene-B4 20-monooxygenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004497; F:monooxygenase activity; TAS:ProtInc.
DR   GO; GO:0019369; P:arachidonic acid metabolic process; TAS:Reactome.
DR   GO; GO:0006690; P:icosanoid metabolic process; TAS:Reactome.
DR   GO; GO:0006691; P:leukotriene metabolic process; TAS:Reactome.
DR   GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR   GO; GO:0006805; P:xenobiotic metabolic process; TAS:Reactome.
DR   Gene3D; 1.10.630.10; -; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002401; Cyt_P450_E_grp-I.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; SSF48264; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   1: Evidence at protein level;
KW   Alternative promoter usage; Alternative splicing; Complete proteome;
KW   Endoplasmic reticulum; Heme; Iron; Lipid metabolism; Membrane;
KW   Metal-binding; Microsome; Monooxygenase; NADP; Oxidoreductase;
KW   Polymorphism; Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN         1    520       Docosahexaenoic acid omega-hydroxylase
FT                                CYP4F3.
FT                                /FTId=PRO_0000051851.
FT   TRANSMEM     11     31       Helical. {ECO:0000255}.
FT   METAL       468    468       Iron (heme axial ligand).
FT                                {ECO:0000250|UniProtKB:P51869}.
FT   BINDING     328    328       Heme (covalent; via 1 link).
FT                                {ECO:0000250|UniProtKB:P51869}.
FT   VAR_SEQ      67    114       IHSSEEGLLYTQSLACTFGDMCCWWVGPWHAIVRIFHPTYI
FT                                KPVLFAP -> VTPTEQGMRVLTQLVATYPQGFKVWMGPIF
FT                                PVIRFCHPNIIRSVINAS (in isoform CYP4F3B).
FT                                {ECO:0000303|PubMed:14702039,
FT                                ECO:0000303|PubMed:15489334,
FT                                ECO:0000303|Ref.3}.
FT                                /FTId=VSP_047193.
FT   VARIANT      96     96       H -> Q (in dbSNP:rs34923393).
FT                                /FTId=VAR_048457.
FT   VARIANT     106    106       Y -> C (in dbSNP:rs35888783).
FT                                /FTId=VAR_048458.
FT   VARIANT     269    269       A -> D (in dbSNP:rs1805040).
FT                                {ECO:0000269|PubMed:8486631,
FT                                ECO:0000269|PubMed:9539102,
FT                                ECO:0000269|Ref.5}.
FT                                /FTId=VAR_001258.
FT   VARIANT     270    270       V -> I (in dbSNP:rs28371536).
FT                                {ECO:0000269|Ref.5}.
FT                                /FTId=VAR_020664.
FT   VARIANT     271    271       I -> T (in dbSNP:rs28371479).
FT                                {ECO:0000269|Ref.5}.
FT                                /FTId=VAR_020665.
FT   CONFLICT    184    186       EGS -> KGY (in Ref. 3; AAC08589).
FT                                {ECO:0000305}.
FT   CONFLICT    488    488       R -> A (in Ref. 1; BAA02144 and 2;
FT                                BAA25990/BAA25991). {ECO:0000305}.
FT   CONFLICT    512    512       L -> I (in Ref. 3; AAC08589).
FT                                {ECO:0000305}.
SQ   SEQUENCE   520 AA;  59847 MW;  2519D875280CF9DC CRC64;
     MPQLSLSSLG LWPMAASPWL LLLLVGASWL LARILAWTYT FYDNCCRLRC FPQPPKRNWF
     LGHLGLIHSS EEGLLYTQSL ACTFGDMCCW WVGPWHAIVR IFHPTYIKPV LFAPAAIVPK
     DKVFYSFLKP WLGDGLLLSA GEKWSRHRRM LTPAFHFNIL KPYMKIFNES VNIMHAKWQL
     LASEGSARLD MFEHISLMTL DSLQKCVFSF DSHCQEKPSE YIAAILELSA LVTKRHQQIL
     LYIDFLYYLT PDGQRFRRAC RLVHDFTDAV IQERRRTLPS QGVDDFLQAK AKSKTLDFID
     VLLLSKDEDG KKLSDEDIRA EADTFMFEGH DTTASGLSWV LYHLAKHPEY QERCRQEVQE
     LLKDREPKEI EWDDLAQLPF LTMCIKESLR LHPPVPAVSR CCTQDIVLPD GRVIPKGIIC
     LISVFGTHHN PAVWPDPEVY DPFRFDPKNI KERSPLAFIP FSAGPRNCIG QAFAMAEMKV
     VLGLTLLRFR VLPDHTEPRR KPELVLRAEG GLWLRVEPLS
//