Q9ULZ1 (APEL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	77 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 component	Secreted
Domain	Signal
Molecular function	Hormone
PTM	Cleavage on pair of basic residues
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	drinking behavior Inferred from electronic annotation. Source: Compara immune response Traceable author statement Ref.2. Source: ProtInc lactation Traceable author statement Ref.2. Source: ProtInc negative regulation of blood pressure Inferred from electronic annotation. Source: Compara negative regulation of vasoconstriction Inferred from electronic annotation. Source: Compara positive regulation of cell proliferation Inferred from electronic annotation. Source: Compara positive regulation of corticotropin secretion Inferred from electronic annotation. Source: Compara positive regulation of corticotropin-releasing hormone secretion Inferred from electronic annotation. Source: Compara positive regulation of heat generation Inferred from electronic annotation. Source: Compara positive regulation of phosphorylation Inferred from electronic annotation. Source: Compara positive regulation of vasodilation Inferred from electronic annotation. Source: Compara regulation of respiratory gaseous exchange Inferred from electronic annotation. Source: Compara regulation of the force of heart contraction Inferred from electronic annotation. Source: Compara signal transduction Traceable author statement Ref.1. Source: ProtInc
Cellular_component	extracellular region Traceable author statement. Source: Reactome extracellular space Inferred from electronic annotation. Source: Compara perinuclear region of cytoplasm Inferred from electronic annotation. Source: Compara
Molecular_function	receptor binding Traceable author statement Ref.2Ref.1. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 22	22	Potential
	Propeptide	23 – 41	19	By similarity		PRO_0000001759
	Peptide	42 – 77	36	Apelin-36 By similarity		PRO_0000001760
	Peptide	47 – 77	31	Apelin-31 By similarity		PRO_0000001761
	Peptide	50 – 77	28	Apelin-28 By similarity		PRO_0000001762
	Peptide	65 – 77	13	Apelin-13 By similarity		PRO_0000001763

Sequences

	Sequence		Length	Mass (Da)
	Q9ULZ1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 41521E0DBE97BFDA	FASTA	77	8,569
	10 20 30 40 50 60 MNLRLCVQAL LLLWLSLTAV CGGSLMPLPD GNGLEDGNVR HLVQPRGSRN GPGPWQGGRR 70 KFRRQRPRLS HKGPMPF

References

	« Hide 'large scale' referencesShow '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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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. , 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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.
IPI	IPI00010087.
RefSeq	NP_059109.3. NM_017413.4.
UniGene	Hs.303084.
3D structure databases
ProteinModelPortal	Q9ULZ1.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9ULZ1. 1 interaction.
STRING	9606.ENSP00000305464.
Proteomic databases
PRIDE	Q9ULZ1.
Protocols and materials databases
DNASU	8862.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000307484; ENSP00000305464; ENSG00000171388.
GeneID	8862.
KEGG	hsa:8862.
UCSC	uc004eus.3. human.
Organism-specific databases
CTD	8862.
GeneCards	GC0XM128779.
HGNC	HGNC:16665. APLN.
MIM	300297. gene.
neXtProt	NX_Q9ULZ1.
PharmGKB	PA134984493.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG86365.
HOGENOM	HOG000033992.
HOVERGEN	HBG018249.
KO	K05225.
Enzyme and pathway databases
Reactome	REACT_111102. Signal Transduction.
Gene expression databases
ArrayExpress	Q9ULZ1.
Bgee	Q9ULZ1.
CleanEx	HS_APLN.
Genevestigator	Q9ULZ1.
Family and domain databases
InterPro	IPR026155. Apelin. [Graphical view]
PANTHER	PTHR15953. PTHR15953. 1 hit.
ProtoNet	Search...
Other
GenomeRNAi	8862.
NextBio	33277.
SOURCE	Search...

Entry information

Entry name

APEL_HUMAN

Accession

Primary (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:	April 3, 2013
This is version 86 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.