Skip Header

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

Antifreeze protein Maxi

Gene
N/A
Organism
Pseudopleuronectes americanus (Winter flounder) (Pleuronectes americanus)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Contributes to protect fish blood from freezing at subzero sea water temperatures. Lowers the blood freezing point by about 1.1 degrees at a concentration of 0.1 mg/ml, and by about 1.5 degrees at a concentration of 0.2 mg/ml. Binds to nascent ice crystals and prevents further growth.4 Publications

Temperature dependencei

Thermolabile, displays irreversible loss of activity and aggregation at room temperature.2 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Antifreeze protein

Names & Taxonomyi

Protein namesi
Recommended name:
Antifreeze protein Maxi
Alternative name(s):
5a-like AFP
Type 1 hyperactive antifreeze protein
Short name:
AFP Hyp-1
OrganismiPseudopleuronectes americanus (Winter flounder) (Pleuronectes americanus)
Taxonomic identifieri8265 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiNeoteleosteiAcanthomorphataCarangariaPleuronectiformesPleuronectoideiPleuronectidaePseudopleuronectes

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 232 PublicationsAdd BLAST23
ChainiPRO_500032091124 – 218Antifreeze protein MaxiAdd BLAST195

Expressioni

Tissue specificityi

Detected in blood serum (at protein level). Detected in liver.3 Publications

Interactioni

Subunit structurei

Homodimer.3 Publications

Protein-protein interaction databases

DIPiDIP-61370N.

Structurei

Secondary structure

1218
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi27 – 117Combined sources91
Helixi123 – 216Combined sources94

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4KE2X-ray1.80A/B/C24-218[»]
SMRiB1P0S1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi28 – 218Ala-richAdd BLAST191

Domaini

The polypeptide has an alpha-hairpin structure. Two subunits dimerize to form a four-helix, rod-like structure. Each subunit is composed of a cap structure and of tandem 11 residue repeats with the sequence [TI]-X-X-X-A-X-X-X-A-X-X. Each repeat forms three helical turns with an average of 3.7 residues per turn, as opposed to 3.6 residues per turn for a classical alpha helix. Contrary to other proteins, where the protein core is stabilized by hydrophobic interactions and contains little water, this protein contains in its interior over 400 ordered water molecules with a semi-clathrate structure. Most likely, the interaction with the surface of ice crystals is mediated by bound water molecules that protrude between the helices.1 Publication

Sequence similaritiesi

Belongs to the type-I AFP family.Curated

Keywords - Domaini

Repeat, Signal

Family and domain databases

InterProiIPR000104. Antifreeze_1.
[Graphical view]
PRINTSiPR00308. ANTIFREEZEI.

Sequencei

Sequence statusi: Complete.

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

B1P0S1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALSLFTVGQ FIFLFWTISI TEANIDPAAR AAAAAAASKA AVTAADAAAA
60 70 80 90 100
AATIAASAAS VAAATAADDA AASIATINAA SAAAKSIAAA AAMAAKDTAA
110 120 130 140 150
AAASAAAAAV ASAAKALETI NVKAAYAAAT TANTAAAAAA ATATTAAAAA
160 170 180 190 200
AAKATIDNAA AAKAAAVATA VSDAAATAAT AAAVAAATLE AAAAKAAATA
210
VSAAAAAAAA AIAFAAAP
Length:218
Mass (Da):19,304
Last modified:April 29, 2008 - v1
Checksum:i5EDA80C716CC9406
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EU188795 mRNA. Translation: ABX38716.1.

Cross-referencesi

Web resourcesi

Protein Spotlight

It did it its way - Issue 162 of July 2014

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EU188795 mRNA. Translation: ABX38716.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4KE2X-ray1.80A/B/C24-218[»]
SMRiB1P0S1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-61370N.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

InterProiIPR000104. Antifreeze_1.
[Graphical view]
PRINTSiPR00308. ANTIFREEZEI.
ProtoNetiSearch...

Entry informationi

Entry nameiANPM_PSEAM
AccessioniPrimary (citable) accession number: B1P0S1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 16, 2014
Last sequence update: April 29, 2008
Last modified: November 2, 2016
This is version 12 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

The concentration in blood serum is about 0.2 mg/ml.

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  3. 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.