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Protein

Gastrotropin

Gene

FABP6

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

Functioni

Binds to bile acids and is involved in enterohepatic bile acid metabolism. Required for efficient apical to basolateral transport of conjugated bile acids in ileal enterocytes (By similarity). In vitro binds to bile acids in the order: deoxycholic acid > cholic acid > chenodeoxycholic acid and respective BA conjugation modifies affinities in the order taurine-conjugated > glycine-conjugated > unconjugated bile acids. Stimulates gastric acid and pepsinogen secretion (By similarity).By similarity2 Publications
Isoform 2: Essential for the survival of colon cancer cells to bile acid-induced apoptosis.1 Publication

GO - Molecular functioni

  • bile acid binding Source: InterPro
  • lipid binding Source: ProtInc
  • transporter activity Source: InterPro

GO - Biological processi

  • bile acid and bile salt transport Source: Reactome
  • bile acid metabolic process Source: InterPro
  • lipid metabolic process Source: ProtInc
  • negative regulation of cell proliferation Source: ProtInc
  • triglyceride catabolic process Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Lipid transport, Transport

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000170231-MONOMER.
ReactomeiR-HSA-159418. Recycling of bile acids and salts.
R-HSA-163560. Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis.

Chemistry databases

SwissLipidsiSLP:000001518.

Names & Taxonomyi

Protein namesi
Recommended name:
Gastrotropin
Short name:
GT
Alternative name(s):
Fatty acid-binding protein 6
Ileal lipid-binding protein
Short name:
ILBP
Intestinal 15 kDa protein
Short name:
I-15P
Intestinal bile acid-binding protein
Short name:
I-BABP
Gene namesi
Name:FABP6
Synonyms:ILBP, ILLBP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:3561. FABP6.

Subcellular locationi

Isoform 1 :
  • Cytoplasm By similarity
  • Membrane; Peripheral membrane protein By similarity; Cytoplasmic side By similarity
Isoform 2 :
  • Cytoplasm 1 Publication

  • Note: Localized close to nucleus on the apical side of both normal and neoplastic cells.1 Publication

GO - Cellular componenti

  • cytoplasm Source: ProtInc
  • cytosol Source: Reactome
  • membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

Pathology & Biotechi

Organism-specific databases

DisGeNETi2172.
OpenTargetsiENSG00000170231.
PharmGKBiPA27962.

Chemistry databases

DrugBankiDB02659. Cholic Acid.

Polymorphism and mutation databases

BioMutaiFABP6.
DMDMi1708457.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000673802 – 128GastrotropinAdd BLAST127

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP51161.
PaxDbiP51161.
PeptideAtlasiP51161.
PRIDEiP51161.

PTM databases

iPTMnetiP51161.
PhosphoSitePlusiP51161.

Expressioni

Tissue specificityi

Isoform 1 is expressed in the jejunum, ileum, cecum and ascending colon intestine. Isoform 2 is xpressed in the gallbladder, duodenum, jejunum, ileum, cecum, ascending, transverse and descending colon, sigmoid colon and rectum. Isoform 2 is expressed in colorectal adenocarcinomas and their adjacent normal mucosa (at protein level).3 Publications

Inductioni

Isoform 1 is up-regulated by chenodeoxycholic acid (CDCA) via the FXR transcription pathway. Isoform 2 is up-regulated by NF-kappa-B and in all stages of colorectal adenocarcinoma. Isoform 1 is not up-regulated in all stages of colorectal adenocarcinoma.1 Publication

Gene expression databases

BgeeiENSG00000170231.
CleanExiHS_FABP6.
ExpressionAtlasiP51161. baseline and differential.
GenevisibleiP51161. HS.

Organism-specific databases

HPAiCAB024713.
HPA012601.

Interactioni

Protein-protein interaction databases

STRINGi9606.ENSP00000377549.

Structurei

Secondary structure

1128
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 14Combined sources10
Helixi15 – 22Combined sources8
Helixi26 – 33Combined sources8
Beta strandi37 – 44Combined sources8
Beta strandi47 – 54Combined sources8
Turni55 – 57Combined sources3
Beta strandi59 – 65Combined sources7
Beta strandi68 – 72Combined sources5
Beta strandi75 – 77Combined sources3
Beta strandi80 – 83Combined sources4
Beta strandi85 – 87Combined sources3
Beta strandi90 – 95Combined sources6
Beta strandi98 – 104Combined sources7
Beta strandi106 – 115Combined sources10
Beta strandi118 – 127Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1O1UNMR-A2-128[»]
1O1VNMR-A2-128[»]
2MM3NMR-A2-128[»]
5L8IX-ray1.88A/B/C1-128[»]
5L8NX-ray2.12A/B/C1-128[»]
5L8OX-ray2.39A/B/C1-128[»]
ProteinModelPortaliP51161.
SMRiP51161.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP51161.

Family & Domainsi

Domaini

Forms a beta-barrel structure that accommodates the hydrophobic ligand in its interior. Can bind at least two ligands per molecule, however, the stoichiometry is debated.2 Publications

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG4015. Eukaryota.
ENOG4111US8. LUCA.
GeneTreeiENSGT00390000012034.
HOGENOMiHOG000004830.
HOVERGENiHBG005633.
InParanoidiP51161.
KOiK08755.
OMAiTVKMEGG.
OrthoDBiEOG091G16BV.
PhylomeDBiP51161.
TreeFamiTF330348.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR012674. Calycin.
IPR011038. Calycin-like.
IPR000463. Fatty_acid-bd.
IPR031257. Gastrotropin.
IPR031259. iLBP.
[Graphical view]
PANTHERiPTHR11955. PTHR11955. 1 hit.
PTHR11955:SF69. PTHR11955:SF69. 1 hit.
PRINTSiPR00178. FATTYACIDBP.
SUPFAMiSSF50814. SSF50814. 1 hit.
PROSITEiPS00214. FABP. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative promoter usage. AlignAdd to basket

Isoform 1 (identifier: P51161-1) [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
MAFTGKFEME SEKNYDEFMK LLGISSDVIE KARNFKIVTE VQQDGQDFTW
60 70 80 90 100
SQHYSGGHTM TNKFTVGKES NIQTMGGKTF KATVQMEGGK LVVNFPNYHQ
110 120
TSEIVGDKLV EVSTIGGVTY ERVSKRLA
Length:128
Mass (Da):14,371
Last modified:January 23, 2007 - v2
Checksum:i173CBC5DBEDADDE1
GO
Isoform 2 (identifier: P51161-2) [UniParc]FASTAAdd to basket
Also known as: IBABP-L

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MKTVTMMMVVEMQALTQVLRAVLSACTWVSRKGDLQRMKQTHKGKPPSSM

Show »
Length:177
Mass (Da):19,874
Checksum:i0ACBAE8E7DF65BF0
GO

Sequence cautioni

The sequence AAH22489 differs from that shown. Reason: Erroneous initiation.Curated

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_03957833R → H.1 PublicationCorresponds to variant rs17856662dbSNPEnsembl.1
Natural variantiVAR_03957955S → Y.1 PublicationCorresponds to variant rs17852045dbSNPEnsembl.1
Natural variantiVAR_03958079T → M May be associated with type 2 diabetes obese individuals. 1 PublicationCorresponds to variant rs1130435dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0380391M → MKTVTMMMVVEMQALTQVLR AVLSACTWVSRKGDLQRMKQ THKGKPPSSM in isoform 2. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U19869 mRNA. Translation: AAB82751.1.
X90908 mRNA. Translation: CAA62415.1.
DQ132786 mRNA. Translation: ABA12611.1.
AC008609 Genomic DNA. No translation available.
AC112191 Genomic DNA. No translation available.
BC022489 mRNA. Translation: AAH22489.1. Different initiation.
AJ250902 Genomic DNA. Translation: CAB65728.1.
CCDSiCCDS43393.1. [P51161-2]
CCDS4349.1. [P51161-1]
PIRiS63983.
RefSeqiNP_001035532.1. NM_001040442.1. [P51161-2]
NP_001124430.1. NM_001130958.1. [P51161-2]
NP_001436.1. NM_001445.2. [P51161-1]
UniGeneiHs.519719.

Genome annotation databases

EnsembliENST00000393980; ENSP00000377549; ENSG00000170231. [P51161-2]
ENST00000402432; ENSP00000385433; ENSG00000170231. [P51161-1]
GeneIDi2172.
KEGGihsa:2172.
UCSCiuc003lxx.2. human. [P51161-1]

Keywords - Coding sequence diversityi

Alternative promoter usage, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U19869 mRNA. Translation: AAB82751.1.
X90908 mRNA. Translation: CAA62415.1.
DQ132786 mRNA. Translation: ABA12611.1.
AC008609 Genomic DNA. No translation available.
AC112191 Genomic DNA. No translation available.
BC022489 mRNA. Translation: AAH22489.1. Different initiation.
AJ250902 Genomic DNA. Translation: CAB65728.1.
CCDSiCCDS43393.1. [P51161-2]
CCDS4349.1. [P51161-1]
PIRiS63983.
RefSeqiNP_001035532.1. NM_001040442.1. [P51161-2]
NP_001124430.1. NM_001130958.1. [P51161-2]
NP_001436.1. NM_001445.2. [P51161-1]
UniGeneiHs.519719.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1O1UNMR-A2-128[»]
1O1VNMR-A2-128[»]
2MM3NMR-A2-128[»]
5L8IX-ray1.88A/B/C1-128[»]
5L8NX-ray2.12A/B/C1-128[»]
5L8OX-ray2.39A/B/C1-128[»]
ProteinModelPortaliP51161.
SMRiP51161.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000377549.

Chemistry databases

DrugBankiDB02659. Cholic Acid.
SwissLipidsiSLP:000001518.

PTM databases

iPTMnetiP51161.
PhosphoSitePlusiP51161.

Polymorphism and mutation databases

BioMutaiFABP6.
DMDMi1708457.

Proteomic databases

MaxQBiP51161.
PaxDbiP51161.
PeptideAtlasiP51161.
PRIDEiP51161.

Protocols and materials databases

DNASUi2172.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000393980; ENSP00000377549; ENSG00000170231. [P51161-2]
ENST00000402432; ENSP00000385433; ENSG00000170231. [P51161-1]
GeneIDi2172.
KEGGihsa:2172.
UCSCiuc003lxx.2. human. [P51161-1]

Organism-specific databases

CTDi2172.
DisGeNETi2172.
GeneCardsiFABP6.
HGNCiHGNC:3561. FABP6.
HPAiCAB024713.
HPA012601.
MIMi600422. gene.
neXtProtiNX_P51161.
OpenTargetsiENSG00000170231.
PharmGKBiPA27962.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4015. Eukaryota.
ENOG4111US8. LUCA.
GeneTreeiENSGT00390000012034.
HOGENOMiHOG000004830.
HOVERGENiHBG005633.
InParanoidiP51161.
KOiK08755.
OMAiTVKMEGG.
OrthoDBiEOG091G16BV.
PhylomeDBiP51161.
TreeFamiTF330348.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000170231-MONOMER.
ReactomeiR-HSA-159418. Recycling of bile acids and salts.
R-HSA-163560. Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis.

Miscellaneous databases

ChiTaRSiFABP6. human.
EvolutionaryTraceiP51161.
GeneWikiiFABP6.
GenomeRNAii2172.
PROiP51161.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000170231.
CleanExiHS_FABP6.
ExpressionAtlasiP51161. baseline and differential.
GenevisibleiP51161. HS.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR012674. Calycin.
IPR011038. Calycin-like.
IPR000463. Fatty_acid-bd.
IPR031257. Gastrotropin.
IPR031259. iLBP.
[Graphical view]
PANTHERiPTHR11955. PTHR11955. 1 hit.
PTHR11955:SF69. PTHR11955:SF69. 1 hit.
PRINTSiPR00178. FATTYACIDBP.
SUPFAMiSSF50814. SSF50814. 1 hit.
PROSITEiPS00214. FABP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFABP6_HUMAN
AccessioniPrimary (citable) accession number: P51161
Secondary accession number(s): Q07DR7, Q8TBI3, Q9UGI7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 154 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, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: 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

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.