ANTF_ANTPS
ID ANTF_ANTPS Reviewed; 20 AA.
AC P86268;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 11-DEC-2019, entry version 11.
DE RecName: Full=Antifreeze protein;
DE Short=AnpAFP;
DE Flags: Fragment;
OS Antarctomyces psychrotrophicus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Thelebolales; Thelebolaceae; Antarctomyces.
OX NCBI_TaxID=89416;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, INDUCTION, GLYCOSYLATION, AND MASS SPECTROMETRY.
RC STRAIN=KG-1;
RX PubMed=20030710; DOI=10.1111/j.1742-4658.2009.07490.x;
RA Xiao N., Suzuki K., Nishimiya Y., Kondo H., Miura A., Tsuda S., Hoshino T.;
RT "Comparison of functional properties of two fungal antifreeze proteins from
RT Antarctomyces psychrotrophicus and Typhula ishikariensis.";
RL FEBS J. 277:394-403(2010).
CC -!- FUNCTION: Antifreeze proteins bind to the surface of ice crystals and
CC inhibit the growth of these crystals, this inhibition causes thermal
CC hysteresis. Causes the shape of ice crystals to change from hexagonal
CC to a bipyramidal shape with rugged facets. Inhibits recrystallization
CC of ice crystals. {ECO:0000269|PubMed:20030710}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 9.3. {ECO:0000269|PubMed:20030710};
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC {ECO:0000269|PubMed:20030710}.
CC -!- INDUCTION: By low temperature. {ECO:0000269|PubMed:20030710}.
CC -!- PTM: N-glycosylated and O-glycosylated. {ECO:0000269|PubMed:20030710}.
CC -!- MASS SPECTROMETRY: Mass=21742.49; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:20030710};
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DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
PE 1: Evidence at protein level;
KW Antifreeze protein; Direct protein sequencing; Glycoprotein; Secreted;
KW Stress response.
FT CHAIN 1..>20
FT /note="Antifreeze protein"
FT /id="PRO_0000373064"
FT NON_TER 20
SQ SEQUENCE 20 AA; 1848 MW; F48180EEC1E885E8 CRC64;
AGLDLGAASX FGALAFEGVA