SPA12_RAT
ID SPA12_RAT Reviewed; 411 AA.
AC Q8R4Z1;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=Serpin A12;
DE AltName: Full=Visceral adipose tissue-derived serine protease inhibitor;
DE Short=Vaspin;
DE AltName: Full=Visceral adipose-specific serpin;
DE Flags: Precursor;
GN Name=Serpina12;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RC STRAIN=OLETF; TISSUE=Adipose tissue;
RX PubMed=16030142; DOI=10.1073/pnas.0504703102;
RA Hida K., Wada J., Eguchi J., Zhang H., Baba M., Seida A., Hashimoto I.,
RA Okada T., Yasuhara A., Nakatsuka A., Shikata K., Hourai S., Futami J.,
RA Watanabe E., Matsuki Y., Hiramatsu R., Akagi S., Makino H., Kanwar Y.S.;
RT "Visceral adipose tissue-derived serine protease inhibitor: a unique
RT insulin-sensitizing adipocytokine in obesity.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:10610-10615(2005).
CC -!- FUNCTION: Adipokine that modulates insulin action by specifically
CC inhibiting its target protease KLK7 in white adipose tissues.
CC {ECO:0000250, ECO:0000269|PubMed:16030142}.
CC -!- ACTIVITY REGULATION: Inhibition of KLK7 is enhanced by heparin.
CC {ECO:0000250|UniProtKB:Q8IW75}.
CC -!- SUBUNIT: Forms a stable complex with KLK7.
CC {ECO:0000250|UniProtKB:Q8IW75}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q7TMF5}.
CC -!- TISSUE SPECIFICITY: Expressed in visceral adipose tissues.
CC {ECO:0000269|PubMed:16030142}.
CC -!- DEVELOPMENTAL STAGE: Barely detectable in at 6 weeks and is highly
CC expressed in adipocytes of visceral white adipose tissues at 30 weeks.
CC {ECO:0000269|PubMed:16030142}.
CC -!- DOMAIN: The reactive center loop (RCL) extends out from the body of the
CC protein and directs binding to the target protease. The protease
CC cleaves the serpin at the reactive site within the RCL, establishing a
CC covalent linkage between the carboxyl group of the serpin reactive site
CC and the serine hydroxyl of the protease. The resulting inactive serpin-
CC protease complex is highly stable. {ECO:0000250|UniProtKB:Q8IW75}.
CC -!- PTM: Glycosylation slightly decreases affinity for heparin, but
CC otherwise has no significant effect on KLK7 inhibitory activity or
CC thermal stability of the protein. {ECO:0000250|UniProtKB:Q8IW75}.
CC -!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}.
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DR EMBL; AF245398; AAL99574.1; -; mRNA.
DR AlphaFoldDB; Q8R4Z1; -.
DR SMR; Q8R4Z1; -.
DR STRING; 10116.ENSRNOP00000012960; -.
DR MEROPS; I04.091; -.
DR GlyGen; Q8R4Z1; 2 sites.
DR iPTMnet; Q8R4Z1; -.
DR PhosphoSitePlus; Q8R4Z1; -.
DR PaxDb; Q8R4Z1; -.
DR UCSC; RGD:708485; rat.
DR RGD; 708485; Serpina12.
DR eggNOG; KOG2392; Eukaryota.
DR InParanoid; Q8R4Z1; -.
DR PhylomeDB; Q8R4Z1; -.
DR PRO; PR:Q8R4Z1; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005615; C:extracellular space; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IBA:GO_Central.
DR GO; GO:0006006; P:glucose metabolic process; IEP:RGD.
DR GO; GO:0010951; P:negative regulation of endopeptidase activity; IBA:GO_Central.
DR GO; GO:0045721; P:negative regulation of gluconeogenesis; ISO:RGD.
DR GO; GO:0051055; P:negative regulation of lipid biosynthetic process; ISO:RGD.
DR GO; GO:0046628; P:positive regulation of insulin receptor signaling pathway; ISO:RGD.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; ISO:RGD.
DR GO; GO:0090181; P:regulation of cholesterol metabolic process; ISO:RGD.
DR GO; GO:0090207; P:regulation of triglyceride metabolic process; ISO:RGD.
DR Gene3D; 2.30.39.10; -; 1.
DR Gene3D; 3.30.497.10; -; 1.
DR InterPro; IPR023796; Serpin_dom.
DR InterPro; IPR000215; Serpin_fam.
DR InterPro; IPR036186; Serpin_sf.
DR InterPro; IPR042178; Serpin_sf_1.
DR InterPro; IPR042185; Serpin_sf_2.
DR PANTHER; PTHR11461; PTHR11461; 1.
DR Pfam; PF00079; Serpin; 1.
DR SMART; SM00093; SERPIN; 1.
DR SUPFAM; SSF56574; SSF56574; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Protease inhibitor; Reference proteome; Secreted;
KW Serine protease inhibitor; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000250"
FT CHAIN 21..411
FT /note="Serpin A12"
FT /id="PRO_0000041978"
FT REGION 364..382
FT /note="Reactive center loop"
FT /evidence="ECO:0000250|UniProtKB:Q8IW75"
FT SITE 378..379
FT /note="Cleavage"
FT /evidence="ECO:0000250|UniProtKB:Q8IW75"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 267
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ 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
