Full text data of APOD
APOD
[Confidence: low (only semi-automatic identification from reviews)]
Apolipoprotein D; Apo-D; ApoD; Flags: Precursor
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Apolipoprotein D; Apo-D; ApoD; Flags: Precursor
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P05090
ID APOD_HUMAN Reviewed; 189 AA.
AC P05090; B2R579; D3DNW6; Q6IBG6;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
read moreDT 13-AUG-1987, sequence version 1.
DT 22-JAN-2014, entry version 159.
DE RecName: Full=Apolipoprotein D;
DE Short=Apo-D;
DE Short=ApoD;
DE Flags: Precursor;
GN Name=APOD;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3453108;
RA Drayna D.T., Fielding C., McLean J.W., Baer B., Castro G., Chen E.,
RA Comstock L., Henzel W., Kohr W., Rhee L., Wion K.L., Lawn R.M.;
RT "Cloning and expression of human apolipoprotein D cDNA.";
RL J. Biol. Chem. 261:16535-16539(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2439269;
RA Drayna D.T., McLean J.W., Wion K.L., Trent J.M., Drabkin H.A.,
RA Lawn R.M.;
RT "Human apolipoprotein D gene: gene sequence, chromosome localization,
RT and homology to the alpha 2u-globulin superfamily.";
RL DNA 6:199-204(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S.,
RA Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
RA Korn B., Zuo D., Hu Y., LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cerebellum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP PROTEIN SEQUENCE OF 21-189, DISULFIDE BONDS, AND GLYCOSYLATION AT
RP ASN-65 AND ASN-98.
RC TISSUE=Plasma;
RX PubMed=7918467; DOI=10.1021/bi00207a011;
RA Yang C.-Y., Gu Z.-W., Blanco-Vaca F., Gaskell S.J., Yang M.,
RA Massey J.B., Gotto A.M. Jr., Pownall H.J.;
RT "Structure of human apolipoprotein D: locations of the intermolecular
RT and intramolecular disulfide links.";
RL Biochemistry 33:12451-12455(1994).
RN [10]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 92-189.
RC TISSUE=Lacrimal gland;
RX PubMed=8549691; DOI=10.1016/S0014-4835(05)80145-9;
RA Holzfeind P., Merschak P., Dieplinger H., Redl B.;
RT "The human lacrimal gland synthesizes apolipoprotein D mRNA in
RT addition to tear prealbumin mRNA, both species encoding members of the
RT lipocalin superfamily.";
RL Exp. Eye Res. 61:495-500(1995).
RN [11]
RP PROTEIN SEQUENCE OF 128-187.
RX PubMed=2244881;
RA Balbin M., Freije J.M.P., Fueyo A., Sanchez L.M., Lopez-Otin C.;
RT "Apolipoprotein D is the major protein component in cyst fluid from
RT women with human breast gross cystic disease.";
RL Biochem. J. 271:803-807(1990).
RN [12]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-98, AND MASS SPECTROMETRY.
RC TISSUE=Plasma;
RX PubMed=14760718; DOI=10.1002/pmic.200300556;
RA Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.;
RT "Screening for N-glycosylated proteins by liquid chromatography mass
RT spectrometry.";
RL Proteomics 4:454-465(2004).
RN [13]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-98, AND MASS SPECTROMETRY.
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.,
RA Moore R.J., 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 [14]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-65 AND ASN-98, AND MASS
RP SPECTROMETRY.
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
RT multiple enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [15]
RP GLYCOSYLATION AT ASN-98.
RX PubMed=19139490; DOI=10.1074/mcp.M800504-MCP200;
RA Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F.,
RA Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y.,
RA Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.;
RT "A strategy for precise and large scale identification of core
RT fucosylated glycoproteins.";
RL Mol. Cell. Proteomics 8:913-923(2009).
RN [16]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-98, STRUCTURE OF
RP CARBOHYDRATES, AND MASS SPECTROMETRY.
RC TISSUE=Cerebrospinal fluid;
RX PubMed=19838169; DOI=10.1038/nmeth.1392;
RA Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E.,
RA Brinkmalm G., Larson G.;
RT "Enrichment of glycopeptides for glycan structure and attachment site
RT identification.";
RL Nat. Methods 6:809-811(2009).
RN [17]
RP GLYCOSYLATION AT ASN-65 AND ASN-98, STRUCTURE OF CARBOHYDRATES, AND
RP MASS SPECTROMETRY.
RX PubMed=22171320; DOI=10.1074/mcp.M111.013649;
RA Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.;
RT "Human urinary glycoproteomics; attachment site specific analysis of
RT N-and O-linked glycosylations by CID and ECD.";
RL Mol. Cell. Proteomics 0:0-0(2011).
RN [18]
RP 3D-STRUCTURE MODELING, AND BILIN-BINDING.
RX PubMed=2083249;
RA Peitsch M.C., Boguski M.S.;
RT "Is apolipoprotein D a mammalian bilin-binding protein?";
RL New Biol. 2:197-206(1990).
RN [19]
RP GLYCOSYLATION AT ASN-65 AND ASN-98.
RX PubMed=7613477;
RA Schindler P.A., Settineri C.A., Collet X., Fielding C.J.,
RA Burlingame A.L.;
RT "Site-specific detection and structural characterization of the
RT glycosylation of human plasma proteins lecithin:cholesterol
RT acyltransferase and apolipoprotein D using HPLC/electrospray mass
RT spectrometry and sequential glycosidase digestion.";
RL Protein Sci. 4:791-803(1995).
RN [20]
RP VARIANTS SER-15; LEU-115 AND LYS-178.
RX PubMed=10391209; DOI=10.1038/10290;
RA Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
RA Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
RA Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
RA Lander E.S.;
RT "Characterization of single-nucleotide polymorphisms in coding regions
RT of human genes.";
RL Nat. Genet. 22:231-238(1999).
RN [21]
RP ERRATUM.
RA Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
RA Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
RA Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
RA Lander E.S.;
RL Nat. Genet. 23:373-373(1999).
CC -!- FUNCTION: APOD occurs in the macromolecular complex with lecithin-
CC cholesterol acyltransferase. It is probably involved in the
CC transport and binding of bilin. Appears to be able to transport a
CC variety of ligands in a number of different contexts.
CC -!- SUBUNIT: Homodimer. In plasma, also exists as a disulfide-linked
CC heterodimer with APOA2.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed in liver, intestine, pancreas,
CC kidney, placenta, adrenal, spleen, fetal brain tissue and tears.
CC -!- PTM: N-glycosylatd. N-glycan heterogeneity at Asn-65: Hex5HexNAc4
CC (major) and Hex6HexNAc5 (minor); at Asn-98: Hex5HexNAc4 (minor),
CC dHex1Hex5HexNAc4 (major), dHex1Hex6HexNAc5 (minor) and
CC dHex1Hex7HexNAc6 (minor).
CC -!- MISCELLANEOUS: APOD is primarily localized in HDL (60-65%), with
CC most of the remainder in VHDL and only trace amounts in VLDL and
CC LDL.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; J02611; AAB59517.1; -; mRNA.
DR EMBL; M16696; AAA51764.1; -; Genomic_DNA.
DR EMBL; BT019860; AAV38663.1; -; mRNA.
DR EMBL; BT019861; AAV38664.1; -; mRNA.
DR EMBL; CR456838; CAG33119.1; -; mRNA.
DR EMBL; CR541773; CAG46572.1; -; mRNA.
DR EMBL; AK312090; BAG35026.1; -; mRNA.
DR EMBL; CH471052; EAW78023.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78024.1; -; Genomic_DNA.
DR EMBL; BC007402; AAH07402.1; -; mRNA.
DR EMBL; S80440; AAB35919.1; -; mRNA.
DR PIR; A26958; LPHUD.
DR RefSeq; NP_001638.1; NM_001647.3.
DR UniGene; Hs.522555; -.
DR PDB; 2APD; Model; -; A=21-189.
DR PDB; 2HZQ; X-ray; 1.80 A; A=23-189.
DR PDB; 2HZR; X-ray; 1.80 A; A=23-189.
DR PDBsum; 2APD; -.
DR PDBsum; 2HZQ; -.
DR PDBsum; 2HZR; -.
DR ProteinModelPortal; P05090; -.
DR SMR; P05090; 23-188.
DR IntAct; P05090; 5.
DR MINT; MINT-1396020; -.
DR STRING; 9606.ENSP00000345179; -.
DR PhosphoSite; P05090; -.
DR DMDM; 114034; -.
DR SWISS-2DPAGE; P05090; -.
DR PaxDb; P05090; -.
DR PeptideAtlas; P05090; -.
DR PRIDE; P05090; -.
DR DNASU; 347; -.
DR Ensembl; ENST00000343267; ENSP00000345179; ENSG00000189058.
DR GeneID; 347; -.
DR KEGG; hsa:347; -.
DR UCSC; uc003fur.2; human.
DR CTD; 347; -.
DR GeneCards; GC03M195295; -.
DR HGNC; HGNC:612; APOD.
DR MIM; 107740; gene.
DR neXtProt; NX_P05090; -.
DR PharmGKB; PA24900; -.
DR eggNOG; COG3040; -.
DR HOGENOM; HOG000061525; -.
DR HOVERGEN; HBG018734; -.
DR InParanoid; P05090; -.
DR KO; K03098; -.
DR PhylomeDB; P05090; -.
DR ChiTaRS; APOD; human.
DR EvolutionaryTrace; P05090; -.
DR GeneWiki; Apolipoprotein_D; -.
DR GenomeRNAi; 347; -.
DR NextBio; 1431; -.
DR PRO; PR:P05090; -.
DR ArrayExpress; P05090; -.
DR Bgee; P05090; -.
DR CleanEx; HS_APOD; -.
DR Genevestigator; P05090; -.
DR GO; GO:0022626; C:cytosolic ribosome; ISS:UniProtKB.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0015485; F:cholesterol binding; IDA:UniProtKB.
DR GO; GO:0005319; F:lipid transporter activity; NAS:UniProtKB.
DR GO; GO:0007568; P:aging; NAS:UniProtKB.
DR GO; GO:0001525; P:angiogenesis; NAS:UniProtKB.
DR GO; GO:0007420; P:brain development; ISS:UniProtKB.
DR GO; GO:0006006; P:glucose metabolic process; IDA:UniProtKB.
DR GO; GO:0006629; P:lipid metabolic process; IDA:UniProtKB.
DR GO; GO:1900016; P:negative regulation of cytokine production involved in inflammatory response; IDA:UniProtKB.
DR GO; GO:0051895; P:negative regulation of focal adhesion assembly; IMP:UniProtKB.
DR GO; GO:0060588; P:negative regulation of lipoprotein lipid oxidation; IDA:UniProtKB.
DR GO; GO:0071638; P:negative regulation of monocyte chemotactic protein-1 production; IDA:UniProtKB.
DR GO; GO:0010642; P:negative regulation of platelet-derived growth factor receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0042308; P:negative regulation of protein import into nucleus; IDA:UniProtKB.
DR GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; IDA:UniProtKB.
DR GO; GO:2000098; P:negative regulation of smooth muscle cell-matrix adhesion; IMP:UniProtKB.
DR GO; GO:2000405; P:negative regulation of T cell migration; IDA:UniProtKB.
DR GO; GO:0014012; P:peripheral nervous system axon regeneration; ISS:UniProtKB.
DR GO; GO:0042493; P:response to drug; ISS:UniProtKB.
DR GO; GO:0000302; P:response to reactive oxygen species; IDA:UniProtKB.
DR GO; GO:0042246; P:tissue regeneration; ISS:UniProtKB.
DR Gene3D; 2.40.128.20; -; 1.
DR InterPro; IPR026222; ApoD_vertbrte.
DR InterPro; IPR002969; ApolipopD.
DR InterPro; IPR012674; Calycin.
DR InterPro; IPR011038; Calycin-like.
DR InterPro; IPR002345; Lipocalin.
DR InterPro; IPR022271; Lipocalin_ApoD.
DR InterPro; IPR022272; Lipocalin_CS.
DR InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
DR Pfam; PF00061; Lipocalin; 1.
DR PIRSF; PIRSF036893; Lipocalin_ApoD; 1.
DR PRINTS; PR02058; APODVERTBRTE.
DR PRINTS; PR01219; APOLIPOPROTD.
DR PRINTS; PR00179; LIPOCALIN.
DR SUPFAM; SSF50814; SSF50814; 1.
DR PROSITE; PS00213; LIPOCALIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Lipid-binding; Polymorphism;
KW Pyrrolidone carboxylic acid; Reference proteome; Secreted; Signal;
KW Transport.
FT SIGNAL 1 20
FT CHAIN 21 189 Apolipoprotein D.
FT /FTId=PRO_0000017872.
FT MOD_RES 21 21 Pyrrolidone carboxylic acid.
FT CARBOHYD 65 65 N-linked (GlcNAc...) (complex).
FT CARBOHYD 98 98 N-linked (GlcNAc...) (complex).
FT DISULFID 28 134
FT DISULFID 61 185
FT DISULFID 136 136 Interchain (with C-29 in APOA2).
FT VARIANT 15 15 F -> S (in dbSNP:rs5952).
FT /FTId=VAR_011931.
FT VARIANT 115 115 S -> L (in dbSNP:rs5954).
FT /FTId=VAR_011932.
FT VARIANT 178 178 T -> K (in dbSNP:rs5955).
FT /FTId=VAR_011933.
FT STRAND 24 27
FT HELIX 39 41
FT STRAND 44 51
FT STRAND 60 68
FT STRAND 74 81
FT STRAND 87 97
FT STRAND 104 108
FT STRAND 116 123
FT STRAND 125 138
FT STRAND 141 153
FT HELIX 157 169
FT STRAND 183 185
SQ SEQUENCE 189 AA; 21276 MW; 0EAA6DE03D5E71A8 CRC64;
MVMLLLLLSA LAGLFGAAEG QAFHLGKCPN PPVQENFDVN KYLGRWYEIE KIPTTFENGR
CIQANYSLME NGKIKVLNQE LRADGTVNQI EGEATPVNLT EPAKLEVKFS WFMPSAPYWI
LATDYENYAL VYSCTCIIQL FHVDFAWILA RNPNLPPETV DSLKNILTSN NIDVKKMTVT
DQVNCPKLS
//
ID APOD_HUMAN Reviewed; 189 AA.
AC P05090; B2R579; D3DNW6; Q6IBG6;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
read moreDT 13-AUG-1987, sequence version 1.
DT 22-JAN-2014, entry version 159.
DE RecName: Full=Apolipoprotein D;
DE Short=Apo-D;
DE Short=ApoD;
DE Flags: Precursor;
GN Name=APOD;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3453108;
RA Drayna D.T., Fielding C., McLean J.W., Baer B., Castro G., Chen E.,
RA Comstock L., Henzel W., Kohr W., Rhee L., Wion K.L., Lawn R.M.;
RT "Cloning and expression of human apolipoprotein D cDNA.";
RL J. Biol. Chem. 261:16535-16539(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2439269;
RA Drayna D.T., McLean J.W., Wion K.L., Trent J.M., Drabkin H.A.,
RA Lawn R.M.;
RT "Human apolipoprotein D gene: gene sequence, chromosome localization,
RT and homology to the alpha 2u-globulin superfamily.";
RL DNA 6:199-204(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S.,
RA Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
RA Korn B., Zuo D., Hu Y., LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cerebellum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP PROTEIN SEQUENCE OF 21-189, DISULFIDE BONDS, AND GLYCOSYLATION AT
RP ASN-65 AND ASN-98.
RC TISSUE=Plasma;
RX PubMed=7918467; DOI=10.1021/bi00207a011;
RA Yang C.-Y., Gu Z.-W., Blanco-Vaca F., Gaskell S.J., Yang M.,
RA Massey J.B., Gotto A.M. Jr., Pownall H.J.;
RT "Structure of human apolipoprotein D: locations of the intermolecular
RT and intramolecular disulfide links.";
RL Biochemistry 33:12451-12455(1994).
RN [10]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 92-189.
RC TISSUE=Lacrimal gland;
RX PubMed=8549691; DOI=10.1016/S0014-4835(05)80145-9;
RA Holzfeind P., Merschak P., Dieplinger H., Redl B.;
RT "The human lacrimal gland synthesizes apolipoprotein D mRNA in
RT addition to tear prealbumin mRNA, both species encoding members of the
RT lipocalin superfamily.";
RL Exp. Eye Res. 61:495-500(1995).
RN [11]
RP PROTEIN SEQUENCE OF 128-187.
RX PubMed=2244881;
RA Balbin M., Freije J.M.P., Fueyo A., Sanchez L.M., Lopez-Otin C.;
RT "Apolipoprotein D is the major protein component in cyst fluid from
RT women with human breast gross cystic disease.";
RL Biochem. J. 271:803-807(1990).
RN [12]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-98, AND MASS SPECTROMETRY.
RC TISSUE=Plasma;
RX PubMed=14760718; DOI=10.1002/pmic.200300556;
RA Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.;
RT "Screening for N-glycosylated proteins by liquid chromatography mass
RT spectrometry.";
RL Proteomics 4:454-465(2004).
RN [13]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-98, AND MASS SPECTROMETRY.
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.,
RA Moore R.J., 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 [14]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-65 AND ASN-98, AND MASS
RP SPECTROMETRY.
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
RT multiple enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [15]
RP GLYCOSYLATION AT ASN-98.
RX PubMed=19139490; DOI=10.1074/mcp.M800504-MCP200;
RA Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F.,
RA Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y.,
RA Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.;
RT "A strategy for precise and large scale identification of core
RT fucosylated glycoproteins.";
RL Mol. Cell. Proteomics 8:913-923(2009).
RN [16]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-98, STRUCTURE OF
RP CARBOHYDRATES, AND MASS SPECTROMETRY.
RC TISSUE=Cerebrospinal fluid;
RX PubMed=19838169; DOI=10.1038/nmeth.1392;
RA Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E.,
RA Brinkmalm G., Larson G.;
RT "Enrichment of glycopeptides for glycan structure and attachment site
RT identification.";
RL Nat. Methods 6:809-811(2009).
RN [17]
RP GLYCOSYLATION AT ASN-65 AND ASN-98, STRUCTURE OF CARBOHYDRATES, AND
RP MASS SPECTROMETRY.
RX PubMed=22171320; DOI=10.1074/mcp.M111.013649;
RA Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.;
RT "Human urinary glycoproteomics; attachment site specific analysis of
RT N-and O-linked glycosylations by CID and ECD.";
RL Mol. Cell. Proteomics 0:0-0(2011).
RN [18]
RP 3D-STRUCTURE MODELING, AND BILIN-BINDING.
RX PubMed=2083249;
RA Peitsch M.C., Boguski M.S.;
RT "Is apolipoprotein D a mammalian bilin-binding protein?";
RL New Biol. 2:197-206(1990).
RN [19]
RP GLYCOSYLATION AT ASN-65 AND ASN-98.
RX PubMed=7613477;
RA Schindler P.A., Settineri C.A., Collet X., Fielding C.J.,
RA Burlingame A.L.;
RT "Site-specific detection and structural characterization of the
RT glycosylation of human plasma proteins lecithin:cholesterol
RT acyltransferase and apolipoprotein D using HPLC/electrospray mass
RT spectrometry and sequential glycosidase digestion.";
RL Protein Sci. 4:791-803(1995).
RN [20]
RP VARIANTS SER-15; LEU-115 AND LYS-178.
RX PubMed=10391209; DOI=10.1038/10290;
RA Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
RA Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
RA Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
RA Lander E.S.;
RT "Characterization of single-nucleotide polymorphisms in coding regions
RT of human genes.";
RL Nat. Genet. 22:231-238(1999).
RN [21]
RP ERRATUM.
RA Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
RA Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
RA Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
RA Lander E.S.;
RL Nat. Genet. 23:373-373(1999).
CC -!- FUNCTION: APOD occurs in the macromolecular complex with lecithin-
CC cholesterol acyltransferase. It is probably involved in the
CC transport and binding of bilin. Appears to be able to transport a
CC variety of ligands in a number of different contexts.
CC -!- SUBUNIT: Homodimer. In plasma, also exists as a disulfide-linked
CC heterodimer with APOA2.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed in liver, intestine, pancreas,
CC kidney, placenta, adrenal, spleen, fetal brain tissue and tears.
CC -!- PTM: N-glycosylatd. N-glycan heterogeneity at Asn-65: Hex5HexNAc4
CC (major) and Hex6HexNAc5 (minor); at Asn-98: Hex5HexNAc4 (minor),
CC dHex1Hex5HexNAc4 (major), dHex1Hex6HexNAc5 (minor) and
CC dHex1Hex7HexNAc6 (minor).
CC -!- MISCELLANEOUS: APOD is primarily localized in HDL (60-65%), with
CC most of the remainder in VHDL and only trace amounts in VLDL and
CC LDL.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; J02611; AAB59517.1; -; mRNA.
DR EMBL; M16696; AAA51764.1; -; Genomic_DNA.
DR EMBL; BT019860; AAV38663.1; -; mRNA.
DR EMBL; BT019861; AAV38664.1; -; mRNA.
DR EMBL; CR456838; CAG33119.1; -; mRNA.
DR EMBL; CR541773; CAG46572.1; -; mRNA.
DR EMBL; AK312090; BAG35026.1; -; mRNA.
DR EMBL; CH471052; EAW78023.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78024.1; -; Genomic_DNA.
DR EMBL; BC007402; AAH07402.1; -; mRNA.
DR EMBL; S80440; AAB35919.1; -; mRNA.
DR PIR; A26958; LPHUD.
DR RefSeq; NP_001638.1; NM_001647.3.
DR UniGene; Hs.522555; -.
DR PDB; 2APD; Model; -; A=21-189.
DR PDB; 2HZQ; X-ray; 1.80 A; A=23-189.
DR PDB; 2HZR; X-ray; 1.80 A; A=23-189.
DR PDBsum; 2APD; -.
DR PDBsum; 2HZQ; -.
DR PDBsum; 2HZR; -.
DR ProteinModelPortal; P05090; -.
DR SMR; P05090; 23-188.
DR IntAct; P05090; 5.
DR MINT; MINT-1396020; -.
DR STRING; 9606.ENSP00000345179; -.
DR PhosphoSite; P05090; -.
DR DMDM; 114034; -.
DR SWISS-2DPAGE; P05090; -.
DR PaxDb; P05090; -.
DR PeptideAtlas; P05090; -.
DR PRIDE; P05090; -.
DR DNASU; 347; -.
DR Ensembl; ENST00000343267; ENSP00000345179; ENSG00000189058.
DR GeneID; 347; -.
DR KEGG; hsa:347; -.
DR UCSC; uc003fur.2; human.
DR CTD; 347; -.
DR GeneCards; GC03M195295; -.
DR HGNC; HGNC:612; APOD.
DR MIM; 107740; gene.
DR neXtProt; NX_P05090; -.
DR PharmGKB; PA24900; -.
DR eggNOG; COG3040; -.
DR HOGENOM; HOG000061525; -.
DR HOVERGEN; HBG018734; -.
DR InParanoid; P05090; -.
DR KO; K03098; -.
DR PhylomeDB; P05090; -.
DR ChiTaRS; APOD; human.
DR EvolutionaryTrace; P05090; -.
DR GeneWiki; Apolipoprotein_D; -.
DR GenomeRNAi; 347; -.
DR NextBio; 1431; -.
DR PRO; PR:P05090; -.
DR ArrayExpress; P05090; -.
DR Bgee; P05090; -.
DR CleanEx; HS_APOD; -.
DR Genevestigator; P05090; -.
DR GO; GO:0022626; C:cytosolic ribosome; ISS:UniProtKB.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0015485; F:cholesterol binding; IDA:UniProtKB.
DR GO; GO:0005319; F:lipid transporter activity; NAS:UniProtKB.
DR GO; GO:0007568; P:aging; NAS:UniProtKB.
DR GO; GO:0001525; P:angiogenesis; NAS:UniProtKB.
DR GO; GO:0007420; P:brain development; ISS:UniProtKB.
DR GO; GO:0006006; P:glucose metabolic process; IDA:UniProtKB.
DR GO; GO:0006629; P:lipid metabolic process; IDA:UniProtKB.
DR GO; GO:1900016; P:negative regulation of cytokine production involved in inflammatory response; IDA:UniProtKB.
DR GO; GO:0051895; P:negative regulation of focal adhesion assembly; IMP:UniProtKB.
DR GO; GO:0060588; P:negative regulation of lipoprotein lipid oxidation; IDA:UniProtKB.
DR GO; GO:0071638; P:negative regulation of monocyte chemotactic protein-1 production; IDA:UniProtKB.
DR GO; GO:0010642; P:negative regulation of platelet-derived growth factor receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0042308; P:negative regulation of protein import into nucleus; IDA:UniProtKB.
DR GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; IDA:UniProtKB.
DR GO; GO:2000098; P:negative regulation of smooth muscle cell-matrix adhesion; IMP:UniProtKB.
DR GO; GO:2000405; P:negative regulation of T cell migration; IDA:UniProtKB.
DR GO; GO:0014012; P:peripheral nervous system axon regeneration; ISS:UniProtKB.
DR GO; GO:0042493; P:response to drug; ISS:UniProtKB.
DR GO; GO:0000302; P:response to reactive oxygen species; IDA:UniProtKB.
DR GO; GO:0042246; P:tissue regeneration; ISS:UniProtKB.
DR Gene3D; 2.40.128.20; -; 1.
DR InterPro; IPR026222; ApoD_vertbrte.
DR InterPro; IPR002969; ApolipopD.
DR InterPro; IPR012674; Calycin.
DR InterPro; IPR011038; Calycin-like.
DR InterPro; IPR002345; Lipocalin.
DR InterPro; IPR022271; Lipocalin_ApoD.
DR InterPro; IPR022272; Lipocalin_CS.
DR InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
DR Pfam; PF00061; Lipocalin; 1.
DR PIRSF; PIRSF036893; Lipocalin_ApoD; 1.
DR PRINTS; PR02058; APODVERTBRTE.
DR PRINTS; PR01219; APOLIPOPROTD.
DR PRINTS; PR00179; LIPOCALIN.
DR SUPFAM; SSF50814; SSF50814; 1.
DR PROSITE; PS00213; LIPOCALIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Lipid-binding; Polymorphism;
KW Pyrrolidone carboxylic acid; Reference proteome; Secreted; Signal;
KW Transport.
FT SIGNAL 1 20
FT CHAIN 21 189 Apolipoprotein D.
FT /FTId=PRO_0000017872.
FT MOD_RES 21 21 Pyrrolidone carboxylic acid.
FT CARBOHYD 65 65 N-linked (GlcNAc...) (complex).
FT CARBOHYD 98 98 N-linked (GlcNAc...) (complex).
FT DISULFID 28 134
FT DISULFID 61 185
FT DISULFID 136 136 Interchain (with C-29 in APOA2).
FT VARIANT 15 15 F -> S (in dbSNP:rs5952).
FT /FTId=VAR_011931.
FT VARIANT 115 115 S -> L (in dbSNP:rs5954).
FT /FTId=VAR_011932.
FT VARIANT 178 178 T -> K (in dbSNP:rs5955).
FT /FTId=VAR_011933.
FT STRAND 24 27
FT HELIX 39 41
FT STRAND 44 51
FT STRAND 60 68
FT STRAND 74 81
FT STRAND 87 97
FT STRAND 104 108
FT STRAND 116 123
FT STRAND 125 138
FT STRAND 141 153
FT HELIX 157 169
FT STRAND 183 185
SQ SEQUENCE 189 AA; 21276 MW; 0EAA6DE03D5E71A8 CRC64;
MVMLLLLLSA LAGLFGAAEG QAFHLGKCPN PPVQENFDVN KYLGRWYEIE KIPTTFENGR
CIQANYSLME NGKIKVLNQE LRADGTVNQI EGEATPVNLT EPAKLEVKFS WFMPSAPYWI
LATDYENYAL VYSCTCIIQL FHVDFAWILA RNPNLPPETV DSLKNILTSN NIDVKKMTVT
DQVNCPKLS
//
MIM
107740
*RECORD*
*FIELD* NO
107740
*FIELD* TI
*107740 APOLIPOPROTEIN D; APOD
*FIELD* TX
DESCRIPTION
Apolipoprotein D (ApoD) is a member of the alpha(2mu)-microglobulin
read moresuperfamily of carrier proteins also known as lipocalins (e.g.,
lipocalin-1; 151675). It is a protein component of high-density
lipoprotein in human plasma, comprising about 5% of total high-density
lipoprotein (Fielding and Fielding, 1980). It is a glycoprotein of
estimated molecular weight 33,000 Da. ApoD is closely associated with
the enzyme lecithin:cholesterol acyltransferase (LCAT; 606967) (summary
by Drayna et al., 1986).
CLONING
Drayna et al. (1986) reported the amino acid sequence of apoD based on
the nucleotide sequence of the coding portion of the APOD gene and on
the cloned cDNA sequence. The 169-amino acid protein bore little
similarity to other lipoprotein sequences but had a high degree of
homology to plasma retinol-binding protein (180250, 180260, 180280,
180290), a member of the alpha(2mu)-globulin superfamily. This
structural similarity may indicate some functional homology of these
proteins. ApoD mRNA has been detected in many tissues. Drayna et al.
(1987) described multiple RFLPs at the APOD locus. Kamboh et al. (1989)
demonstrated for the first time polymorphism of apolipoprotein D by an
isoelectric focusing-immunoblotting technique.
Zeng et al. (1996) identified apoD as apocrine secretion odor-binding
protein-2 (ASOB2), 1 of 2 glycoproteins that bind E-3-methyl-2-hexenoic
acid (E-3M2H), the most abundant axillary odor component in human males.
The authors used mass spectrometry to determine the amino acid sequence
and glycosylation pattern of ASOB2. The pattern of glycosylation for
axillary apoD differs from that reported for plasma apoD, suggesting to
Zeng et al. (1996) that there are different sites of expression for the
2 glycoproteins. In situ hybridization of an oligonucleotide probe
against apoD mRNA with axillary tissue demonstrated that the message for
synthesis of this protein is specific to the apocrine glands. These
results suggested a remarkable similarity between human axillary
secretions and nonhuman mammalian odor sources, where lipocalins have
been shown to carry the odoriferous signals used in pheromonal
communication.
GENE FUNCTION
Zeng et al. (1996) noted several studies in humans suggesting that
axillary odors and secretions from both males and females are a source
of chemical signals containing physiologically active components capable
of altering the female menstrual cycle. These alterations include the
menstrual synchrony effect first documented by McClintock (1971) in an
all-female living group and later replicated by others in coeducational
facilities (Graham and McGrew, 1980; Quadagno et al., 1981). In nonhuman
mammals such as rodents, estrous synchrony has been shown to be mediated
by airborne chemical signals (McClintock, 1978). Certain axillary
components currently function as chemical signals involved in the
regulation of reproductive function via alteration of the
hypothalamic-pituitary-gonadal axis; chemical signals for this mode of
action are termed primer pheromones. Characterization of the source of
the odor in the human axillary region is not only of commercial interest
but is also important biologically because axillary extracts can alter
the length and timing of the female menstrual cycle. In males, the most
abundant odor component is known to be E-3-methyl-2-hexenoic acid
(E-3M2H), which is liberated from nonodorous apocrine secretions by
axillary microorganisms. In the apocrine gland secretions, 3M2H is
carried on the skin surface bound to 2 proteins, apocrine secretion
odor-binding proteins 1 and 2 (ASOB1 and ASOB2) with apparent molecular
masses of 45 kD and 26 kD, respectively (summary by Zeng et al., 1996).
MAPPING
Drayna et al. (1987) assigned the gene for APOD to 3p14.2-qter by dot
blot hybridization to DNA from sorted human chromosomes and by in situ
hybridization. Cellular retinol-binding proteins (180260, 180280) are
coded by chromosome 3; interstitial RBP (180290) is coded by a gene on
chromosome 10. Warden et al. (1992) demonstrated that the ApoD gene is
located on mouse chromosome 16.
*FIELD* RF
1. Drayna, D.; Fielding, C.; McLean, J.; Baer, B.; Castro, G.; Chen,
E.; Comstock, L.; Henzel, W.; Kohr, W.; Rhee, L.; Wion, K.; Lawn,
R.: Cloning and expression of human apolipoprotein D cDNA. J. Biol.
Chem. 261: 16535-16539, 1986.
2. Drayna, D.; Scott, J. D.; Lawn, R.: Multiple RFLPs at the human
apolipoprotein D (APOD) locus. Nucleic Acids Res. 15: 9617 only,
1987.
3. Drayna, D. T.; McLean, J. W.; Wion, K. L.; Trent, J. M.; Drabkin,
H. A.; Lawn, R. M.: Human apolipoprotein D gene: gene sequence, chromosome
localization, and homology to the alpha-2mu-globulin superfamily. DNA 6:
199-204, 1987.
4. Fielding, P. E.; Fielding, C. J.: A cholesteryl ester transfer
complex in human plasma. Proc. Nat. Acad. Sci. 77: 3327-3330, 1980.
5. Graham, C. A.; McGrew, W. C.: Menstrual synchrony in female undergaduates
living on a coeducational campus. Psychoneuroendocrinology 5: 245-252,
1980.
6. Kamboh, M. I.; Albers, J. J.; Majumder, P. P.; Ferrell, R. E.:
Genetic studies of human apolipoproteins. IX. Apolipoprotein D polymorphism
and its relation to serum lipoprotein lipid levels. Am. J. Hum. Genet. 45:
147-154, 1989.
7. McClintock, M. K.: Menstrual synchrony and suppression. Nature 229:
244-245, 1971. Note: Erratum: Nature 229: 643 only, 1971.
8. McClintock, M. K.: Estrous synchrony and its mediation by airborn
chemical communication (Rattus norvegicus). Horm. Behav. 10: 264-276,
1978.
9. Quadagno, D. M.; Shubeita, H. E.; Deck, J.; Francoeur, D.: Influence
of male social contacts, exercise and all-female living conditions
on the menstrual cycle. Psychoneuroendocrinology 6: 239-244, 1981.
10. Warden, C. H.; Diep, A.; Taylor, B. A.; Lusis, A. J.: Localization
of the gene for apolipoprotein D on mouse chromosome 16. Genomics 12:
851-852, 1992.
11. Zeng, C.; Spielman, A. I.; Vowels, B. R.; Leyden, J. J.; Biemann,
K.; Preti, G.: A human axillary odorant is carried by apolipoprotein
D. Proc. Nat. Acad. Sci. 93: 6626-6630, 1996.
*FIELD* CD
Victor A. McKusick: 2/9/1987
*FIELD* ED
terry: 11/29/2012
alopez: 7/16/2012
wwang: 1/9/2008
ckniffin: 5/29/2002
jamie: 10/23/1996
jamie: 10/16/1996
mark: 10/11/1996
terry: 9/20/1996
carol: 4/1/1992
supermim: 3/16/1992
supermim: 3/20/1990
ddp: 10/26/1989
root: 8/16/1989
marie: 3/25/1988
*RECORD*
*FIELD* NO
107740
*FIELD* TI
*107740 APOLIPOPROTEIN D; APOD
*FIELD* TX
DESCRIPTION
Apolipoprotein D (ApoD) is a member of the alpha(2mu)-microglobulin
read moresuperfamily of carrier proteins also known as lipocalins (e.g.,
lipocalin-1; 151675). It is a protein component of high-density
lipoprotein in human plasma, comprising about 5% of total high-density
lipoprotein (Fielding and Fielding, 1980). It is a glycoprotein of
estimated molecular weight 33,000 Da. ApoD is closely associated with
the enzyme lecithin:cholesterol acyltransferase (LCAT; 606967) (summary
by Drayna et al., 1986).
CLONING
Drayna et al. (1986) reported the amino acid sequence of apoD based on
the nucleotide sequence of the coding portion of the APOD gene and on
the cloned cDNA sequence. The 169-amino acid protein bore little
similarity to other lipoprotein sequences but had a high degree of
homology to plasma retinol-binding protein (180250, 180260, 180280,
180290), a member of the alpha(2mu)-globulin superfamily. This
structural similarity may indicate some functional homology of these
proteins. ApoD mRNA has been detected in many tissues. Drayna et al.
(1987) described multiple RFLPs at the APOD locus. Kamboh et al. (1989)
demonstrated for the first time polymorphism of apolipoprotein D by an
isoelectric focusing-immunoblotting technique.
Zeng et al. (1996) identified apoD as apocrine secretion odor-binding
protein-2 (ASOB2), 1 of 2 glycoproteins that bind E-3-methyl-2-hexenoic
acid (E-3M2H), the most abundant axillary odor component in human males.
The authors used mass spectrometry to determine the amino acid sequence
and glycosylation pattern of ASOB2. The pattern of glycosylation for
axillary apoD differs from that reported for plasma apoD, suggesting to
Zeng et al. (1996) that there are different sites of expression for the
2 glycoproteins. In situ hybridization of an oligonucleotide probe
against apoD mRNA with axillary tissue demonstrated that the message for
synthesis of this protein is specific to the apocrine glands. These
results suggested a remarkable similarity between human axillary
secretions and nonhuman mammalian odor sources, where lipocalins have
been shown to carry the odoriferous signals used in pheromonal
communication.
GENE FUNCTION
Zeng et al. (1996) noted several studies in humans suggesting that
axillary odors and secretions from both males and females are a source
of chemical signals containing physiologically active components capable
of altering the female menstrual cycle. These alterations include the
menstrual synchrony effect first documented by McClintock (1971) in an
all-female living group and later replicated by others in coeducational
facilities (Graham and McGrew, 1980; Quadagno et al., 1981). In nonhuman
mammals such as rodents, estrous synchrony has been shown to be mediated
by airborne chemical signals (McClintock, 1978). Certain axillary
components currently function as chemical signals involved in the
regulation of reproductive function via alteration of the
hypothalamic-pituitary-gonadal axis; chemical signals for this mode of
action are termed primer pheromones. Characterization of the source of
the odor in the human axillary region is not only of commercial interest
but is also important biologically because axillary extracts can alter
the length and timing of the female menstrual cycle. In males, the most
abundant odor component is known to be E-3-methyl-2-hexenoic acid
(E-3M2H), which is liberated from nonodorous apocrine secretions by
axillary microorganisms. In the apocrine gland secretions, 3M2H is
carried on the skin surface bound to 2 proteins, apocrine secretion
odor-binding proteins 1 and 2 (ASOB1 and ASOB2) with apparent molecular
masses of 45 kD and 26 kD, respectively (summary by Zeng et al., 1996).
MAPPING
Drayna et al. (1987) assigned the gene for APOD to 3p14.2-qter by dot
blot hybridization to DNA from sorted human chromosomes and by in situ
hybridization. Cellular retinol-binding proteins (180260, 180280) are
coded by chromosome 3; interstitial RBP (180290) is coded by a gene on
chromosome 10. Warden et al. (1992) demonstrated that the ApoD gene is
located on mouse chromosome 16.
*FIELD* RF
1. Drayna, D.; Fielding, C.; McLean, J.; Baer, B.; Castro, G.; Chen,
E.; Comstock, L.; Henzel, W.; Kohr, W.; Rhee, L.; Wion, K.; Lawn,
R.: Cloning and expression of human apolipoprotein D cDNA. J. Biol.
Chem. 261: 16535-16539, 1986.
2. Drayna, D.; Scott, J. D.; Lawn, R.: Multiple RFLPs at the human
apolipoprotein D (APOD) locus. Nucleic Acids Res. 15: 9617 only,
1987.
3. Drayna, D. T.; McLean, J. W.; Wion, K. L.; Trent, J. M.; Drabkin,
H. A.; Lawn, R. M.: Human apolipoprotein D gene: gene sequence, chromosome
localization, and homology to the alpha-2mu-globulin superfamily. DNA 6:
199-204, 1987.
4. Fielding, P. E.; Fielding, C. J.: A cholesteryl ester transfer
complex in human plasma. Proc. Nat. Acad. Sci. 77: 3327-3330, 1980.
5. Graham, C. A.; McGrew, W. C.: Menstrual synchrony in female undergaduates
living on a coeducational campus. Psychoneuroendocrinology 5: 245-252,
1980.
6. Kamboh, M. I.; Albers, J. J.; Majumder, P. P.; Ferrell, R. E.:
Genetic studies of human apolipoproteins. IX. Apolipoprotein D polymorphism
and its relation to serum lipoprotein lipid levels. Am. J. Hum. Genet. 45:
147-154, 1989.
7. McClintock, M. K.: Menstrual synchrony and suppression. Nature 229:
244-245, 1971. Note: Erratum: Nature 229: 643 only, 1971.
8. McClintock, M. K.: Estrous synchrony and its mediation by airborn
chemical communication (Rattus norvegicus). Horm. Behav. 10: 264-276,
1978.
9. Quadagno, D. M.; Shubeita, H. E.; Deck, J.; Francoeur, D.: Influence
of male social contacts, exercise and all-female living conditions
on the menstrual cycle. Psychoneuroendocrinology 6: 239-244, 1981.
10. Warden, C. H.; Diep, A.; Taylor, B. A.; Lusis, A. J.: Localization
of the gene for apolipoprotein D on mouse chromosome 16. Genomics 12:
851-852, 1992.
11. Zeng, C.; Spielman, A. I.; Vowels, B. R.; Leyden, J. J.; Biemann,
K.; Preti, G.: A human axillary odorant is carried by apolipoprotein
D. Proc. Nat. Acad. Sci. 93: 6626-6630, 1996.
*FIELD* CD
Victor A. McKusick: 2/9/1987
*FIELD* ED
terry: 11/29/2012
alopez: 7/16/2012
wwang: 1/9/2008
ckniffin: 5/29/2002
jamie: 10/23/1996
jamie: 10/16/1996
mark: 10/11/1996
terry: 9/20/1996
carol: 4/1/1992
supermim: 3/16/1992
supermim: 3/20/1990
ddp: 10/26/1989
root: 8/16/1989
marie: 3/25/1988