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Protein

Gastric inhibitory polypeptide receptor

Gene

GIPR

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

Functioni

This is a receptor for GIP. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase.

GO - Molecular functioni

GO - Biological processi

  • activation of adenylate cyclase activity Source: ProtInc
  • cell surface receptor signaling pathway Source: ProtInc
  • desensitization of G-protein coupled receptor protein signaling pathway Source: Ensembl
  • endocrine pancreas development Source: Ensembl
  • generation of precursor metabolites and energy Source: ProtInc
  • positive regulation of cytosolic calcium ion concentration Source: Ensembl
  • positive regulation of insulin secretion Source: Ensembl
  • regulation of insulin secretion Source: ParkinsonsUK-UCL
  • response to axon injury Source: Ensembl
  • response to calcium ion Source: Ensembl
  • response to fatty acid Source: Ensembl
  • response to glucose Source: Ensembl
  • response to nutrient Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

G-protein coupled receptor, Receptor, Transducer

Enzyme and pathway databases

ReactomeiR-HSA-418555. G alpha (s) signalling events.
R-HSA-420092. Glucagon-type ligand receptors.

Protein family/group databases

TCDBi9.A.14.4.5. the g-protein-coupled receptor (gpcr) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Gastric inhibitory polypeptide receptor
Short name:
GIP-R
Alternative name(s):
Glucose-dependent insulinotropic polypeptide receptor
Gene namesi
Name:GIPR
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:4271. GIPR.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini22 – 138117ExtracellularSequence analysisAdd
BLAST
Transmembranei139 – 16123Helical; Name=1Sequence analysisAdd
BLAST
Topological domaini162 – 1698CytoplasmicSequence analysis
Transmembranei170 – 18920Helical; Name=2Sequence analysisAdd
BLAST
Topological domaini190 – 21728ExtracellularSequence analysisAdd
BLAST
Transmembranei218 – 24225Helical; Name=3Sequence analysisAdd
BLAST
Topological domaini243 – 25412CytoplasmicSequence analysisAdd
BLAST
Transmembranei255 – 27824Helical; Name=4Sequence analysisAdd
BLAST
Topological domaini279 – 29315ExtracellularSequence analysisAdd
BLAST
Transmembranei294 – 31926Helical; Name=5Sequence analysisAdd
BLAST
Topological domaini320 – 34122CytoplasmicSequence analysisAdd
BLAST
Transmembranei342 – 36221Helical; Name=6Sequence analysisAdd
BLAST
Topological domaini363 – 37715ExtracellularSequence analysisAdd
BLAST
Transmembranei378 – 39821Helical; Name=7Sequence analysisAdd
BLAST
Topological domaini399 – 46668CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • cytosol Source: Ensembl
  • integral component of membrane Source: ProtInc
  • plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA28682.

Chemistry

ChEMBLiCHEMBL4383.
GuidetoPHARMACOLOGYi248.

Polymorphism and mutation databases

BioMutaiGIPR.
DMDMi1346133.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence analysisAdd
BLAST
Chaini22 – 466445Gastric inhibitory polypeptide receptorPRO_0000012825Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi46 ↔ 701 Publication
Disulfide bondi61 ↔ 1031 Publication
Glycosylationi62 – 621N-linked (GlcNAc...)1 Publication
Glycosylationi77 – 771N-linked (GlcNAc...)1 Publication
Disulfide bondi84 ↔ 1181 Publication

Post-translational modificationi

N-glycosylation is required for cell surface expression and lengthens receptor half-life by preventing degradation in the ER.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP48546.
PRIDEiP48546.

Expressioni

Gene expression databases

BgeeiP48546.
CleanExiHS_GIPR.
ExpressionAtlasiP48546. baseline and differential.
GenevisibleiP48546. HS.

Organism-specific databases

HPAiCAB022710.

Interactioni

Subunit structurei

May form homodimers and heterodimers with GLP1R.2 Publications

Protein-protein interaction databases

BioGridi108963. 1 interaction.
DIPiDIP-46468N.
STRINGi9606.ENSP00000467494.

Chemistry

BindingDBiP48546.

Structurei

Secondary structure

1
466
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi32 – 5221Combined sources
Beta strandi67 – 715Combined sources
Beta strandi78 – 836Combined sources
Beta strandi86 – 883Combined sources
Helixi91 – 944Combined sources
Beta strandi98 – 1036Combined sources
Beta strandi105 – 1073Combined sources
Beta strandi109 – 1146Combined sources
Helixi116 – 1183Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2QKHX-ray1.90A24-138[»]
4HJ0X-ray3.00A/B24-138[»]
ProteinModelPortaliP48546.
SMRiP48546. Positions 29-122, 137-402.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP48546.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG4564. Eukaryota.
ENOG410XRS2. LUCA.
GeneTreeiENSGT00760000118800.
HOGENOMiHOG000008250.
HOVERGENiHBG008318.
InParanoidiP48546.
KOiK04580.
OMAiGELYQRW.
OrthoDBiEOG7TF78W.
PhylomeDBiP48546.

Family and domain databases

InterProiIPR017981. GPCR_2-like.
IPR001879. GPCR_2_extracellular_dom.
IPR001749. GPCR_2_GIP_rcpt.
IPR000832. GPCR_2_secretin-like.
IPR017983. GPCR_2_secretin-like_CS.
[Graphical view]
PfamiPF00002. 7tm_2. 1 hit.
PF02793. HRM. 1 hit.
[Graphical view]
PRINTSiPR01129. GIPRECEPTOR.
PR00249. GPCRSECRETIN.
SMARTiSM00008. HormR. 1 hit.
[Graphical view]
PROSITEiPS00649. G_PROTEIN_RECEP_F2_1. 1 hit.
PS00650. G_PROTEIN_RECEP_F2_2. 1 hit.
PS50227. G_PROTEIN_RECEP_F2_3. 1 hit.
PS50261. G_PROTEIN_RECEP_F2_4. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P48546-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MTTSPILQLL LRLSLCGLLL QRAETGSKGQ TAGELYQRWE RYRRECQETL
60 70 80 90 100
AAAEPPSGLA CNGSFDMYVC WDYAAPNATA RASCPWYLPW HHHVAAGFVL
110 120 130 140 150
RQCGSDGQWG LWRDHTQCEN PEKNEAFLDQ RLILERLQVM YTVGYSLSLA
160 170 180 190 200
TLLLALLILS LFRRLHCTRN YIHINLFTSF MLRAAAILSR DRLLPRPGPY
210 220 230 240 250
LGDQALALWN QALAACRTAQ IVTQYCVGAN YTWLLVEGVY LHSLLVLVGG
260 270 280 290 300
SEEGHFRYYL LLGWGAPALF VIPWVIVRYL YENTQCWERN EVKAIWWIIR
310 320 330 340 350
TPILMTILIN FLIFIRILGI LLSKLRTRQM RCRDYRLRLA RSTLTLVPLL
360 370 380 390 400
GVHEVVFAPV TEEQARGALR FAKLGFEIFL SSFQGFLVSV LYCFINKEVQ
410 420 430 440 450
SEIRRGWHHC RLRRSLGEEQ RQLPERAFRA LPSGSGPGEV PTSRGLSSGT
460
LPGPGNEASR ELESYC
Length:466
Mass (Da):53,157
Last modified:February 1, 1996 - v1
Checksum:iCA5CF86BA0E32383
GO
Isoform 2 (identifier: P48546-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     400-419: QSEIRRGWHHCRLRRSLGEE → GRDPAAAPALWRQRGVRRRL
     420-466: Missing.

Show »
Length:419
Mass (Da):48,071
Checksum:i688BE1EFDD62D9FF
GO
Isoform 3 (identifier: P48546-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     58-93: Missing.

Show »
Length:430
Mass (Da):49,062
Checksum:i3CCE33270176FC7C
GO

Sequence cautioni

The sequence CAA57426.1 differs from that shown. Reason: Frameshift at several positions. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti12 – 121R → G in AAB35419 (PubMed:7589426).Curated
Sequence conflicti104 – 1041G → R in AAB35419 (PubMed:7589426).Curated
Sequence conflicti117 – 1171Missing in CAA57426 (PubMed:7556958).Curated
Sequence conflicti337 – 3371L → V in AAB35419 (PubMed:7589426).Curated
Sequence conflicti367 – 3715GALRF → APCV in CAA57426 (PubMed:7556958).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti136 – 1361R → W.
Corresponds to variant rs13306402 [ dbSNP | Ensembl ].
VAR_029333
Natural varianti207 – 2071A → V.
Corresponds to variant rs1800436 [ dbSNP | Ensembl ].
VAR_011808
Natural varianti262 – 2621L → V.
Corresponds to variant rs5392 [ dbSNP | Ensembl ].
VAR_011809
Natural varianti354 – 3541E → Q.
Corresponds to variant rs1800437 [ dbSNP | Ensembl ].
VAR_011810

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei58 – 9336Missing in isoform 3. 1 PublicationVSP_053866Add
BLAST
Alternative sequencei400 – 41920QSEIR…SLGEE → GRDPAAAPALWRQRGVRRRL in isoform 2. 1 PublicationVSP_053867Add
BLAST
Alternative sequencei420 – 46647Missing in isoform 2. 1 PublicationVSP_053868Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U39231 mRNA. Translation: AAA84418.1.
S79852 mRNA. Translation: AAB35419.2.
X81832 mRNA. Translation: CAA57426.1. Frameshift.
D49559 Genomic DNA. Translation: BAA08503.1.
AC006132 Genomic DNA. Translation: AAC97984.1.
AC007191 Genomic DNA. Translation: AAD22674.1.
BC093723 mRNA. Translation: AAH93723.1.
BC101673 mRNA. Translation: AAI01674.1.
BC143300 mRNA. Translation: AAI43301.1.
CCDSiCCDS12671.1. [P48546-1]
PIRiG02234.
I37411.
S66676.
RefSeqiNP_000155.1. NM_000164.3. [P48546-1]
NP_001295347.1. NM_001308418.1. [P48546-3]
XP_011525014.1. XM_011526712.1. [P48546-3]
UniGeneiHs.251412.
Hs.658534.

Genome annotation databases

EnsembliENST00000263281; ENSP00000263281; ENSG00000010310. [P48546-2]
ENST00000304207; ENSP00000305321; ENSG00000010310. [P48546-3]
ENST00000590918; ENSP00000467494; ENSG00000010310. [P48546-1]
GeneIDi2696.
KEGGihsa:2696.
UCSCiuc002pct.2. human. [P48546-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U39231 mRNA. Translation: AAA84418.1.
S79852 mRNA. Translation: AAB35419.2.
X81832 mRNA. Translation: CAA57426.1. Frameshift.
D49559 Genomic DNA. Translation: BAA08503.1.
AC006132 Genomic DNA. Translation: AAC97984.1.
AC007191 Genomic DNA. Translation: AAD22674.1.
BC093723 mRNA. Translation: AAH93723.1.
BC101673 mRNA. Translation: AAI01674.1.
BC143300 mRNA. Translation: AAI43301.1.
CCDSiCCDS12671.1. [P48546-1]
PIRiG02234.
I37411.
S66676.
RefSeqiNP_000155.1. NM_000164.3. [P48546-1]
NP_001295347.1. NM_001308418.1. [P48546-3]
XP_011525014.1. XM_011526712.1. [P48546-3]
UniGeneiHs.251412.
Hs.658534.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2QKHX-ray1.90A24-138[»]
4HJ0X-ray3.00A/B24-138[»]
ProteinModelPortaliP48546.
SMRiP48546. Positions 29-122, 137-402.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108963. 1 interaction.
DIPiDIP-46468N.
STRINGi9606.ENSP00000467494.

Chemistry

BindingDBiP48546.
ChEMBLiCHEMBL4383.
GuidetoPHARMACOLOGYi248.

Protein family/group databases

TCDBi9.A.14.4.5. the g-protein-coupled receptor (gpcr) family.
GPCRDBiSearch...

Polymorphism and mutation databases

BioMutaiGIPR.
DMDMi1346133.

Proteomic databases

PaxDbiP48546.
PRIDEiP48546.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000263281; ENSP00000263281; ENSG00000010310. [P48546-2]
ENST00000304207; ENSP00000305321; ENSG00000010310. [P48546-3]
ENST00000590918; ENSP00000467494; ENSG00000010310. [P48546-1]
GeneIDi2696.
KEGGihsa:2696.
UCSCiuc002pct.2. human. [P48546-1]

Organism-specific databases

CTDi2696.
GeneCardsiGIPR.
HGNCiHGNC:4271. GIPR.
HPAiCAB022710.
MIMi137241. gene.
neXtProtiNX_P48546.
PharmGKBiPA28682.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4564. Eukaryota.
ENOG410XRS2. LUCA.
GeneTreeiENSGT00760000118800.
HOGENOMiHOG000008250.
HOVERGENiHBG008318.
InParanoidiP48546.
KOiK04580.
OMAiGELYQRW.
OrthoDBiEOG7TF78W.
PhylomeDBiP48546.

Enzyme and pathway databases

ReactomeiR-HSA-418555. G alpha (s) signalling events.
R-HSA-420092. Glucagon-type ligand receptors.

Miscellaneous databases

EvolutionaryTraceiP48546.
GeneWikiiGastric_inhibitory_polypeptide_receptor.
GenomeRNAii2696.
NextBioi10664.
PROiP48546.
SOURCEiSearch...

Gene expression databases

BgeeiP48546.
CleanExiHS_GIPR.
ExpressionAtlasiP48546. baseline and differential.
GenevisibleiP48546. HS.

Family and domain databases

InterProiIPR017981. GPCR_2-like.
IPR001879. GPCR_2_extracellular_dom.
IPR001749. GPCR_2_GIP_rcpt.
IPR000832. GPCR_2_secretin-like.
IPR017983. GPCR_2_secretin-like_CS.
[Graphical view]
PfamiPF00002. 7tm_2. 1 hit.
PF02793. HRM. 1 hit.
[Graphical view]
PRINTSiPR01129. GIPRECEPTOR.
PR00249. GPCRSECRETIN.
SMARTiSM00008. HormR. 1 hit.
[Graphical view]
PROSITEiPS00649. G_PROTEIN_RECEP_F2_1. 1 hit.
PS00650. G_PROTEIN_RECEP_F2_2. 1 hit.
PS50227. G_PROTEIN_RECEP_F2_3. 1 hit.
PS50261. G_PROTEIN_RECEP_F2_4. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The human GIP receptor: gene structure, functional expression of its cDNA, and chromosomal location."
    Usdin T.B., Gruber C., Modi W., Bonner T.I.
    Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Molecular cloning, functional expression, and signal transduction of the GIP-receptor cloned from a human insulinoma."
    Volz A., Goke R., Lankat-Buttgereit B., Fehmann H.C., Bode H.P., Goke B.
    FEBS Lett. 373:23-29(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "Cloning, functional expression, and chromosomal localization of the human pancreatic islet glucose-dependent insulinotropic polypeptide receptor."
    Gremlich S., Porret A., Hani E.H., Cherif D., Vionnet N., Froguel P., Thorens B.
    Diabetes 44:1202-1208(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Pancreas.
  4. "Human gastric inhibitory polypeptide receptor: cloning of the gene (GIPR) and cDNA."
    Yamada Y., Hayami T., Nakamura K., Kaisaki P.J., Someya Y., Wang C.Z., Seino S., Seino Y.
    Genomics 29:773-776(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
  5. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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] (ISOFORMS 1 AND 3).
    Tissue: Colon.
  7. "Regulation of GIP and GLP1 receptor cell surface expression by N-glycosylation and receptor heteromerization."
    Whitaker G.M., Lynn F.C., McIntosh C.H., Accili E.A.
    PLoS ONE 7:E32675-E32675(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT ASN-62 AND ASN-77, SUBUNIT.
  8. Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 24-138 IN COMPLEX WITH GIP, DISULFIDE BONDS.

Entry informationi

Entry nameiGIPR_HUMAN
AccessioniPrimary (citable) accession number: P48546
Secondary accession number(s): B7WP14
, B7ZKQ0, Q14401, Q16400, Q52M04, Q9UPI1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: May 11, 2016
This is version 143 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
  2. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

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 one 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.