SERPINA12
entrez
145264
canonical
uniprot
Q8IW75
canonical
ensembl
ENSG00000165953
resolver
ensp
ENSP00000342109
resolver
ensp
ENSP00000451738
resolver
ensp
ENSP00000503935
resolver
ensp
ENSP00000531563
resolver
ensp
ENSP00000531564
resolver
enst
ENST00000341228
resolver
enst
ENST00000556881
resolver
enst
ENST00000677451
resolver
enst
ENST00000861504
resolver
enst
ENST00000861505
resolver
genesymbol
SERPINA12
resolver
hgnc
HGNC:18359
resolver
uniprot_entry
SPA12_HUMAN
resolver
activity_regulation
ACTIVITY REGULATION: Inhibition of KLK7 is enhanced by heparin. {ECO:0000269|PubMed:26199422, ECO:0000269|PubMed:28668641}.
uniprot
proteins
amino_acid_sequence
MNPTLGLAIFLAVLLTVKGLLKPSFSPRNYKALSEVQGWKQRMAAKELARQNMDLGFKLLKKLAFYNPGRNIFLSPLSISTAFSMLCLGAQDSTLDEIKQGFNFRKMPEKDLHEGFHYIIHELTQKTQDLKLSIGNTLFIDQRLQPQRKFLEDAKNFYSAETILTNFQNLEMAQKQINDFISQKTHGKINNLIENIDPGTVMLLANYIFFRARWKHEFDPNVTKEEDFFLEKNSSVKVPMMFRSGIYQVGYDDKLSCTILEIPYQKNITAIFILPDEGKLKHLEKGLQVDTFSRWKTLLSRRVVDVSVPRLHMTGTFDLKKTLSYIGVSKIFEEHGDLTKIAPHRSLKVGEAVHKAELKMDERGTEGAAGTGAQTLPMETPLVVKIDKPYLLLIYSEKIPSVLFLGKIVNPIGK
uniprot
proteins
function
FUNCTION: Adipokine that modulates insulin action by specifically inhibiting its target protease KLK7 in white adipose tissues. {ECO:0000269|PubMed:16030142, ECO:0000269|PubMed:23370777, ECO:0000269|PubMed:26199422, ECO:0000269|PubMed:28668641}.
uniprot
proteins
mass_dalton
47175
uniprot
proteins
mutagenesis
MUTAGEN 221; /note="N->A: Reduced N-glycosylation. Loss of N-glycosylation; when associated with A-233 and A-267."; /evidence="ECO:0000269|PubMed:28668641"; MUTAGEN 233; /note="N->A: Reduced N-glycosylation. Loss of N-glycosylation; when associated with A-221 and A-267."; /evidence="ECO:0000269|PubMed:28668641"; MUTAGEN 267; /note="N->A: Reduced N-glycosylation. Loss of N-glycosylation; when associated with A-221 and A-233."; /evidence="ECO:0000269|PubMed:28668641"; MUTAGEN 302; /note="R->A,E: Significantly impairs KLK7 inhibition activity. Slightly enhances KLK7 inhibition activity; when associated with S-379."; /evidence="ECO:0000269|PubMed:26199422"; MUTAGEN 305; /note="D->C: Results in formation of an artificial disulfide bond which stabilizes the reactive center loop and enhances KLK7 inhibition activity; when associated with C-383."; /evidence="ECO:0000269|PubMed:26199422"; MUTAGEN 365; /note="T->R: Fails to inhibit KLK7 activity. Increased protein stability in cleaved form and conformational changes which may allow escape of the substrate."; /evidence="ECO:0000269|PubMed:23370777, ECO:0000269|PubMed:26529565"; MUTAGEN 369; /note="A->P: Fails to inhibit KLK7 activity. Increased protein stability in cleaved form and conformational changes which may allow escape of the substrate."; /evidence="ECO:0000269|PubMed:23370777, ECO:0000269|PubMed:26529565"; MUTAGEN 379; /note="E->S: Significantly enhances KLK7 inhibition activity. Slightly enhances KLK7 inhibition activity; when associated with E-302."; /evidence="ECO:0000269|PubMed:26199422"; MUTAGEN 383; /note="V->C: Results in formation of an artificial disulfide bond which stabilizes the reactive center loop and enhances KLK7 inhibition activity; when associated with C-305."; /evidence="ECO:0000269|PubMed:26199422
uniprot
proteins
post_translational_modification
PTM: Glycosylation slightly decreases affinity for heparin, but otherwise has no significant effect on KLK7 inhibitory activity or thermal stability of the protein. {ECO:0000269|PubMed:28668641}.
uniprot
proteins
protein_family
Serpin family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16030142
uniprot
proteins
pubmed
23370777
uniprot
proteins
pubmed
26199422
uniprot
proteins
pubmed
26529565
uniprot
proteins
pubmed
27693231
uniprot
proteins
pubmed
28668641
uniprot
proteins
sequence_length
414
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:28668641}.
uniprot
proteins