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Q13790 (APOF_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Apolipoprotein F

Short name=Apo-F
Alternative name(s):
Lipid transfer inhibitor protein
Short name=LTIP
Gene names
Name:APOF
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length326 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Minor apolipoprotein that associates with LDL. Inhibits cholesteryl ester transfer protein (CETP) activity and appears to be an important regulator of cholesterol transport. Also associates to a lesser degree with VLDL, Apo-AI and Apo-AII. Ref.2

Subcellular location

Secreted.

Tissue specificity

Expressed by the liver and secreted in plasma. Ref.1

Post-translational modification

O-glycosylated with core 1 or possibly core 8 glycans. Ref.6

Caution

It is uncertain whether Met-1 or Met-12 is the initiator.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3535 Potential
Propeptide36 – 164129
PRO_0000002051
Chain165 – 326162Apolipoprotein F
PRO_0000002052

Amino acid modifications

Glycosylation1181N-linked (GlcNAc...) Potential
Glycosylation2741O-linked (GalNAc...) Ref.6

Natural variations

Natural variant1781A → G.
Corresponds to variant rs11575216 [ dbSNP | Ensembl ].
VAR_055520

Sequences

Sequence LengthMass (Da)Tools
Q13790 [UniParc].

Last modified April 5, 2011. Version 2.
Checksum: 046A1E775E7D4320

FASTA32635,399
        10         20         30         40         50         60 
MTGLCGYSAP DMRGLRLIMI PVELLLCYLL LHPVDATSYG KQTNVLMHFP LSLESQTPSS 

        70         80         90        100        110        120 
DPLSCQFLHP KSLPGFSHMA PLPKFLVSLA LRNALEEAGC QADVWALQLQ LYRQGGVNAT 

       130        140        150        160        170        180 
QVLIQHLRGL QKGRSTERNV SVEALASALQ LLAREQQSTG RVGRSLPTED CENEKEQAVH 

       190        200        210        220        230        240 
NVVQLLPGVG TFYNLGTALY YATQNCLGKA RERGRDGAID LGYDLLMTMA GMSGGPMGLA 

       250        260        270        280        290        300 
ISAALKPALR SGVQQLIQYY QDQKDANISQ PETTKEGLRA ISDVSDLEET TTLASFISEV 

       310        320 
VSSAPYWGWA IIKSYDLDPG AGSLEI 

« Hide

References

« Hide 'large scale' references
[1]"Purification and molecular cloning of human apolipoprotein F."
Day J.R., Albers J.J., Gilbert T.L., Whitmore T.E., McConathy W.J., Wolfbauer G.
Biochem. Biophys. Res. Commun. 203:1146-1151(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 165-194 AND 251-265, TISSUE SPECIFICITY.
Tissue: Hepatoma.
[2]"Molecular cloning and expression of lipid transfer inhibitor protein reveals its identity with apolipoprotein F."
Wang X., Driscoll D.M., Morton R.E.
J. Biol. Chem. 274:1814-1820(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 165-178, FUNCTION.
Tissue: Liver and Plasma.
[3]"The finished DNA sequence of human chromosome 12."
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. expand/collapse author list , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Liver.
[5]"Isolation and partial characterization of a new acidic apolipoprotein (apolipoprotein F) from high density lipoproteins of human plasma."
Olofsson S.-O., McConathy W.J., Alaupovic P.
Biochemistry 17:1032-1036(1978) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[6]"Human urinary glycoproteomics; attachment site specific analysis of N-and O-linked glycosylations by CID and ECD."
Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.
Mol. Cell. Proteomics 0:0-0(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT THR-274, STRUCTURE OF CARBOHYDRATES, IDENTIFICATION BY MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L27050 mRNA. Translation: AAA65642.1.
AC025574 Genomic DNA. No translation available.
BC026257 mRNA. Translation: AAH26257.1.
PIRJC2549.
RefSeqNP_001629.1. NM_001638.2.
UniGeneHs.534302.

3D structure databases

ProteinModelPortalQ13790.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106816. 2 interactions.
STRING9606.ENSP00000381250.

Polymorphism databases

DMDM327478500.

Proteomic databases

PaxDbQ13790.
PRIDEQ13790.

Protocols and materials databases

DNASU319.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000398189; ENSP00000381250; ENSG00000175336.
GeneID319.
KEGGhsa:319.
UCSCuc001sle.1. human.

Organism-specific databases

CTD319.
GeneCardsGC12M056754.
HGNCHGNC:615. APOF.
MIM107760. gene.
neXtProtNX_Q13790.
PharmGKBPA24902.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG68175.
HOGENOMHOG000034007.
HOVERGENHBG050551.
InParanoidQ13790.
OMAPKSLPGF.
PhylomeDBQ13790.
TreeFamTF338778.

Gene expression databases

ArrayExpressQ13790.
BgeeQ13790.
CleanExHS_APOF.
GenevestigatorQ13790.

Family and domain databases

InterProIPR026114. APOF.
[Graphical view]
PANTHERPTHR15011. PTHR15011. 1 hit.
PfamPF15148. Apolipo_F. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiAPOF.
GenomeRNAi319.
NextBio1307.
PROQ13790.
SOURCESearch...

Entry information

Entry nameAPOF_HUMAN
AccessionPrimary (citable) accession number: Q13790
Secondary accession number(s): Q8TC13
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: April 5, 2011
Last modified: April 16, 2014
This is version 103 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM