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Reviewed, UniProtKB/Swiss-Prot P05090 (APOD_HUMAN)

Last modified July 22, 2008. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Apolipoprotein D
      Short name=Apo-D
      Short name=ApoD
Gene names
Name: APOD
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length189 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

APOD occurs in the macromolecular complex with lecithin-cholesterol acyltransferase. It is probably involved in the transport and binding of bilin. Appears to be able to transport a variety of ligands in a number of different contexts.

Subunit structure

Homodimer. In plasma, also exists as a disulfide-linked heterodimer with APOA2.

Subcellular location

Secreted.

Tissue specificity

Expressed in liver, intestine, pancreas, kidney, placenta, adrenal, spleen, fetal brain tissue and tears.

Miscellaneous

APOD is primarily localized in HDL (60-65%), with most of the remainder in VHDL and only trace amounts in VLDL and LDL.

Sequence similarities

Belongs to the calycin superfamily. Lipocalin family.

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Ontologies

Keywords

   Biological processTransport
   Cellular componentSecreted
   Coding sequence diversityPolymorphism
   DomainSignal
   LigandLipid-binding
   PTMGlycoprotein
Pyrrolidone carboxylic acid
   Technical term3D-structure
Direct protein sequencing

Gene Ontology (GO)

   Biological processlipid metabolic process Ref.1

Traceable author statement. Source: ProtInc

   Cellular componentextracellular space Ref.1

Traceable author statement. Source: ProtInc

   Molecular functionlipid transporter activity Ref.1

Traceable author statement. Source: ProtInc

protein binding Ref.7

Inferred from physical interaction. Source: UniProtKB

Complete GO annotation...

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Binary interactions

With

Entry

#Exp.

IntAct

Notes

STK24Q5T5B31EBI-715495,EBI-1054809

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical view

Molecule processing

Signal peptide1 – 2020
Chain21 – 189169Apolipoprotein D

Amino acid modifications

Modified residue211Pyrrolidone carboxylic acid
Glycosylation651N-linked (GlcNAc...)
Glycosylation981N-linked (GlcNAc...)
Disulfide bond28 ↔ 134
Disulfide bond61 ↔ 185
Disulfide bond136Interchain (with C-29 in APOA2)

Natural variations

Natural variant151F → S: dbSNP rs5952.
Natural variant1151S → L: dbSNP rs5954.
Natural variant1781T → K: dbSNP rs5955.

Secondary structure

1 ............................ 189
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P05090-1 [UniParc].

Last modified August 13, 1987. Version 1.
Checksum: 0EAA6DE03D5E71A8

FASTA18921,276
        10         20         30         40         50         60 
MVMLLLLLSA LAGLFGAAEG QAFHLGKCPN PPVQENFDVN KYLGRWYEIE KIPTTFENGR 

        70         80         90        100        110        120 
CIQANYSLME NGKIKVLNQE LRADGTVNQI EGEATPVNLT EPAKLEVKFS WFMPSAPYWI 

       130        140        150        160        170        180 
LATDYENYAL VYSCTCIIQL FHVDFAWILA RNPNLPPETV DSLKNILTSN NIDVKKMTVT 


DQVNCPKLS

« Hide

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References

« Hide 'large scale' references
[1]"Cloning and expression of human apolipoprotein D cDNA."
Drayna D.T., Fielding C., McLean J.W., Baer B., Castro G., Chen E., Comstock L., Henzel W., Kohr W., Rhee L., Wion K.L., Lawn R.M.
J. Biol. Chem. 261:16535-16539(1986) [PubMed: 3453108] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Human apolipoprotein D gene: gene sequence, chromosome localization, and homology to the alpha 2u-globulin superfamily."
Drayna D.T., McLean J.W., Wion K.L., Trent J.M., Drabkin H.A., Lawn R.M.
DNA 6:199-204(1987) [PubMed: 2439269] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Skin.
[7]"Structure of human apolipoprotein D: locations of the intermolecular and intramolecular disulfide links."
Yang C.-Y., Gu Z.-W., Blanco-Vaca F., Gaskell S.J., Yang M., Massey J.B., Gotto A.M. Jr., Pownall H.J.
Biochemistry 33:12451-12455(1994) [PubMed: 7918467] [Abstract]
Cited for: PROTEIN SEQUENCE OF 21-189, DISULFIDE BONDS, GLYCOSYLATION AT ASN-65 AND ASN-98.
Tissue: Plasma.
[8]"The human lacrimal gland synthesizes apolipoprotein D mRNA in addition to tear prealbumin mRNA, both species encoding members of the lipocalin superfamily."
Holzfeind P., Merschak P., Dieplinger H., Redl B.
Exp. Eye Res. 61:495-500(1995) [PubMed: 8549691] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 92-189.
Tissue: Lacrimal gland.
[9]"Apolipoprotein D is the major protein component in cyst fluid from women with human breast gross cystic disease."
Balbin M., Freije J.M.P., Fueyo A., Sanchez L.M., Lopez-Otin C.
Biochem. J. 271:803-807(1990) [PubMed: 2244881] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE OF 128-187.
[10]"Screening for N-glycosylated proteins by liquid chromatography mass spectrometry."
Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.
Proteomics 4:454-465(2004) [PubMed: 14760718] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-98, MASS SPECTROMETRY.
Tissue: Plasma.
[11]"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
J. Proteome Res. 4:2070-2080(2005) [PubMed: 16335952] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-98, MASS SPECTROMETRY.
Tissue: Plasma.
[12]"Is apolipoprotein D a mammalian bilin-binding protein?"
Peitsch M.C., Boguski M.S.
New Biol. 2:197-206(1990) [PubMed: 2083249] [Abstract]
Cited for: 3D-STRUCTURE MODELING, BILIN-BINDING.
[13]"Site-specific detection and structural characterization of the glycosylation of human plasma proteins lecithin:cholesterol acyltransferase and apolipoprotein D using HPLC/electrospray mass spectrometry and sequential glycosidase digestion."
Schindler P.A., Settineri C.A., Collet X., Fielding C.J., Burlingame A.L.
Protein Sci. 4:791-803(1995) [PubMed: 7613477] [Abstract]
Cited for: GLYCOSYLATION AT ASN-65 AND ASN-98.
[14]"Characterization of single-nucleotide polymorphisms in coding regions of human genes."
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S.
Nat. Genet. 22:231-238(1999) [PubMed: 10391209] [Abstract]
Cited for: VARIANTS SER-15; LEU-115 AND LYS-178.
[15]Erratum
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S.
Nat. Genet. 23:373-373(1999)
+Additional computationally mapped references.

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Cross-references

Sequence databases

J02611 mRNA. Translation: AAB59517.1.
M16696 Genomic DNA. Translation: AAA51764.1.
BT019860 mRNA. Translation: AAV38663.1.
BT019861 mRNA. Translation: AAV38664.1.
CR456838 mRNA. Translation: CAG33119.1.
CR541773 mRNA. Translation: CAG46572.1.
BC007402 mRNA. Translation: AAH07402.1.
S80440 mRNA. Translation: AAB35919.1.
PIRLPHUD. A26958.
RefSeqNP_001638.1.
UniGeneHs.522555

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2APDmodel-A21-189[»]
2HZQX-ray1.80A23-189[»]
2HZRX-ray1.80A23-189[»]
ModBaseSearch...

Protein-protein interaction databases

IntActP05090.

2-D gel databases

SWISS-2DPAGEP05090.

Proteomic databases

PeptideAtlasP05090.

Genome annotation databases

EnsemblENSG00000189058. Homo sapiens. [Contig view]
GeneID347.
KEGGhsa:347.

Organism-specific databases

H-InvDBHIX0003987.
HGNCHGNC:612. APOD.
MIM107740. gene.
PharmGKBPA24900.
GenAtlasSearch...
GeneCardsSearch...

Phylogenomic databases

HOGENOMP05090.
HOVERGENP05090.

Gene expression databases

ArrayExpressP05090.
CleanExHS_APOD.
GermOnlineENSG00000189058. Homo sapiens.

Family and domain databases

InterProIPR002969. ApolipopD.
IPR012674. Calycin.
IPR002345. Lipocalin.
IPR000566. Lipocln_cytFABP.
IPR002449. Retinol_bd.
[Graphical view]
Gene3DG3DSA:2.40.128.20. Calycin. 1 hit.
PANTHERPTHR11873. Retinol_bd. 1 hit.
PfamPF00061. Lipocalin. 1 hit.
[Graphical view]
PRINTSPR01219. APOLIPOPROTD.
PR00179. LIPOCALIN.
PROSITEPS00213. LIPOCALIN. 1 hit.
[Graphical view]
ProDomP05090.
[Graphical view] [Entries sharing at least one domain]
BLOCKSSearch...

Other Resources

SOURCESearch...
ProtoNetSearch...

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Entry information

Entry nameAPOD_HUMAN
AccessionPrimary (citable) accession number: P05090
Secondary accession number(s): Q6IBG6
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: July 22, 2008
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents