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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
 
 
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