FETUA_BOVIN
ID FETUA_BOVIN Reviewed; 359 AA.
AC P12763; A6QLF7;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Alpha-2-HS-glycoprotein;
DE AltName: Full=Asialofetuin;
DE AltName: Full=Fetuin-A;
DE Flags: Precursor;
GN Name=AHSG; Synonyms=FETUA;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=1689725; DOI=10.1016/s0021-9258(19)39571-7;
RA Dziegielewska K.D., Brown W.M., Casey S.J., Christie D.L., Foreman R.C.,
RA Hill R.M., Saunders N.R.;
RT "The complete cDNA and amino acid sequence of bovine fetuin. Its homology
RT with alpha 2HS glycoprotein and relation to other members of the cystatin
RT superfamily.";
RL J. Biol. Chem. 265:4354-4357(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 19-123 AND 188-243.
RX PubMed=2436943; DOI=10.1016/0014-5793(87)80010-8;
RA Christie D.L., Dziegielewska K.M., Hill R.M., Saunders N.R.;
RT "Fetuin: the bovine homologue of human alpha 2HS glycoprotein.";
RL FEBS Lett. 214:45-49(1987).
RN [4]
RP PROTEIN SEQUENCE OF 19-62.
RX PubMed=6165360; DOI=10.1016/0006-291x(81)91708-3;
RA Alcaraz G., Marti J., Moinier D., Fougereau M.;
RT "NH2-terminal sequence of calf fetuin.";
RL Biochem. Biophys. Res. Commun. 99:30-36(1981).
RN [5]
RP PROTEIN SEQUENCE OF 72-103 AND 144-187, AND GLYCOSYLATION AT ASN-99;
RP ASN-156 AND ASN-176.
RX PubMed=2447075; DOI=10.1016/s0021-9258(19)57364-1;
RA Yet M.G., Chin C.C.Q., Wold F.;
RT "The covalent structure of individual N-linked glycopeptides from ovomucoid
RT and asialofetuin.";
RL J. Biol. Chem. 263:111-117(1988).
RN [6]
RP GLYCOSYLATION AT SER-271; THR-280; SER-282 AND SER-341.
RA Pisano A., Jardine D.R., Packer N.H., Farnsworth V., Carson W., Cartier P.,
RA Redmond J.W., Williams K.L., Gooley A.A.;
RT "Identifying sites of glycosylation in proteins.";
RL (In) Townsend R.R., Hotchkiss A.T. Jr. (eds.);
RL Techniques in glycobiology, pp.299-320, Marcel Dekker, New York (1996).
RN [7]
RP GLYCOSYLATION AT ASN-99; ASN-156 AND ASN-176, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=15253437; DOI=10.1021/pr034112b;
RA Hagglund P., Bunkenborg J., Elortza F., Jensen O.N., Roepstorff P.;
RT "A new strategy for identification of N-glycosylated proteins and
RT unambiguous assignment of their glycosylation sites using HILIC enrichment
RT and partial deglycosylation.";
RL J. Proteome Res. 3:556-566(2004).
RN [8]
RP GLYCOSYLATION AT ASN-99; ASN-156 AND ASN-176.
RX PubMed=19358553; DOI=10.1021/ac900231w;
RA Thaysen-Andersen M., Mysling S., Hojrup P.;
RT "Site-specific glycoprofiling of N-linked glycopeptides using MALDI-TOF MS:
RT strong correlation between signal strength and glycoform quantities.";
RL Anal. Chem. 81:3933-3943(2009).
RN [9]
RP GLYCOSYLATION AT SER-296; THR-334 AND SER-341, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=19674964; DOI=10.1074/mcp.m900211-mcp200;
RA Darula Z., Medzihradszky K.F.;
RT "Affinity enrichment and characterization of mucin core-1 type
RT glycopeptides from bovine serum.";
RL Mol. Cell. Proteomics 8:2515-2526(2009).
RN [10]
RP GLYCOSYLATION AT SER-271; THR-280; SER-282; SER-296 AND SER-341,
RP PHOSPHORYLATION AT SER-138, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=25456591; DOI=10.1016/j.chroma.2014.10.046;
RA Huang L.J., Lin J.H., Tsai J.H., Chu Y.Y., Chen Y.W., Chen S.L., Chen S.H.;
RT "Identification of protein O-glycosylation site and corresponding glycans
RT using liquid chromatography-tandem mass spectrometry via mapping accurate
RT mass and retention time shift.";
RL J. Chromatogr. A 1371:136-145(2014).
RN [11]
RP GLYCOSYLATION AT ASN-99; ASN-156; ASN-176; SER-271; THR-280; SER-282;
RP SER-296 AND SER-341, PHOSPHORYLATION AT SER-138; SER-320; SER-323 AND
RP SER-325, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=24907489; DOI=10.1016/j.jprot.2014.05.022;
RA Windwarder M., Altmann F.;
RT "Site-specific analysis of the O-glycosylation of bovine fetuin by
RT electron-transfer dissociation mass spectrometry.";
RL J. Proteomics 108:258-268(2014).
CC -!- FUNCTION: Promotes endocytosis, possesses opsonic properties and
CC influences the mineral phase of bone. Suggested to have lymphocyte
CC stimulating properties, lipid binding capability and to bind thyroid
CC hormone.
CC -!- INTERACTION:
CC P12763; P17931: LGALS3; Xeno; NbExp=2; IntAct=EBI-9396660, EBI-1170392;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Liver and bone.
CC -!- PTM: Phosphorylated by FAM20C in the extracellular medium.
CC {ECO:0000250|UniProtKB:P02765}.
CC -!- SIMILARITY: Belongs to the fetuin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00861}.
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; X16577; CAA34596.1; -; mRNA.
DR EMBL; BC147948; AAI47949.1; -; mRNA.
DR PIR; A35714; A35714.
DR RefSeq; NP_776409.1; NM_173984.3.
DR AlphaFoldDB; P12763; -.
DR SMR; P12763; -.
DR IntAct; P12763; 2.
DR STRING; 9913.ENSBTAP00000000673; -.
DR MEROPS; I25.020; -.
DR MEROPS; I25.021; -.
DR GlyConnect; 22; 54 N-Linked glycans (3 sites), 13 O-Linked glycans (6 sites).
DR iPTMnet; P12763; -.
DR PaxDb; P12763; -.
DR PeptideAtlas; P12763; -.
DR PRIDE; P12763; -.
DR Ensembl; ENSBTAT00000000673; ENSBTAP00000000673; ENSBTAG00000000522.
DR GeneID; 280988; -.
DR KEGG; bta:280988; -.
DR CTD; 197; -.
DR VEuPathDB; HostDB:ENSBTAG00000000522; -.
DR VGNC; VGNC:25756; AHSG.
DR eggNOG; ENOG502RYRI; Eukaryota.
DR GeneTree; ENSGT00950000182930; -.
DR HOGENOM; CLU_052519_0_0_1; -.
DR InParanoid; P12763; -.
DR OMA; VRKVCPQ; -.
DR OrthoDB; 913381at2759; -.
DR TreeFam; TF333729; -.
DR Reactome; R-BTA-114608; Platelet degranulation.
DR Reactome; R-BTA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-BTA-6798695; Neutrophil degranulation.
DR Reactome; R-BTA-8957275; Post-translational protein phosphorylation.
DR Proteomes; UP000009136; Chromosome 1.
DR Bgee; ENSBTAG00000000522; Expressed in liver and 64 other tissues.
DR ExpressionAtlas; P12763; baseline and differential.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0065010; C:extracellular membrane-bounded organelle; IDA:AgBase.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; TAS:AgBase.
DR GO; GO:0031982; C:vesicle; IDA:AgBase.
DR GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IEA:InterPro.
DR GO; GO:0004866; F:endopeptidase inhibitor activity; IBA:GO_Central.
DR GO; GO:0006953; P:acute-phase response; ISS:UniProtKB.
DR GO; GO:0030502; P:negative regulation of bone mineralization; ISS:UniProtKB.
DR GO; GO:0010951; P:negative regulation of endopeptidase activity; IBA:GO_Central.
DR GO; GO:0001503; P:ossification; IEA:Ensembl.
DR GO; GO:0050766; P:positive regulation of phagocytosis; ISS:UniProtKB.
DR GO; GO:0050727; P:regulation of inflammatory response; ISS:UniProtKB.
DR CDD; cd00042; CY; 2.
DR InterPro; IPR000010; Cystatin_dom.
DR InterPro; IPR025760; Cystatin_Fetuin_A.
DR InterPro; IPR046350; Cystatin_sf.
DR InterPro; IPR001363; Prot_inh_fetuin_CS.
DR Pfam; PF00031; Cystatin; 1.
DR SMART; SM00043; CY; 2.
DR SUPFAM; SSF54403; SSF54403; 2.
DR PROSITE; PS51529; CYSTATIN_FETUIN_A; 2.
DR PROSITE; PS01254; FETUIN_1; 1.
DR PROSITE; PS01255; FETUIN_2; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Mineral balance;
KW Phosphoprotein; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:2436943,
FT ECO:0000269|PubMed:6165360"
FT CHAIN 19..359
FT /note="Alpha-2-HS-glycoprotein"
FT /id="PRO_0000008885"
FT DOMAIN 27..133
FT /note="Cystatin fetuin-A-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00861"
FT DOMAIN 144..256
FT /note="Cystatin fetuin-A-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00861"
FT REGION 257..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 143..144
FT /note="Cleavage; by trypsin"
FT /evidence="ECO:0000255"
FT MOD_RES 134
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02765"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02765"
FT MOD_RES 138
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:24907489,
FT ECO:0000269|PubMed:25456591"
FT MOD_RES 314
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02765"
FT MOD_RES 316
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P24090"
FT MOD_RES 320
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:24907489"
FT MOD_RES 323
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:24907489"
FT MOD_RES 325
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:24907489"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15253437,
FT ECO:0000269|PubMed:19358553, ECO:0000269|PubMed:2447075,
FT ECO:0000269|PubMed:24907489"
FT /id="CAR_000061"
FT CARBOHYD 156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15253437,
FT ECO:0000269|PubMed:19358553, ECO:0000269|PubMed:2447075,
FT ECO:0000269|PubMed:24907489"
FT /id="CAR_000062"
FT CARBOHYD 176
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15253437,
FT ECO:0000269|PubMed:19358553, ECO:0000269|PubMed:2447075,
FT ECO:0000269|PubMed:24907489"
FT /id="CAR_000063"
FT CARBOHYD 271
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000269|PubMed:24907489,
FT ECO:0000269|PubMed:25456591, ECO:0000269|Ref.6"
FT CARBOHYD 280
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:24907489,
FT ECO:0000269|PubMed:25456591, ECO:0000269|Ref.6"
FT CARBOHYD 282
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000269|PubMed:24907489,
FT ECO:0000269|PubMed:25456591, ECO:0000269|Ref.6"
FT CARBOHYD 296
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000269|PubMed:19674964,
FT ECO:0000269|PubMed:24907489, ECO:0000269|PubMed:25456591"
FT CARBOHYD 334
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:19674964"
FT CARBOHYD 341
FT /note="O-linked (GalNAc...) serine; partial"
FT /evidence="ECO:0000269|PubMed:19674964,
FT ECO:0000269|PubMed:24907489, ECO:0000269|PubMed:25456591,
FT ECO:0000269|Ref.6"
FT DISULFID 32..350
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00861"
FT DISULFID 89..100
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00861"
FT DISULFID 114..132
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00861"
FT DISULFID 146..149
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00861"
FT DISULFID 208..219
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00861"
FT DISULFID 230..248
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00861"
FT CONFLICT 57..58
FT /note="KH -> VK (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 72
FT /note="R -> Q (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 106
FT /note="T -> H (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 116..121
FT /note="IHVLKQ -> FSVVKL (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 186
FT /note="S -> R (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 195
FT /note="V -> P (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 359 AA; 38419 MW; ED8F685C44CCE49B CRC64;
MKSFVLLFCL AQLWGCHSIP LDPVAGYKEP ACDDPDTEQA ALAAVDYINK HLPRGYKHTL
NQIDSVKVWP RRPTGEVYDI EIDTLETTCH VLDPTPLANC SVRQQTQHAV EGDCDIHVLK
QDGQFSVLFT KCDSSPDSAE DVRKLCPDCP LLAPLNDSRV VHAVEVALAT FNAESNGSYL
QLVEISRAQF VPLPVSVSVE FAVAATDCIA KEVVDPTKCN LLAEKQYGFC KGSVIQKALG
GEDVRVTCTL FQTQPVIPQP QPDGAEAEAP SAVPDAAGPT PSAAGPPVAS VVVGPSVVAV
PLPLHRAHYD LRHTFSGVAS VESSSGEAFH VGKTPIVGQP SIPGGPVRLC PGRIRYFKI
