ID   SPA3K_CAVPO             Reviewed;         410 AA.
AC   P22323;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Serine proteinase inhibitor A3K;
DE            Short=Serpin A3K;
DE   AltName: Full=Contrapsin;
DE            Short=CP;
DE   Flags: Precursor;
GN   Name=SERPINA3K;
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 25-44.
RX   PubMed=1985973; DOI=10.1016/s0021-9258(17)35262-6;
RA   Suzuki Y., Yoshida K., Honda E., Sinohara H.;
RT   "Molecular cloning and sequence analysis of cDNAs coding for guinea pig
RT   alpha 1-antiproteinases S and F and contrapsin.";
RL   J. Biol. Chem. 266:928-932(1991).
CC   -!- FUNCTION: Contrapsin inhibits trypsin-like proteases.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
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 carboxyl group of the serpin reactive site
CC       and the serine hydroxyl of the protease. The resulting inactive serpin-
CC       protease complex is highly stable (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}.
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DR   EMBL; M57269; AAA62806.1; -; mRNA.
DR   PIR; C39088; C39088.
DR   RefSeq; NP_001166484.1; NM_001173013.1.
DR   AlphaFoldDB; P22323; -.
DR   SMR; P22323; -.
DR   STRING; 10141.ENSCPOP00000013842; -.
DR   MEROPS; I04.001; -.
DR   GeneID; 100135614; -.
DR   KEGG; cpoc:100135614; -.
DR   CTD; 20714; -.
DR   eggNOG; KOG2392; Eukaryota.
DR   InParanoid; P22323; -.
DR   OrthoDB; 1124079at2759; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
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   Direct protein sequencing; Glycoprotein; Protease inhibitor;
KW   Reference proteome; Secreted; Serine protease inhibitor; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000269|PubMed:1985973"
FT   CHAIN           25..410
FT                   /note="Serine proteinase inhibitor A3K"
FT                   /id="PRO_0000032424"
FT   REGION          360..381
FT                   /note="RCL"
FT   SITE            374..375
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        62
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        99
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        162
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        229
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        263
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   410 AA;  45599 MW;  A5931286FA4605A0 CRC64;
     MPSAISRGLL LLAGLCYLVF GIMAEDIQVA QVPSQHMPSH KVPRSLAHFA HSMHRVLTQQ
     SNTSNIFFSP VSIATALAMV SLGAKGDTHT QILRSLEFNL TEIAEADIHD GFQNLLHTLN
     RPHSEHQLTT GNGLFLDQNL KLKEKFSGDV KTLYHAEAFP TNFSNPKEAE KQINAYVEKG
     TQGKIVDLVK DLGADTVLAL VNYIFFRGKW EKPFDVKHTT QEDFHVDANT TVKVPMMKQQ
     GMHKAFHCST IQSWVLLLDY EGNVTALFLL PDEGKMQHLE ETLTPELVFK FLRKTETMPA
     YVSLPKLSIS GTYDLKEVLR DLGITNVFSG AADLSGITED MPLKISKGLH KALLTIDEEG
     TEAAAATVLE ATRTARPPRL SFNKPFFFLI IDHSTDTPLF VGKVMDPTKK