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Protein

Serpin A12

Gene

SERPINA12

Organism
Homo sapiens (Human)
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.1 Publication

GO - Molecular functioni

  1. serine-type endopeptidase inhibitor activity Source: GO_Central

GO - Biological processi

  1. negative regulation of endopeptidase activity Source: GO_Central
  2. negative regulation of gluconeogenesis Source: Ensembl
  3. negative regulation of lipid biosynthetic process Source: Ensembl
  4. positive regulation of insulin receptor signaling pathway Source: Ensembl
  5. positive regulation of phosphatidylinositol 3-kinase signaling Source: Ensembl
  6. regulation of cholesterol metabolic process Source: Ensembl
  7. regulation of triglyceride metabolic process Source: Ensembl
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):
OL-64
Visceral adipose tissue-derived serine protease inhibitor
Short name:
Vaspin
Visceral adipose-specific serpin
Gene namesi
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:18359. SERPINA12.

Subcellular locationi

GO - Cellular componenti

  1. extracellular space Source: GO_Central
  2. plasma membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi365 – 3651T → R: Fails to inhibit KLK7 activity. 1 Publication
Mutagenesisi369 – 3691A → P: Fails to inhibit KLK7 activity. 1 Publication

Organism-specific databases

PharmGKBiPA134863157.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020By similarityAdd
BLAST
Chaini21 – 414394Serpin A12PRO_0000041976Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi221 – 2211N-linked (GlcNAc...)Sequence Analysis
Glycosylationi233 – 2331N-linked (GlcNAc...)Sequence Analysis
Glycosylationi267 – 2671N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ8IW75.
PRIDEiQ8IW75.

PTM databases

PhosphoSiteiQ8IW75.

Expressioni

Tissue specificityi

Expressed in visceral adipose tissues.1 Publication

Gene expression databases

BgeeiQ8IW75.
CleanExiHS_SERPINA12.
GenevestigatoriQ8IW75.

Interactioni

Subunit structurei

Forms a stable complex with KLK7.1 Publication

Protein-protein interaction databases

BioGridi126901. 13 interactions.
IntActiQ8IW75. 1 interaction.
STRINGi9606.ENSP00000342109.

Structurei

Secondary structure

1
414
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi39 – 6628Combined sources
Beta strandi72 – 743Combined sources
Helixi76 – 8611Combined sources
Turni87 – 893Combined sources
Helixi92 – 10110Combined sources
Helixi109 – 12315Combined sources
Beta strandi125 – 14117Combined sources
Helixi148 – 15811Combined sources
Beta strandi161 – 1655Combined sources
Helixi170 – 18415Combined sources
Turni185 – 1873Combined sources
Beta strandi202 – 21211Combined sources
Beta strandi214 – 2163Combined sources
Helixi220 – 2223Combined sources
Beta strandi224 – 23310Combined sources
Beta strandi235 – 25218Combined sources
Turni253 – 2564Combined sources
Beta strandi257 – 27519Combined sources
Helixi280 – 2867Combined sources
Helixi289 – 2979Combined sources
Beta strandi300 – 30910Combined sources
Beta strandi311 – 3188Combined sources
Helixi319 – 3224Combined sources
Helixi323 – 3264Combined sources
Helixi330 – 3323Combined sources
Turni339 – 3413Combined sources
Beta strandi351 – 36010Combined sources
Beta strandi382 – 3854Combined sources
Beta strandi390 – 3967Combined sources
Turni397 – 4004Combined sources
Beta strandi401 – 4099Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4IF8X-ray2.08A/B22-414[»]
ProteinModelPortaliQ8IW75.
SMRiQ8IW75. Positions 37-414.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni364 – 38219RCLAdd
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

eggNOGiCOG4826.
GeneTreeiENSGT00760000118839.
HOGENOMiHOG000238521.
HOVERGENiHBG005957.
InParanoidiQ8IW75.
OMAiYIFFRAR.
OrthoDBiEOG7QC7W9.
PhylomeDBiQ8IW75.
TreeFamiTF343201.

Family and domain databases

InterProiIPR023796. 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.

Sequencei

Sequence statusi: Complete.

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

Q8IW75-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNPTLGLAIF LAVLLTVKGL LKPSFSPRNY KALSEVQGWK QRMAAKELAR
60 70 80 90 100
QNMDLGFKLL KKLAFYNPGR NIFLSPLSIS TAFSMLCLGA QDSTLDEIKQ
110 120 130 140 150
GFNFRKMPEK DLHEGFHYII HELTQKTQDL KLSIGNTLFI DQRLQPQRKF
160 170 180 190 200
LEDAKNFYSA ETILTNFQNL EMAQKQINDF ISQKTHGKIN NLIENIDPGT
210 220 230 240 250
VMLLANYIFF RARWKHEFDP NVTKEEDFFL EKNSSVKVPM MFRSGIYQVG
260 270 280 290 300
YDDKLSCTIL EIPYQKNITA IFILPDEGKL KHLEKGLQVD TFSRWKTLLS
310 320 330 340 350
RRVVDVSVPR LHMTGTFDLK KTLSYIGVSK IFEEHGDLTK IAPHRSLKVG
360 370 380 390 400
EAVHKAELKM DERGTEGAAG TGAQTLPMET PLVVKIDKPY LLLIYSEKIP
410
SVLFLGKIVN PIGK
Length:414
Mass (Da):47,175
Last modified:March 1, 2003 - v1
Checksum:i5C70F1AB5935661C
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti142 – 1421Q → K.
Corresponds to variant rs17090972 [ dbSNP | Ensembl ].
VAR_051943
Natural varianti394 – 3941I → V.
Corresponds to variant rs34519784 [ dbSNP | Ensembl ].
VAR_051944

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY326420 mRNA. Translation: AAP88384.1.
AY177692 mRNA. Translation: AAO18649.1.
BC040857 mRNA. Translation: AAH40857.1.
CCDSiCCDS9926.1.
RefSeqiNP_776249.1. NM_173850.2.
XP_005267408.1. XM_005267351.1.
UniGeneiHs.99476.

Genome annotation databases

EnsembliENST00000341228; ENSP00000342109; ENSG00000165953.
ENST00000556881; ENSP00000451738; ENSG00000165953.
GeneIDi145264.
KEGGihsa:145264.
UCSCiuc001ydj.3. human.

Polymorphism databases

DMDMi74728144.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY326420 mRNA. Translation: AAP88384.1.
AY177692 mRNA. Translation: AAO18649.1.
BC040857 mRNA. Translation: AAH40857.1.
CCDSiCCDS9926.1.
RefSeqiNP_776249.1. NM_173850.2.
XP_005267408.1. XM_005267351.1.
UniGeneiHs.99476.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4IF8X-ray2.08A/B22-414[»]
ProteinModelPortaliQ8IW75.
SMRiQ8IW75. Positions 37-414.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi126901. 13 interactions.
IntActiQ8IW75. 1 interaction.
STRINGi9606.ENSP00000342109.

Protein family/group databases

MEROPSiI04.091.

PTM databases

PhosphoSiteiQ8IW75.

Polymorphism databases

DMDMi74728144.

Proteomic databases

PaxDbiQ8IW75.
PRIDEiQ8IW75.

Protocols and materials databases

DNASUi145264.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000341228; ENSP00000342109; ENSG00000165953.
ENST00000556881; ENSP00000451738; ENSG00000165953.
GeneIDi145264.
KEGGihsa:145264.
UCSCiuc001ydj.3. human.

Organism-specific databases

CTDi145264.
GeneCardsiGC14M094954.
HGNCiHGNC:18359. SERPINA12.
neXtProtiNX_Q8IW75.
PharmGKBiPA134863157.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG4826.
GeneTreeiENSGT00760000118839.
HOGENOMiHOG000238521.
HOVERGENiHBG005957.
InParanoidiQ8IW75.
OMAiYIFFRAR.
OrthoDBiEOG7QC7W9.
PhylomeDBiQ8IW75.
TreeFamiTF343201.

Miscellaneous databases

GenomeRNAii145264.
NextBioi85065.
PROiQ8IW75.

Gene expression databases

BgeeiQ8IW75.
CleanExiHS_SERPINA12.
GenevestigatoriQ8IW75.

Family and domain databases

InterProiIPR023796. 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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
  2. Chen S., Guo J.H., Yu L.
    Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Heart.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Skin.
  4. Cited for: X-RAY CRYSTALLOGRAPHY (2.08 ANGSTROMS) OF 22-414, MUTAGENESIS OF THR-365 AND ALA-369, SUBUNIT.

Entry informationi

Entry nameiSPA12_HUMAN
AccessioniPrimary (citable) accession number: Q8IW75
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 27, 2005
Last sequence update: March 1, 2003
Last modified: March 4, 2015
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.