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UniProtKB/Swiss-Prot entry Q7TMF5


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name SPA12_MOUSE
Primary accession number Q7TMF5
Secondary accession number Q9CQ32
Integrated into Swiss-Prot on September 27, 2005
Sequence was last modified on September 27, 2005 (Sequence version 2)
Annotations were last modified on    June 16, 2009 (Entry version 42)
Name and origin of the protein
Protein name Serpin A12 [Precursor]
Synonyms Visceral adipose tissue-derived serine protease inhibitor
Vaspin
Visceral adipose-specific serpin
Gene name
Name: Serpina12
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, PROTEIN SEQUENCE OF N-TERMINUS, AND TISSUE SPECIFICITY.
STRAIN=Swiss Webster;
DOI=10.1073/pnas.0504703102; PubMed=16030142 [NCBI, ExPASy, EBI, Israel, Japan]
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].
STRAIN=C57BL/6J;
TISSUE=Head, and Skin;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AY326419; AAP88383.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK014346; BAB29287.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK014589; BAB29447.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00131951; -.
RefSeq NP_080811.1; -.
UniGene Mm.20286
3D structure databases
HSSP P01008; 1ATH. [HSSP ENTRY / PDB]
ModBase Q7TMF5.
Protein family/group databases
MEROPS I04.965; -.
Organism-specific databases
MGI MGI:1915304; Serpina12.
Gene expression databases
ArrayExpress Q7TMF5; -.
Bgee Q7TMF5; -.
GermOnline ENSMUSG00000041567; Mus musculus.
Ontologies
GO
GO:0005576; Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-SubCell).
GO:0004867; Molecular function: serine-type endopeptidase inhibitor activity (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR000295; Prot_inh_Lserp2.
IPR000215; Protease_inhib_I4_serpin.
Graphical view of domain structure.
PANTHER PTHR11461; Prot_inh_serpin; 1.
Pfam PF00079; Serpin; 1.
Pfam graphical view of domain structure.
PRINTS PR00780; LEUSERPINII.
SMART SM00093; SERPIN; 1.
SMART graphical view of domain structure.
PROSITE PS00284; SERPIN; 1.
Proteomic databases
PRIDE Q7TMF5; -.
Genome annotation databases
Ensembl ENSMUSG00000041567; Mus musculus. [Contig view]
GeneID 68054; -.
KEGG mmu:68054; -.
Phylogenomic databases
HOGENOM Q7TMF5; -.
HOVERGEN Q7TMF5; -.
OMA Q7TMF5; AQTLPME.
Other
NextBio 326328; -.
SOURCE Serpina12; Mus musculus.
ProtoNet Q7TMF5.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Direct protein sequencing; Glycoprotein; Protease inhibitor; Secreted; Serine protease inhibitor; Signal.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
SIGNAL   1    20  20      
CHAIN   21   413  393     Serpin A12. PRO_0000041977
CARBOHYD   92    92        N-linked (GlcNAc...) (Potential). 
CARBOHYD   267   267        N-linked (GlcNAc...) (Potential). 
CONFLICT   69    69        Q -> R (in Ref. 1; AAP88383). 
CONFLICT   110   110        W -> R (in Ref. 1; AAP88383). 
CONFLICT   183   183        Q -> R (in Ref. 1; AAP88383). 
CONFLICT   403   403        V -> I (in Ref. 1; AAP88383). 
Sequence information
Length: 413 AA [This is the length of the unprocessed precursor] Molecular weight: 47634 Da [This is the MW of the unprocessed precursor] CRC64: D0AE8E1EE24FD60A [This is a checksum on the sequence]
        10         20         30         40         50         60 
MTRMLDLGLF LAGLLTVKGL LQDRDAPDMY DSPVRVQEWR GKKDARQLAR HNMEFGFKLL 

        70         80         90        100        110        120 
QRLASNSPQG NIFLSPLSIS TAFSMLSLGA QNSTLEEIRE GFNFKEMSNW DVHAAFHYLL 

       130        140        150        160        170        180 
HKLNQETEDT KMNLGNALFM DQKLRPQQRF LNLAKNVYDA DMVLTNFQDL ENTQKDINRY 

       190        200        210        220        230        240 
ISQKTHSRIK NMVKSIDPGT VMILTNYIYF RGRWQYEFDP KQTKEEEFFI EKGKTVKVPM 

       250        260        270        280        290        300 
MFQRGLYDMA YDSQLSCTIL EIPYRGNITA TFVLPDNGKL KLLEQGLQAD IFAKWKSLLS 

       310        320        330        340        350        360 
KRVVDVWVPK LRISSTYNMK KVLSRLGISK IFEENGDLTR ISSHRSLKVG EAVHKAELKM 

       370        380        390        400        410 
DEKGMEGAAG SGAQTLPMET PRHMKLDRPF LMMIYENFMP SMVFLARIYD PSG 

Q7TMF5 in FASTA format

View entry in raw text format (no links)
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