Skip Header

Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q9ULZ1 (APEL_HUMAN)

Last modified March 2, 2010. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
Apelin
Alternative name(s):
APJ endogenous ligand

Cleaved into the following 4 chains:

  1. Apelin-36
  2. Apelin-31
  3. Apelin-28
  4. Apelin-13
Gene names
Name:APLN
Synonyms:APEL
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length77 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

Endogenous ligand for APJ, an alternative coreceptor with CD4 for HIV-1 infection. Inhibits HIV-1 entry in cells coexpressing CD4 and APJ. Apelin-36 has a greater inhibitory activity on HIV infection than other synthetic apelin derivatives. The oral intake in the colostrum and the milk could have a role in the modulation of the immune responses in neonates. May also have a role in the central control of body fluid homeostasis by influencing AVP release and drinking behavior. Ref.6

Subcellular location

Secreted.

Tissue specificity

Expressed in the brain with highest levels in the frontal cortex, thalamus, hypothalamus and midbrain. Secreted by the mammary gland into the colostrum and the milk.

Post-translational modification

Several active peptides may be produced by proteolytic processing of the peptide precursor.

Sequence similarities

Belongs to the apelin family.

Sequence caution

The sequence CAI95697.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   Molecular functionHormone
   PTMCleavage on pair of basic residues
Pyrrolidone carboxylic acid
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processG-protein coupled receptor protein signaling pathway

Inferred from Experiment. Source: Reactome

immune response Ref.2

Traceable author statement. Source: ProtInc

lactation Ref.2

Traceable author statement. Source: ProtInc

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionhormone activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Propeptide23 – 4119 By similarity
PRO_0000001759
Peptide42 – 7736Apelin-36 By similarity
PRO_0000001760
Peptide47 – 7731Apelin-31 By similarity
PRO_0000001761
Peptide50 – 7728Apelin-28 By similarity
PRO_0000001762
Peptide65 – 7713Apelin-13 By similarity
PRO_0000001763

Amino acid modifications

Modified residue651Pyrrolidone carboxylic acid By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9ULZ1-1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 41521E0DBE97BFDA

FASTA778,569
        10         20         30         40         50         60 
MNLRLCVQAL LLLWLSLTAV CGGSLMPLPD GNGLEDGNVR HLVQPRGSRN GPGPWQGGRR 

        70 
KFRRQRPRLS HKGPMPF 

« Hide

References

« Hide 'large scale' references
[1]"Isolation and characterization of a novel endogenous peptide ligand for the human APJ receptor."
Tatemoto K., Hosoya M., Habata Y., Fujii R., Kakegawa T., Zou M.-X., Kawamata Y., Fukusumi S., Hinuma S., Kitada C., Kurokawa T., Onda H., Fujino M.
Biochem. Biophys. Res. Commun. 251:471-476(1998) [PubMed: 9792798] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[2]"Apelin, the natural ligand of the orphan receptor APJ, is abundantly secreted in the colostrum."
Habata Y., Fujii R., Hosoya M., Fukusumi S., Kawamata Y., Hinuma S., Kitada C., Nishizawa N., Murosaki S., Kurokawa T., Onda H., Tatemoto K., Fujino M.
Biochim. Biophys. Acta 1452:25-35(1999) [PubMed: 10525157] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[3]"Characterization of apelin, the ligand for the APJ receptor."
Lee D.K., Cheng R., Nguyen T., Fan T., Kariyawasam A.P., Liu Y., Osmond D.H., George S.R., O'Dowd B.F.
J. Neurochem. 74:34-41(2000) [PubMed: 10617103] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Hypothalamus.
[4]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [PubMed: 15772651] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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: Kidney.
[6]"Apelin, the natural ligand of the orphan seven-transmembrane receptor APJ, inhibits human immunodeficiency virus type 1 entry."
Cayabyab M., Hinuma S., Farzan M., Choe H., Fukusumi S., Kitada C., Nishizawa N., Hosoya M., Nishimura O., Messele T., Pollakis G., Goudsmit J., Fujino M., Sodroski J.
J. Virol. 74:11972-11976(2000) [PubMed: 11090199] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB023493 mRNA. Translation: BAA84975.1.
AF179680 Genomic DNA. Translation: AAF25815.1.
AL022162 Genomic DNA. Translation: CAI95697.1. Sequence problems.
BC021104 mRNA. Translation: AAH21104.2.
IPIIPI00010087.
RefSeqNP_059109.3.
UniGeneHs.303084

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

IntActQ9ULZ1. 1 interaction.

Genome annotation databases

EnsemblENST00000307484; ENSP00000305464; ENSG00000171388; Homo sapiens. [Genome view]
GeneID8862.
KEGGhsa:8862.
UCSCuc004eus.1. human.

Organism-specific databases

CTD8862.
GeneCardsGC0XM128607.
H-InvDBHIX0017039.
HGNCHGNC:16665. APLN.
MIM300297. gene.
PharmGKBPA134984493.
GenAtlasSearch...

Phylogenomic databases

HOVERGENHBG018249.
OrthoDBEOG9G7FK1.

Enzyme and pathway databases

ReactomeREACT_14797. Signaling by GPCR.

Gene expression databases

ArrayExpressQ9ULZ1.
BgeeQ9ULZ1.
CleanExHS_APLN.
GenevestigatorQ9ULZ1.

Family and domain databases

ProtoNetSearch...

Other Resources

NextBio33277.
SOURCESearch...

Entry information

Entry nameAPEL_HUMAN
AccessionPrimary (citable) accession number: Q9ULZ1
Secondary accession number(s): Q4VY08, Q8WU89
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: May 1, 2000
Last modified: March 2, 2010
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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

Human chromosome X

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

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families

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