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Serpin A12 (Visceral adipose tissue-derived serine protease inhibitor) (Vaspin) (Visceral adipose-specific serpin)

 SPA12_RAT               Reviewed;         411 AA.
Q8R4Z1;
27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
01-JUN-2002, sequence version 1.
22-NOV-2017, entry version 89.
RecName: Full=Serpin A12;
AltName: Full=Visceral adipose tissue-derived serine protease inhibitor;
Short=Vaspin;
AltName: Full=Visceral adipose-specific serpin;
Flags: Precursor;
Name=Serpina12;
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], FUNCTION, TISSUE SPECIFICITY, AND
DEVELOPMENTAL STAGE.
STRAIN=OLETF; TISSUE=Adipose tissue;
PubMed=16030142; DOI=10.1073/pnas.0504703102;
Hida K., Wada J., Eguchi J., Zhang H., Baba M., Seida A.,
Hashimoto I., Okada T., Yasuhara A., Nakatsuka A., Shikata K.,
Hourai S., Futami J., Watanabe E., Matsuki Y., Hiramatsu R., Akagi S.,
Makino H., Kanwar Y.S.;
"Visceral adipose tissue-derived serine protease inhibitor: a unique
insulin-sensitizing adipocytokine in obesity.";
Proc. Natl. Acad. Sci. U.S.A. 102:10610-10615(2005).
-!- FUNCTION: Adipokine that modulates insulin action by specifically
inhibiting its target protease KLK7 in white adipose tissues.
{ECO:0000250, ECO:0000269|PubMed:16030142}.
-!- SUBUNIT: Forms a stable complex with KLK7. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in visceral adipose tissues.
{ECO:0000269|PubMed:16030142}.
-!- DEVELOPMENTAL STAGE: Barely detectable in at 6 weeks and is highly
expressed in adipocytes of visceral white adipose tissues at 30
weeks. {ECO:0000269|PubMed:16030142}.
-!- DOMAIN: The reactive center loop (RCL) extends out from the body
of the protein and directs binding to the target protease. The
protease cleaves the serpin at the reactive site within the RCL,
establishing a covalent linkage between the carboxyl group of the
serpin reactive site and the serine hydroxyl of the protease. The
resulting inactive serpin-protease complex is highly stable (By
similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}.
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EMBL; AF245398; AAL99574.1; -; mRNA.
UniGene; Rn.79035; -.
ProteinModelPortal; Q8R4Z1; -.
SMR; Q8R4Z1; -.
STRING; 10116.ENSRNOP00000012960; -.
MEROPS; I04.091; -.
iPTMnet; Q8R4Z1; -.
PhosphoSitePlus; Q8R4Z1; -.
PaxDb; Q8R4Z1; -.
PRIDE; Q8R4Z1; -.
UCSC; RGD:708485; rat.
RGD; 708485; Serpina12.
eggNOG; KOG2392; Eukaryota.
eggNOG; COG4826; LUCA.
HOGENOM; HOG000238521; -.
HOVERGEN; HBG005957; -.
InParanoid; Q8R4Z1; -.
PhylomeDB; Q8R4Z1; -.
PRO; PR:Q8R4Z1; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005615; C:extracellular space; ISO:RGD.
GO; GO:0005886; C:plasma membrane; ISO:RGD.
GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IBA:GO_Central.
GO; GO:0006006; P:glucose metabolic process; IEP:RGD.
GO; GO:0045721; P:negative regulation of gluconeogenesis; ISO:RGD.
GO; GO:0051055; P:negative regulation of lipid biosynthetic process; ISO:RGD.
GO; GO:0046628; P:positive regulation of insulin receptor signaling pathway; ISO:RGD.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; ISO:RGD.
GO; GO:0090181; P:regulation of cholesterol metabolic process; ISO:RGD.
GO; GO:0090207; P:regulation of triglyceride metabolic process; ISO:RGD.
InterPro; IPR023796; Serpin_dom.
InterPro; IPR000215; Serpin_fam.
InterPro; IPR036186; Serpin_sf.
PANTHER; PTHR11461; PTHR11461; 1.
Pfam; PF00079; Serpin; 1.
SMART; SM00093; SERPIN; 1.
SUPFAM; SSF56574; SSF56574; 1.
2: Evidence at transcript level;
Complete proteome; Glycoprotein; Protease inhibitor;
Reference proteome; Secreted; Serine protease inhibitor; Signal.
SIGNAL 1 20 {ECO:0000250}.
CHAIN 21 411 Serpin A12.
/FTId=PRO_0000041978.
REGION 364 382 RCL. {ECO:0000250}.
CARBOHYD 92 92 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 267 267 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
SEQUENCE 411 AA; 47527 MW; 29FA271FF8CC8A2D CRC64;
MNLVLGLGLF LAGLLTVKGL LQDRDAPDTY ESPVRVQEWR GKKDARELTR HNMEFGFKLL
QRLASNSRQG NIFLSPLSIS TAFSMLSLGA QNSTLEEIRE GFNFKEMSDR DMHMGFHYLL
QKLNRETQDV KMSIGNALFM DQRLRPQQRF LKLAKNLYDA DMILTNFQDL ENTQKNINKY
ISRKTHNRIE NMVKNIDPGT VMLLTNYIYF QGRWQYEFDP KQTKEEDFFI EEGKTVKVPM
MFQRGMYDMA YDSQLSCTIL EMPYRGNITA TFVLPDSGKL RLLEQGLQAD IFAKWKSLLS
KRVVDVWVPR LHISATYNMK KVLSRLGISK IFEEHGDLTR ISSHRSLKVG EAVHKAELRM
NEKGTEGAAG SGAQTLPMET PRRMKLNAPF LMMIYENLMP SMIFLARIYN P


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