ID   PLTP_HUMAN              Reviewed;         493 AA.
AC   P55058; A8K006; B4DDD5; B4DRB4; E1P5N8; E7EV16; Q8WTT1; Q9BR07;
AC   Q9BSH8;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   11-NOV-2015, entry version 152.
DE   RecName: Full=Phospholipid transfer protein;
DE   AltName: Full=Lipid transfer protein II;
DE   Flags: Precursor;
GN   Name=PLTP;
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 1), AND PROTEIN SEQUENCE OF 18-27
RP   AND 163-184.
RC   TISSUE=Umbilical vein endothelial cell;
RX   PubMed=8132678;
RA   Day J.R., Albers J.J., Lofton-Day C.E., Gilbert T.L., Ching A.F.T.,
RA   Grant F.J., O'Hara P.J., Marcovina S.M., Adolphson J.L.;
RT   "Complete cDNA encoding human phospholipid transfer protein from human
RT   endothelial cells.";
RL   J. Biol. Chem. 269:9388-9391(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Placenta;
RA   Kobayashi Y., Ohshiro N., Shibusawa A., Sasaki T., Tokuyama S.,
RA   Yamamoto T.;
RT   "Molecular cloning and functional characterization of phospholipid
RT   transfer protein from human placenta cDNA library.";
RL   Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM1 1),
RP   AND VARIANTS TYR-124 AND ILE-425.
RG   SeattleSNPs variation discovery resource;
RL   Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4).
RC   TISSUE=Adipose tissue;
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 [LARGE SCALE GENOMIC DNA].
RX   PubMed=11780052; DOI=10.1038/414865a;
RA   Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA   Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA   Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
RA   Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
RA   Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
RA   Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
RA   Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
RA   Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
RA   Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA   Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA   Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA   Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA   Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA   Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA   Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA   Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA   Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
RA   Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
RA   Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
RA   Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
RA   Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
RA   Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
RA   Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
RA   Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 20.";
RL   Nature 414:865-871(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Brain, and Placenta;
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   [8]
RP   DISULFIDE BOND.
RX   PubMed=10333293; DOI=10.1023/A:1020628006453;
RA   Qu S.J., Fan H.Z., Kilinc C., Pownall H.J.;
RT   "Role of cysteine residues in human plasma phospholipid transfer
RT   protein.";
RL   J. Protein Chem. 18:193-198(1999).
RN   [9]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-64; ASN-94; ASN-143;
RP   ASN-245 AND ASN-398.
RC   TISSUE=Plasma;
RX   PubMed=16335952; DOI=10.1021/pr0502065;
RA   Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
RA   Moore R.J., Smith R.D.;
RT   "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT   hydrazide chemistry, and mass spectrometry.";
RL   J. Proteome Res. 4:2070-2080(2005).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [11]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-64.
RC   TISSUE=Liver;
RX   PubMed=19159218; DOI=10.1021/pr8008012;
RA   Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT   "Glycoproteomics analysis of human liver tissue by combination of
RT   multiple enzyme digestion and hydrazide chemistry.";
RL   J. Proteome Res. 8:651-661(2009).
RN   [12]
RP   GLYCOSYLATION AT ASN-64; ASN-143 AND ASN-245.
RX   PubMed=19139490; DOI=10.1074/mcp.M800504-MCP200;
RA   Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F.,
RA   Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y.,
RA   Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.;
RT   "A strategy for precise and large scale identification of core
RT   fucosylated glycoproteins.";
RL   Mol. Cell. Proteomics 8:913-923(2009).
RN   [13]
RP   REVIEW ON FUNCTION.
RX   PubMed=21736953; DOI=10.1016/j.bbalip.2011.06.013;
RA   Albers J.J., Vuletic S., Cheung M.C.;
RT   "Role of plasma phospholipid transfer protein in lipid and lipoprotein
RT   metabolism.";
RL   Biochim. Biophys. Acta 1821:345-357(2012).
RN   [14]
RP   VARIANTS GLN-282; HIS-372 AND TRP-380.
RX   PubMed=12966036; DOI=10.1093/hmg/ddg314;
RA   Morabia A., Cayanis E., Costanza M.C., Ross B.M., Flaherty M.S.,
RA   Alvin G.B., Das K., Gilliam T.C.;
RT   "Association of extreme blood lipid profile phenotypic variation with
RT   11 reverse cholesterol transport genes and 10 non-genetic
RT   cardiovascular disease risk factors.";
RL   Hum. Mol. Genet. 12:2733-2743(2003).
CC   -!- FUNCTION: Facilitates the transfer of a spectrum of different
CC       lipid molecules, including diacylglycerol, phosphatidic acid,
CC       sphingomyelin, phosphatidylcholine, phosphatidylglycerol,
CC       cerebroside and phosphatidyl ethanolamine. Essential for the
CC       transfer of excess surface lipids from triglyceride-rich
CC       lipoproteins to HDL, thereby facilitating the formation of smaller
CC       lipoprotein remnants, contributing to the formation of LDL, and
CC       assisting in the maturation of HDL particles. PLTP also plays a
CC       key role in the uptake of cholesterol from peripheral cells and
CC       tissues that is subsequently transported to the liver for
CC       degradation and excretion. Two distinct forms of PLTP exist in
CC       plasma: an active form that can transfer PC from phospholipid
CC       vesicles to high-density lipoproteins (HDL), and an inactive form
CC       that lacks this capability.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=P55058-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P55058-2; Sequence=VSP_003050;
CC       Name=3;
CC         IsoId=P55058-3; Sequence=VSP_045877;
CC         Note=No experimental confirmation available.;
CC       Name=4;
CC         IsoId=P55058-4; Sequence=VSP_054028;
CC         Note=No experimental confirmation available.;
CC   -!- TISSUE SPECIFICITY: Wide tissue distribution. Placenta > pancreas
CC       > lung > kidney > heart > liver > skeletal muscle > brain.
CC   -!- SIMILARITY: Belongs to the BPI/LBP/Plunc superfamily. BPI/LBP
CC       family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=SeattleSNPs;
CC       URL="http://pga.gs.washington.edu/data/pltp/";
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DR   EMBL; L26232; AAA36443.1; -; mRNA.
DR   EMBL; AB076694; BAB79630.1; -; mRNA.
DR   EMBL; AL008726; CAA15499.1; -; Genomic_DNA.
DR   EMBL; AK289371; BAF82060.1; -; mRNA.
DR   EMBL; AK293150; BAG56696.1; -; mRNA.
DR   EMBL; AK299181; BAG61226.1; -; mRNA.
DR   EMBL; AL008726; CAC36020.1; -; Genomic_DNA.
DR   EMBL; AY509570; AAR87775.1; -; Genomic_DNA.
DR   EMBL; CH471077; EAW75782.1; -; Genomic_DNA.
DR   EMBL; CH471077; EAW75781.1; -; Genomic_DNA.
DR   EMBL; CH471077; EAW75783.1; -; Genomic_DNA.
DR   EMBL; CH471077; EAW75785.1; -; Genomic_DNA.
DR   EMBL; CH471077; EAW75787.1; -; Genomic_DNA.
DR   EMBL; BC005045; AAH05045.1; -; mRNA.
DR   EMBL; BC019847; AAH19847.1; -; mRNA.
DR   EMBL; BC019898; AAH19898.1; -; mRNA.
DR   CCDS; CCDS13386.1; -. [P55058-1]
DR   CCDS; CCDS13387.1; -. [P55058-2]
DR   CCDS; CCDS56196.1; -. [P55058-4]
DR   CCDS; CCDS56197.1; -. [P55058-3]
DR   PIR; A53533; A53533.
DR   RefSeq; NP_001229849.1; NM_001242920.1. [P55058-3]
DR   RefSeq; NP_001229850.1; NM_001242921.1. [P55058-4]
DR   RefSeq; NP_006218.1; NM_006227.3. [P55058-1]
DR   RefSeq; NP_872617.1; NM_182676.2. [P55058-2]
DR   UniGene; Hs.439312; -.
DR   ProteinModelPortal; P55058; -.
DR   SMR; P55058; 20-462.
DR   BioGrid; 111374; 32.
DR   STRING; 9606.ENSP00000361508; -.
DR   BindingDB; P55058; -.
DR   ChEMBL; CHEMBL5962; -.
DR   TCDB; 1.C.40.1.4; the bactericidal permeability increasing protein (bpip) family.
DR   PhosphoSite; P55058; -.
DR   BioMuta; PLTP; -.
DR   DMDM; 1709662; -.
DR   MaxQB; P55058; -.
DR   PaxDb; P55058; -.
DR   PRIDE; P55058; -.
DR   DNASU; 5360; -.
DR   Ensembl; ENST00000354050; ENSP00000335290; ENSG00000100979. [P55058-2]
DR   Ensembl; ENST00000372420; ENSP00000361497; ENSG00000100979. [P55058-4]
DR   Ensembl; ENST00000372431; ENSP00000361508; ENSG00000100979. [P55058-1]
DR   Ensembl; ENST00000420868; ENSP00000411671; ENSG00000100979. [P55058-3]
DR   Ensembl; ENST00000477313; ENSP00000417138; ENSG00000100979. [P55058-1]
DR   GeneID; 5360; -.
DR   KEGG; hsa:5360; -.
DR   UCSC; uc002xql.2; human. [P55058-1]
DR   UCSC; uc002xqo.2; human. [P55058-2]
DR   CTD; 5360; -.
DR   GeneCards; PLTP; -.
DR   HGNC; HGNC:9093; PLTP.
DR   HPA; CAB032873; -.
DR   HPA; HPA047207; -.
DR   MIM; 172425; gene.
DR   neXtProt; NX_P55058; -.
DR   PharmGKB; PA273; -.
DR   eggNOG; KOG4160; Eukaryota.
DR   eggNOG; ENOG410Z88E; LUCA.
DR   GeneTree; ENSGT00730000110583; -.
DR   HOGENOM; HOG000231006; -.
DR   HOVERGEN; HBG103156; -.
DR   InParanoid; P55058; -.
DR   KO; K08761; -.
DR   OMA; AFSEFFF; -.
DR   OrthoDB; EOG76739B; -.
DR   PhylomeDB; P55058; -.
DR   TreeFam; TF315617; -.
DR   Reactome; R-HSA-194223; HDL-mediated lipid transport.
DR   SignaLink; P55058; -.
DR   GeneWiki; Phospholipid_transfer_protein; -.
DR   GenomeRNAi; 5360; -.
DR   NextBio; 20778; -.
DR   PMAP-CutDB; P55058; -.
DR   PRO; PR:P55058; -.
DR   Proteomes; UP000005640; Chromosome 20.
DR   Bgee; P55058; -.
DR   CleanEx; HS_PLTP; -.
DR   Genevisible; P55058; HS.
DR   GO; GO:0005576; C:extracellular region; TAS:ProtInc.
DR   GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR   GO; GO:0008289; F:lipid binding; IEA:InterPro.
DR   GO; GO:0034375; P:high-density lipoprotein particle remodeling; IDA:AgBase.
DR   GO; GO:0006629; P:lipid metabolic process; TAS:ProtInc.
DR   GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR   GO; GO:0010875; P:positive regulation of cholesterol efflux; IDA:AgBase.
DR   GO; GO:0030317; P:sperm motility; IEA:Ensembl.
DR   GO; GO:0010189; P:vitamin E biosynthetic process; IEA:Ensembl.
DR   InterPro; IPR017943; Bactericidal_perm-incr_a/b_dom.
DR   InterPro; IPR030675; BPI/LBP.
DR   InterPro; IPR001124; Lipid-bd_serum_glycop_C.
DR   InterPro; IPR017954; Lipid-bd_serum_glycop_CS.
DR   InterPro; IPR017942; Lipid-bd_serum_glycop_N.
DR   InterPro; IPR030179; PLTP.
DR   PANTHER; PTHR10504:SF16; PTHR10504:SF16; 1.
DR   Pfam; PF01273; LBP_BPI_CETP; 1.
DR   Pfam; PF02886; LBP_BPI_CETP_C; 1.
DR   PIRSF; PIRSF002417; Lipid_binding_protein; 1.
DR   SMART; SM00328; BPI1; 1.
DR   SMART; SM00329; BPI2; 1.
DR   SUPFAM; SSF55394; SSF55394; 2.
DR   PROSITE; PS00400; LBP_BPI_CETP; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Complete proteome; Direct protein sequencing;
KW   Disulfide bond; Glycoprotein; Lipid transport; Polymorphism;
KW   Reference proteome; Secreted; Signal; Transport.
FT   SIGNAL        1     17       {ECO:0000269|PubMed:8132678}.
FT   CHAIN        18    493       Phospholipid transfer protein.
FT                                /FTId=PRO_0000017162.
FT   CARBOHYD     64     64       N-linked (GlcNAc...) (complex).
FT                                {ECO:0000269|PubMed:16335952,
FT                                ECO:0000269|PubMed:19139490,
FT                                ECO:0000269|PubMed:19159218}.
FT   CARBOHYD     94     94       N-linked (GlcNAc...).
FT                                {ECO:0000269|PubMed:16335952}.
FT   CARBOHYD    117    117       N-linked (GlcNAc...) (complex).
FT   CARBOHYD    143    143       N-linked (GlcNAc...).
FT                                {ECO:0000269|PubMed:16335952,
FT                                ECO:0000269|PubMed:19139490}.
FT   CARBOHYD    245    245       N-linked (GlcNAc...) (complex).
FT                                {ECO:0000269|PubMed:16335952,
FT                                ECO:0000269|PubMed:19139490}.
FT   CARBOHYD    398    398       N-linked (GlcNAc...).
FT                                {ECO:0000269|PubMed:16335952}.
FT   DISULFID    146    185       {ECO:0000269|PubMed:10333293}.
FT   VAR_SEQ       1     88       Missing (in isoform 4).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_054028.
FT   VAR_SEQ      68    162       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_045877.
FT   VAR_SEQ     110    162       FYDGGYINASAEGVSIRTGLELSRDPAGRMKVSNVSCQASV
FT                                SRMHAAFGGTFK -> L (in isoform 2).
FT                                {ECO:0000303|PubMed:14702039,
FT                                ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_003050.
FT   VARIANT     124    124       S -> Y (in dbSNP:rs11569636).
FT                                {ECO:0000269|Ref.3}.
FT                                /FTId=VAR_018879.
FT   VARIANT     282    282       R -> Q. {ECO:0000269|PubMed:12966036}.
FT                                /FTId=VAR_017020.
FT   VARIANT     372    372       R -> H. {ECO:0000269|PubMed:12966036}.
FT                                /FTId=VAR_017021.
FT   VARIANT     380    380       R -> W (in dbSNP:rs6065903).
FT                                {ECO:0000269|PubMed:12966036}.
FT                                /FTId=VAR_017022.
FT   VARIANT     425    425       M -> I (in dbSNP:rs11569675).
FT                                {ECO:0000269|Ref.3}.
FT                                /FTId=VAR_018880.
FT   VARIANT     444    444       F -> L (in dbSNP:rs1804161).
FT                                /FTId=VAR_012073.
FT   VARIANT     487    487       T -> K (in dbSNP:rs1056929).
FT                                /FTId=VAR_012074.
FT   CONFLICT     18     18       E -> V (in Ref. 7; AAH19847/AAH19898).
FT                                {ECO:0000305}.
FT   CONFLICT    331    331       A -> V (in Ref. 4; BAG61226).
FT                                {ECO:0000305}.
FT   CONFLICT    375    375       A -> S (in Ref. 4; BAG56696).
FT                                {ECO:0000305}.
SQ   SEQUENCE   493 AA;  54739 MW;  C6E4852F18E12317 CRC64;
     MALFGALFLA LLAGAHAEFP GCKIRVTSKA LELVKQEGLR FLEQELETIT IPDLRGKEGH
     FYYNISEVKV TELQLTSSEL DFQPQQELML QITNASLGLR FRRQLLYWFF YDGGYINASA
     EGVSIRTGLE LSRDPAGRMK VSNVSCQASV SRMHAAFGGT FKKVYDFLST FITSGMRFLL
     NQQICPVLYH AGTVLLNSLL DTVPVRSSVD ELVGIDYSLM KDPVASTSNL DMDFRGAFFP
     LTERNWSLPN RAVEPQLQEE ERMVYVAFSE FFFDSAMESY FRAGALQLLL VGDKVPHDLD
     MLLRATYFGS IVLLSPAVID SPLKLELRVL APPRCTIKPS GTTISVTASV TIALVPPDQP
     EVQLSSMTMD ARLSAKMALR GKALRTQLDL RRFRIYSNHS ALESLALIPL QAPLKTMLQI
     GVMPMLNERT WRGVQIPLPE GINFVHEVVT NHAGFLTIGA DLHFAKGLRE VIEKNRPADV
     RASTAPTPST AAV
//