ID H2US31_TAKRU Unreviewed; 359 AA.
AC H2US31;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=N-acetylneuraminate synthase {ECO:0000313|Ensembl:ENSTRUP00000039754.1};
GN Name=nans {ECO:0000313|Ensembl:ENSTRUP00000039754.1};
OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000039754.1, ECO:0000313|Proteomes:UP000005226};
RN [1] {ECO:0000313|Ensembl:ENSTRUP00000039754.1, ECO:0000313|Proteomes:UP000005226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551351;
RA Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT "Integration of the genetic map and genome assembly of fugu facilitates
RT insights into distinct features of genome evolution in teleosts and
RT mammals.";
RL Genome Biol. Evol. 3:424-442(2011).
RN [2] {ECO:0000313|Ensembl:ENSTRUP00000039754.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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}.
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DR RefSeq; XP_003972558.1; XM_003972509.2.
DR AlphaFoldDB; H2US31; -.
DR STRING; 31033.ENSTRUP00000039754; -.
DR Ensembl; ENSTRUT00000039895.3; ENSTRUP00000039754.1; ENSTRUG00000015552.3.
DR GeneID; 778024; -.
DR KEGG; tru:778024; -.
DR CTD; 322780; -.
DR eggNOG; ENOG502QR5J; Eukaryota.
DR GeneTree; ENSGT00390000011081; -.
DR HOGENOM; CLU_040465_1_0_1; -.
DR InParanoid; H2US31; -.
DR OMA; MTYIDYR; -.
DR OrthoDB; 3716025at2759; -.
DR TreeFam; TF324826; -.
DR Proteomes; UP000005226; Chromosome 17.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016051; P:carbohydrate biosynthetic process; IEA:InterPro.
DR CDD; cd11615; SAF_NeuB_like; 1.
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:UP000005226};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 294..353
FT /note="AFP-like"
FT /evidence="ECO:0000259|PROSITE:PS50844"
SQ SEQUENCE 359 AA; 40111 MW; 6938816DB5B72EB4 CRC64;
MPLEFELCPG RVVGGNHPCF IIAEIGQNHQ GDIEIAKKMI KMAKDCGADC AKFQKSELKY
KFNKRALERP YTSKHSWGKT YGEHKHHLEF THEQYKQLQK YAQEVGIFFT ASGMDEMAVE
FLHELNVPFF KVGSGDTNNF PYLEKTAKKG RPMVVSSGMQ SMQTMRRVYK TVKEHNPKFA
ILQCTSAYPL EAEDVNLRVI TEYQKEFPDI PIGYSGHESG VSITVAAVAL GAKIVERHVT
LDKTWKGSDH AASLEPPELA ELVRSIRLVE RALGSGVKRM LPCEKPCHDK LGKSVVAKTK
IPKGTVLTAD MLTVKVAEPM GVKAEDIFEL VGNTMMENVE EDESIAPELV DSYGKKAKC
//
