ID   APOM_PONAB              Reviewed;         188 AA.
AC   Q5R894;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Apolipoprotein M;
DE            Short=Apo-M;
DE            Short=ApoM;
GN   Name=APOM;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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 {ECO:0000250}. Note=Present in high
CC       density lipoprotein (HDL) and to a lesser extent in triglyceride-rich
CC       lipoproteins (TGRLP) and low density lipoproteins (LDL). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
CC       Highly divergent. {ECO:0000305}.
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DR   EMBL; CR859860; CAH92016.1; -; mRNA.
DR   RefSeq; NP_001126170.1; NM_001132698.1.
DR   AlphaFoldDB; Q5R894; -.
DR   SMR; Q5R894; -.
DR   STRING; 9601.ENSPPYP00000018389; -.
DR   Ensembl; ENSPPYT00000051584; ENSPPYP00000039558; ENSPPYG00000035537.
DR   GeneID; 100173132; -.
DR   KEGG; pon:100173132; -.
DR   CTD; 55937; -.
DR   eggNOG; ENOG502S2IN; Eukaryota.
DR   GeneTree; ENSGT00390000001026; -.
DR   HOGENOM; CLU_105274_0_0_1; -.
DR   InParanoid; Q5R894; -.
DR   OMA; GYQRFLF; -.
DR   OrthoDB; 1302737at2759; -.
DR   TreeFam; TF330771; -.
DR   Proteomes; UP000001595; Chromosome 6.
DR   GO; GO:0034364; C:high-density lipoprotein particle; IEA:UniProtKB-KW.
DR   GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
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   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; HDL; Lipid transport; Reference proteome;
KW   Secreted; Signal; Transport.
FT   CHAIN           1..188
FT                   /note="Apolipoprotein M"
FT                   /id="PRO_0000223280"
FT   SIGNAL          1..?22
FT                   /note="Not cleaved"
FT                   /evidence="ECO:0000250"
FT   BINDING         136
FT                   /ligand="tetradecanoate"
FT                   /ligand_id="ChEBI:CHEBI:30807"
FT                   /evidence="ECO:0000250|UniProtKB:O95445"
FT   BINDING         143
FT                   /ligand="tetradecanoate"
FT                   /ligand_id="ChEBI:CHEBI:30807"
FT                   /evidence="ECO:0000250|UniProtKB:O95445"
FT   CARBOHYD        135
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        23..167
FT                   /evidence="ECO:0000250"
FT   DISULFID        95..183
FT                   /evidence="ECO:0000250"
FT   DISULFID        128..157
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   188 AA;  21244 MW;  9D09D9FC61E43055 CRC64;
     MFHQIWAALL YFYGIILNSI YQCPEHSQLT TLGVDGKEFP EVHLGQWYFI AGAAPTKEEL
     ATFDPVDNII FNMAAGSAPT QLHLRATIRM KDGLCVPRKW IYHLTEGSTD LRTEGRPDMK
     TELFSSSCPG GIMLNETGQG YQRFLFYNRS PHPPEKCVEE FKSLTSCLDS KAFLLTPRNQ
     EACELSSN