APOM_HUMAN
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 03-AUG-2022, entry version 184.
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; 52.
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 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; O95445; -.
DR PeptideAtlas; O95445; -.
DR PRIDE; O95445; -.
DR ProteomicsDB; 50881; -. [O95445-1]
DR ProteomicsDB; 63861; -.
DR Antibodypedia; 27445; 535 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 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; GYQRFLF; -.
DR OrthoDB; 1302737at2759; -.
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; 16 hits in 1075 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 96 other tissues.
DR ExpressionAtlas; O95445; baseline and differential.
DR Genevisible; O95445; HS.
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 Gene3D; 2.40.128.20; -; 1.
DR InterPro; IPR022734; ApoM.
DR InterPro; IPR012674; Calycin.
DR PANTHER; PTHR32028; PTHR32028; 1.
DR Pfam; PF11032; ApoM; 1.
DR SUPFAM; SSF50814; SSF50814; 1.
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
