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Q9Y5Q6 (INSL5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Insulin-like peptide INSL5

Short name=Insulin-like peptide 5
Gene names
Name:INSL5
ORF Names:UNQ156/PRO182
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length135 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May have a role in gut contractility or in thymic development and regulation. Activates RXFP4 with high potency and appears to be the endogenous ligand for this receptor.

Subunit structure

Heterodimer of a B chain and an A chain linked by two disulfide bonds.

Subcellular location

Secreted.

Tissue specificity

Highly expressed in rectum with lower levels in uterus and ascending and descending colon. Ref.1

Sequence similarities

Belongs to the insulin family.

Ontologies

Keywords
   Cellular componentSecreted
   Coding sequence diversityPolymorphism
   DomainSignal
   Molecular functionHormone
   PTMCleavage on pair of basic residues
Disulfide bond
Pyrrolidone carboxylic acid
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Cellular_componentextracellular region

Traceable author statement. Source: Reactome

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Ref.5
Peptide23 – 4624Insulin-like peptide INSL5 B chain
PRO_0000016163
Propeptide49 – 11466Connecting peptide Potential
PRO_0000016164
Peptide115 – 13521Insulin-like peptide INSL5 A chain
PRO_0000016165

Amino acid modifications

Modified residue1151Pyrrolidone carboxylic acid
Disulfide bond29 ↔ 122Interchain (between B and A chains) Ref.7
Disulfide bond41 ↔ 135Interchain (between B and A chains) Ref.7
Disulfide bond121 ↔ 126 Ref.7

Natural variations

Natural variant501Q → L. Ref.1 Ref.2 Ref.4
Corresponds to variant rs549148 [ dbSNP | Ensembl ].
VAR_046099

Secondary structure

......... 135
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9Y5Q6 [UniParc].

Last modified September 2, 2008. Version 2.
Checksum: A932D7EDE9D173F5

FASTA13515,333
        10         20         30         40         50         60 
MKGSIFTLFL FSVLFAISEV RSKESVRLCG LEYIRTVIYI CASSRWRRHQ EGIPQAQQAE 

        70         80         90        100        110        120 
TGNSFQLPHK REFSEENPAQ NLPKVDASGE DRLWGGQMPT EELWKSKKHS VMSRQDLQTL 

       130 
CCTDGCSMTD LSALC 

« Hide

References

« Hide 'large scale' references
[1]"Identification of INSL5, a new member of the insulin superfamily."
Conklin D., Lofton-Day C.E., Haldeman B.A., Ching A., Whitmore T.E., Lok S., Jaspers S.
Genomics 60:50-56(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, VARIANT LEU-50.
Tissue: Colon.
[2]"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment."
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. expand/collapse author list , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.
Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT LEU-50.
[3]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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], VARIANT LEU-50.
Tissue: Brain.
[5]"Signal peptide prediction based on analysis of experimentally verified cleavage sites."
Zhang Z., Henzel W.J.
Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 23-37.
[6]"INSL5 is a high affinity specific agonist for GPCR142 (GPR100)."
Liu C., Kuei C., Sutton S., Chen J., Bonaventure P., Wu J., Nepomuceno D., Kamme F., Tran D.T., Zhu J., Wilkinson T., Bathgate R., Eriste E., Sillard R., Lovenberg T.W.
J. Biol. Chem. 280:292-300(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: BINDING TO RXFP4.
[7]"Synthesis, conformation, and activity of human insulin-like peptide 5 (INSL5)."
Akhter Hossain M., Bathgate R.A.D., Kong C.K., Shabanpoor F., Zhang S., Haugaard-Joensson L.M., Rosengren K.J., Tregear G.W., Wade J.D.
ChemBioChem 9:1816-1822(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: SYNTHESIS OF 23-46 AND 115-135, DISULFIDE BONDS, PYROGLUTAMATE FORMATION AT GLN-115.
[8]"Structure of human insulin-like peptide 5 and characterization of conserved hydrogen bonds and electrostatic interactions within the relaxin framework."
Haugaard-Joensson L.M., Hossain M.A., Daly N.L., Craik D.J., Wade J.D., Rosengren K.J.
Biochem. J. 419:619-627(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 23-46 AND 115-135.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF133816 mRNA. Translation: AAD29686.1.
AY359030 mRNA. Translation: AAQ89389.1.
AL354978 Genomic DNA. Translation: CAH71844.1.
BC101646 mRNA. Translation: AAI01647.1.
BC101648 mRNA. Translation: AAI01649.1.
RefSeqNP_005469.2. NM_005478.4.
UniGeneHs.251380.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2K1VNMR-A116-135[»]
2KBCNMR-A116-135[»]
B23-46[»]
ProteinModelPortalQ9Y5Q6.
SMRQ9Y5Q6. Positions 21-46, 110-135.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000302724.

Polymorphism databases

DMDM205371762.

Proteomic databases

PaxDbQ9Y5Q6.
PRIDEQ9Y5Q6.

Protocols and materials databases

DNASU10022.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000304526; ENSP00000302724; ENSG00000172410.
GeneID10022.
KEGGhsa:10022.
UCSCuc001dcw.3. human.

Organism-specific databases

CTD10022.
GeneCardsGC01M067223.
H-InvDBHIX0028561.
HGNCHGNC:6088. INSL5.
HPACAB033849.
HPA030100.
MIM606413. gene.
neXtProtNX_Q9Y5Q6.
PharmGKBPA29895.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG38979.
HOGENOMHOG000111888.
HOVERGENHBG052135.
InParanoidQ9Y5Q6.
OMAIRTVIYI.
OrthoDBEOG73V6N0.
PhylomeDBQ9Y5Q6.
TreeFamTF333404.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.

Gene expression databases

BgeeQ9Y5Q6.
CleanExHS_INSL5.
GenevestigatorQ9Y5Q6.

Family and domain databases

InterProIPR016179. Insulin-like.
IPR022353. Insulin_CS.
[Graphical view]
PfamPF00049. Insulin. 1 hit.
[Graphical view]
SMARTSM00078. IlGF. 1 hit.
[Graphical view]
SUPFAMSSF56994. SSF56994. 2 hits.
PROSITEPS00262. INSULIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9Y5Q6.
GeneWikiINSL5.
GenomeRNAi10022.
NextBio37869.
PROQ9Y5Q6.
SOURCESearch...

Entry information

Entry nameINSL5_HUMAN
AccessionPrimary (citable) accession number: Q9Y5Q6
Secondary accession number(s): Q3MIY4, Q5VYD8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: September 2, 2008
Last modified: March 19, 2014
This is version 115 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM