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Protein

Alpha-2-HS-glycoprotein

Gene

Ahsg

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Could inhibit both insulin-receptor tyrosine kinase activity and insulin-stimulated receptor autophosphorylation and, concomitantly, antagonize the mitogenic effect of the hormone in cultured rat hepatoma cells.

GO - Molecular functioni

GO - Biological processi

  • acute-phase response Source: UniProtKB
  • cellular response to insulin stimulus Source: RGD
  • cerebral cortex development Source: RGD
  • male gonad development Source: RGD
  • negative regulation of bone mineralization Source: UniProtKB
  • negative regulation of cell growth Source: RGD
  • negative regulation of insulin receptor signaling pathway Source: RGD
  • organ regeneration Source: RGD
  • positive regulation of bone resorption Source: RGD
  • positive regulation of phagocytosis Source: UniProtKB
  • protein complex assembly Source: RGD
  • regulation of inflammatory response Source: UniProtKB
Complete GO annotation...

Protein family/group databases

MEROPSiI25.020.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-2-HS-glycoprotein
Alternative name(s):
59 kDa bone sialic acid-containing protein
Short name:
BSP
Fetuin-A
Glycoprotein PP63
Gene namesi
Name:Ahsg
Synonyms:Fetua
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2075. Ahsg.

Subcellular locationi

GO - Cellular componenti

  • blood microparticle Source: GO_Central
  • extracellular matrix Source: RGD
  • extracellular space Source: RGD
  • protein complex Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 18181 PublicationAdd
BLAST
Chaini19 – 352334Alpha-2-HS-glycoproteinPRO_0000008897Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi32 ↔ 343PROSITE-ProRule annotation
Disulfide bondi89 ↔ 100PROSITE-ProRule annotation
Glycosylationi99 – 991N-linked (GlcNAc...)Sequence analysis
Disulfide bondi114 ↔ 132PROSITE-ProRule annotation
Modified residuei134 – 1341PhosphoserineBy similarity
Modified residuei135 – 1351PhosphothreonineBy similarity
Modified residuei138 – 1381PhosphoserineCombined sources
Disulfide bondi146 ↔ 149PROSITE-ProRule annotation
Glycosylationi156 – 1561N-linked (GlcNAc...)Sequence analysis
Glycosylationi176 – 1761N-linked (GlcNAc...)Sequence analysis
Disulfide bondi208 ↔ 219PROSITE-ProRule annotation
Disulfide bondi230 ↔ 247PROSITE-ProRule annotation
Modified residuei309 – 3091PhosphoserineCombined sources
Modified residuei313 – 3131PhosphoserineCombined sources
Modified residuei316 – 3161PhosphoserineCombined sources
Modified residuei318 – 3181PhosphoserineCombined sources

Post-translational modificationi

Undergoes complex post-translational modification involving N-glycosylation, and addition of fucose and sialic acid residues. Phosphorylation occurs at a serine residue.
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

PRIDEiP24090.

PTM databases

iPTMnetiP24090.
PhosphoSiteiP24090.

Expressioni

Tissue specificityi

Synthesized in liver and secreted by the hepatocytes in the blood.

Interactioni

Protein-protein interaction databases

IntActiP24090. 2 interactions.

Structurei

3D structure databases

ProteinModelPortaliP24090.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini19 – 133115Cystatin fetuin-A-type 1PROSITE-ProRule annotationAdd
BLAST
Domaini144 – 250107Cystatin 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

HOGENOMiHOG000290189.
HOVERGENiHBG051607.
InParanoidiP24090.

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.

P24090-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKSLVLLLCF AQLWSCQSAP QGAGLGFREL ACDDPETEHV ALIAVDYLNK
60 70 80 90 100
HLLQGFRQIL NQIDKVKVWS RRPFGEVYEL EIDTLETTCH ALDPTPLANC
110 120 130 140 150
SVRQQAEHAV EGDCDFHILK QDGQFRVLHA QCHSTPDSAE DVRKFCPRCP
160 170 180 190 200
ILIRFNDTNV VHTVKTALAA FNAQNNGTYF KLVEISRAQN VPFPVSTLVE
210 220 230 240 250
FVIAATDCTG QEVTDPAKCN LLAEKQYGFC KATLIHRLGG EEVSVACKLF
260 270 280 290 300
QTQPQPANAN PAGPAPTVGQ AAPVAPPAGP PESVVVGPVA VPLGLPDHRT
310 320 330 340 350
HHDLRHAFSP VASVESASGE VLHSPKVGQP GDAGAAGPVA PLCPGRVRYF

KI
Length:352
Mass (Da):37,982
Last modified:April 1, 1993 - v2
Checksum:i43564F60F3C7C90A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti21 – 211Q → E AA sequence (PubMed:1860865).Curated
Sequence conflicti29 – 291E → Q AA sequence (PubMed:1860865).Curated
Sequence conflicti33 – 342DD → NN AA sequence (PubMed:1860865).Curated
Sequence conflicti46 – 461D → H in AAA75502 (PubMed:1849862).Curated
Sequence conflicti76 – 761E → Q in AAA75502 (PubMed:1849862).Curated
Sequence conflicti236 – 2372HR → QF AA sequence (PubMed:1860865).Curated
Sequence conflicti241 – 2422EE → QQ AA sequence (PubMed:1860865).Curated
Sequence conflicti329 – 3291Q → E AA sequence (PubMed:1860865).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X63446 mRNA. Translation: CAA45042.1.
M29758 mRNA. Translation: AAA75502.1.
D10261 mRNA. Translation: BAA01101.1.
BC091118 mRNA. Translation: AAH91118.1.
PIRiA32827.
RefSeqiNP_037030.1. NM_012898.4.
UniGeneiRn.32083.

Genome annotation databases

GeneIDi25373.
KEGGirno:25373.
UCSCiRGD:2075. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X63446 mRNA. Translation: CAA45042.1.
M29758 mRNA. Translation: AAA75502.1.
D10261 mRNA. Translation: BAA01101.1.
BC091118 mRNA. Translation: AAH91118.1.
PIRiA32827.
RefSeqiNP_037030.1. NM_012898.4.
UniGeneiRn.32083.

3D structure databases

ProteinModelPortaliP24090.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP24090. 2 interactions.

Protein family/group databases

MEROPSiI25.020.

PTM databases

iPTMnetiP24090.
PhosphoSiteiP24090.

Proteomic databases

PRIDEiP24090.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi25373.
KEGGirno:25373.
UCSCiRGD:2075. rat.

Organism-specific databases

CTDi197.
RGDi2075. Ahsg.

Phylogenomic databases

HOGENOMiHOG000290189.
HOVERGENiHBG051607.
InParanoidiP24090.

Miscellaneous databases

PROiP24090.

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 nucleotide and partial amino acid sequences of rat fetuin. Identity with the natural tyrosine kinase inhibitor of the rat insulin receptor."
    Rauth G., Poeschke O., Fink E., Eulitz M., Tippmer S., Kellerer M., Haering H., Nawratil P., Haasemann M., Jahnen-Dechent W., Mueller-Esterl W.
    Eur. J. Biochem. 204:523-529(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Characterization of a natural inhibitor of the insulin receptor tyrosine kinase: cDNA cloning, purification, and anti-mitogenic activity."
    Auberger P., Falquerho L., Contreres J.O., Pages G., le Cam G., Rossi B., le Cam A.
    Cell 58:631-640(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  3. "Primary structure of the rat gene encoding an inhibitor of the insulin receptor tyrosine kinase."
    Falquerho L., Patey G., Paqureau L., Rossi V., Lahuna O., Szpirer J., Szpirer C., Levan G., le Cam A.
    Gene 98:209-216(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SEQUENCE REVISION.
  4. "Molecular cloning and sequence analysis of cDNA for a 59 kD bone sialoprotein of the rat: demonstration that it is a counterpart of human alpha 2-HS glycoprotein and bovine fetuin."
    Ohnishi T., Nakamura O., Ozawa M., Arakaki N., Muramatsu T., Daikuhara Y.
    J. Bone Miner. Res. 8:367-377(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Spleen.
  6. "Purification, characterization, and studies on biosynthesis of a 59-kDa bone sialic acid-containing protein (BSP) from rat mandible using a monoclonal antibody. Evidence that 59-kDa BSP may be the rat counterpart of human alpha 2-HS glycoprotein and is synthesized by both hepatocytes and osteoblasts."
    Ohnishi T., Arakaki N., Nakamura O., Hirono S., Daikuhara Y.
    J. Biol. Chem. 266:14636-14645(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 19-35; 51-64; 165-180; 231-247 AND 327-348.
    Tissue: Mandible.
  7. "Rat tyrosine kinase inhibitor shows sequence similarity to human alpha 2-HS glycoprotein and bovine fetuin."
    Haasemann M., Nawratil P., Mueller-Esterl W.
    Biochem. J. 274:899-902(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTITY OF PP63 WITH FETUIN.
  8. "The rat protein encoded by clone pp63 is a fetuin/alpha 2-HS glycoprotein-like molecule, but is it the tyrosine kinase inhibitor pp63?"
    Brown W.M., Christie D.L., Dziegielewska K.M., Saunders N.R., Yang F.
    Cell 68:7-8(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTITY OF PP63 WITH FETUIN.
  9. "Quantitative phosphoproteomics of vasopressin-sensitive renal cells: regulation of aquaporin-2 phosphorylation at two sites."
    Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.
    Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138; SER-309; SER-313; SER-316 AND SER-318, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiFETUA_RAT
AccessioniPrimary (citable) accession number: P24090
Secondary accession number(s): Q5BKD2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: April 1, 1993
Last modified: July 6, 2016
This is version 127 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.