APOD_HUMAN
ID APOD_HUMAN Reviewed; 189 AA.
AC P05090; B2R579; D3DNW6; Q6IBG6;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 226.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3453108; DOI=10.1016/s0021-9258(18)66599-8;
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; DOI=10.1089/dna.1987.6.199;
RA Drayna D.T., McLean J.W., Wion K.L., Trent J.M., Drabkin H.A., Lawn R.M.;
RT "Human apolipoprotein D gene: gene sequence, chromosome localization, and
RT 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., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA 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 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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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., 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 (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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP PROTEIN SEQUENCE OF 21-189, DISULFIDE BONDS, PYROGLUTAMATE FORMATION AT
RP GLN-21, AND GLYCOSYLATION AT 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., Massey J.B.,
RA Gotto A.M. Jr., Pownall H.J.;
RT "Structure of human apolipoprotein D: locations of the intermolecular and
RT 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 addition to
RT tear prealbumin mRNA, both species encoding members of the lipocalin
RT superfamily.";
RL Exp. Eye Res. 61:495-500(1995).
RN [11]
RP PROTEIN SEQUENCE OF 128-187.
RX PubMed=2244881; DOI=10.1042/bj2710803;
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 women
RT with human breast gross cystic disease.";
RL Biochem. J. 271:803-807(1990).
RN [12]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-98.
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.
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 [14]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-65 AND ASN-98.
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 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., Zheng Z.B.,
RA Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L.,
RA Ying W.T., He S.M., Qian X.H.;
RT "A strategy for precise and large scale identification of core fucosylated
RT glycoproteins.";
RL Mol. Cell. Proteomics 8:913-923(2009).
RN [16]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-98, AND STRUCTURE OF
RP CARBOHYDRATES.
RC TISSUE=Cerebrospinal fluid;
RX PubMed=19838169; DOI=10.1038/nmeth.1392;
RA Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E., Brinkmalm G.,
RA 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 IDENTIFICATION BY 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 N- and
RT O-linked glycosylations by CID and ECD.";
RL Mol. Cell. Proteomics 11:1-17(2012).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [19]
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 [20]
RP GLYCOSYLATION AT ASN-65 AND ASN-98.
RX PubMed=7613477; DOI=10.1002/pro.5560040419;
RA Schindler P.A., Settineri C.A., Collet X., Fielding C.J., Burlingame A.L.;
RT "Site-specific detection and structural characterization of the
RT glycosylation of human plasma proteins lecithin:cholesterol acyltransferase
RT and apolipoprotein D using HPLC/electrospray mass spectrometry and
RT sequential glycosidase digestion.";
RL Protein Sci. 4:791-803(1995).
RN [21]
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 of
RT human genes.";
RL Nat. Genet. 22:231-238(1999).
RN [22]
RP ERRATUM OF PUBMED:10391209.
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 transport
CC and binding of bilin. Appears to be able to transport a variety of
CC ligands in a number of different contexts.
CC -!- SUBUNIT: Homodimer. In plasma, also exists as a disulfide-linked
CC heterodimer with APOA2. {ECO:0000269|PubMed:7918467}.
CC -!- INTERACTION:
CC P05090; Q9NVV5-2: AIG1; NbExp=3; IntAct=EBI-715495, EBI-11957045;
CC P05090; Q96BI3: APH1A; NbExp=3; IntAct=EBI-715495, EBI-2606935;
CC P05090; O43315: AQP9; NbExp=3; IntAct=EBI-715495, EBI-17444777;
CC P05090; Q99437: ATP6V0B; NbExp=3; IntAct=EBI-715495, EBI-3904417;
CC P05090; O15342: ATP6V0E1; NbExp=3; IntAct=EBI-715495, EBI-12935759;
CC P05090; Q9BXK5: BCL2L13; NbExp=3; IntAct=EBI-715495, EBI-747430;
CC P05090; Q13323: BIK; NbExp=3; IntAct=EBI-715495, EBI-700794;
CC P05090; P19397: CD53; NbExp=3; IntAct=EBI-715495, EBI-6657396;
CC P05090; P11912: CD79A; NbExp=3; IntAct=EBI-715495, EBI-7797864;
CC P05090; O95471: CLDN7; NbExp=3; IntAct=EBI-715495, EBI-740744;
CC P05090; Q8IUN9: CLEC10A; NbExp=3; IntAct=EBI-715495, EBI-2873246;
CC P05090; Q7Z7G2: CPLX4; NbExp=3; IntAct=EBI-715495, EBI-18013275;
CC P05090; O43889-2: CREB3; NbExp=4; IntAct=EBI-715495, EBI-625022;
CC P05090; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-715495, EBI-6942903;
CC P05090; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-715495, EBI-781551;
CC P05090; P34910-2: EVI2B; NbExp=3; IntAct=EBI-715495, EBI-17640610;
CC P05090; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-715495, EBI-18304435;
CC P05090; O15552: FFAR2; NbExp=3; IntAct=EBI-715495, EBI-2833872;
CC P05090; Q9Y680: FKBP7; NbExp=3; IntAct=EBI-715495, EBI-3918971;
CC P05090; P25090: FPR2; NbExp=3; IntAct=EBI-715495, EBI-17291771;
CC P05090; Q8TB36: GDAP1; NbExp=3; IntAct=EBI-715495, EBI-11110431;
CC P05090; P48165: GJA8; NbExp=3; IntAct=EBI-715495, EBI-17458373;
CC P05090; Q5T7V8: GORAB; NbExp=3; IntAct=EBI-715495, EBI-3917143;
CC P05090; Q8TDV0: GPR151; NbExp=3; IntAct=EBI-715495, EBI-11955647;
CC P05090; O15529: GPR42; NbExp=3; IntAct=EBI-715495, EBI-18076404;
CC P05090; Q8TED1: GPX8; NbExp=3; IntAct=EBI-715495, EBI-11721746;
CC P05090; P48051: KCNJ6; NbExp=3; IntAct=EBI-715495, EBI-12017638;
CC P05090; P43628: KIR2DL3; NbExp=3; IntAct=EBI-715495, EBI-8632435;
CC P05090; Q9GZY8-5: MFF; NbExp=3; IntAct=EBI-715495, EBI-11956541;
CC P05090; O14880: MGST3; NbExp=3; IntAct=EBI-715495, EBI-724754;
CC P05090; Q49AM1: MTERF2; NbExp=3; IntAct=EBI-715495, EBI-17857560;
CC P05090; Q9H2K0: MTIF3; NbExp=3; IntAct=EBI-715495, EBI-3923617;
CC P05090; Q6IBW4-4: NCAPH2; NbExp=3; IntAct=EBI-715495, EBI-10247000;
CC P05090; Q13113: PDZK1IP1; NbExp=3; IntAct=EBI-715495, EBI-716063;
CC P05090; O75783: RHBDL1; NbExp=3; IntAct=EBI-715495, EBI-12104986;
CC P05090; Q8N7X8: SIGLECL1; NbExp=3; IntAct=EBI-715495, EBI-18052611;
CC P05090; Q3KNW5: SLC10A6; NbExp=3; IntAct=EBI-715495, EBI-18159983;
CC P05090; Q9NQQ7-3: SLC35C2; NbExp=3; IntAct=EBI-715495, EBI-17295964;
CC P05090; Q8N6K0: TEX29; NbExp=3; IntAct=EBI-715495, EBI-19027521;
CC P05090; Q96Q45-2: TMEM237; NbExp=5; IntAct=EBI-715495, EBI-10982110;
CC P05090; Q96B21: TMEM45B; NbExp=3; IntAct=EBI-715495, EBI-3923061;
CC P05090; Q4KMG9: TMEM52B; NbExp=3; IntAct=EBI-715495, EBI-18178701;
CC P05090; Q9BSE2: TMEM79; NbExp=3; IntAct=EBI-715495, EBI-8649725;
CC P05090; Q9P0L0: VAPA; NbExp=6; IntAct=EBI-715495, EBI-1059156;
CC P05090; Q9H7M9: VSIR; NbExp=3; IntAct=EBI-715495, EBI-744988;
CC P05090; A8KA83; NbExp=3; IntAct=EBI-715495, EBI-10174961;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed in liver, intestine, pancreas, kidney,
CC 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 dHex1Hex7HexNAc6
CC (minor). {ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16335952,
CC ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218,
CC ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:22171320,
CC ECO:0000269|PubMed:7613477, ECO:0000269|PubMed:7918467}.
CC -!- MISCELLANEOUS: APOD is primarily localized in HDL (60-65%), with most
CC of the remainder in VHDL and only trace amounts in VLDL and LDL.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
CC {ECO:0000305}.
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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 CCDS; CCDS33925.1; -.
DR PIR; A26958; LPHUD.
DR RefSeq; NP_001638.1; NM_001647.3.
DR PDB; 2HZQ; X-ray; 1.80 A; A=23-189.
DR PDB; 2HZR; X-ray; 1.80 A; A=23-189.
DR PDBsum; 2HZQ; -.
DR PDBsum; 2HZR; -.
DR AlphaFoldDB; P05090; -.
DR SASBDB; P05090; -.
DR SMR; P05090; -.
DR BioGRID; 106844; 193.
DR IntAct; P05090; 94.
DR MINT; P05090; -.
DR STRING; 9606.ENSP00000345179; -.
DR DrugBank; DB09130; Copper.
DR DrugBank; DB11886; Infigratinib.
DR DrugBank; DB00877; Sirolimus.
DR DrugBank; DB00162; Vitamin A.
DR SwissLipids; SLP:000001524; -.
DR GlyConnect; 677; 90 N-Linked glycans (2 sites).
DR GlyGen; P05090; 3 sites, 115 N-linked glycans (2 sites), 1 O-linked glycan (1 site).
DR iPTMnet; P05090; -.
DR MetOSite; P05090; -.
DR PhosphoSitePlus; P05090; -.
DR BioMuta; APOD; -.
DR DMDM; 114034; -.
DR SWISS-2DPAGE; P05090; -.
DR CPTAC; non-CPTAC-1086; -.
DR jPOST; P05090; -.
DR MassIVE; P05090; -.
DR MaxQB; P05090; -.
DR PaxDb; P05090; -.
DR PeptideAtlas; P05090; -.
DR PRIDE; P05090; -.
DR ProteomicsDB; 51787; -.
DR Antibodypedia; 19470; 378 antibodies from 37 providers.
DR DNASU; 347; -.
DR Ensembl; ENST00000343267.8; ENSP00000345179.3; ENSG00000189058.9.
DR GeneID; 347; -.
DR KEGG; hsa:347; -.
DR MANE-Select; ENST00000343267.8; ENSP00000345179.3; NM_001647.4; NP_001638.1.
DR UCSC; uc003fur.2; human.
DR CTD; 347; -.
DR DisGeNET; 347; -.
DR GeneCards; APOD; -.
DR HGNC; HGNC:612; APOD.
DR HPA; ENSG00000189058; Tissue enhanced (breast).
DR MIM; 107740; gene.
DR neXtProt; NX_P05090; -.
DR OpenTargets; ENSG00000189058; -.
DR PharmGKB; PA24900; -.
DR VEuPathDB; HostDB:ENSG00000189058; -.
DR eggNOG; KOG4824; Eukaryota.
DR GeneTree; ENSGT00510000046981; -.
DR InParanoid; P05090; -.
DR OMA; TPYWILS; -.
DR OrthoDB; 1402758at2759; -.
DR PhylomeDB; P05090; -.
DR TreeFam; TF324836; -.
DR PathwayCommons; P05090; -.
DR Reactome; R-HSA-804914; Transport of fatty acids.
DR Reactome; R-HSA-9029569; NR1H3 & NR1H2 regulate gene expression linked to cholesterol transport and efflux.
DR SignaLink; P05090; -.
DR BioGRID-ORCS; 347; 7 hits in 1065 CRISPR screens.
DR ChiTaRS; APOD; human.
DR EvolutionaryTrace; P05090; -.
DR GeneWiki; Apolipoprotein_D; -.
DR GenomeRNAi; 347; -.
DR Pharos; P05090; Tbio.
DR PRO; PR:P05090; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P05090; protein.
DR Bgee; ENSG00000189058; Expressed in olfactory bulb and 194 other tissues.
DR ExpressionAtlas; P05090; baseline and differential.
DR Genevisible; P05090; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; HDA:BHF-UCL.
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:0048678; P:response to axon injury; 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; IPR022271; Lipocalin_ApoD.
DR InterPro; IPR022272; Lipocalin_CS.
DR InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
DR Pfam; PF08212; Lipocalin_2; 1.
DR PIRSF; PIRSF036893; Lipocalin_ApoD; 1.
DR PRINTS; PR02058; APODVERTBRTE.
DR PRINTS; PR01219; APOLIPOPROTD.
DR SUPFAM; SSF50814; SSF50814; 1.
DR PROSITE; PS00213; LIPOCALIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Lipid-binding; Pyrrolidone carboxylic acid; Reference proteome; Secreted;
KW Signal; Transport.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:7918467"
FT CHAIN 21..189
FT /note="Apolipoprotein D"
FT /id="PRO_0000017872"
FT MOD_RES 21
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:3453108,
FT ECO:0000269|PubMed:7918467"
FT CARBOHYD 65
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218,
FT ECO:0000269|PubMed:22171320, ECO:0000269|PubMed:7613477,
FT ECO:0000269|PubMed:7918467"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:14760718,
FT ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490,
FT ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169,
FT ECO:0000269|PubMed:22171320, ECO:0000269|PubMed:7613477,
FT ECO:0000269|PubMed:7918467"
FT DISULFID 28..134
FT /evidence="ECO:0000269|PubMed:7918467"
FT DISULFID 61..185
FT /evidence="ECO:0000269|PubMed:7918467"
FT DISULFID 136
FT /note="Interchain (with C-29 in APOA2)"
FT /evidence="ECO:0000269|PubMed:7918467"
FT VARIANT 15
FT /note="F -> S (in dbSNP:rs5952)"
FT /evidence="ECO:0000269|PubMed:10391209"
FT /id="VAR_011931"
FT VARIANT 115
FT /note="S -> L (in dbSNP:rs5954)"
FT /evidence="ECO:0000269|PubMed:10391209"
FT /id="VAR_011932"
FT VARIANT 178
FT /note="T -> K (in dbSNP:rs5955)"
FT /evidence="ECO:0000269|PubMed:10391209"
FT /id="VAR_011933"
FT STRAND 24..27
FT /evidence="ECO:0007829|PDB:2HZQ"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:2HZQ"
FT STRAND 44..51
FT /evidence="ECO:0007829|PDB:2HZQ"
FT STRAND 60..68
FT /evidence="ECO:0007829|PDB:2HZQ"
FT STRAND 74..81
FT /evidence="ECO:0007829|PDB:2HZQ"
FT STRAND 87..97
FT /evidence="ECO:0007829|PDB:2HZQ"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:2HZQ"
FT STRAND 116..123
FT /evidence="ECO:0007829|PDB:2HZQ"
FT STRAND 125..138
FT /evidence="ECO:0007829|PDB:2HZQ"
FT STRAND 141..153
FT /evidence="ECO:0007829|PDB:2HZQ"
FT HELIX 157..169
FT /evidence="ECO:0007829|PDB:2HZQ"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:2HZQ"
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
