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Protein

Apelin

Gene

APLN

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

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.1 Publication

GO - Molecular functioni

  1. G-protein coupled receptor binding Source: GO_Central
  2. receptor binding Source: ProtInc

GO - Biological processi

  1. immune response Source: ProtInc
  2. lactation Source: ProtInc
  3. signaling Source: GO_Central
  4. signal transduction Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Hormone

Enzyme and pathway databases

ReactomeiREACT_14819. Peptide ligand-binding receptors.
REACT_19231. G alpha (i) signalling events.

Names & Taxonomyi

Protein namesi
Recommended name:
Apelin
Alternative name(s):
APJ endogenous ligand
Cleaved into the following 4 chains:
Gene namesi
Name:APLN
Synonyms:APEL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Unplaced

Organism-specific databases

HGNCiHGNC:16665. APLN.

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: Reactome
  2. extracellular space Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134984493.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Sequence AnalysisAdd
BLAST
Propeptidei23 – 4119By similarityPRO_0000001759Add
BLAST
Peptidei42 – 7736Apelin-36By similarityPRO_0000001760Add
BLAST
Peptidei47 – 7731Apelin-31By similarityPRO_0000001761Add
BLAST
Peptidei50 – 7728Apelin-28By similarityPRO_0000001762Add
BLAST
Peptidei65 – 7713Apelin-13By similarityPRO_0000001763Add
BLAST

Post-translational modificationi

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

Keywords - PTMi

Cleavage on pair of basic residues

Proteomic databases

PRIDEiQ9ULZ1.

Expressioni

Tissue specificityi

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.

Gene expression databases

BgeeiQ9ULZ1.
CleanExiHS_APLN.
GenevestigatoriQ9ULZ1.

Interactioni

Protein-protein interaction databases

BioGridi114385. 4 interactions.
IntActiQ9ULZ1. 1 interaction.
STRINGi9606.ENSP00000305464.

Structurei

3D structure databases

ProteinModelPortaliQ9ULZ1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the apelin family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG86365.
HOGENOMiHOG000033992.
HOVERGENiHBG018249.
InParanoidiQ9ULZ1.
KOiK05225.
OMAiLVKPRTS.
OrthoDBiEOG7W6WNK.
PhylomeDBiQ9ULZ1.
TreeFamiTF339660.

Family and domain databases

InterProiIPR026155. Apelin.
[Graphical view]
PANTHERiPTHR15953. PTHR15953. 1 hit.
PfamiPF15360. Apelin. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9ULZ1-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNLRLCVQAL LLLWLSLTAV CGGSLMPLPD GNGLEDGNVR HLVQPRGSRN
60 70
GPGPWQGGRR KFRRQRPRLS HKGPMPF
Length:77
Mass (Da):8,569
Last modified:May 1, 2000 - v1
Checksum:i41521E0DBE97BFDA
GO

Sequence cautioni

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB023493 mRNA. Translation: BAA84975.1.
AF179680 Genomic DNA. Translation: AAF25815.1.
AL022162 Genomic DNA. Translation: CAI95697.1. Sequence problems.
BC021104 mRNA. Translation: AAH21104.2.
RefSeqiNP_059109.3. NM_017413.4.
UniGeneiHs.303084.

Genome annotation databases

EnsembliENST00000307484; ENSP00000305464; ENSG00000171388.
GeneIDi8862.
KEGGihsa:8862.
UCSCiuc004eus.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB023493 mRNA. Translation: BAA84975.1.
AF179680 Genomic DNA. Translation: AAF25815.1.
AL022162 Genomic DNA. Translation: CAI95697.1. Sequence problems.
BC021104 mRNA. Translation: AAH21104.2.
RefSeqiNP_059109.3. NM_017413.4.
UniGeneiHs.303084.

3D structure databases

ProteinModelPortaliQ9ULZ1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114385. 4 interactions.
IntActiQ9ULZ1. 1 interaction.
STRINGi9606.ENSP00000305464.

Proteomic databases

PRIDEiQ9ULZ1.

Protocols and materials databases

DNASUi8862.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000307484; ENSP00000305464; ENSG00000171388.
GeneIDi8862.
KEGGihsa:8862.
UCSCiuc004eus.3. human.

Organism-specific databases

CTDi8862.
GeneCardsiGC0XM128779.
HGNCiHGNC:16665. APLN.
MIMi300297. gene.
neXtProtiNX_Q9ULZ1.
PharmGKBiPA134984493.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG86365.
HOGENOMiHOG000033992.
HOVERGENiHBG018249.
InParanoidiQ9ULZ1.
KOiK05225.
OMAiLVKPRTS.
OrthoDBiEOG7W6WNK.
PhylomeDBiQ9ULZ1.
TreeFamiTF339660.

Enzyme and pathway databases

ReactomeiREACT_14819. Peptide ligand-binding receptors.
REACT_19231. G alpha (i) signalling events.

Miscellaneous databases

ChiTaRSiAPLN. human.
GeneWikiiApelin.
GenomeRNAii8862.
NextBioi33277.
PROiQ9ULZ1.
SOURCEiSearch...

Gene expression databases

BgeeiQ9ULZ1.
CleanExiHS_APLN.
GenevestigatoriQ9ULZ1.

Family and domain databases

InterProiIPR026155. Apelin.
[Graphical view]
PANTHERiPTHR15953. PTHR15953. 1 hit.
PfamiPF15360. Apelin. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. 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. 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.

Entry informationi

Entry nameiAPEL_HUMAN
AccessioniPrimary (citable) accession number: Q9ULZ1
Secondary accession number(s): Q4VY08, Q8WU89
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: May 1, 2000
Last modified: February 4, 2015
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.