P35751 (ANP1_RHIDE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Ice-structuring protein RD1 Short name=ISP RD1 Alternative name(s): Antifreeze peptide RD1
Organism	Rhigophila dearborni (Antarctic eelpout) (Lycodichthys dearborni)
Taxonomic identifier	8201 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Actinopterygii › Actinopteri › Neopterygii › Teleostei › Elopocephala › Clupeocephala › Euteleostei › Neognathi › Neoteleostei › Eurypterygii › Ctenosquamata › Acanthomorpha › Euacanthomorpha › Holacanthopterygii › Acanthopterygii › Euacanthopterygii › Percomorpha › Perciformes › Zoarcoidei › Zoarcidae › Lycodinae › Lycodichthys

Protein attributes

Sequence length	64 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Antifreeze proteins lower the blood freezing point by absorbing ice and inhibiting its growth.
Subcellular location	Secreted.
Sequence similarities	Belongs to the type-III AFP family. Contains 1 AFP-like domain.

Ontologies

Keywords
Cellular component	Secreted
Molecular function	Antifreeze protein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological_process	response to freezing Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 64

64

Ice-structuring protein RD1

PRO_0000155151

Regions

Domain

4 – 63

60

AFP-like

Sites

Site

9

1

Important for ice-binding By similarity

Site

14

1

Important for ice-binding By similarity

Site

18

1

Important for ice-binding By similarity

Site

44

1

Important for ice-binding By similarity

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

64

Helix Strand Turn

Details...

Beta strand

4 – 9

6

Helix

19 – 21

3

Beta strand

22 – 25

4

Helix

34 – 36

3

Helix

37 – 40

4

Beta strand

44 – 47

4

Helix

57 – 59

3

Sequences

	Sequence		Length	Mass (Da)
	P35751 [UniParc]. Last modified June 1, 1994. Version 1. Checksum: 154C6BE62D913192	FASTA	64	6,906
	10 20 30 40 50 60 NKASVVANQL IPINTALTLI MMKAEVVTPM GIPAEEIPKL VGMQVNRAVP LGTTLMPDMV KNYE

References

[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.
[2]	"The refined crystal structure of an eel pout type III antifreeze protein RD1 at 0.62-A resolution reveals structuRAl microheterogeneity of protein and solvation." Ko T.-P., Robinson H., Gao Y.-G., Cheng C.H.-C., DeVries A.L., Wang A.H.-J. Biophys. J. 84:1228-1237(2003) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (0.62 ANGSTROMS).

Cross-references

Sequence databases

PIR

S53512.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1UCS	X-ray	0.62	A	1-64	[»]

ProteinModelPortal

P35751.

SMR

P35751. Positions 1-64.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Phylogenomic databases

HOVERGEN

HBG004237.

Family and domain databases

Gene3D

3.90.1210.10. 1 hit.

InterPro

IPR006190. AFP_Neu5c_C.
IPR006013. Antifreeze_III.
IPR013974. SAF.
[Graphical view]

Pfam

PF08666. SAF. 1 hit.
[Graphical view]

PRINTS

PR00357. ANTIFREEZIII.

SUPFAM

SSF51269. AFP_Neu5c_C. 1 hit.

PROSITE

PS50844. AFP_LIKE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P35751.

Entry information

Entry name

ANP1_RHIDE

Accession

Primary (citable) accession number: P35751

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	June 1, 1994
Last modified:	April 3, 2013
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program