SPA3C_MOUSE
ID SPA3C_MOUSE Reviewed; 417 AA.
AC P29621;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Serine protease inhibitor A3C;
DE Short=Serpin A3C;
DE AltName: Full=Kallikrein-binding protein;
DE Short=KBP;
DE Flags: Precursor;
GN Name=Serpina3c; Synonyms=Klkbp;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1756173; DOI=10.1016/0167-4781(91)90227-d;
RA Chai K.X., Chao J., Chao L.;
RT "Molecular cloning and sequence analysis of the mouse kallikrein-binding
RT protein gene.";
RL Biochim. Biophys. Acta 1129:127-130(1991).
RN [2]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=12659817; DOI=10.1016/s0888-7543(02)00041-1;
RA Forsyth S., Horvath A., Coughlin P.;
RT "A review and comparison of the murine alpha1-antitrypsin and alpha1-
RT antichymotrypsin multigene clusters with the human clade A serpins.";
RL Genomics 81:336-345(2003).
RN [3]
RP REGION RCL.
RX PubMed=15638460; DOI=10.1007/s00239-004-2640-9;
RA Horvath A.J., Forsyth S.L., Coughlin P.B.;
RT "Expression patterns of murine antichymotrypsin-like genes reflect
RT evolutionary divergence at the Serpina3 locus.";
RL J. Mol. Evol. 59:488-497(2004).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- DOMAIN: The reactive center loop (RCL) extends out from the body of the
CC protein and directs binding to the target protease. The protease
CC cleaves the serpin at the reactive site within the RCL, establishing a
CC covalent linkage between the serpin reactive site and the protease. The
CC resulting inactive serpin-protease complex is highly stable (By
CC similarity). Variability within the reactive center loop (RCL)
CC sequences of Serpina3 paralogs may determine target protease
CC specificity. {ECO:0000250}.
CC -!- MISCELLANEOUS: The single human alpha1-antichymotrypsin gene (SERPINA3)
CC is represented by a cluster of 14 individual murine paralogs.
CC -!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}.
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DR EMBL; X61597; CAA43794.1; -; Genomic_DNA.
DR CCDS; CCDS26148.1; -.
DR PIR; S15631; S15631.
DR PIR; S19724; S19724.
DR RefSeq; NP_032484.1; NM_008458.2.
DR AlphaFoldDB; P29621; -.
DR SMR; P29621; -.
DR BioGRID; 200987; 7.
DR STRING; 10090.ENSMUSP00000082125; -.
DR MEROPS; I04.053; -.
DR GlyGen; P29621; 5 sites.
DR iPTMnet; P29621; -.
DR PhosphoSitePlus; P29621; -.
DR CPTAC; non-CPTAC-3750; -.
DR CPTAC; non-CPTAC-3947; -.
DR jPOST; P29621; -.
DR MaxQB; P29621; -.
DR PaxDb; P29621; -.
DR PeptideAtlas; P29621; -.
DR PRIDE; P29621; -.
DR ProteomicsDB; 261558; -.
DR DNASU; 16625; -.
DR Ensembl; ENSMUST00000085050; ENSMUSP00000082125; ENSMUSG00000066361.
DR GeneID; 16625; -.
DR KEGG; mmu:16625; -.
DR UCSC; uc007owv.1; mouse.
DR CTD; 16625; -.
DR MGI; MGI:102848; Serpina3c.
DR VEuPathDB; HostDB:ENSMUSG00000066361; -.
DR eggNOG; KOG2392; Eukaryota.
DR GeneTree; ENSGT00940000154392; -.
DR HOGENOM; CLU_023330_2_1_1; -.
DR InParanoid; P29621; -.
DR OMA; SLQPRHI; -.
DR OrthoDB; 1124079at2759; -.
DR PhylomeDB; P29621; -.
DR TreeFam; TF343201; -.
DR BioGRID-ORCS; 16625; 3 hits in 75 CRISPR screens.
DR PRO; PR:P29621; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; P29621; protein.
DR Bgee; ENSMUSG00000066361; Expressed in epididymal fat pad and 65 other tissues.
DR Genevisible; P29621; MM.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IBA:GO_Central.
DR GO; GO:0010951; P:negative regulation of endopeptidase activity; IBA:GO_Central.
DR GO; GO:0034097; P:response to cytokine; IDA:MGI.
DR GO; GO:0043434; P:response to peptide hormone; IDA:MGI.
DR Gene3D; 2.30.39.10; -; 1.
DR Gene3D; 3.30.497.10; -; 1.
DR InterPro; IPR023796; Serpin_dom.
DR InterPro; IPR000215; Serpin_fam.
DR InterPro; IPR036186; Serpin_sf.
DR InterPro; IPR042178; Serpin_sf_1.
DR InterPro; IPR042185; Serpin_sf_2.
DR PANTHER; PTHR11461; PTHR11461; 1.
DR Pfam; PF00079; Serpin; 1.
DR SMART; SM00093; SERPIN; 1.
DR SUPFAM; SSF56574; SSF56574; 1.
DR PROSITE; PS00284; SERPIN; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Protease inhibitor; Reference proteome; Secreted;
KW Serine protease inhibitor; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..417
FT /note="Serine protease inhibitor A3C"
FT /id="PRO_0000032416"
FT REGION 367..392
FT /note="RCL"
FT SITE 381..382
FT /note="Reactive bond"
FT /evidence="ECO:0000250"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 269
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 390
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 417 AA; 46766 MW; 5486D39E2C5156E4 CRC64;
MAFIVALGLV ITGICPGVLC FPDGTLERDT LFHKDKENGT QLDSLTLASI NTDFAFSLYK
KLALKNPDTN IVFSPLSISA ALAIVSLGAK GNTLEEILEG LNFNLTETPE ADIHQGFGHL
LQRLSHPGEQ VQISTGSALF VEKHLQILAE FQEKARALYQ AEAFTADFQQ PLEATKLIND
YVSNQTQRKI KGLISDLDTD TLMVLVNYIY FKGKWKMPFN PRDTFESEFY LDVKRSVKVP
MMKIKTLTTP YFRDEELSCT VVELKYKGNA SALFILPDQG RMQQVEASLQ PETLRKWKNS
LRPRKMGELY LPKFSISTDY SLKNILPELG IKEIFSKQAD LSGITGTKDL IVSQMVHKAV
LDVAETGTEG VAATGVNFRI LSRRTSLWFN RTFLMVISHT DVQTTLFIAK ITHPKRA
