Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q8IW75

- SPA12_HUMAN

UniProt

Q8IW75 - SPA12_HUMAN

Protein

Serpin A12

Gene

SERPINA12

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 95 (01 Oct 2014)
      Sequence version 1 (01 Mar 2003)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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: RefGenome

    GO - Biological processi

    1. negative regulation of endopeptidase activity Source: RefGenome
    2. regulation of proteolysis Source: RefGenome

    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: InterPro

    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. 2 interactions.
    IntActiQ8IW75. 1 interaction.
    STRINGi9606.ENSP00000342109.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    HOGENOMiHOG000238521.
    HOVERGENiHBG005957.
    InParanoidiQ8IW75.
    OMAiIFFRARW.
    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

    MNPTLGLAIF LAVLLTVKGL LKPSFSPRNY KALSEVQGWK QRMAAKELAR    50
    QNMDLGFKLL KKLAFYNPGR NIFLSPLSIS TAFSMLCLGA QDSTLDEIKQ 100
    GFNFRKMPEK DLHEGFHYII HELTQKTQDL KLSIGNTLFI DQRLQPQRKF 150
    LEDAKNFYSA ETILTNFQNL EMAQKQINDF ISQKTHGKIN NLIENIDPGT 200
    VMLLANYIFF RARWKHEFDP NVTKEEDFFL EKNSSVKVPM MFRSGIYQVG 250
    YDDKLSCTIL EIPYQKNITA IFILPDEGKL KHLEKGLQVD TFSRWKTLLS 300
    RRVVDVSVPR LHMTGTFDLK KTLSYIGVSK IFEEHGDLTK IAPHRSLKVG 350
    EAVHKAELKM DERGTEGAAG TGAQTLPMET PLVVKIDKPY LLLIYSEKIP 400
    SVLFLGKIVN PIGK 414
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY326420 mRNA. Translation: AAP88384.1 .
    AY177692 mRNA. Translation: AAO18649.1 .
    BC040857 mRNA. Translation: AAH40857.1 .
    CCDSi CCDS9926.1.
    RefSeqi NP_776249.1. NM_173850.2.
    XP_005267408.1. XM_005267351.1.
    UniGenei Hs.99476.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4IF8 X-ray 2.08 A/B 22-414 [» ]
    ProteinModelPortali Q8IW75.
    SMRi Q8IW75. Positions 37-414.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 126901. 2 interactions.
    IntActi Q8IW75. 1 interaction.
    STRINGi 9606.ENSP00000342109.

    Protein family/group databases

    MEROPSi I04.091.

    PTM databases

    PhosphoSitei Q8IW75.

    Polymorphism databases

    DMDMi 74728144.

    Proteomic databases

    PaxDbi Q8IW75.
    PRIDEi Q8IW75.

    Protocols and materials databases

    DNASUi 145264.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000341228 ; ENSP00000342109 ; ENSG00000165953 .
    ENST00000556881 ; ENSP00000451738 ; ENSG00000165953 .
    GeneIDi 145264.
    KEGGi hsa:145264.
    UCSCi uc001ydj.3. human.

    Organism-specific databases

    CTDi 145264.
    GeneCardsi GC14M094954.
    HGNCi HGNC:18359. SERPINA12.
    neXtProti NX_Q8IW75.
    PharmGKBi PA134863157.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG4826.
    HOGENOMi HOG000238521.
    HOVERGENi HBG005957.
    InParanoidi Q8IW75.
    OMAi IFFRARW.
    OrthoDBi EOG7QC7W9.
    PhylomeDBi Q8IW75.
    TreeFami TF343201.

    Miscellaneous databases

    GenomeRNAii 145264.
    NextBioi 85065.
    PROi Q8IW75.

    Gene expression databases

    Bgeei Q8IW75.
    CleanExi HS_SERPINA12.
    Genevestigatori Q8IW75.

    Family and domain databases

    InterProi IPR023796. Serpin_dom.
    IPR000215. Serpin_fam.
    [Graphical view ]
    PANTHERi PTHR11461. PTHR11461. 1 hit.
    Pfami PF00079. Serpin. 1 hit.
    [Graphical view ]
    SMARTi SM00093. SERPIN. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56574. SSF56574. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 95 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