Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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

GO - Biological processi

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
Proteomesi
  • UP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:18359. SERPINA12.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi365T → R: Fails to inhibit KLK7 activity. 1 Publication1
Mutagenesisi369A → P: Fails to inhibit KLK7 activity. 1 Publication1

Organism-specific databases

DisGeNETi145264.
OpenTargetsiENSG00000165953.
PharmGKBiPA134863157.

Polymorphism and mutation databases

BioMutaiSERPINA12.
DMDMi74728144.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20By similarityAdd BLAST20
ChainiPRO_000004197621 – 414Serpin A12Add BLAST394

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi221N-linked (GlcNAc...)Sequence analysis1
Glycosylationi233N-linked (GlcNAc...)Sequence analysis1
Glycosylationi267N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ8IW75.
PeptideAtlasiQ8IW75.
PRIDEiQ8IW75.
TopDownProteomicsiQ8IW75.

PTM databases

iPTMnetiQ8IW75.
PhosphoSitePlusiQ8IW75.

Expressioni

Tissue specificityi

Expressed in visceral adipose tissues.1 Publication

Gene expression databases

BgeeiENSG00000165953.
CleanExiHS_SERPINA12.
GenevisibleiQ8IW75. HS.

Interactioni

Subunit structurei

Forms a stable complex with KLK7.1 Publication

Protein-protein interaction databases

BioGridi126901. 39 interactors.
IntActiQ8IW75. 1 interactor.
STRINGi9606.ENSP00000342109.

Structurei

Secondary structure

1414
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi39 – 66Combined sources28
Beta strandi72 – 74Combined sources3
Helixi76 – 86Combined sources11
Turni87 – 89Combined sources3
Helixi92 – 101Combined sources10
Beta strandi105 – 107Combined sources3
Helixi109 – 123Combined sources15
Beta strandi125 – 141Combined sources17
Helixi148 – 158Combined sources11
Beta strandi161 – 165Combined sources5
Helixi170 – 184Combined sources15
Turni185 – 187Combined sources3
Beta strandi202 – 212Combined sources11
Beta strandi214 – 216Combined sources3
Helixi220 – 222Combined sources3
Beta strandi224 – 233Combined sources10
Beta strandi235 – 252Combined sources18
Turni253 – 256Combined sources4
Beta strandi257 – 275Combined sources19
Helixi280 – 286Combined sources7
Helixi289 – 297Combined sources9
Beta strandi300 – 309Combined sources10
Beta strandi311 – 318Combined sources8
Helixi319 – 322Combined sources4
Helixi323 – 326Combined sources4
Helixi330 – 332Combined sources3
Turni339 – 341Combined sources3
Beta strandi351 – 360Combined sources10
Beta strandi362 – 376Combined sources15
Beta strandi382 – 385Combined sources4
Beta strandi390 – 396Combined sources7
Turni397 – 400Combined sources4
Beta strandi401 – 409Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4IF8X-ray2.08A/B22-414[»]
4Y3KX-ray2.20A/B22-414[»]
4Y40X-ray2.20A/B22-414[»]
5EI0X-ray2.50A/E22-414[»]
ProteinModelPortaliQ8IW75.
SMRiQ8IW75.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni364 – 382RCLAdd BLAST19

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.
InParanoidiQ8IW75.
KOiK04525.
OMAiYIFFRAR.
OrthoDBiEOG091G0ION.
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)DescriptionActionsGraphical viewLength
Natural variantiVAR_051943142Q → K.Corresponds to variant rs17090972dbSNPEnsembl.1
Natural variantiVAR_051944394I → V.Corresponds to variant rs34519784dbSNPEnsembl.1

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_001291390.1. NM_001304461.1.
NP_776249.1. NM_173850.3.
XP_011534753.1. XM_011536451.2.
XP_011534754.1. XM_011536452.2.
XP_011534755.1. XM_011536453.2.
XP_011534756.1. XM_011536454.2.
XP_016876478.1. XM_017020989.1.
XP_016876479.1. XM_017020990.1.
UniGeneiHs.99476.

Genome annotation databases

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

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_001291390.1. NM_001304461.1.
NP_776249.1. NM_173850.3.
XP_011534753.1. XM_011536451.2.
XP_011534754.1. XM_011536452.2.
XP_011534755.1. XM_011536453.2.
XP_011534756.1. XM_011536454.2.
XP_016876478.1. XM_017020989.1.
XP_016876479.1. XM_017020990.1.
UniGeneiHs.99476.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4IF8X-ray2.08A/B22-414[»]
4Y3KX-ray2.20A/B22-414[»]
4Y40X-ray2.20A/B22-414[»]
5EI0X-ray2.50A/E22-414[»]
ProteinModelPortaliQ8IW75.
SMRiQ8IW75.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi126901. 39 interactors.
IntActiQ8IW75. 1 interactor.
STRINGi9606.ENSP00000342109.

Protein family/group databases

MEROPSiI04.091.

PTM databases

iPTMnetiQ8IW75.
PhosphoSitePlusiQ8IW75.

Polymorphism and mutation databases

BioMutaiSERPINA12.
DMDMi74728144.

Proteomic databases

PaxDbiQ8IW75.
PeptideAtlasiQ8IW75.
PRIDEiQ8IW75.
TopDownProteomicsiQ8IW75.

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.
DisGeNETi145264.
GeneCardsiSERPINA12.
HGNCiHGNC:18359. SERPINA12.
neXtProtiNX_Q8IW75.
OpenTargetsiENSG00000165953.
PharmGKBiPA134863157.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2392. Eukaryota.
COG4826. LUCA.
GeneTreeiENSGT00760000118839.
HOGENOMiHOG000238521.
HOVERGENiHBG005957.
InParanoidiQ8IW75.
KOiK04525.
OMAiYIFFRAR.
OrthoDBiEOG091G0ION.
PhylomeDBiQ8IW75.
TreeFamiTF343201.

Miscellaneous databases

GenomeRNAii145264.
PROiQ8IW75.

Gene expression databases

BgeeiENSG00000165953.
CleanExiHS_SERPINA12.
GenevisibleiQ8IW75. HS.

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...

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: November 2, 2016
This is version 115 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

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.