ID   APOM_HUMAN              Reviewed;         188 AA.
AC   O95445; B0UX98; Q5SRP4; Q9P046; Q9UMP6;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 2.
DT   24-JAN-2024, entry version 192.
DE   RecName: Full=Apolipoprotein M;
DE            Short=Apo-M;
DE            Short=ApoM;
DE   AltName: Full=Protein G3a;
GN   Name=APOM; Synonyms=G3A, NG20; ORFNames=HSPC336;
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), AND PROTEIN SEQUENCE OF 1-15.
RC   TISSUE=Liver;
RX   PubMed=10531326; DOI=10.1074/jbc.274.44.31286;
RA   Xu N., Dahlbaeck B.;
RT   "A novel human apolipoprotein (apoM).";
RL   J. Biol. Chem. 274:31286-31290(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Thomson W., Campbell R.D.;
RT   "Characterisation of the novel gene G3a located in the class III region of
RT   the human major histocompatibility complex.";
RL   Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Umbilical cord blood;
RA   Ye M., Zhang Q.-H., Zhou J., Shen Y., Wu X.-Y., Guan Z.Q., Wang L.,
RA   Fan H.-Y., Mao Y.-F., Dai M., Huang Q.-H., Chen S.-J., Chen Z.;
RT   "Human partial CDS from CD34+ stem cells.";
RL   Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Shiina S., Tamiya G., Oka A., Inoko H.;
RT   "Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region.";
RL   Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=14656967; DOI=10.1101/gr.1736803;
RA   Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D.,
RA   Hood L.;
RT   "Analysis of the gene-dense major histocompatibility complex class III
RT   region and its comparison to mouse.";
RL   Genome Res. 13:2621-2636(2003).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Embryonic stem cell;
RX   PubMed=15146197; DOI=10.1038/nbt971;
RA   Brandenberger R., Wei H., Zhang S., Lei S., Murage J., Fisk G.J., Li Y.,
RA   Xu C., Fang R., Guegler K., Rao M.S., Mandalam R., Lebkowski J.,
RA   Stanton L.W.;
RT   "Transcriptome characterization elucidates signaling networks that control
RT   human ES cell growth and differentiation.";
RL   Nat. Biotechnol. 22:707-716(2004).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=14574404; DOI=10.1038/nature02055;
RA   Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA   Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA   Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA   Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA   Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA   Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA   French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA   Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA   Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA   Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA   Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA   Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA   Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA   Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA   Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA   Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA   Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA   Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA   Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA   Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA   West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA   Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA   Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA   Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [8]
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   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Liver;
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   [10]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-135.
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., Moore R.J.,
RA   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   [11]
RP   FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLN-22.
RX   PubMed=17525477; DOI=10.1194/jlr.m700103-jlr200;
RA   Ahnstrom J., Faber K., Axler O., Dahlback B.;
RT   "Hydrophobic ligand binding properties of the human lipocalin
RT   apolipoprotein M.";
RL   J. Lipid Res. 48:1754-1762(2007).
RN   [12]
RP   SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLN-22.
RX   PubMed=18279674; DOI=10.1016/j.febslet.2008.02.007;
RA   Axler O., Ahnstrom J., Dahlback B.;
RT   "Apolipoprotein M associates to lipoproteins through its retained signal
RT   peptide.";
RL   FEBS Lett. 582:826-828(2008).
RN   [13]
RP   SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLN-22.
RX   PubMed=18460466; DOI=10.1074/jbc.m800695200;
RA   Christoffersen C., Ahnstrom J., Axler O., Christensen E.I., Dahlback B.,
RA   Nielsen L.B.;
RT   "The signal peptide anchors apolipoprotein M in plasma lipoproteins and
RT   prevents rapid clearance of apolipoprotein M from plasma.";
RL   J. Biol. Chem. 283:18765-18772(2008).
RN   [14]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-135.
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 multiple
RT   enzyme digestion and hydrazide chemistry.";
RL   J. Proteome Res. 8:651-661(2009).
RN   [15]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [16]
RP   3D-STRUCTURE MODELING, AND MUTAGENESIS.
RX   PubMed=11418126; DOI=10.1016/s0014-5793(01)02544-3;
RA   Duan J., Dahlbaeck B., Villoutreix B.O.;
RT   "Proposed lipocalin fold for apolipoprotein M based on bioinformatics and
RT   site-directed mutagenesis.";
RL   FEBS Lett. 499:127-132(2001).
RN   [17]
RP   X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 22-188 IN COMPLEX WITH FATTY
RP   ACIDS, DISULFIDE BONDS, AND FUNCTION.
RX   PubMed=19733574; DOI=10.1016/j.jmb.2009.08.071;
RA   Sevvana M., Ahnstrom J., Egerer-Sieber C., Lange H.A., Dahlback B.,
RA   Muller Y.A.;
RT   "Serendipitous fatty acid binding reveals the structural determinants for
RT   ligand recognition in apolipoprotein M.";
RL   J. Mol. Biol. 393:920-936(2009).
CC   -!- FUNCTION: Probably involved in lipid transport. Can bind sphingosine-1-
CC       phosphate, myristic acid, palmitic acid and stearic acid, retinol, all-
CC       trans-retinoic acid and 9-cis-retinoic acid.
CC       {ECO:0000269|PubMed:17525477, ECO:0000269|PubMed:19733574}.
CC   -!- SUBUNIT: Interacts with LRP2; LRP2 mediates APOM renal uptake and
CC       subsequent lysosomal degradation. {ECO:0000250|UniProtKB:Q9Z1R3}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17525477,
CC       ECO:0000269|PubMed:18279674, ECO:0000269|PubMed:18460466}. Note=Present
CC       in high density lipoprotein (HDL) and to a lesser extent in
CC       triglyceride-rich lipoproteins (TGRLP) and low density lipoproteins
CC       (LDL).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=O95445-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O95445-2; Sequence=VSP_045586;
CC   -!- TISSUE SPECIFICITY: Plasma protein. Expressed in liver and kidney.
CC   -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
CC       Highly divergent. {ECO:0000305}.
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DR   EMBL; AF118393; AAD11443.2; -; mRNA.
DR   EMBL; AJ245434; CAB51604.1; -; mRNA.
DR   EMBL; AF161454; AAF29014.1; -; mRNA.
DR   EMBL; AF129756; AAD18084.1; -; Genomic_DNA.
DR   EMBL; CN428415; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BA000025; BAB63389.1; -; Genomic_DNA.
DR   EMBL; AL662801; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL670886; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL805934; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BX511262; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CR753842; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CR354443; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CR759761; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471081; EAX03461.1; -; Genomic_DNA.
DR   EMBL; CH471081; EAX03463.1; -; Genomic_DNA.
DR   EMBL; BC020683; AAH20683.1; -; mRNA.
DR   CCDS; CCDS4710.1; -. [O95445-1]
DR   CCDS; CCDS59004.1; -. [O95445-2]
DR   RefSeq; NP_001243098.1; NM_001256169.1. [O95445-2]
DR   RefSeq; NP_061974.2; NM_019101.2. [O95445-1]
DR   PDB; 2WEW; X-ray; 1.95 A; A=22-188.
DR   PDB; 2WEX; X-ray; 2.00 A; A=22-188.
DR   PDB; 2YG2; X-ray; 1.70 A; A/B=22-188.
DR   PDBsum; 2WEW; -.
DR   PDBsum; 2WEX; -.
DR   PDBsum; 2YG2; -.
DR   AlphaFoldDB; O95445; -.
DR   SMR; O95445; -.
DR   BioGRID; 121006; 53.
DR   IntAct; O95445; 8.
DR   STRING; 9606.ENSP00000365081; -.
DR   DrugBank; DB11886; Infigratinib.
DR   DrugBank; DB08231; Myristic acid.
DR   DrugBank; DB00877; Sirolimus.
DR   GlyConnect; 1015; 6 N-Linked glycans (1 site).
DR   GlyCosmos; O95445; 1 site, 11 glycans.
DR   GlyGen; O95445; 1 site, 12 N-linked glycans (1 site).
DR   iPTMnet; O95445; -.
DR   PhosphoSitePlus; O95445; -.
DR   BioMuta; APOM; -.
DR   CPTAC; non-CPTAC-1088; -.
DR   CPTAC; non-CPTAC-2630; -.
DR   jPOST; O95445; -.
DR   MassIVE; O95445; -.
DR   MaxQB; O95445; -.
DR   PaxDb; 9606-ENSP00000365081; -.
DR   PeptideAtlas; O95445; -.
DR   ProteomicsDB; 50881; -. [O95445-1]
DR   ProteomicsDB; 63861; -.
DR   Antibodypedia; 27445; 574 antibodies from 38 providers.
DR   DNASU; 55937; -.
DR   Ensembl; ENST00000375916.4; ENSP00000365081.3; ENSG00000204444.11. [O95445-1]
DR   Ensembl; ENST00000375920.8; ENSP00000365085.4; ENSG00000204444.11. [O95445-2]
DR   Ensembl; ENST00000383438.4; ENSP00000372930.4; ENSG00000206409.8. [O95445-1]
DR   Ensembl; ENST00000400157.7; ENSP00000383021.3; ENSG00000206409.8. [O95445-2]
DR   Ensembl; ENST00000416324.5; ENSP00000393581.1; ENSG00000224290.7. [O95445-2]
DR   Ensembl; ENST00000422771.6; ENSP00000392021.2; ENSG00000226215.6. [O95445-2]
DR   Ensembl; ENST00000425177.5; ENSP00000403062.1; ENSG00000235754.7. [O95445-2]
DR   Ensembl; ENST00000426800.2; ENSP00000405730.2; ENSG00000227567.7. [O95445-1]
DR   Ensembl; ENST00000430282.2; ENSP00000401684.2; ENSG00000224290.7. [O95445-1]
DR   Ensembl; ENST00000432598.2; ENSP00000389591.2; ENSG00000235754.7. [O95445-1]
DR   Ensembl; ENST00000436931.2; ENSP00000394610.2; ENSG00000231974.6. [O95445-1]
DR   Ensembl; ENST00000439902.5; ENSP00000413446.1; ENSG00000227567.7. [O95445-2]
DR   Ensembl; ENST00000441436.2; ENSP00000398944.2; ENSG00000226215.6. [O95445-1]
DR   Ensembl; ENST00000443975.6; ENSP00000416335.2; ENSG00000231974.6. [O95445-2]
DR   GeneID; 55937; -.
DR   KEGG; hsa:55937; -.
DR   MANE-Select; ENST00000375916.4; ENSP00000365081.3; NM_019101.3; NP_061974.2.
DR   UCSC; uc003nvk.5; human. [O95445-1]
DR   AGR; HGNC:13916; -.
DR   CTD; 55937; -.
DR   DisGeNET; 55937; -.
DR   GeneCards; APOM; -.
DR   HGNC; HGNC:13916; APOM.
DR   HPA; ENSG00000204444; Tissue enriched (liver).
DR   MIM; 606907; gene.
DR   neXtProt; NX_O95445; -.
DR   OpenTargets; ENSG00000204444; -.
DR   PharmGKB; PA38370; -.
DR   VEuPathDB; HostDB:ENSG00000204444; -.
DR   eggNOG; ENOG502S2IN; Eukaryota.
DR   GeneTree; ENSGT00390000001026; -.
DR   HOGENOM; CLU_2096113_0_0_1; -.
DR   InParanoid; O95445; -.
DR   OMA; FCVPRKW; -.
DR   OrthoDB; 4570312at2759; -.
DR   PhylomeDB; O95445; -.
DR   TreeFam; TF330771; -.
DR   PathwayCommons; O95445; -.
DR   Reactome; R-HSA-975634; Retinoid metabolism and transport.
DR   SignaLink; O95445; -.
DR   BioGRID-ORCS; 55937; 18 hits in 1153 CRISPR screens.
DR   ChiTaRS; APOM; human.
DR   EvolutionaryTrace; O95445; -.
DR   GeneWiki; APOM; -.
DR   GenomeRNAi; 55937; -.
DR   Pharos; O95445; Tbio.
DR   PRO; PR:O95445; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   RNAct; O95445; Protein.
DR   Bgee; ENSG00000204444; Expressed in right lobe of liver and 98 other cell types or tissues.
DR   ExpressionAtlas; O95445; baseline and differential.
DR   GO; GO:0034365; C:discoidal high-density lipoprotein particle; IDA:BHF-UCL.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0034364; C:high-density lipoprotein particle; IDA:BHF-UCL.
DR   GO; GO:0034362; C:low-density lipoprotein particle; IDA:BHF-UCL.
DR   GO; GO:0034366; C:spherical high-density lipoprotein particle; IDA:BHF-UCL.
DR   GO; GO:0034361; C:very-low-density lipoprotein particle; IDA:BHF-UCL.
DR   GO; GO:0016209; F:antioxidant activity; IDA:BHF-UCL.
DR   GO; GO:0005319; F:lipid transporter activity; IDA:BHF-UCL.
DR   GO; GO:0005543; F:phospholipid binding; IDA:BHF-UCL.
DR   GO; GO:0033344; P:cholesterol efflux; IDA:BHF-UCL.
DR   GO; GO:0042632; P:cholesterol homeostasis; IC:BHF-UCL.
DR   GO; GO:0034380; P:high-density lipoprotein particle assembly; ISS:BHF-UCL.
DR   GO; GO:0034384; P:high-density lipoprotein particle clearance; ISS:BHF-UCL.
DR   GO; GO:0034375; P:high-density lipoprotein particle remodeling; IMP:BHF-UCL.
DR   GO; GO:0042157; P:lipoprotein metabolic process; IEA:Ensembl.
DR   GO; GO:0034445; P:negative regulation of plasma lipoprotein oxidation; IDA:BHF-UCL.
DR   GO; GO:0043691; P:reverse cholesterol transport; ISS:BHF-UCL.
DR   CDD; cd19450; lipocalin_ApoM; 1.
DR   Gene3D; 2.40.128.20; -; 1.
DR   InterPro; IPR022734; ApoM.
DR   InterPro; IPR012674; Calycin.
DR   PANTHER; PTHR32028; APOLIPOPROTEIN M; 1.
DR   PANTHER; PTHR32028:SF1; APOLIPOPROTEIN M; 1.
DR   Pfam; PF11032; ApoM; 1.
DR   SUPFAM; SSF50814; Lipocalins; 1.
DR   Genevisible; O95445; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Direct protein sequencing;
KW   Disulfide bond; Glycoprotein; HDL; Lipid transport; Reference proteome;
KW   Secreted; Signal; Transport.
FT   CHAIN           1..188
FT                   /note="Apolipoprotein M"
FT                   /id="PRO_0000223278"
FT   SIGNAL          1..?22
FT                   /note="Not cleaved"
FT   BINDING         136
FT                   /ligand="tetradecanoate"
FT                   /ligand_id="ChEBI:CHEBI:30807"
FT                   /evidence="ECO:0000269|PubMed:19733574,
FT                   ECO:0007744|PDB:2WEW"
FT   BINDING         143
FT                   /ligand="tetradecanoate"
FT                   /ligand_id="ChEBI:CHEBI:30807"
FT                   /evidence="ECO:0000269|PubMed:19733574,
FT                   ECO:0007744|PDB:2WEW"
FT   CARBOHYD        135
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:16335952,
FT                   ECO:0000269|PubMed:19159218"
FT   DISULFID        23..167
FT                   /evidence="ECO:0000269|PubMed:19733574"
FT   DISULFID        95..183
FT                   /evidence="ECO:0000269|PubMed:19733574"
FT   DISULFID        128..157
FT                   /evidence="ECO:0000269|PubMed:19733574"
FT   VAR_SEQ         1..72
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15146197"
FT                   /id="VSP_045586"
FT   MUTAGEN         22
FT                   /note="Q->A: Introduces a signal cleavage site. Abolishes
FT                   interaction with lipoprotein particles. Leads to rapid
FT                   elimination from plasma."
FT                   /evidence="ECO:0000269|PubMed:17525477,
FT                   ECO:0000269|PubMed:18279674, ECO:0000269|PubMed:18460466"
FT   MUTAGEN         135
FT                   /note="N->Q: Loss of glycosylation."
FT                   /evidence="ECO:0000269|PubMed:11418126"
FT   MUTAGEN         148
FT                   /note="N->Q: No loss of glycosylation."
FT                   /evidence="ECO:0000269|PubMed:11418126"
FT   CONFLICT        1..38
FT                   /note="MFHQIWAALLYFYGIILNSIYQCPEHSQLTTLGVDGKE -> RFPDSIWGSR
FT                   SDTSGSPQVPKLYFCGARRESPQPQT (in Ref. 3; AAF29014)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        175..188
FT                   /note="LTPRNQEACELSNN -> VDS (in Ref. 2; CAB51604)"
FT                   /evidence="ECO:0000305"
FT   HELIX           36..38
FT                   /evidence="ECO:0007829|PDB:2WEW"
FT   HELIX           39..42
FT                   /evidence="ECO:0007829|PDB:2YG2"
FT   STRAND          45..56
FT                   /evidence="ECO:0007829|PDB:2YG2"
FT   HELIX           57..63
FT                   /evidence="ECO:0007829|PDB:2YG2"
FT   STRAND          66..75
FT                   /evidence="ECO:0007829|PDB:2YG2"
FT   STRAND          81..90
FT                   /evidence="ECO:0007829|PDB:2YG2"
FT   STRAND          95..104
FT                   /evidence="ECO:0007829|PDB:2YG2"
FT   STRAND          111..113
FT                   /evidence="ECO:0007829|PDB:2YG2"
FT   STRAND          116..124
FT                   /evidence="ECO:0007829|PDB:2YG2"
FT   STRAND          131..138
FT                   /evidence="ECO:0007829|PDB:2YG2"
FT   STRAND          141..152
FT                   /evidence="ECO:0007829|PDB:2YG2"
FT   HELIX           155..167
FT                   /evidence="ECO:0007829|PDB:2YG2"
FT   STRAND          172..175
FT                   /evidence="ECO:0007829|PDB:2YG2"
SQ   SEQUENCE   188 AA;  21253 MW;  E4C35FEC32B7CB86 CRC64;
     MFHQIWAALL YFYGIILNSI YQCPEHSQLT TLGVDGKEFP EVHLGQWYFI AGAAPTKEEL
     ATFDPVDNIV FNMAAGSAPM QLHLRATIRM KDGLCVPRKW IYHLTEGSTD LRTEGRPDMK
     TELFSSSCPG GIMLNETGQG YQRFLLYNRS PHPPEKCVEE FKSLTSCLDS KAFLLTPRNQ
     EACELSNN
//