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Serpin A12 (OL-64) (Visceral adipose tissue-derived serine protease inhibitor) (Vaspin) (Visceral adipose-specific serpin)

 SPA12_HUMAN             Reviewed;         414 AA.
Q8IW75;
27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 1.
07-NOV-2018, entry version 125.
RecName: Full=Serpin A12;
AltName: Full=OL-64;
AltName: Full=Visceral adipose tissue-derived serine protease inhibitor;
Short=Vaspin;
AltName: Full=Visceral adipose-specific serpin;
Flags: Precursor;
Name=SERPINA12;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
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).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Heart;
Chen S., Guo J.H., Yu L.;
Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Skin;
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).
[4]
FUNCTION, ACTIVITY REGULATION, SUBCELLULAR LOCATION, GLYCOSYLATION AT
ASN-221; ASN-233 AND ASN-267, AND MUTAGENESIS OF ASN-221; ASN-233 AND
ASN-267.
PubMed=28668641; DOI=10.1016/j.bbapap.2017.06.020;
Oertwig K., Ulbricht D., Hanke S., Pippel J., Bellmann-Sickert K.,
Straeter N., Heiker J.T.;
"Glycosylation of human vaspin (SERPINA12) and its impact on serpin
activity, heparin binding and thermal stability.";
Biochim. Biophys. Acta 1865:1188-1194(2017).
[5]
X-RAY CRYSTALLOGRAPHY (2.08 ANGSTROMS) OF 22-414, FUNCTION, DOMAIN,
MUTAGENESIS OF THR-365 AND ALA-369, AND SUBUNIT.
PubMed=23370777; DOI=10.1007/s00018-013-1258-8;
Heiker J.T., Kloting N., Kovacs P., Kuettner E.B., Strater N.,
Schultz S., Kern M., Stumvoll M., Bluher M., Beck-Sickinger A.G.;
"Vaspin inhibits kallikrein 7 by serpin mechanism.";
Cell. Mol. Life Sci. 70:2569-2583(2013).
[6] {ECO:0000244|PDB:4Y3K, ECO:0000244|PDB:4Y40}
X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 22-414 OF MUTANTS CYS-305;
ALA-379 AND CYS-383, FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
PROPERTIES, DOMAIN, AND MUTAGENESIS OF ARG-302; ASP-305; GLU-379 AND
VAL-383.
PubMed=26199422; DOI=10.1042/BJ20150643;
Ulbricht D., Pippel J., Schultz S., Meier R., Strater N., Heiker J.T.;
"A unique serpin P1' glutamate and a conserved beta-sheet C arginine
are key residues for activity, protease recognition and stability of
serpinA12 (vaspin).";
Biochem. J. 470:357-367(2015).
[7] {ECO:0000244|PDB:5EI0}
X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 22-414, BIOPHYSICOCHEMICAL
PROPERTIES, DOMAIN, PROTEOLYTIC CLEAVAGE, AND MUTAGENESIS OF THR-365
AND ALA-369.
PubMed=26529565; DOI=10.1515/hsz-2015-0229;
Pippel J., Kuettner E.B., Ulbricht D., Daberger J., Schultz S.,
Heiker J.T., Strater N.;
"Crystal structure of cleaved vaspin (serpinA12).";
Biol. Chem. 397:111-123(2016).
[8]
VARIANT GLY-219.
PubMed=27693231; DOI=10.1016/j.ajhg.2016.08.020;
Parry D.A., Smith C.E., El-Sayed W., Poulter J.A., Shore R.C.,
Logan C.V., Mogi C., Sato K., Okajima F., Harada A., Zhang H.,
Koruyucu M., Seymen F., Hu J.C., Simmer J.P., Ahmed M., Jafri H.,
Johnson C.A., Inglehearn C.F., Mighell A.J.;
"Mutations in the pH-sensing G-protein-coupled receptor GPR68 cause
amelogenesis imperfecta.";
Am. J. Hum. Genet. 99:984-990(2016).
-!- FUNCTION: Adipokine that modulates insulin action by specifically
inhibiting its target protease KLK7 in white adipose tissues.
{ECO:0000269|PubMed:16030142, ECO:0000269|PubMed:23370777,
ECO:0000269|PubMed:26199422, ECO:0000269|PubMed:28668641}.
-!- ACTIVITY REGULATION: Inhibition of KLK7 is enhanced by heparin.
{ECO:0000269|PubMed:26199422, ECO:0000269|PubMed:28668641}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Temperature dependence:
Highly thermostable, with a Tm value of 70 degrees Celsius.
Incubation at 60 degrees Celsius for two hours has no apparent
effect on KLK7 inhibition activity. Polymerization is observed
at 70 degrees Celsius and above. {ECO:0000269|PubMed:26199422,
ECO:0000269|PubMed:26529565};
-!- SUBUNIT: Forms a stable complex with KLK7.
{ECO:0000269|PubMed:23370777}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:28668641}.
-!- TISSUE SPECIFICITY: Expressed in visceral adipose tissues.
{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.
{ECO:0000305|PubMed:23370777, ECO:0000305|PubMed:26199422,
ECO:0000305|PubMed:26529565}.
-!- PTM: Glycosylation slightly decreases affinity for heparin, but
otherwise has no significant effect on KLK7 inhibitory activity or
thermal stability of the protein. {ECO:0000269|PubMed:28668641}.
-!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AY326420; AAP88384.1; -; mRNA.
EMBL; AY177692; AAO18649.1; -; mRNA.
EMBL; BC040857; AAH40857.1; -; mRNA.
CCDS; CCDS9926.1; -.
RefSeq; NP_001291390.1; NM_001304461.1.
RefSeq; NP_776249.1; NM_173850.3.
RefSeq; XP_011534753.1; XM_011536451.2.
RefSeq; XP_011534754.1; XM_011536452.2.
RefSeq; XP_011534755.1; XM_011536453.2.
RefSeq; XP_011534756.1; XM_011536454.2.
RefSeq; XP_016876478.1; XM_017020989.1.
RefSeq; XP_016876479.1; XM_017020990.1.
UniGene; Hs.99476; -.
PDB; 4IF8; X-ray; 2.08 A; A/B=22-414.
PDB; 4Y3K; X-ray; 2.20 A; A/B=22-414.
PDB; 4Y40; X-ray; 2.20 A; A/B=22-414.
PDB; 5EI0; X-ray; 2.50 A; A/E=22-414.
PDBsum; 4IF8; -.
PDBsum; 4Y3K; -.
PDBsum; 4Y40; -.
PDBsum; 5EI0; -.
ProteinModelPortal; Q8IW75; -.
SMR; Q8IW75; -.
BioGrid; 126901; 48.
IntAct; Q8IW75; 1.
STRING; 9606.ENSP00000342109; -.
MEROPS; I04.091; -.
iPTMnet; Q8IW75; -.
PhosphoSitePlus; Q8IW75; -.
BioMuta; SERPINA12; -.
DMDM; 74728144; -.
PaxDb; Q8IW75; -.
PeptideAtlas; Q8IW75; -.
PRIDE; Q8IW75; -.
ProteomicsDB; 70821; -.
TopDownProteomics; Q8IW75; -.
DNASU; 145264; -.
Ensembl; ENST00000341228; ENSP00000342109; ENSG00000165953.
Ensembl; ENST00000556881; ENSP00000451738; ENSG00000165953.
GeneID; 145264; -.
KEGG; hsa:145264; -.
UCSC; uc001ydj.3; human.
CTD; 145264; -.
DisGeNET; 145264; -.
EuPathDB; HostDB:ENSG00000165953.9; -.
GeneCards; SERPINA12; -.
HGNC; HGNC:18359; SERPINA12.
MIM; 617471; gene.
neXtProt; NX_Q8IW75; -.
OpenTargets; ENSG00000165953; -.
PharmGKB; PA134863157; -.
eggNOG; KOG2392; Eukaryota.
eggNOG; COG4826; LUCA.
GeneTree; ENSGT00760000118839; -.
HOGENOM; HOG000238521; -.
HOVERGEN; HBG005957; -.
InParanoid; Q8IW75; -.
KO; K04525; -.
OMA; RWQHEFD; -.
OrthoDB; EOG091G0ION; -.
PhylomeDB; Q8IW75; -.
TreeFam; TF343201; -.
GenomeRNAi; 145264; -.
PRO; PR:Q8IW75; -.
Proteomes; UP000005640; Chromosome 14.
Bgee; ENSG00000165953; Expressed in 65 organ(s), highest expression level in skin of leg.
CleanEx; HS_SERPINA12; -.
Genevisible; Q8IW75; HS.
GO; GO:0005615; C:extracellular space; IBA:GO_Central.
GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IBA:GO_Central.
GO; GO:0010951; P:negative regulation of endopeptidase activity; IBA:GO_Central.
GO; GO:0045721; P:negative regulation of gluconeogenesis; IEA:Ensembl.
GO; GO:0051055; P:negative regulation of lipid biosynthetic process; IEA:Ensembl.
GO; GO:0046628; P:positive regulation of insulin receptor signaling pathway; IEA:Ensembl.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IEA:Ensembl.
GO; GO:0090181; P:regulation of cholesterol metabolic process; IEA:Ensembl.
GO; GO:0090207; P:regulation of triglyceride metabolic process; IEA:Ensembl.
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.
1: Evidence at protein level;
3D-structure; Complete proteome; Glycoprotein; Polymorphism;
Protease inhibitor; Reference proteome; Secreted;
Serine protease inhibitor; Signal.
SIGNAL 1 20 {ECO:0000250}.
CHAIN 21 414 Serpin A12.
/FTId=PRO_0000041976.
REGION 364 382 Reactive center loop.
{ECO:0000269|PubMed:26529565,
ECO:0000305|PubMed:23370777,
ECO:0000305|PubMed:26199422}.
SITE 378 379 Cleavage. {ECO:0000269|PubMed:26529565}.
CARBOHYD 221 221 N-linked (GlcNAc...) (complex)
asparagine.
{ECO:0000269|PubMed:28668641}.
CARBOHYD 233 233 N-linked (GlcNAc...) (complex)
asparagine.
{ECO:0000269|PubMed:28668641}.
CARBOHYD 267 267 N-linked (GlcNAc...) (high mannose)
asparagine.
{ECO:0000269|PubMed:28668641}.
VARIANT 142 142 Q -> K (in dbSNP:rs17090972).
/FTId=VAR_051943.
VARIANT 219 219 D -> G (in dbSNP:rs192558870).
{ECO:0000269|PubMed:27693231}.
/FTId=VAR_077875.
VARIANT 394 394 I -> V (in dbSNP:rs34519784).
/FTId=VAR_051944.
MUTAGEN 221 221 N->A: Reduced N-glycosylation. Loss of N-
glycosylation; when associated with A-233
and A-267. {ECO:0000269|PubMed:28668641}.
MUTAGEN 233 233 N->A: Reduced N-glycosylation. Loss of N-
glycosylation; when associated with A-221
and A-267. {ECO:0000269|PubMed:28668641}.
MUTAGEN 267 267 N->A: Reduced N-glycosylation. Loss of N-
glycosylation; when associated with A-221
and A-233. {ECO:0000269|PubMed:28668641}.
MUTAGEN 302 302 R->A,E: Significantly impairs KLK7
inhibition activity. Slightly enhances
KLK7 inhibition activity; when associated
with S-379.
{ECO:0000269|PubMed:26199422}.
MUTAGEN 305 305 D->C: Results in formation of an
artificial disulfide bond which
stabilizes the reactive center loop and
enhances KLK7 inhibition activity; when
associated with C-383.
{ECO:0000269|PubMed:26199422}.
MUTAGEN 365 365 T->R: Fails to inhibit KLK7 activity.
Increased protein stability in cleaved
form and conformational changes which may
allow escape of the substrate.
{ECO:0000269|PubMed:23370777,
ECO:0000269|PubMed:26529565}.
MUTAGEN 369 369 A->P: Fails to inhibit KLK7 activity.
Increased protein stability in cleaved
form and conformational changes which may
allow escape of the substrate.
{ECO:0000269|PubMed:23370777,
ECO:0000269|PubMed:26529565}.
MUTAGEN 379 379 E->S: Significantly enhances KLK7
inhibition activity. Slightly enhances
KLK7 inhibition activity; when associated
with E-302.
{ECO:0000269|PubMed:26199422}.
MUTAGEN 383 383 V->C: Results in formation of an
artificial disulfide bond which
stabilizes the reactive center loop and
enhances KLK7 inhibition activity; when
associated with C-305.
{ECO:0000269|PubMed:26199422}.
HELIX 39 66 {ECO:0000244|PDB:4IF8}.
STRAND 72 74 {ECO:0000244|PDB:4IF8}.
HELIX 76 86 {ECO:0000244|PDB:4IF8}.
TURN 87 89 {ECO:0000244|PDB:4IF8}.
HELIX 92 101 {ECO:0000244|PDB:4IF8}.
STRAND 105 107 {ECO:0000244|PDB:5EI0}.
HELIX 109 123 {ECO:0000244|PDB:4IF8}.
STRAND 125 141 {ECO:0000244|PDB:4IF8}.
HELIX 148 158 {ECO:0000244|PDB:4IF8}.
STRAND 161 165 {ECO:0000244|PDB:4IF8}.
HELIX 170 184 {ECO:0000244|PDB:4IF8}.
TURN 185 187 {ECO:0000244|PDB:4IF8}.
STRAND 202 212 {ECO:0000244|PDB:4IF8}.
STRAND 214 216 {ECO:0000244|PDB:4IF8}.
HELIX 220 222 {ECO:0000244|PDB:4IF8}.
STRAND 224 233 {ECO:0000244|PDB:4IF8}.
STRAND 235 252 {ECO:0000244|PDB:4IF8}.
TURN 253 256 {ECO:0000244|PDB:4IF8}.
STRAND 257 275 {ECO:0000244|PDB:4IF8}.
HELIX 280 286 {ECO:0000244|PDB:4IF8}.
HELIX 289 297 {ECO:0000244|PDB:4IF8}.
STRAND 300 309 {ECO:0000244|PDB:4IF8}.
STRAND 311 318 {ECO:0000244|PDB:4IF8}.
HELIX 319 322 {ECO:0000244|PDB:4IF8}.
HELIX 323 326 {ECO:0000244|PDB:4IF8}.
HELIX 330 332 {ECO:0000244|PDB:4IF8}.
TURN 339 341 {ECO:0000244|PDB:4IF8}.
STRAND 351 360 {ECO:0000244|PDB:4IF8}.
STRAND 362 376 {ECO:0000244|PDB:5EI0}.
STRAND 382 385 {ECO:0000244|PDB:4IF8}.
STRAND 390 396 {ECO:0000244|PDB:4IF8}.
TURN 397 400 {ECO:0000244|PDB:4IF8}.
STRAND 401 409 {ECO:0000244|PDB:4IF8}.
SEQUENCE 414 AA; 47175 MW; 5C70F1AB5935661C CRC64;
MNPTLGLAIF LAVLLTVKGL LKPSFSPRNY KALSEVQGWK QRMAAKELAR QNMDLGFKLL
KKLAFYNPGR NIFLSPLSIS TAFSMLCLGA QDSTLDEIKQ GFNFRKMPEK DLHEGFHYII
HELTQKTQDL KLSIGNTLFI DQRLQPQRKF LEDAKNFYSA ETILTNFQNL EMAQKQINDF
ISQKTHGKIN NLIENIDPGT VMLLANYIFF RARWKHEFDP NVTKEEDFFL EKNSSVKVPM
MFRSGIYQVG YDDKLSCTIL EIPYQKNITA IFILPDEGKL KHLEKGLQVD TFSRWKTLLS
RRVVDVSVPR LHMTGTFDLK KTLSYIGVSK IFEEHGDLTK IAPHRSLKVG EAVHKAELKM
DERGTEGAAG TGAQTLPMET PLVVKIDKPY LLLIYSEKIP SVLFLGKIVN PIGK


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