APOM_RAT
ID APOM_RAT Reviewed; 190 AA.
AC P14630; Q5EBB9; Q9QXI9;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2001, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Apolipoprotein M;
DE Short=Apo-M;
DE Short=ApoM;
DE AltName: Full=Protein Px;
DE Flags: Precursor;
GN Name=Apom;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; 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=Brown Norway;
RX PubMed=15060004; DOI=10.1101/gr.1987704;
RA Hurt P., Walter L., Sudbrak R., Klages S., Mueller I., Shiina T., Inoko H.,
RA Lehrach H., Guenther E., Reinhardt R., Himmelbauer H.;
RT "The genomic sequence and comparative analysis of the rat major
RT histocompatibility complex.";
RL Genome Res. 14:631-639(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP PROTEIN SEQUENCE OF 18-33.
RX PubMed=2297521; DOI=10.1016/0005-2760(90)90051-x;
RA Blatter M.-C., James R.W., Borghini I., Martin B.M., Hochstrasser A.-C.,
RA Pometta D.;
RT "A novel high-density lipoprotein particle and associated protein in rat
RT plasma.";
RL Biochim. Biophys. Acta 1042:19-27(1990).
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:0000250|UniProtKB:Q9Z1R3}.
CC -!- SUBCELLULAR LOCATION: Secreted. Note=Associated with HDL.
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; AF207821; AAF23408.1; -; mRNA.
DR EMBL; BX883045; CAE83996.1; -; Genomic_DNA.
DR EMBL; BC089807; AAH89807.1; -; mRNA.
DR RefSeq; NP_062246.1; NM_019373.2.
DR AlphaFoldDB; P14630; -.
DR SMR; P14630; -.
DR STRING; 10116.ENSRNOP00000001126; -.
DR PhosphoSitePlus; P14630; -.
DR PaxDb; P14630; -.
DR GeneID; 55939; -.
DR KEGG; rno:55939; -.
DR UCSC; RGD:620773; rat.
DR CTD; 55937; -.
DR RGD; 620773; Apom.
DR VEuPathDB; HostDB:ENSRNOG00000000850; -.
DR eggNOG; ENOG502S2IN; Eukaryota.
DR HOGENOM; CLU_105274_0_0_1; -.
DR InParanoid; P14630; -.
DR OMA; GYQRFLF; -.
DR OrthoDB; 1302737at2759; -.
DR PhylomeDB; P14630; -.
DR TreeFam; TF330771; -.
DR Reactome; R-RNO-975634; Retinoid metabolism and transport.
DR PRO; PR:P14630; -.
DR Proteomes; UP000002494; Chromosome 20.
DR Bgee; ENSRNOG00000000850; Expressed in adult mammalian kidney and 18 other tissues.
DR Genevisible; P14630; RN.
DR GO; GO:0034365; C:discoidal high-density lipoprotein particle; ISO:RGD.
DR GO; GO:0005576; C:extracellular region; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0034364; C:high-density lipoprotein particle; ISO:RGD.
DR GO; GO:0034362; C:low-density lipoprotein particle; ISO:RGD.
DR GO; GO:0034366; C:spherical high-density lipoprotein particle; ISO:RGD.
DR GO; GO:0034361; C:very-low-density lipoprotein particle; ISO:RGD.
DR GO; GO:0016209; F:antioxidant activity; ISO:RGD.
DR GO; GO:0005319; F:lipid transporter activity; ISO:RGD.
DR GO; GO:0005543; F:phospholipid binding; ISO:RGD.
DR GO; GO:0033344; P:cholesterol efflux; ISO:RGD.
DR GO; GO:0034380; P:high-density lipoprotein particle assembly; ISO:RGD.
DR GO; GO:0034384; P:high-density lipoprotein particle clearance; ISO:RGD.
DR GO; GO:0034375; P:high-density lipoprotein particle remodeling; ISO:RGD.
DR GO; GO:0042157; P:lipoprotein metabolic process; ISO:RGD.
DR GO; GO:0034445; P:negative regulation of plasma lipoprotein oxidation; ISO:RGD.
DR GO; GO:0009749; P:response to glucose; IEP:RGD.
DR GO; GO:0043691; P:reverse cholesterol transport; ISO:RGD.
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 Direct protein sequencing; Disulfide bond; HDL; Lipid transport;
KW Reference proteome; Secreted; Signal; Transport.
FT SIGNAL 1..17
FT /evidence="ECO:0000269|PubMed:2297521"
FT CHAIN 18..190
FT /note="Apolipoprotein M"
FT /id="PRO_0000017877"
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:0000250"
FT DISULFID 130..159
FT /evidence="ECO:0000250"
FT CONFLICT 30
FT /note="M -> T (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 190 AA; 21513 MW; E507BD6C202CBBAF CRC64;
MFHQVWAALL YLYGLLFNSM NQCPEHSQLM TLGMDDKETP EPHLGLWYFI AGAAPTMEEL
ATFDQVDNIV FNMAAGSAPR QLQLRATIRT KNGVCVPRKW TYHLTEGKGN TELRTEGRPD
MKTDLFSISC PGGIMLKETG QGYQRFLLYN RSPHPPEECV EEFQSLTSCL DFKAFLVTPR
NQEACPLSSK
