ID   ZPI_PONAB               Reviewed;         443 AA.
AC   Q5RDA8;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Protein Z-dependent protease inhibitor;
DE            Short=PZ-dependent protease inhibitor;
DE            Short=PZI;
DE   AltName: Full=Serpin A10;
DE   Flags: Precursor;
GN   Name=SERPINA10; Synonyms=ZPI;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Inhibits activity of the coagulation protease factor Xa in
CC       the presence of PROZ, calcium and phospholipids. Also inhibits factor
CC       XIa in the absence of cofactors (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- PTM: Phosphorylated by FAM20C in the extracellular medium.
CC       {ECO:0000250|UniProtKB:Q9UK55}.
CC   -!- MISCELLANEOUS: Heparin acts as an important cofactor, producing 20 to
CC       100-fold accelerations of SERPINA10 reactions with factor Xa and factor
CC       XIa. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}.
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DR   EMBL; CR858006; CAH90249.1; -; mRNA.
DR   RefSeq; NP_001125107.1; NM_001131635.1.
DR   AlphaFoldDB; Q5RDA8; -.
DR   SMR; Q5RDA8; -.
DR   STRING; 9601.ENSPPYP00000006936; -.
DR   MEROPS; I04.005; -.
DR   PRIDE; Q5RDA8; -.
DR   GeneID; 100171989; -.
DR   KEGG; pon:100171989; -.
DR   CTD; 51156; -.
DR   eggNOG; KOG2392; Eukaryota.
DR   InParanoid; Q5RDA8; -.
DR   OrthoDB; 1124079at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
DR   CDD; cd02055; serpinA10_PZI; 1.
DR   Gene3D; 2.30.39.10; -; 1.
DR   Gene3D; 3.30.497.10; -; 1.
DR   InterPro; IPR033835; PZI_serpin_dom.
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.
PE   2: Evidence at transcript level;
KW   Blood coagulation; Glycoprotein; Hemostasis; Heparin-binding;
KW   Phosphoprotein; Protease inhibitor; Reference proteome; Secreted;
KW   Serine protease inhibitor; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..443
FT                   /note="Protein Z-dependent protease inhibitor"
FT                   /id="PRO_0000032484"
FT   REGION          24..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          136..153
FT                   /note="Heparin-binding"
FT                   /evidence="ECO:0000250"
FT   SITE            261
FT                   /note="Essential for interaction with PROZ"
FT                   /evidence="ECO:0000250"
FT   SITE            314
FT                   /note="Essential for interaction with PROZ"
FT                   /evidence="ECO:0000250"
FT   SITE            407..408
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         56
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UK55"
FT   CARBOHYD        36
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        180
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        295
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   443 AA;  50412 MW;  1A7B210E9BD62EFD CRC64;
     MKVVPSLLLS VLLAQVWLVP GLAPSPQSPE TPAPQNQTSR VVQAPREEEE DEQEASEEKA
     GDEEKAWLTA SRQQLAKETS NFGFSLLRKI SMRHDGNIVF SPFGTSLAMT GLMLGATGLT
     ETQIKRGLHL QALNPTKPGL LPSLFKGLRE TLSRNLELGL TQGSFAFIHK DFDVKETFLN
     LSKRYFDTEC VPMNFRNASQ AKRLMNHYIN KETRGKIPKL FDEINPETKL ILVDYILFKG
     KWLTPFDPVF TEVDTFHQDK YKTIKVPMMY GAGKFASTFD KNFCCHVLKL PYQGNVTMLV
     VLMEKMGDQL ALEDYLTTDL VETWLRNMKT RNMEVFFPKF KLDQKYEMHE LLRQMGIRRI
     SPFADLSELS ATGRNLQVSR VLQRTVIEVD ERGTEAVAAI LSEIIAYSMP PAIKVDRPFH
     FMIYEETSGM LLFLGRVVNP TLL