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Q9ULZ1

- APEL_HUMAN

UniProt

Q9ULZ1 - APEL_HUMAN

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Protein

Apelin

Gene

APLN

Organism
Homo sapiens (Human)
Status
Reviewed - 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. receptor binding Source: ProtInc

GO - Biological processi

  1. immune response Source: ProtInc
  2. lactation Source: ProtInc
  3. 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
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. 2 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.
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 .
RefSeqi NP_059109.3. NM_017413.4.
UniGenei Hs.303084.

3D structure databases

ProteinModelPortali Q9ULZ1.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114385. 2 interactions.
IntActi Q9ULZ1. 1 interaction.
STRINGi 9606.ENSP00000305464.

Proteomic databases

PRIDEi Q9ULZ1.

Protocols and materials databases

DNASUi 8862.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000307484 ; ENSP00000305464 ; ENSG00000171388 .
GeneIDi 8862.
KEGGi hsa:8862.
UCSCi uc004eus.3. human.

Organism-specific databases

CTDi 8862.
GeneCardsi GC0XM128779.
HGNCi HGNC:16665. APLN.
MIMi 300297. gene.
neXtProti NX_Q9ULZ1.
PharmGKBi PA134984493.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG86365.
HOGENOMi HOG000033992.
HOVERGENi HBG018249.
InParanoidi Q9ULZ1.
KOi K05225.
OrthoDBi EOG7W6WNK.
PhylomeDBi Q9ULZ1.
TreeFami TF339660.

Enzyme and pathway databases

Reactomei REACT_14819. Peptide ligand-binding receptors.
REACT_19231. G alpha (i) signalling events.

Miscellaneous databases

ChiTaRSi APLN. human.
GeneWikii Apelin.
GenomeRNAii 8862.
NextBioi 33277.
PROi Q9ULZ1.
SOURCEi Search...

Gene expression databases

Bgeei Q9ULZ1.
CleanExi HS_APLN.
Genevestigatori Q9ULZ1.

Family and domain databases

InterProi IPR026155. Apelin.
[Graphical view ]
PANTHERi PTHR15953. PTHR15953. 1 hit.
Pfami PF15360. Apelin. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: November 26, 2014
This is version 98 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