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Protein

Apolipoprotein A-IV

Gene

Apoa4

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May have a role in chylomicrons and VLDL secretion and catabolism. Required for efficient activation of lipoprotein lipase by ApoC-II; potent activator of LCAT. Apoa-IV is a major component of HDL and chylomicrons.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Lipid transport, Transport

Enzyme and pathway databases

ReactomeiR-MMU-174800. Chylomicron-mediated lipid transport.
R-MMU-975634. Retinoid metabolism and transport.

Names & Taxonomyi

Protein namesi
Recommended name:
Apolipoprotein A-IV
Short name:
Apo-AIV
Short name:
ApoA-IV
Alternative name(s):
Apolipoprotein A4
Gene namesi
Name:Apoa4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:88051. Apoa4.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chylomicron, HDL, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Add
BLAST
Chaini21 – 395375Apolipoprotein A-IVPRO_0000001977Add
BLAST

Proteomic databases

EPDiP06728.
MaxQBiP06728.
PaxDbiP06728.
PeptideAtlasiP06728.
PRIDEiP06728.

PTM databases

iPTMnetiP06728.
PhosphoSiteiP06728.

Expressioni

Tissue specificityi

Secreted in plasma.

Gene expression databases

BgeeiP06728.
CleanExiMM_APOA4.
GenevisibleiP06728. MM.

Interactioni

Subunit structurei

Homodimer.By similarity

GO - Molecular functioni

Protein-protein interaction databases

IntActiP06728. 2 interactions.
MINTiMINT-1856096.
STRINGi10090.ENSMUSP00000034585.

Structurei

3D structure databases

ProteinModelPortaliP06728.
SMRiP06728. Positions 25-364.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati33 – 54221Add
BLAST
Repeati60 – 81222Add
BLAST
Repeati82 – 103223Add
BLAST
Repeati115 – 136224Add
BLAST
Repeati137 – 158225Add
BLAST
Repeati159 – 180226Add
BLAST
Repeati181 – 202227Add
BLAST
Repeati203 – 224228Add
BLAST
Repeati225 – 246229Add
BLAST
Repeati247 – 2682210Add
BLAST
Repeati269 – 2861811Add
BLAST
Repeati287 – 3082212Add
BLAST
Repeati309 – 3302213Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni33 – 33029813 X 22 AA approximate tandem repeatsAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi366 – 38924Gln/Glu-richAdd
BLAST

Domaini

Nine of the thirteen 22-amino acid tandem repeats (each 22-mer is actually a tandem array of two, A and B, related 11-mers) occurring in this sequence are predicted to be highly alpha-helical, and many of these helices are amphipathic. They may therefore serve as lipid-binding domains with lecithin:cholesterol acyltransferase (LCAT) activating abilities.

Sequence similaritiesi

Belongs to the apolipoprotein A1/A4/E family.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiENOG410IKU1. Eukaryota.
ENOG41119VI. LUCA.
GeneTreeiENSGT00530000063081.
HOGENOMiHOG000037942.
HOVERGENiHBG105707.
InParanoidiP06728.
KOiK08760.
OMAiRTQVNTQ.
OrthoDBiEOG7K9K48.
TreeFamiTF334458.

Family and domain databases

InterProiIPR000074. ApoA_E.
[Graphical view]
PfamiPF01442. Apolipoprotein. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P06728-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFLKAAVLTL ALVAITGTRA EVTSDQVANV VWDYFTQLSN NAKEAVEQFQ
60 70 80 90 100
KTDVTQQLST LFQDKLGDAS TYADGVHNKL VPFVVQLSGH LAQETERVKE
110 120 130 140 150
EIKKELEDLR DRMMPHANKV TQTFGENMQK LQEHLKPYAV DLQDQINTQT
160 170 180 190 200
QEMKLQLTPY IQRMQTTIKE NVDNLHTSMM PLATNLKDKF NRNMEELKGH
210 220 230 240 250
LTPRANELKA TIDQNLEDLR RSLAPLTVGV QEKLNHQMEG LAFQMKKNAE
260 270 280 290 300
ELQTKVSAKI DQLQKNLAPL VEDVQSKVKG NTEGLQKSLE DLNRQLEQQV
310 320 330 340 350
EEFRRTVEPM GEMFNKALVQ QLEQFRQQLG PNSGEVESHL SFLEKSLREK
360 370 380 390
VNSFMSTLEK KGSPDQPQAL PLPEQAQEQA QEQAQEQVQP KPLES
Length:395
Mass (Da):45,029
Last modified:July 27, 2011 - v3
Checksum:iC48BE32EED441F71
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti15 – 151Missing in AAA37253 (PubMed:3796595).Curated
Sequence conflicti63 – 631Q → K in AAA37253 (PubMed:3796595).Curated
Sequence conflicti93 – 931Q → K in AAA37253 (PubMed:3796595).Curated
Sequence conflicti93 – 931Q → K in AAA37214 (PubMed:1648102).Curated
Sequence conflicti93 – 931Q → K in AAA37215 (PubMed:1648102).Curated
Sequence conflicti207 – 2071E → R in AAA37253 (PubMed:3796595).Curated
Sequence conflicti288 – 2881S → A in AAA37253 (PubMed:3796595).Curated
Sequence conflicti294 – 2952RQ → KA in AAA37253 (PubMed:3796595).Curated
Sequence conflicti315 – 3162NK → GG in AAA37253 (PubMed:3796595).Curated

Polymorphismi

There is a polymorphism within a series of imperfect repeats encoding the sequence E-Q-[AV]-Q. Insertions or deletions of 12 nucleotides have given rise to three forms characterized by three (129), four (C57BL/6), or five (M.castaneus) copies of the repeat unit.1 Publication

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti382 – 3854Missing in strain: various strains.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M13966 Genomic DNA. Translation: AAA37253.1.
M64248 mRNA. Translation: AAA37214.1.
M64249 mRNA. Translation: AAA37215.1.
AK161535 mRNA. Translation: BAE36447.1.
AK168687 mRNA. Translation: BAE40533.1.
CH466522 Genomic DNA. Translation: EDL25684.1.
BC010769 mRNA. Translation: AAH10769.1.
CCDSiCCDS23142.1.
PIRiA25281.
A40892.
B40892.
RefSeqiNP_031494.2. NM_007468.2.
UniGeneiMm.4533.

Genome annotation databases

EnsembliENSMUST00000034585; ENSMUSP00000034585; ENSMUSG00000032080.
GeneIDi11808.
KEGGimmu:11808.
UCSCiuc009phd.1. mouse.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M13966 Genomic DNA. Translation: AAA37253.1.
M64248 mRNA. Translation: AAA37214.1.
M64249 mRNA. Translation: AAA37215.1.
AK161535 mRNA. Translation: BAE36447.1.
AK168687 mRNA. Translation: BAE40533.1.
CH466522 Genomic DNA. Translation: EDL25684.1.
BC010769 mRNA. Translation: AAH10769.1.
CCDSiCCDS23142.1.
PIRiA25281.
A40892.
B40892.
RefSeqiNP_031494.2. NM_007468.2.
UniGeneiMm.4533.

3D structure databases

ProteinModelPortaliP06728.
SMRiP06728. Positions 25-364.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP06728. 2 interactions.
MINTiMINT-1856096.
STRINGi10090.ENSMUSP00000034585.

PTM databases

iPTMnetiP06728.
PhosphoSiteiP06728.

Proteomic databases

EPDiP06728.
MaxQBiP06728.
PaxDbiP06728.
PeptideAtlasiP06728.
PRIDEiP06728.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000034585; ENSMUSP00000034585; ENSMUSG00000032080.
GeneIDi11808.
KEGGimmu:11808.
UCSCiuc009phd.1. mouse.

Organism-specific databases

CTDi337.
MGIiMGI:88051. Apoa4.

Phylogenomic databases

eggNOGiENOG410IKU1. Eukaryota.
ENOG41119VI. LUCA.
GeneTreeiENSGT00530000063081.
HOGENOMiHOG000037942.
HOVERGENiHBG105707.
InParanoidiP06728.
KOiK08760.
OMAiRTQVNTQ.
OrthoDBiEOG7K9K48.
TreeFamiTF334458.

Enzyme and pathway databases

ReactomeiR-MMU-174800. Chylomicron-mediated lipid transport.
R-MMU-975634. Retinoid metabolism and transport.

Miscellaneous databases

ChiTaRSiApoa4. mouse.
PROiP06728.
SOURCEiSearch...

Gene expression databases

BgeeiP06728.
CleanExiMM_APOA4.
GenevisibleiP06728. MM.

Family and domain databases

InterProiIPR000074. ApoA_E.
[Graphical view]
PfamiPF01442. Apolipoprotein. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Mouse apolipoprotein A-IV gene: nucleotide sequence and induction by a high-lipid diet."
    Williams S.C., Bruckheimer S.M., Lusis A.J., LeBoeuf R.C., Kinniburgh A.J.
    Mol. Cell. Biol. 6:3807-3814(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Kinniburgh A.J.
    Submitted (DEC-1986) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  3. "Genetic variation in mouse apolipoprotein A-IV due to insertion and deletion in a region of tandem repeats."
    Reue K., Leete T.H.
    J. Biol. Chem. 266:12715-12721(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], POLYMORPHISM.
    Strain: 129/J and C57BL/6J.
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Amnion.
  5. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Kidney.
  7. "Mass spectral analysis of the apolipoproteins on mouse high density lipoproteins. Detection of post-translational modifications."
    Puppione D.L., Yam L.M., Bassilian S., Souda P., Castellani L.W., Schumaker V.N., Whitelegge J.P.
    Biochim. Biophys. Acta 1764:1363-1371(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 52-97; 155-163; 193-204; 222-233 AND 306-326, IDENTIFICATION BY MASS SPECTROMETRY.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiAPOA4_MOUSE
AccessioniPrimary (citable) accession number: P06728
Secondary accession number(s): Q91XF8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: July 27, 2011
Last modified: July 6, 2016
This is version 138 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.