ID A0A0F8AWR3_LARCR Unreviewed; 348 AA.
AC A0A0F8AWR3;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 22-FEB-2023, entry version 19.
DE SubName: Full=Sialic acid synthase N-acetylneuraminate synthase {ECO:0000313|EMBL:KAE8300761.1};
GN ORFNames=D5F01_LYC00908 {ECO:0000313|EMBL:KAE8300761.1};
OS Larimichthys crocea (Large yellow croaker) (Pseudosciaena crocea).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Sciaenidae; Larimichthys.
OX NCBI_TaxID=215358 {ECO:0000313|EMBL:KAE8300761.1, ECO:0000313|Proteomes:UP000424527};
RN [1] {ECO:0000313|EMBL:KAE8300761.1, ECO:0000313|Proteomes:UP000424527}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JMULYC20181020 {ECO:0000313|EMBL:KAE8300761.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:KAE8300761.1};
RA Xiao S.;
RT "Chromosome genome assembly for large yellow croaker.";
RL Submitted (JUL-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Contributes to protect fish blood from freezing at subzero
CC sea water temperatures. Lowers the blood freezing point. Binds to
CC nascent ice crystals and prevents further growth.
CC {ECO:0000256|ARBA:ARBA00024935}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the type-III AFP family.
CC {ECO:0000256|ARBA:ARBA00007445}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAE8300761.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; REGW02000001; KAE8300761.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F8AWR3; -.
DR eggNOG; ENOG502QR5J; Eukaryota.
DR Proteomes; UP000424527; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016051; P:carbohydrate biosynthetic process; IEA:InterPro.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 3.90.1210.10; Antifreeze-like/N-acetylneuraminic acid synthase C-terminal domain; 1.
DR InterPro; IPR006190; AFP_Neu5c_C.
DR InterPro; IPR036732; AFP_Neu5c_C_sf.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR006013; Antifreeze_III.
DR InterPro; IPR013132; Neu5Ac_N.
DR InterPro; IPR013974; SAF.
DR PANTHER; PTHR42966; N-ACETYLNEURAMINATE SYNTHASE; 1.
DR PANTHER; PTHR42966:SF1; SIALIC ACID SYNTHASE; 1.
DR Pfam; PF03102; NeuB; 1.
DR Pfam; PF08666; SAF; 1.
DR PRINTS; PR00357; ANTIFREEZIII.
DR SMART; SM00858; SAF; 1.
DR SUPFAM; SSF51269; AFP III-like domain; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR PROSITE; PS50844; AFP_LIKE; 1.
PE 3: Inferred from homology;
KW Antifreeze protein {ECO:0000256|ARBA:ARBA00023076};
KW Reference proteome {ECO:0000313|Proteomes:UP000424527};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
SQ SEQUENCE 348 AA; 38849 MW; A9A2BF12560246F2 CRC64;
MIGGNHPCFI IAEIGQNHQG DIEIAKKMIK MAKDCGADCA KFQKSELEYK FNKRALERPY
TSQHSWGKTY GEHKRHLELS HEQYRELQKY AEEVGIFFTA SGMDEMAVEF LHELNVPFFK
VGSGDTNNFP YLEKTAKKGR PMVVSSGMQS METMRRVYKT VKEHNQNFTI LQCTSAYPLE
AEDVNLRVIS EYQKEFPDIP IGYSGHESGI SISVAAVALG AKVIERHVTL DKTWKGNDHS
ASLEPSELTE LVRSIRLVER ALGSGIKRML PCEKPCHDKL GKSVVAKVKI PGGTVLTLDM
LTVKVADPMG VAAEDIFELV GKTVTEDVEE DESVTPEVVD SYGKKAKC
//
