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Q01758 (ISP2_OSMMO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Type-2 ice-structuring protein
Alternative name(s):
Type II antifreeze protein
Short name=AFP
OrganismOsmerus mordax (Rainbow smelt) (Atherina mordax)
Taxonomic identifier8014 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiEuteleosteiProtacanthopterygiiOsmeriformesOsmeridaeOsmerus

Protein attributes

Sequence length175 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Antifreeze proteins lower the blood freezing point.

Subcellular location

Secreted.

Sequence similarities

Contains 1 C-type lectin domain.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   LigandLectin
   Molecular functionAntifreeze protein
   PTMDisulfide bond
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processresponse to freezing

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncarbohydrate binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1616 Potential
Propeptide17 – 3317 Potential
PRO_0000017546
Chain34 – 175142Type-2 ice-structuring protein
PRO_0000017547

Regions

Domain36 – 163128C-type lectin

Amino acid modifications

Disulfide bond38 ↔ 49 By similarity
Disulfide bond66 ↔ 159 By similarity
Disulfide bond103 ↔ 134 By similarity
Disulfide bond123 ↔ 145 By similarity
Disulfide bond135 ↔ 151 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q01758 [UniParc].

Last modified July 1, 1993. Version 1.
Checksum: E2A72D8C030AFAA3

FASTA17519,054
        10         20         30         40         50         60 
MLAALLVCAM VALTRAANGD TGKEAVMTGS SGKNLTECPT DWKMFNGRCF LFNPLQLHWA 

        70         80         90        100        110        120 
HAQISCMKDG ANLASIHSLE EYAFVKELTT AGLIPAWIGG SDCHVSTYWF WMDSTSMDFT 

       130        140        150        160        170 
DWCAAQPDFT LTECCIQINV GVGKCWNDTP CTHLHASVCA KPATVIPEVT PPSIM 

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References

[1]"Structural and functional similarity between fish antifreeze proteins and calcium-dependent lectins."
Ewart K.V., Rubinsky B., Fletcher G.L.
Biochem. Biophys. Res. Commun. 185:335-340(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 49-65; 69-78; 145-154 AND 161-173.
Tissue: Liver.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M96154 mRNA. Translation: AAA49442.1.
PIRJH0626.

3D structure databases

ProteinModelPortalQ01758.
SMRQ01758. Positions 38-162.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG004151.

Family and domain databases

Gene3D3.10.100.10. 1 hit.
InterProIPR002353. AntifreezeII.
IPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR018378. C-type_lectin_CS.
IPR016187. C-type_lectin_fold.
[Graphical view]
PfamPF00059. Lectin_C. 1 hit.
[Graphical view]
PRINTSPR00356. ANTIFREEZEII.
SMARTSM00034. CLECT. 1 hit.
[Graphical view]
SUPFAMSSF56436. C-type_lectin_fold. 1 hit.
PROSITEPS00615. C_TYPE_LECTIN_1. 1 hit.
PS50041. C_TYPE_LECTIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameISP2_OSMMO
AccessionPrimary (citable) accession number: Q01758
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: April 3, 2013
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families