SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9Y5Q6

- INSL5_HUMAN

UniProt

Q9Y5Q6 - INSL5_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Insulin-like peptide INSL5
Gene
INSL5, UNQ156/PRO182
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.

Keywords - Molecular functioni

Hormone

Enzyme and pathway databases

ReactomeiREACT_19231. G alpha (i) signalling events.
REACT_21314. Relaxin receptors.

Names & Taxonomyi

Protein namesi
Recommended name:
Insulin-like peptide INSL5
Short name:
Insulin-like peptide 5
Cleaved into the following 2 chains:
Gene namesi
Name:INSL5
ORF Names:UNQ156/PRO182
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:6088. INSL5.

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29895.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 22221 Publication
Add
BLAST
Peptidei23 – 4624Insulin-like peptide INSL5 B chain
PRO_0000016163Add
BLAST
Propeptidei49 – 11466Connecting peptide Reviewed prediction
PRO_0000016164Add
BLAST
Peptidei115 – 13521Insulin-like peptide INSL5 A chain
PRO_0000016165Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi29 ↔ 122Interchain (between B and A chains)1 Publication
Disulfide bondi41 ↔ 135Interchain (between B and A chains)1 Publication
Modified residuei115 – 1151Pyrrolidone carboxylic acid
Disulfide bondi121 ↔ 1261 Publication

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Pyrrolidone carboxylic acid

Proteomic databases

PaxDbiQ9Y5Q6.
PRIDEiQ9Y5Q6.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiQ9Y5Q6.
CleanExiHS_INSL5.
GenevestigatoriQ9Y5Q6.

Organism-specific databases

HPAiCAB033849.
HPA030100.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi9606.ENSP00000302724.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi31 – 4515
Turni116 – 1183
Helixi119 – 1235
Helixi128 – 1314
Turni132 – 1343

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2K1VNMR-A116-135[»]
2KBCNMR-A116-135[»]
B23-46[»]
ProteinModelPortaliQ9Y5Q6.
SMRiQ9Y5Q6. Positions 21-46, 110-135.

Miscellaneous databases

EvolutionaryTraceiQ9Y5Q6.

Family & Domainsi

Sequence similaritiesi

Belongs to the insulin family.

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG38979.
HOGENOMiHOG000111888.
HOVERGENiHBG052135.
InParanoidiQ9Y5Q6.
OMAiIRTVIYI.
OrthoDBiEOG73V6N0.
PhylomeDBiQ9Y5Q6.
TreeFamiTF333404.

Family and domain databases

InterProiIPR016179. Insulin-like.
IPR022353. Insulin_CS.
[Graphical view]
PfamiPF00049. Insulin. 1 hit.
[Graphical view]
SMARTiSM00078. IlGF. 1 hit.
[Graphical view]
SUPFAMiSSF56994. SSF56994. 2 hits.
PROSITEiPS00262. INSULIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9Y5Q6-1 [UniParc]FASTAAdd to Basket

« Hide

MKGSIFTLFL FSVLFAISEV RSKESVRLCG LEYIRTVIYI CASSRWRRHQ    50
EGIPQAQQAE TGNSFQLPHK REFSEENPAQ NLPKVDASGE DRLWGGQMPT 100
EELWKSKKHS VMSRQDLQTL CCTDGCSMTD LSALC 135
Length:135
Mass (Da):15,333
Last modified:September 2, 2008 - v2
Checksum:iA932D7EDE9D173F5
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti50 – 501Q → L.3 Publications
Corresponds to variant rs549148 [ dbSNP | Ensembl ].
VAR_046099

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS634.1.
RefSeqiNP_005469.2. NM_005478.4.
UniGeneiHs.251380.

Genome annotation databases

EnsembliENST00000304526; ENSP00000302724; ENSG00000172410.
GeneIDi10022.
KEGGihsa:10022.
UCSCiuc001dcw.3. human.

Polymorphism databases

DMDMi205371762.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS634.1.
RefSeqi NP_005469.2. NM_005478.4.
UniGenei Hs.251380.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2K1V NMR - A 116-135 [» ]
2KBC NMR - A 116-135 [» ]
B 23-46 [» ]
ProteinModelPortali Q9Y5Q6.
SMRi Q9Y5Q6. Positions 21-46, 110-135.
ModBasei Search...

Protein-protein interaction databases

STRINGi 9606.ENSP00000302724.

Polymorphism databases

DMDMi 205371762.

Proteomic databases

PaxDbi Q9Y5Q6.
PRIDEi Q9Y5Q6.

Protocols and materials databases

DNASUi 10022.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000304526 ; ENSP00000302724 ; ENSG00000172410 .
GeneIDi 10022.
KEGGi hsa:10022.
UCSCi uc001dcw.3. human.

Organism-specific databases

CTDi 10022.
GeneCardsi GC01M067223.
H-InvDB HIX0028561.
HGNCi HGNC:6088. INSL5.
HPAi CAB033849.
HPA030100.
MIMi 606413. gene.
neXtProti NX_Q9Y5Q6.
PharmGKBi PA29895.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG38979.
HOGENOMi HOG000111888.
HOVERGENi HBG052135.
InParanoidi Q9Y5Q6.
OMAi IRTVIYI.
OrthoDBi EOG73V6N0.
PhylomeDBi Q9Y5Q6.
TreeFami TF333404.

Enzyme and pathway databases

Reactomei REACT_19231. G alpha (i) signalling events.
REACT_21314. Relaxin receptors.

Miscellaneous databases

EvolutionaryTracei Q9Y5Q6.
GeneWikii INSL5.
GenomeRNAii 10022.
NextBioi 37869.
PROi Q9Y5Q6.
SOURCEi Search...

Gene expression databases

Bgeei Q9Y5Q6.
CleanExi HS_INSL5.
Genevestigatori Q9Y5Q6.

Family and domain databases

InterProi IPR016179. Insulin-like.
IPR022353. Insulin_CS.
[Graphical view ]
Pfami PF00049. Insulin. 1 hit.
[Graphical view ]
SMARTi SM00078. IlGF. 1 hit.
[Graphical view ]
SUPFAMi SSF56994. SSF56994. 2 hits.
PROSITEi PS00262. INSULIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.
    , 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. Cited for: BINDING TO RXFP4.
  7. 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.

Entry informationi

Entry nameiINSL5_HUMAN
AccessioniPrimary (citable) accession number: Q9Y5Q6
Secondary accession number(s): Q3MIY4, Q5VYD8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: September 2, 2008
Last modified: September 3, 2014
This is version 117 of the entry and version 2 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi