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Protein

Serpin A12

Gene

Serpina12

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Adipokine that modulates insulin action by specifically inhibiting its target protease KLK7 in white adipose tissues.2 Publications

GO - Molecular functioni

GO - Biological processi

  • glucose metabolic process Source: Ensembl
  • negative regulation of gluconeogenesis Source: MGI
  • negative regulation of lipid biosynthetic process Source: MGI
  • positive regulation of insulin receptor signaling pathway Source: MGI
  • positive regulation of phosphatidylinositol 3-kinase signaling Source: MGI
  • regulation of cholesterol metabolic process Source: MGI
  • regulation of triglyceride metabolic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Protease inhibitor, Serine protease inhibitor

Protein family/group databases

MEROPSiI04.091.

Names & Taxonomyi

Protein namesi
Recommended name:
Serpin A12
Alternative name(s):
Visceral adipose tissue-derived serine protease inhibitor
Short name:
Vaspin
Visceral adipose-specific serpin
Gene namesi
Name:Serpina12
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 12

Organism-specific databases

MGIiMGI:1915304. Serpina12.

Subcellular locationi

GO - Cellular componenti

  • extracellular space Source: MGI
  • plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 20201 PublicationAdd
BLAST
Chaini21 – 413393Serpin A12PRO_0000041977Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi92 – 921N-linked (GlcNAc...)Sequence analysis
Glycosylationi267 – 2671N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ7TMF5.
PRIDEiQ7TMF5.

PTM databases

PhosphoSiteiQ7TMF5.

Expressioni

Tissue specificityi

Expressed in visceral adipose tissues.1 Publication

Gene expression databases

BgeeiQ7TMF5.
GenevisibleiQ7TMF5. MM.

Interactioni

Subunit structurei

Forms a stable complex with KLK7.By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000045572.

Structurei

3D structure databases

ProteinModelPortaliQ7TMF5.
SMRiQ7TMF5. Positions 37-413.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni364 – 38219RCLBy similarityAdd
BLAST

Domaini

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).By similarity

Sequence similaritiesi

Belongs to the serpin family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG2392. Eukaryota.
COG4826. LUCA.
GeneTreeiENSGT00760000118839.
HOGENOMiHOG000238521.
HOVERGENiHBG005957.
InParanoidiQ7TMF5.
KOiK04525.
OMAiYISQKTH.
OrthoDBiEOG7QC7W9.
PhylomeDBiQ7TMF5.
TreeFamiTF343201.

Family and domain databases

InterProiIPR023795. Serpin_CS.
IPR023796. Serpin_dom.
IPR000215. Serpin_fam.
[Graphical view]
PANTHERiPTHR11461. PTHR11461. 1 hit.
PfamiPF00079. Serpin. 1 hit.
[Graphical view]
SMARTiSM00093. SERPIN. 1 hit.
[Graphical view]
SUPFAMiSSF56574. SSF56574. 1 hit.
PROSITEiPS00284. SERPIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q7TMF5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTRMLDLGLF LAGLLTVKGL LQDRDAPDMY DSPVRVQEWR GKKDARQLAR
60 70 80 90 100
HNMEFGFKLL QRLASNSPQG NIFLSPLSIS TAFSMLSLGA QNSTLEEIRE
110 120 130 140 150
GFNFKEMSNW DVHAAFHYLL HKLNQETEDT KMNLGNALFM DQKLRPQQRF
160 170 180 190 200
LNLAKNVYDA DMVLTNFQDL ENTQKDINRY ISQKTHSRIK NMVKSIDPGT
210 220 230 240 250
VMILTNYIYF RGRWQYEFDP KQTKEEEFFI EKGKTVKVPM MFQRGLYDMA
260 270 280 290 300
YDSQLSCTIL EIPYRGNITA TFVLPDNGKL KLLEQGLQAD IFAKWKSLLS
310 320 330 340 350
KRVVDVWVPK LRISSTYNMK KVLSRLGISK IFEENGDLTR ISSHRSLKVG
360 370 380 390 400
EAVHKAELKM DEKGMEGAAG SGAQTLPMET PRHMKLDRPF LMMIYENFMP
410
SMVFLARIYD PSG
Length:413
Mass (Da):47,634
Last modified:September 27, 2005 - v2
Checksum:iD0AE8E1EE24FD60A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti69 – 691Q → R in AAP88383 (PubMed:16030142).Curated
Sequence conflicti110 – 1101W → R in AAP88383 (PubMed:16030142).Curated
Sequence conflicti183 – 1831Q → R in AAP88383 (PubMed:16030142).Curated
Sequence conflicti403 – 4031V → I in AAP88383 (PubMed:16030142).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY326419 mRNA. Translation: AAP88383.1.
AK014346 mRNA. Translation: BAB29287.1.
AK014589 mRNA. Translation: BAB29447.1.
CCDSiCCDS26145.1.
RefSeqiNP_080811.1. NM_026535.2.
UniGeneiMm.20286.

Genome annotation databases

EnsembliENSMUST00000043915; ENSMUSP00000045572; ENSMUSG00000041567.
GeneIDi68054.
KEGGimmu:68054.
UCSCiuc007owp.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY326419 mRNA. Translation: AAP88383.1.
AK014346 mRNA. Translation: BAB29287.1.
AK014589 mRNA. Translation: BAB29447.1.
CCDSiCCDS26145.1.
RefSeqiNP_080811.1. NM_026535.2.
UniGeneiMm.20286.

3D structure databases

ProteinModelPortaliQ7TMF5.
SMRiQ7TMF5. Positions 37-413.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000045572.

Protein family/group databases

MEROPSiI04.091.

PTM databases

PhosphoSiteiQ7TMF5.

Proteomic databases

PaxDbiQ7TMF5.
PRIDEiQ7TMF5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000043915; ENSMUSP00000045572; ENSMUSG00000041567.
GeneIDi68054.
KEGGimmu:68054.
UCSCiuc007owp.1. mouse.

Organism-specific databases

CTDi145264.
MGIiMGI:1915304. Serpina12.

Phylogenomic databases

eggNOGiKOG2392. Eukaryota.
COG4826. LUCA.
GeneTreeiENSGT00760000118839.
HOGENOMiHOG000238521.
HOVERGENiHBG005957.
InParanoidiQ7TMF5.
KOiK04525.
OMAiYISQKTH.
OrthoDBiEOG7QC7W9.
PhylomeDBiQ7TMF5.
TreeFamiTF343201.

Miscellaneous databases

ChiTaRSiSerpina12. mouse.
PROiQ7TMF5.
SOURCEiSearch...

Gene expression databases

BgeeiQ7TMF5.
GenevisibleiQ7TMF5. MM.

Family and domain databases

InterProiIPR023795. Serpin_CS.
IPR023796. Serpin_dom.
IPR000215. Serpin_fam.
[Graphical view]
PANTHERiPTHR11461. PTHR11461. 1 hit.
PfamiPF00079. Serpin. 1 hit.
[Graphical view]
SMARTiSM00093. SERPIN. 1 hit.
[Graphical view]
SUPFAMiSSF56574. SSF56574. 1 hit.
PROSITEiPS00284. SERPIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, PROTEIN SEQUENCE OF N-TERMINUS, TISSUE SPECIFICITY.
    Strain: Swiss Webster.
  2. "The transcriptional landscape of the mammalian genome."
    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.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Head and Skin.
  3. Cited for: FUNCTION, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiSPA12_MOUSE
AccessioniPrimary (citable) accession number: Q7TMF5
Secondary accession number(s): Q9CQ32
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 27, 2005
Last sequence update: September 27, 2005
Last modified: June 8, 2016
This is version 92 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.