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Protein

Trefoil factor 2

Gene

TFF2

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Inhibits gastrointestinal motility and gastric acid secretion. Could function as a structural component of gastric mucus, possibly by stabilizing glycoproteins in the mucus gel through interactions with carbohydrate side chains.

Keywords - Molecular functioni

Growth factor

Names & Taxonomyi

Protein namesi
Recommended name:
Trefoil factor 2
Alternative name(s):
Pancreatic spasmolytic polypeptide
Short name:
PSP
Spasmolytic polypeptide
Short name:
SP
Gene namesi
Name:TFF2
Synonyms:SML1
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei‹1 – 21›211 PublicationAdd
BLAST
Chaini22 – 127106Trefoil factor 2PRO_0000023462Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei22 – 221Pyrrolidone carboxylic acid
Disulfide bondi27 ↔ 125
Disulfide bondi29 ↔ 56
Disulfide bondi40 ↔ 55
Disulfide bondi50 ↔ 67
Disulfide bondi79 ↔ 105
Disulfide bondi89 ↔ 104
Disulfide bondi99 ↔ 116

Keywords - PTMi

Disulfide bond, Pyrrolidone carboxylic acid

Proteomic databases

PaxDbiP01359.

Expressioni

Tissue specificityi

Found in pancreas.

Interactioni

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000025323.

Structurei

Secondary structure

1
127
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi26 – 305Combined sources
Helixi34 – 363Combined sources
Helixi47 – 526Combined sources
Beta strandi61 – 644Combined sources
Beta strandi66 – 683Combined sources
Beta strandi74 – 763Combined sources
Helixi77 – 793Combined sources
Helixi83 – 853Combined sources
Helixi96 – 1016Combined sources
Beta strandi110 – 1134Combined sources
Beta strandi115 – 1173Combined sources
Helixi122 – 1243Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PCPNMR-A23-127[»]
1POSX-ray2.60A/B23-127[»]
1PSPX-ray2.50A/B23-127[»]
2PSPX-ray1.95A/B23-127[»]
ProteinModelPortaliP01359.
SMRiP01359. Positions 22-127.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01359.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini27 – 7145P-type 1PROSITE-ProRule annotationAdd
BLAST
Domaini77 – 12044P-type 2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 2 P-type (trefoil) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiENOG410IZEH. Eukaryota.
ENOG410Y3PX. LUCA.
HOVERGENiHBG004363.
InParanoidiP01359.

Family and domain databases

Gene3Di4.10.110.10. 2 hits.
InterProiIPR017994. P_trefoil_chordata.
IPR017957. P_trefoil_CS.
IPR000519. P_trefoil_dom.
[Graphical view]
PfamiPF00088. Trefoil. 2 hits.
[Graphical view]
PRINTSiPR00680. PTREFOIL.
SMARTiSM00018. PD. 2 hits.
[Graphical view]
SUPFAMiSSF57492. SSF57492. 2 hits.
PROSITEiPS00025. P_TREFOIL_1. 2 hits.
PS51448. P_TREFOIL_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

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

P01359-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
EPQRPAPGHP PPAGAVCLTG AQKPAACRCS RQDPKNRVNC GFPGITSDQC
60 70 80 90 100
FTSGCCFDSQ VPGVPWCFKP LPAQESEECV MEVSARKNCG YPGISPEDCA
110 120
RRNCCFSDTI PEVPWCFFPM SVEDCHY
Length:127
Mass (Da):13,834
Last modified:October 1, 1994 - v4
Checksum:iF9012134CE13CF5C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11
Sequence conflicti82 – 821E → Q AA sequence (PubMed:2857575).Curated
Sequence conflicti101 – 1011R → A AA sequence (PubMed:2857575).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X51696 mRNA. Translation: CAA35993.1.
PIRiS12373. JOPGP.
UniGeneiSsc.650.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X51696 mRNA. Translation: CAA35993.1.
PIRiS12373. JOPGP.
UniGeneiSsc.650.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PCPNMR-A23-127[»]
1POSX-ray2.60A/B23-127[»]
1PSPX-ray2.50A/B23-127[»]
2PSPX-ray1.95A/B23-127[»]
ProteinModelPortaliP01359.
SMRiP01359. Positions 22-127.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000025323.

Proteomic databases

PaxDbiP01359.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG410IZEH. Eukaryota.
ENOG410Y3PX. LUCA.
HOVERGENiHBG004363.
InParanoidiP01359.

Miscellaneous databases

EvolutionaryTraceiP01359.

Family and domain databases

Gene3Di4.10.110.10. 2 hits.
InterProiIPR017994. P_trefoil_chordata.
IPR017957. P_trefoil_CS.
IPR000519. P_trefoil_dom.
[Graphical view]
PfamiPF00088. Trefoil. 2 hits.
[Graphical view]
PRINTSiPR00680. PTREFOIL.
SMARTiSM00018. PD. 2 hits.
[Graphical view]
SUPFAMiSSF57492. SSF57492. 2 hits.
PROSITEiPS00025. P_TREFOIL_1. 2 hits.
PS51448. P_TREFOIL_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "hSP, the domain-duplicated homolog of pS2 protein, is co-expressed with pS2 in stomach but not in breast carcinoma."
    Tomasetto C., Rio M.C., Gautier C., Wolf C., Hareuveni M., Chambon P., Lathe R.
    EMBO J. 9:407-414(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The amino acid sequence of pancreatic spasmolytic polypeptide."
    Thim L., Thomsen J., Christensen M., Joergensen K.H.
    Biochim. Biophys. Acta 827:410-418(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 22-127.
  3. "Revised amino acid sequence of pancreatic spasmolytic polypeptide exhibits greater similarity with an inducible pS2 peptide found in a human breast cancer cell line."
    Rose K., Savoy L.-A., Thim L., Christensen M., Joergensen K.H.
    Biochim. Biophys. Acta 998:297-300(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION TO 69; 84; 89 AND 95.
  4. "Crystal structure of a disulfide-linked 'trefoil' motif found in a large family of putative growth factors."
    De A., Brown D., Gorman M., Carr M., Sanderson M.R., Freemont P.S.
    Proc. Natl. Acad. Sci. U.S.A. 91:1084-1088(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
  5. "Pancreatic spasmolytic polypeptide: crystallization, circular dichroism analysis, and preliminary X-ray diffraction studies."
    Gajhede M., Thim L., Joergensen K.H., Melberg S.G.
    Proteins 13:364-368(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
  6. "Pancreatic spasmolytic polypeptide: first three-dimensional structure of a member of the mammalian trefoil family of peptides."
    Gajhede M., Petersen T.N., Henriksen A., Petersen J.F.W., Dauter Z., Wilson K.S., Thim L.
    Structure 1:253-262(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
    Tissue: Pancreas.
  7. "Structure of porcine pancreatic spasmolytic polypeptide at 1.95-A resolution."
    Petersen T.N., Henriksen A., Gajhede M.
    Acta Crystallogr. D 52:730-737(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS).
    Tissue: Pancreas.
  8. "1H NMR-based determination of the secondary structure of porcine pancreatic spasmolytic polypeptide: one of a new family of 'trefoil' motif containing cell growth factors."
    Carr M.D.
    Biochemistry 31:1998-2004(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  9. "Solution structure of a trefoil-motif-containing cell growth factor, porcine spasmolytic protein."
    Carr M.D., Bauer C.J., Gradwell M.J., Feeney J.
    Proc. Natl. Acad. Sci. U.S.A. 91:2206-2210(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.

Entry informationi

Entry nameiTFF2_PIG
AccessioniPrimary (citable) accession number: P01359
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 1, 1994
Last modified: November 11, 2015
This is version 106 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

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

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.