ID   SPA12_MOUSE             Reviewed;         413 AA.
AC   Q7TMF5; Q9CQ32;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 2.
DT   16-NOV-2011, entry version 62.
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   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, PROTEIN SEQUENCE OF N-TERMINUS,
RP   AND TISSUE SPECIFICITY.
RC   STRAIN=Swiss Webster;
RX   PubMed=16030142; DOI=10.1073/pnas.0504703102;
RA   Hida K., Wada J., Eguchi J., Zhang H., Baba M., Seida A.,
RA   Hashimoto I., Okada T., Yasuhara A., Nakatsuka A., Shikata K.,
RA   Hourai S., Futami J., Watanabe E., Matsuki Y., Hiramatsu R., Akagi S.,
RA   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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Head, and Skin;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: May modulates insulin action conceivably only in the
CC       presence of its yet undefined target proteases in white adipose
CC       tissues.
CC   -!- SUBCELLULAR LOCATION: Secreted (Potential).
CC   -!- TISSUE SPECIFICITY: Expressed in visceral adipose tissues.
CC   -!- SIMILARITY: Belongs to the serpin family.
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DR   EMBL; AY326419; AAP88383.1; -; mRNA.
DR   EMBL; AK014346; BAB29287.1; -; mRNA.
DR   EMBL; AK014589; BAB29447.1; -; mRNA.
DR   IPI; IPI00131951; -.
DR   RefSeq; NP_080811.1; NM_026535.2.
DR   UniGene; Mm.20286; -.
DR   ProteinModelPortal; Q7TMF5; -.
DR   SMR; Q7TMF5; 44-412.
DR   STRING; Q7TMF5; -.
DR   MEROPS; I04.965; -.
DR   PhosphoSite; Q7TMF5; -.
DR   PRIDE; Q7TMF5; -.
DR   Ensembl; ENSMUST00000043915; ENSMUSP00000045572; ENSMUSG00000041567.
DR   GeneID; 68054; -.
DR   KEGG; mmu:68054; -.
DR   UCSC; uc007owp.1; mouse.
DR   CTD; 145264; -.
DR   MGI; MGI:1915304; Serpina12.
DR   GeneTree; ENSGT00560000076583; -.
DR   HOGENOM; HBG714743; -.
DR   HOVERGEN; HBG005957; -.
DR   InParanoid; Q7TMF5; -.
DR   OMA; PMMYRGG; -.
DR   OrthoDB; EOG4CG088; -.
DR   PhylomeDB; Q7TMF5; -.
DR   NextBio; 326328; -.
DR   ArrayExpress; Q7TMF5; -.
DR   Bgee; Q7TMF5; -.
DR   Genevestigator; Q7TMF5; -.
DR   GermOnline; ENSMUSG00000041567; Mus musculus.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IBA:RefGenome.
DR   GO; GO:0030162; P:regulation of proteolysis; IBA:RefGenome.
DR   InterPro; IPR000295; Prot_inh_Lserp2.
DR   InterPro; IPR000215; Protease_inhib_I4_serpin.
DR   InterPro; IPR023795; Protease_inhib_I4_serpin_CS.
DR   InterPro; IPR023796; Sepin_dom.
DR   PANTHER; PTHR11461; Prot_inh_serpin; 1.
DR   Pfam; PF00079; Serpin; 1.
DR   PRINTS; PR00780; LEUSERPINII.
DR   SMART; SM00093; SERPIN; 1.
DR   SUPFAM; SSF56574; Prot_inh_serpin; 1.
DR   PROSITE; PS00284; SERPIN; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Direct protein sequencing; Glycoprotein;
KW   Protease inhibitor; Reference proteome; Secreted;
KW   Serine protease inhibitor; Signal.
FT   SIGNAL        1     20
FT   CHAIN        21    413       Serpin A12.
FT                                /FTId=PRO_0000041977.
FT   CARBOHYD     92     92       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    267    267       N-linked (GlcNAc...) (Potential).
FT   CONFLICT     69     69       Q -> R (in Ref. 1; AAP88383).
FT   CONFLICT    110    110       W -> R (in Ref. 1; AAP88383).
FT   CONFLICT    183    183       Q -> R (in Ref. 1; AAP88383).
FT   CONFLICT    403    403       V -> I (in Ref. 1; AAP88383).
SQ   SEQUENCE   413 AA;  47634 MW;  D0AE8E1EE24FD60A CRC64;
     MTRMLDLGLF LAGLLTVKGL LQDRDAPDMY DSPVRVQEWR GKKDARQLAR HNMEFGFKLL
     QRLASNSPQG NIFLSPLSIS TAFSMLSLGA QNSTLEEIRE GFNFKEMSNW DVHAAFHYLL
     HKLNQETEDT KMNLGNALFM DQKLRPQQRF LNLAKNVYDA DMVLTNFQDL ENTQKDINRY
     ISQKTHSRIK NMVKSIDPGT VMILTNYIYF RGRWQYEFDP KQTKEEEFFI EKGKTVKVPM
     MFQRGLYDMA YDSQLSCTIL EIPYRGNITA TFVLPDNGKL KLLEQGLQAD IFAKWKSLLS
     KRVVDVWVPK LRISSTYNMK KVLSRLGISK IFEENGDLTR ISSHRSLKVG EAVHKAELKM
     DEKGMEGAAG SGAQTLPMET PRHMKLDRPF LMMIYENFMP SMVFLARIYD PSG
//