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Protein

Alpha-2-HS-glycoprotein

Gene

AHSG

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Promotes endocytosis, possesses opsonic properties and influences the mineral phase of bone. Suggested to have lymphocyte stimulating properties, lipid binding capability and to bind thyroid hormone.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Mineral balance

Protein family/group databases

MEROPSiI25.020.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-2-HS-glycoprotein
Alternative name(s):
Asialofetuin
Fetuin-A
Gene namesi
Name:AHSG
Synonyms:FETUA
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 1

Subcellular locationi

GO - Cellular componenti

  • blood microparticle Source: GO_Central
  • extracellular exosome Source: Ensembl
  • extracellular matrix Source: GO_Central
  • extracellular membrane-bounded organelle Source: AgBase
  • plasma membrane Source: AgBase
  • vesicle Source: AgBase
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 18182 PublicationsAdd
BLAST
Chaini19 – 359341Alpha-2-HS-glycoproteinPRO_0000008885Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi32 ↔ 350PROSITE-ProRule annotation
Disulfide bondi89 ↔ 100PROSITE-ProRule annotation
Glycosylationi99 – 991N-linked (GlcNAc...)4 PublicationsCAR_000061
Disulfide bondi114 ↔ 132PROSITE-ProRule annotation
Modified residuei134 – 1341PhosphoserineBy similarity
Modified residuei135 – 1351PhosphoserineBy similarity
Modified residuei138 – 1381Phosphoserine2 Publications
Disulfide bondi146 ↔ 149PROSITE-ProRule annotation
Glycosylationi156 – 1561N-linked (GlcNAc...)4 PublicationsCAR_000062
Glycosylationi176 – 1761N-linked (GlcNAc...)4 PublicationsCAR_000063
Disulfide bondi208 ↔ 219PROSITE-ProRule annotation
Disulfide bondi230 ↔ 248PROSITE-ProRule annotation
Glycosylationi271 – 2711O-linked (GalNAc...)3 Publications
Glycosylationi280 – 2801O-linked (GalNAc...)3 Publications
Glycosylationi282 – 2821O-linked (GalNAc...)3 Publications
Glycosylationi296 – 2961O-linked (GalNAc...)3 Publications
Modified residuei314 – 3141PhosphothreonineBy similarity
Modified residuei316 – 3161PhosphoserineBy similarity
Modified residuei320 – 3201Phosphoserine1 Publication
Modified residuei323 – 3231Phosphoserine1 Publication
Modified residuei325 – 3251Phosphoserine1 Publication
Glycosylationi334 – 3341O-linked (GalNAc...)1 Publication
Glycosylationi341 – 3411O-linked (GalNAc...); partial4 Publications

Post-translational modificationi

Phosphorylated by FAM20C in the extracellular medium.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei143 – 1442Cleavage; by trypsinSequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP12763.
PRIDEiP12763.

PTM databases

iPTMnetiP12763.
UniCarbKBiP12763.

Miscellaneous databases

PMAP-CutDBP12763.

Expressioni

Tissue specificityi

Liver and bone.

Gene expression databases

ExpressionAtlasiP12763. baseline and differential.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
LGALS3P179312EBI-9396660,EBI-1170392From a different organism.

Protein-protein interaction databases

IntActiP12763. 1 interaction.
STRINGi9913.ENSBTAP00000000673.

Structurei

3D structure databases

ProteinModelPortaliP12763.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini27 – 133107Cystatin fetuin-A-type 1PROSITE-ProRule annotationAdd
BLAST
Domaini144 – 256113Cystatin fetuin-A-type 2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the fetuin family.PROSITE-ProRule annotation
Contains 2 cystatin fetuin-A-type domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiENOG410IK8F. Eukaryota.
ENOG4111RIP. LUCA.
GeneTreeiENSGT00530000063413.
HOGENOMiHOG000290189.
HOVERGENiHBG051607.
InParanoidiP12763.
OMAiRAHYDLR.
OrthoDBiEOG71K63R.
TreeFamiTF333729.

Family and domain databases

InterProiIPR000010. Cystatin_dom.
IPR025760. Cystatin_Fetuin_A.
IPR001363. Prot_inh_fetuin_CS.
[Graphical view]
PfamiPF00031. Cystatin. 1 hit.
[Graphical view]
SMARTiSM00043. CY. 2 hits.
[Graphical view]
PROSITEiPS51529. CYSTATIN_FETUIN_A. 2 hits.
PS01254. FETUIN_1. 1 hit.
PS01255. FETUIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P12763-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKSFVLLFCL AQLWGCHSIP LDPVAGYKEP ACDDPDTEQA ALAAVDYINK
60 70 80 90 100
HLPRGYKHTL NQIDSVKVWP RRPTGEVYDI EIDTLETTCH VLDPTPLANC
110 120 130 140 150
SVRQQTQHAV EGDCDIHVLK QDGQFSVLFT KCDSSPDSAE DVRKLCPDCP
160 170 180 190 200
LLAPLNDSRV VHAVEVALAT FNAESNGSYL QLVEISRAQF VPLPVSVSVE
210 220 230 240 250
FAVAATDCIA KEVVDPTKCN LLAEKQYGFC KGSVIQKALG GEDVRVTCTL
260 270 280 290 300
FQTQPVIPQP QPDGAEAEAP SAVPDAAGPT PSAAGPPVAS VVVGPSVVAV
310 320 330 340 350
PLPLHRAHYD LRHTFSGVAS VESSSGEAFH VGKTPIVGQP SIPGGPVRLC

PGRIRYFKI
Length:359
Mass (Da):38,419
Last modified:August 1, 1990 - v2
Checksum:iED8F685C44CCE49B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti57 – 582KH → VK AA sequence (PubMed:6165360).Curated
Sequence conflicti72 – 721R → Q AA sequence (PubMed:2436943).Curated
Sequence conflicti106 – 1061T → H AA sequence (PubMed:2436943).Curated
Sequence conflicti116 – 1216IHVLKQ → FSVVKL AA sequence (PubMed:2436943).Curated
Sequence conflicti186 – 1861S → R AA sequence (PubMed:2447075).Curated
Sequence conflicti195 – 1951V → P AA sequence (PubMed:2436943).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X16577 mRNA. Translation: CAA34596.1.
BC147948 mRNA. Translation: AAI47949.1.
PIRiA35714.
RefSeqiNP_776409.1. NM_173984.3.
UniGeneiBt.23250.

Genome annotation databases

EnsembliENSBTAT00000000673; ENSBTAP00000000673; ENSBTAG00000000522.
GeneIDi280988.
KEGGibta:280988.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X16577 mRNA. Translation: CAA34596.1.
BC147948 mRNA. Translation: AAI47949.1.
PIRiA35714.
RefSeqiNP_776409.1. NM_173984.3.
UniGeneiBt.23250.

3D structure databases

ProteinModelPortaliP12763.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP12763. 1 interaction.
STRINGi9913.ENSBTAP00000000673.

Protein family/group databases

MEROPSiI25.020.

PTM databases

iPTMnetiP12763.
UniCarbKBiP12763.

Proteomic databases

PaxDbiP12763.
PRIDEiP12763.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000000673; ENSBTAP00000000673; ENSBTAG00000000522.
GeneIDi280988.
KEGGibta:280988.

Organism-specific databases

CTDi197.

Phylogenomic databases

eggNOGiENOG410IK8F. Eukaryota.
ENOG4111RIP. LUCA.
GeneTreeiENSGT00530000063413.
HOGENOMiHOG000290189.
HOVERGENiHBG051607.
InParanoidiP12763.
OMAiRAHYDLR.
OrthoDBiEOG71K63R.
TreeFamiTF333729.

Miscellaneous databases

NextBioi20805089.
PMAP-CutDBP12763.

Gene expression databases

ExpressionAtlasiP12763. baseline and differential.

Family and domain databases

InterProiIPR000010. Cystatin_dom.
IPR025760. Cystatin_Fetuin_A.
IPR001363. Prot_inh_fetuin_CS.
[Graphical view]
PfamiPF00031. Cystatin. 1 hit.
[Graphical view]
SMARTiSM00043. CY. 2 hits.
[Graphical view]
PROSITEiPS51529. CYSTATIN_FETUIN_A. 2 hits.
PS01254. FETUIN_1. 1 hit.
PS01255. FETUIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The complete cDNA and amino acid sequence of bovine fetuin. Its homology with alpha 2HS glycoprotein and relation to other members of the cystatin superfamily."
    Dziegielewska K.D., Brown W.M., Casey S.J., Christie D.L., Foreman R.C., Hill R.M., Saunders N.R.
    J. Biol. Chem. 265:4354-4357(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  2. NIH - Mammalian Gene Collection (MGC) project
    Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Fetal liver.
  3. "Fetuin: the bovine homologue of human alpha 2HS glycoprotein."
    Christie D.L., Dziegielewska K.M., Hill R.M., Saunders N.R.
    FEBS Lett. 214:45-49(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 19-123 AND 188-243.
  4. Cited for: PROTEIN SEQUENCE OF 19-62.
  5. "The covalent structure of individual N-linked glycopeptides from ovomucoid and asialofetuin."
    Yet M.G., Chin C.C.Q., Wold F.
    J. Biol. Chem. 263:111-117(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 72-103 AND 144-187, GLYCOSYLATION AT ASN-99; ASN-156 AND ASN-176.
  6. "Identifying sites of glycosylation in proteins."
    Pisano A., Jardine D.R., Packer N.H., Farnsworth V., Carson W., Cartier P., Redmond J.W., Williams K.L., Gooley A.A.
    (In) Townsend R.R., Hotchkiss A.T. Jr. (eds.); Techniques in glycobiology, pp.299-320, Marcel Dekker, New York (1996)
    Cited for: GLYCOSYLATION AT SER-271; THR-280; SER-282 AND SER-341.
  7. "A new strategy for identification of N-glycosylated proteins and unambiguous assignment of their glycosylation sites using HILIC enrichment and partial deglycosylation."
    Hagglund P., Bunkenborg J., Elortza F., Jensen O.N., Roepstorff P.
    J. Proteome Res. 3:556-566(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT ASN-99; ASN-156 AND ASN-176, IDENTIFICATION BY MASS SPECTROMETRY.
  8. "Site-specific glycoprofiling of N-linked glycopeptides using MALDI-TOF MS: strong correlation between signal strength and glycoform quantities."
    Thaysen-Andersen M., Mysling S., Hojrup P.
    Anal. Chem. 81:3933-3943(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT ASN-99; ASN-156 AND ASN-176.
  9. "Affinity enrichment and characterization of mucin core-1 type glycopeptides from bovine serum."
    Darula Z., Medzihradszky K.F.
    Mol. Cell. Proteomics 8:2515-2526(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT SER-296; THR-334 AND SER-341, IDENTIFICATION BY MASS SPECTROMETRY.
  10. "Identification of protein O-glycosylation site and corresponding glycans using liquid chromatography-tandem mass spectrometry via mapping accurate mass and retention time shift."
    Huang L.J., Lin J.H., Tsai J.H., Chu Y.Y., Chen Y.W., Chen S.L., Chen S.H.
    J. Chromatogr. A 1371:136-145(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT SER-271; THR-280; SER-282; SER-296 AND SER-341, PHOSPHORYLATION AT SER-138, IDENTIFICATION BY MASS SPECTROMETRY.
  11. "Site-specific analysis of the O-glycosylation of bovine fetuin by electron-transfer dissociation mass spectrometry."
    Windwarder M., Altmann F.
    J. Proteomics 108:258-268(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT ASN-99; ASN-156; ASN-176; SER-271; THR-280; SER-282; SER-296 AND SER-341, PHOSPHORYLATION AT SER-138; SER-320; SER-323 AND SER-325, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiFETUA_BOVIN
AccessioniPrimary (citable) accession number: P12763
Secondary accession number(s): A6QLF7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: August 1, 1990
Last modified: February 17, 2016
This is version 122 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.