APOM_MOUSE
ID APOM_MOUSE Reviewed; 190 AA.
AC Q9Z1R3;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Apolipoprotein M;
DE Short=Apo-M;
DE Short=ApoM;
GN Name=Apom; Synonyms=Ng20;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RA Xu N., Dahlbaeck B.;
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=129;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP INTERACTION WITH LRP2.
RX PubMed=16099815; DOI=10.1210/me.2005-0209;
RA Faber K., Hvidberg V., Moestrup S.K., Dahlbaeck B., Nielsen L.B.;
RT "Megalin is a receptor for apolipoprotein M, and kidney-specific megalin-
RT deficiency confers urinary excretion of apolipoprotein M.";
RL Mol. Endocrinol. 20:212-218(2006).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 20-90, AND DISULFIDE BONDS.
RX PubMed=20932978; DOI=10.1016/j.jmb.2010.09.062;
RA Sevvana M., Kassler K., Ahnstrom J., Weiler S., Dahlback B., Sticht H.,
RA Muller Y.A.;
RT "Mouse ApoM displays an unprecedented seven-stranded lipocalin fold:
RT folding decoy or alternative native fold?";
RL J. Mol. Biol. 404:363-371(2010).
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 (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with LRP2; LRP2 mediates APOM renal uptake and
CC subsequent lysosomal degradation. {ECO:0000269|PubMed:16099815}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed by the liver; secreted in plasma.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
CC Highly divergent. {ECO:0000305}.
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DR EMBL; AF207820; AAF23407.1; -; mRNA.
DR EMBL; AF109719; AAC82478.1; -; Genomic_DNA.
DR EMBL; AK004530; BAB23349.1; -; mRNA.
DR CCDS; CCDS28687.1; -.
DR RefSeq; NP_061286.1; NM_018816.1.
DR PDB; 2XKL; X-ray; 2.50 A; A=20-190.
DR PDBsum; 2XKL; -.
DR AlphaFoldDB; Q9Z1R3; -.
DR SMR; Q9Z1R3; -.
DR STRING; 10090.ENSMUSP00000025249; -.
DR iPTMnet; Q9Z1R3; -.
DR PhosphoSitePlus; Q9Z1R3; -.
DR CPTAC; non-CPTAC-5575; -.
DR MaxQB; Q9Z1R3; -.
DR PaxDb; Q9Z1R3; -.
DR PeptideAtlas; Q9Z1R3; -.
DR PRIDE; Q9Z1R3; -.
DR ProteomicsDB; 281801; -.
DR Antibodypedia; 27445; 535 antibodies from 38 providers.
DR DNASU; 55938; -.
DR Ensembl; ENSMUST00000025249; ENSMUSP00000025249; ENSMUSG00000024391.
DR GeneID; 55938; -.
DR KEGG; mmu:55938; -.
DR UCSC; uc008cga.1; mouse.
DR CTD; 55937; -.
DR MGI; MGI:1930124; Apom.
DR VEuPathDB; HostDB:ENSMUSG00000024391; -.
DR eggNOG; ENOG502S2IN; Eukaryota.
DR GeneTree; ENSGT00390000001026; -.
DR HOGENOM; CLU_105274_0_0_1; -.
DR InParanoid; Q9Z1R3; -.
DR OMA; GYQRFLF; -.
DR OrthoDB; 1302737at2759; -.
DR PhylomeDB; Q9Z1R3; -.
DR TreeFam; TF330771; -.
DR Reactome; R-MMU-975634; Retinoid metabolism and transport.
DR BioGRID-ORCS; 55938; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Apom; mouse.
DR EvolutionaryTrace; Q9Z1R3; -.
DR PRO; PR:Q9Z1R3; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q9Z1R3; protein.
DR Bgee; ENSMUSG00000024391; Expressed in yolk sac and 98 other tissues.
DR Genevisible; Q9Z1R3; MM.
DR GO; GO:0034365; C:discoidal high-density lipoprotein particle; IDA:BHF-UCL.
DR GO; GO:0005576; C:extracellular region; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0034364; C:high-density lipoprotein particle; IDA:BHF-UCL.
DR GO; GO:0034362; C:low-density lipoprotein particle; ISO:MGI.
DR GO; GO:0034366; C:spherical high-density lipoprotein particle; ISO:MGI.
DR GO; GO:0034361; C:very-low-density lipoprotein particle; ISO:MGI.
DR GO; GO:0016209; F:antioxidant activity; IDA:BHF-UCL.
DR GO; GO:0005319; F:lipid transporter activity; ISO:MGI.
DR GO; GO:0005543; F:phospholipid binding; ISS:BHF-UCL.
DR GO; GO:0033344; P:cholesterol efflux; IMP:BHF-UCL.
DR GO; GO:0034380; P:high-density lipoprotein particle assembly; IMP:BHF-UCL.
DR GO; GO:0034384; P:high-density lipoprotein particle clearance; IMP:BHF-UCL.
DR GO; GO:0034375; P:high-density lipoprotein particle remodeling; IMP:BHF-UCL.
DR GO; GO:0042157; P:lipoprotein metabolic process; IMP:MGI.
DR GO; GO:0034445; P:negative regulation of plasma lipoprotein oxidation; IDA:BHF-UCL.
DR GO; GO:0043691; P:reverse cholesterol transport; IMP:MGI.
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; Disulfide bond; HDL; Lipid transport; Reference proteome;
KW Secreted; Signal; Transport.
FT CHAIN 1..190
FT /note="Apolipoprotein M"
FT /id="PRO_0000223279"
FT SIGNAL 1..?22
FT /note="Not cleaved"
FT /evidence="ECO:0000255"
FT BINDING 138
FT /ligand="tetradecanoate"
FT /ligand_id="ChEBI:CHEBI:30807"
FT /evidence="ECO:0000250|UniProtKB:O95445"
FT BINDING 145
FT /ligand="tetradecanoate"
FT /ligand_id="ChEBI:CHEBI:30807"
FT /evidence="ECO:0000250|UniProtKB:O95445"
FT DISULFID 23..169
FT /evidence="ECO:0000250"
FT DISULFID 95..185
FT /evidence="ECO:0000269|PubMed:20932978"
FT DISULFID 130..159
FT /evidence="ECO:0000269|PubMed:20932978"
FT STRAND 28..34
FT /evidence="ECO:0007829|PDB:2XKL"
FT STRAND 47..56
FT /evidence="ECO:0007829|PDB:2XKL"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:2XKL"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:2XKL"
FT STRAND 66..75
FT /evidence="ECO:0007829|PDB:2XKL"
FT STRAND 81..90
FT /evidence="ECO:0007829|PDB:2XKL"
FT STRAND 95..104
FT /evidence="ECO:0007829|PDB:2XKL"
FT HELIX 125..129
FT /evidence="ECO:0007829|PDB:2XKL"
FT STRAND 133..140
FT /evidence="ECO:0007829|PDB:2XKL"
FT STRAND 143..154
FT /evidence="ECO:0007829|PDB:2XKL"
FT HELIX 157..169
FT /evidence="ECO:0007829|PDB:2XKL"
FT STRAND 174..177
FT /evidence="ECO:0007829|PDB:2XKL"
SQ SEQUENCE 190 AA; 21273 MW; 3D5614DADF2B77C4 CRC64;
MFHQVWAALL SLYGLLFNSM NQCPEHSQLT ALGMDDTETP EPHLGLWYFI AGAASTTEEL
ATFDPVDNIV FNMAAGSAPR QLQLRATIRT KSGVCVPRKW TYRLTEGKGN MELRTEGRPD
MKTDLFSSSC PGGIMLKETG QGYQRFLLYN RSPHPPEKCV EEFQSLTSCL DFKAFLVTPR
NQEACPLSSK
