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 02-OCT-2024, entry version 195. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 43. 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 PaxDb; 9606-ENSP00000365081; -. DR PeptideAtlas; O95445; -. DR ProteomicsDB; 50881; -. [O95445-1] DR ProteomicsDB; 63861; -. DR Antibodypedia; 27445; 565 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. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Direct protein sequencing; KW Disulfide bond; Glycoprotein; HDL; Lipid transport; KW Proteomics identification; Reference proteome; 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 //