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Protein

Ice-structuring protein RD3

Gene
N/A
Organism
Lycodichthys dearborni (Antarctic eelpout) (Rhigophila dearborni)
Status
Reviewed-Annotation score: Annotation score: 2 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. Binds to nascent ice crystals and prevents further growth (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei9 – 91Important for ice-bindingBy similarity
Sitei14 – 141Important for ice-bindingBy similarity
Sitei18 – 181Important for ice-bindingBy similarity
Sitei44 – 441Important for ice-bindingBy similarity
Sitei79 – 791Important for ice-bindingBy similarity
Sitei84 – 841Important for ice-bindingBy similarity
Sitei88 – 881Important for ice-bindingBy similarity
Sitei114 – 1141Important for ice-bindingBy similarity

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Antifreeze protein

Names & Taxonomyi

Protein namesi
Recommended name:
Ice-structuring protein RD3
Short name:
ISP RD3
Alternative name(s):
Antifreeze peptide RD3
OrganismiLycodichthys dearborni (Antarctic eelpout) (Rhigophila dearborni)
Taxonomic identifieri8201 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiNeoteleosteiAcanthomorphataEupercariaPerciformesCottioideiZoarcalesZoarcidaeLycodinaeLycodichthys

Subcellular locationi

  • Secreted 1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 134134Ice-structuring protein RD3PRO_0000155153Add
BLAST

Expressioni

Tissue specificityi

Detected in blood serum (at protein level).1 Publication

Structurei

Secondary structure

1
134
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 96Combined sources
Turni19 – 213Combined sources
Beta strandi22 – 254Combined sources
Beta strandi32 – 343Combined sources
Helixi37 – 404Combined sources
Beta strandi45 – 473Combined sources
Turni57 – 593Combined sources
Beta strandi60 – 623Combined sources
Beta strandi71 – 799Combined sources
Turni89 – 913Combined sources
Beta strandi93 – 964Combined sources
Beta strandi103 – 1064Combined sources
Helixi107 – 1104Combined sources
Beta strandi121 – 1244Combined sources
Turni127 – 1293Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1C89NMR-A1-134[»]
1C8ANMR-A1-134[»]
3NLANMR-A1-73[»]
3RDNNMR-A1-73[»]
ProteinModelPortaliP35753.
SMRiP35753. Positions 1-134.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP35753.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 6360AFP-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini74 – 13360AFP-like 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni65 – 706Linker

Sequence similaritiesi

Belongs to the type-III AFP family.Curated
Contains 2 AFP-like domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

HOVERGENiHBG004240.

Family and domain databases

Gene3Di3.90.1210.10. 2 hits.
InterProiIPR006190. AFP_Neu5c_C.
IPR006013. Antifreeze_III.
IPR013974. SAF.
[Graphical view]
PRINTSiPR00357. ANTIFREEZIII.
SMARTiSM00858. SAF. 2 hits.
[Graphical view]
SUPFAMiSSF51269. SSF51269. 2 hits.
PROSITEiPS50844. AFP_LIKE. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P35753-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
NKASVVANQL IPINTALTLI MMKAEVVTPM GIPAEEIPNL VGMQVNRAVP
60 70 80 90 100
LGTTLMPDMV KNYEDGTTSP GLKSVVANQL IPINTALTLV MMKAEEVSPK
110 120 130
GIPSEEISKL VGMQVNRAVY LDQTLMPDMV KNYE
Length:134
Mass (Da):14,480
Last modified:June 1, 1994 - v1
Checksum:iF7F208BF3E2CAA54
GO

Sequence databases

PIRiS53514.

Cross-referencesi

Sequence databases

PIRiS53514.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1C89NMR-A1-134[»]
1C8ANMR-A1-134[»]
3NLANMR-A1-73[»]
3RDNNMR-A1-73[»]
ProteinModelPortaliP35753.
SMRiP35753. Positions 1-134.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG004240.

Miscellaneous databases

EvolutionaryTraceiP35753.

Family and domain databases

Gene3Di3.90.1210.10. 2 hits.
InterProiIPR006190. AFP_Neu5c_C.
IPR006013. Antifreeze_III.
IPR013974. SAF.
[Graphical view]
PRINTSiPR00357. ANTIFREEZIII.
SMARTiSM00858. SAF. 2 hits.
[Graphical view]
SUPFAMiSSF51269. SSF51269. 2 hits.
PROSITEiPS50844. AFP_LIKE. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Antifreeze peptide heterogeneity in an antarctic eel pout includes an unusually large major variant comprised of two 7 kDa type III AFPs linked in tandem."
    Wang X., Devries A.L., Cheng C.-H.C.
    Biochim. Biophys. Acta 1247:163-172(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  2. "Determination of the solution structure of the N-domain plus linker of antarctic eel pout antifreeze protein RD3."
    Miura K., Ohgiya S., Hoshino T., Nemoto N., Odaira M., Nitta K., Tsuda S.
    J. Biochem. 126:387-394(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1-73.
  3. "NMR analysis of type III antifreeze protein intramolecular dimer. Structural basis for enhanced activity."
    Miura K., Ohgiya S., Hoshino T., Nemoto N., Suetake T., Miura A., Spyracopoulos L., Kondo H., Tsuda S.
    J. Biol. Chem. 276:1304-1310(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.

Entry informationi

Entry nameiANP3_LYCDA
AccessioniPrimary (citable) accession number: P35753
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: October 14, 2015
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

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.