SPA3F_MOUSE
ID SPA3F_MOUSE Reviewed; 445 AA.
AC Q80X76; B2RT49;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Serine protease inhibitor A3F;
DE Short=Serpin A3F;
GN Name=Serpina3f;
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 [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Salivary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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).
RN [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-174.
RC STRAIN=C57BL/6J; TISSUE=Plasma;
RX PubMed=16944957; DOI=10.1021/pr060186m;
RA Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.;
RT "Proteome-wide characterization of N-glycosylation events by diagonal
RT chromatography.";
RL J. Proteome Res. 5:2438-2447(2006).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH49975.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC049975; AAH49975.1; ALT_INIT; mRNA.
DR EMBL; BC139132; AAI39133.1; -; mRNA.
DR EMBL; BC139133; AAI39134.1; -; mRNA.
DR CCDS; CCDS26149.1; -.
DR RefSeq; NP_001028507.2; NM_001033335.3.
DR RefSeq; NP_001161766.1; NM_001168294.1.
DR RefSeq; NP_001161767.1; NM_001168295.1.
DR AlphaFoldDB; Q80X76; -.
DR SMR; Q80X76; -.
DR STRING; 10090.ENSMUSP00000113945; -.
DR MEROPS; I04.045; -.
DR MEROPS; I04.078; -.
DR GlyGen; Q80X76; 4 sites.
DR iPTMnet; Q80X76; -.
DR PhosphoSitePlus; Q80X76; -.
DR CPTAC; non-CPTAC-4009; -.
DR EPD; Q80X76; -.
DR jPOST; Q80X76; -.
DR MaxQB; Q80X76; -.
DR PaxDb; Q80X76; -.
DR PRIDE; Q80X76; -.
DR ProteomicsDB; 257333; -.
DR DNASU; 238393; -.
DR Ensembl; ENSMUST00000101080; ENSMUSP00000098641; ENSMUSG00000066363.
DR Ensembl; ENSMUST00000121337; ENSMUSP00000113945; ENSMUSG00000066363.
DR Ensembl; ENSMUST00000167049; ENSMUSP00000126520; ENSMUSG00000066363.
DR GeneID; 238393; -.
DR KEGG; mmu:238393; -.
DR UCSC; uc007oww.2; mouse.
DR CTD; 238393; -.
DR MGI; MGI:2182838; Serpina3f.
DR VEuPathDB; HostDB:ENSMUSG00000066363; -.
DR eggNOG; KOG2392; Eukaryota.
DR GeneTree; ENSGT00940000154392; -.
DR HOGENOM; CLU_023330_2_1_1; -.
DR InParanoid; Q80X76; -.
DR OMA; ICIIASH; -.
DR OrthoDB; 1124079at2759; -.
DR PhylomeDB; Q80X76; -.
DR TreeFam; TF343201; -.
DR Reactome; R-MMU-114608; Platelet degranulation.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 238393; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Serpina3f; mouse.
DR PRO; PR:Q80X76; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q80X76; protein.
DR Bgee; ENSMUSG00000066363; Expressed in spleen and 19 other tissues.
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:0009617; P:response to bacterium; IEP:MGI.
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; IPR023795; Serpin_CS.
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 1: Evidence at protein level;
KW Glycoprotein; Protease inhibitor; Reference proteome;
KW Serine protease inhibitor.
FT CHAIN 1..445
FT /note="Serine protease inhibitor A3F"
FT /id="PRO_0000094097"
FT REGION 357..382
FT /note="RCL"
FT SITE 371..372
FT /note="Reactive bond"
FT /evidence="ECO:0000250"
FT CARBOHYD 28
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 174
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16944957"
FT CARBOHYD 259
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 73
FT /note="A -> T (in Ref. 1; AAH49975)"
FT /evidence="ECO:0000305"
FT CONFLICT 175
FT /note="H -> Q (in Ref. 1; AAH49975)"
FT /evidence="ECO:0000305"
FT CONFLICT 297
FT /note="N -> D (in Ref. 1; AAH49975)"
FT /evidence="ECO:0000305"
FT CONFLICT 406
FT /note="S -> T (in Ref. 1; AAH49975)"
FT /evidence="ECO:0000305"
FT CONFLICT 444
FT /note="R -> T (in Ref. 1; AAH49975)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 445 AA; 50003 MW; A6FA96BBBA6F39E1 CRC64;
MAGVSPAVFG CPDVTLGRNT AVREVQENIT SVDSLTLASS NTDFAFSLYK ELVLKNPDEN
VVFSPFSICT ALALLSLGAK SNTLKEILEG LKFNLTETPE PDIHQGFRYL LDLLSQPGNQ
VQISTGSALF IEKHLQILAE FKEKARALYQ AEAFTADFQQ PLEATKLIND YVSNHTQGKI
KELISDLDKR TLMVLVNYIY FKGKWEMPFD PDDTCKSEFY LDENRSVKVP MMKINNLTTP
YFRDEELSCT VVELKYTGNA SAMFILPDQG KMQQVEASLQ PETLRNWKDS LKPRLINELC
LPKFSISTDY SLEHILPELG IRELFSTQAD LSAITGTKDL RTSQVVHKAV LDVAETGTEA
AAGTGYQNLQ CCQGVIYSMK IYFDRPFLMI ISDTNTHIAL FMAKVSNPES DENFLNVEYA
FPQVLEIMPE YRSVCTCCLP CLTRQ
