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Alpha-2-HS-glycoprotein (59 kDa bone sialic acid-containing protein) (BSP) (Fetuin-A) (Glycoprotein PP63)

 FETUA_RAT               Reviewed;         352 AA.
P24090; Q5BKD2;
01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
01-APR-1993, sequence version 2.
23-MAY-2018, entry version 137.
RecName: Full=Alpha-2-HS-glycoprotein;
AltName: Full=59 kDa bone sialic acid-containing protein;
Short=BSP;
AltName: Full=Fetuin-A;
AltName: Full=Glycoprotein PP63;
Flags: Precursor;
Name=Ahsg; Synonyms=Fetua;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1371750; DOI=10.1111/j.1432-1033.1992.tb16663.x;
Rauth G., Poeschke O., Fink E., Eulitz M., Tippmer S., Kellerer M.,
Haering H., Nawratil P., Haasemann M., Jahnen-Dechent W.,
Mueller-Esterl W.;
"The nucleotide and partial amino acid sequences of rat fetuin.
Identity with the natural tyrosine kinase inhibitor of the rat insulin
receptor.";
Eur. J. Biochem. 204:523-529(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=2766355; DOI=10.1016/0092-8674(89)90098-6;
Auberger P., Falquerho L., Contreres J.O., Pages G., le Cam G.,
Rossi B., le Cam A.;
"Characterization of a natural inhibitor of the insulin receptor
tyrosine kinase: cDNA cloning, purification, and anti-mitogenic
activity.";
Cell 58:631-640(1989).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND SEQUENCE REVISION.
PubMed=1849862; DOI=10.1016/0378-1119(91)90175-B;
Falquerho L., Patey G., Paqureau L., Rossi V., Lahuna O., Szpirer J.,
Szpirer C., Levan G., le Cam A.;
"Primary structure of the rat gene encoding an inhibitor of the
insulin receptor tyrosine kinase.";
Gene 98:209-216(1991).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=7681247; DOI=10.1002/jbmr.5650080314;
Ohnishi T., Nakamura O., Ozawa M., Arakaki N., Muramatsu T.,
Daikuhara Y.;
"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.";
J. Bone Miner. Res. 8:367-377(1993).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Spleen;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PROTEIN SEQUENCE OF 19-35; 51-64; 165-180; 231-247 AND 327-348.
TISSUE=Mandible;
PubMed=1860865;
Ohnishi T., Arakaki N., Nakamura O., Hirono S., Daikuhara Y.;
"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.";
J. Biol. Chem. 266:14636-14645(1991).
[7]
IDENTITY OF PP63 WITH FETUIN.
PubMed=1707273; DOI=10.1042/bj2740899;
Haasemann M., Nawratil P., Mueller-Esterl W.;
"Rat tyrosine kinase inhibitor shows sequence similarity to human
alpha 2-HS glycoprotein and bovine fetuin.";
Biochem. J. 274:899-902(1991).
[8]
IDENTITY OF PP63 WITH FETUIN.
PubMed=1370655; DOI=10.1016/0092-8674(92)90200-V;
Brown W.M., Christie D.L., Dziegielewska K.M., Saunders N.R., Yang F.;
"The rat protein encoded by clone pp63 is a fetuin/alpha 2-HS
glycoprotein-like molecule, but is it the tyrosine kinase inhibitor
pp63?";
Cell 68:7-8(1992).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=16641100; DOI=10.1073/pnas.0600895103;
Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
"Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
regulation of aquaporin-2 phosphorylation at two sites.";
Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138; SER-309; SER-313;
SER-316 AND SER-318, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: 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.
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Synthesized in liver and secreted by the
hepatocytes in the blood.
-!- PTM: Undergoes complex post-translational modification involving
N-glycosylation, and addition of fucose and sialic acid residues.
Phosphorylation occurs at a serine residue.
-!- PTM: Phosphorylated by FAM20C in the extracellular medium.
{ECO:0000250|UniProtKB:P02765}.
-!- SIMILARITY: Belongs to the fetuin family. {ECO:0000255|PROSITE-
ProRule:PRU00861}.
-----------------------------------------------------------------------
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EMBL; X63446; CAA45042.1; -; mRNA.
EMBL; M29758; AAA75502.1; -; mRNA.
EMBL; D10261; BAA01101.1; -; mRNA.
EMBL; BC091118; AAH91118.1; -; mRNA.
PIR; A32827; A32827.
RefSeq; NP_037030.1; NM_012898.4.
UniGene; Rn.32083; -.
ProteinModelPortal; P24090; -.
SMR; P24090; -.
IntAct; P24090; 2.
MEROPS; I25.020; -.
iPTMnet; P24090; -.
PhosphoSitePlus; P24090; -.
SwissPalm; P24090; -.
PRIDE; P24090; -.
GeneID; 25373; -.
KEGG; rno:25373; -.
UCSC; RGD:2075; rat.
CTD; 197; -.
RGD; 2075; Ahsg.
HOGENOM; HOG000290189; -.
HOVERGEN; HBG051607; -.
InParanoid; P24090; -.
PRO; PR:P24090; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0072562; C:blood microparticle; IBA:GO_Central.
GO; GO:0031012; C:extracellular matrix; IDA:RGD.
GO; GO:0005615; C:extracellular space; IDA:RGD.
GO; GO:0032991; C:protein-containing complex; IDA:RGD.
GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IEA:InterPro.
GO; GO:0004866; F:endopeptidase inhibitor activity; IBA:GO_Central.
GO; GO:0019210; F:kinase inhibitor activity; NAS:UniProtKB.
GO; GO:0030294; F:receptor signaling protein tyrosine kinase inhibitor activity; IDA:RGD.
GO; GO:0006953; P:acute-phase response; ISS:UniProtKB.
GO; GO:0031100; P:animal organ regeneration; IEP:RGD.
GO; GO:0032869; P:cellular response to insulin stimulus; IEP:RGD.
GO; GO:0021987; P:cerebral cortex development; IEP:RGD.
GO; GO:0008584; P:male gonad development; IMP:RGD.
GO; GO:0030502; P:negative regulation of bone mineralization; IMP:RGD.
GO; GO:0030308; P:negative regulation of cell growth; IDA:RGD.
GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; IDA:RGD.
GO; GO:0045780; P:positive regulation of bone resorption; IMP:RGD.
GO; GO:0050766; P:positive regulation of phagocytosis; ISS:UniProtKB.
GO; GO:0050727; P:regulation of inflammatory response; ISS:UniProtKB.
CDD; cd00042; CY; 2.
InterPro; IPR000010; Cystatin_dom.
InterPro; IPR025760; Cystatin_Fetuin_A.
InterPro; IPR001363; Prot_inh_fetuin_CS.
Pfam; PF00031; Cystatin; 1.
SMART; SM00043; CY; 2.
PROSITE; PS51529; CYSTATIN_FETUIN_A; 2.
PROSITE; PS01254; FETUIN_1; 1.
PROSITE; PS01255; FETUIN_2; 1.
1: Evidence at protein level;
Complete proteome; Direct protein sequencing; Disulfide bond;
Glycoprotein; Phosphoprotein; Reference proteome; Repeat; Secreted;
Signal.
SIGNAL 1 18 {ECO:0000269|PubMed:1860865}.
CHAIN 19 352 Alpha-2-HS-glycoprotein.
/FTId=PRO_0000008897.
DOMAIN 19 133 Cystatin fetuin-A-type 1.
{ECO:0000255|PROSITE-ProRule:PRU00861}.
DOMAIN 144 250 Cystatin fetuin-A-type 2.
{ECO:0000255|PROSITE-ProRule:PRU00861}.
SITE 143 144 Cleavage; by trypsin. {ECO:0000255}.
MOD_RES 134 134 Phosphoserine.
{ECO:0000250|UniProtKB:P02765}.
MOD_RES 135 135 Phosphothreonine.
{ECO:0000250|UniProtKB:P29699}.
MOD_RES 138 138 Phosphoserine.
{ECO:0000244|PubMed:16641100,
ECO:0000244|PubMed:22673903}.
MOD_RES 309 309 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 313 313 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 316 316 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 318 318 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
CARBOHYD 99 99 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 156 156 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 176 176 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 32 343 {ECO:0000255|PROSITE-ProRule:PRU00861}.
DISULFID 89 100 {ECO:0000255|PROSITE-ProRule:PRU00861}.
DISULFID 114 132 {ECO:0000255|PROSITE-ProRule:PRU00861}.
DISULFID 146 149 {ECO:0000255|PROSITE-ProRule:PRU00861}.
DISULFID 208 219 {ECO:0000255|PROSITE-ProRule:PRU00861}.
DISULFID 230 247 {ECO:0000255|PROSITE-ProRule:PRU00861}.
CONFLICT 21 21 Q -> E (in Ref. 6; AA sequence).
{ECO:0000305}.
CONFLICT 29 29 E -> Q (in Ref. 6; AA sequence).
{ECO:0000305}.
CONFLICT 33 34 DD -> NN (in Ref. 6; AA sequence).
{ECO:0000305}.
CONFLICT 46 46 D -> H (in Ref. 3; AAA75502).
{ECO:0000305}.
CONFLICT 76 76 E -> Q (in Ref. 3; AAA75502).
{ECO:0000305}.
CONFLICT 236 237 HR -> QF (in Ref. 6; AA sequence).
{ECO:0000305}.
CONFLICT 241 242 EE -> QQ (in Ref. 6; AA sequence).
{ECO:0000305}.
CONFLICT 329 329 Q -> E (in Ref. 6; AA sequence).
{ECO:0000305}.
SEQUENCE 352 AA; 37982 MW; 43564F60F3C7C90A CRC64;
MKSLVLLLCF AQLWSCQSAP QGAGLGFREL ACDDPETEHV ALIAVDYLNK HLLQGFRQIL
NQIDKVKVWS RRPFGEVYEL EIDTLETTCH ALDPTPLANC SVRQQAEHAV EGDCDFHILK
QDGQFRVLHA QCHSTPDSAE DVRKFCPRCP ILIRFNDTNV VHTVKTALAA FNAQNNGTYF
KLVEISRAQN VPFPVSTLVE FVIAATDCTG QEVTDPAKCN LLAEKQYGFC KATLIHRLGG
EEVSVACKLF QTQPQPANAN PAGPAPTVGQ AAPVAPPAGP PESVVVGPVA VPLGLPDHRT
HHDLRHAFSP VASVESASGE VLHSPKVGQP GDAGAAGPVA PLCPGRVRYF KI


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