ID   ZPI_RAT                 Reviewed;         436 AA.
AC   Q62975; Q5M8C2;
DT   24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 2.
DT   27-MAR-2024, entry version 151.
DE   RecName: Full=Protein Z-dependent protease inhibitor;
DE            Short=PZ-dependent protease inhibitor;
DE            Short=PZI;
DE   AltName: Full=Regeneration-associated serpin 1;
DE            Short=RASP-1;
DE   AltName: Full=Serpin A10;
DE   Flags: Precursor;
GN   Name=Serpina10; Synonyms=Rasp1, Zpi;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   STRAIN=Long Evans; TISSUE=Liver;
RX   PubMed=8670294; DOI=10.1006/bbrc.1996.0906;
RA   New L., Liu K., Kamali V., Plowman G., Naughton B.A., Purchio A.F.;
RT   "cDNA cloning of rasp-1, a novel gene encoding a plasma protein associated
RT   with liver regeneration.";
RL   Biochem. Biophys. Res. Commun. 223:404-412(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver;
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).
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.
CC   -!- TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.
CC       {ECO:0000269|PubMed:8670294}.
CC   -!- DEVELOPMENTAL STAGE: In regenerating livers, it showed maximal
CC       expression 48 hours after hepatectomy, expression remaining elevated up
CC       to 2 weeks after liver removal. {ECO:0000269|PubMed:8670294}.
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; U55765; AAC52624.1; -; mRNA.
DR   EMBL; BC088113; AAH88113.1; -; mRNA.
DR   PIR; JC4841; JC4841.
DR   RefSeq; NP_598301.2; NM_133617.2.
DR   RefSeq; XP_003750275.1; XM_003750227.3.
DR   AlphaFoldDB; Q62975; -.
DR   SMR; Q62975; -.
DR   STRING; 10116.ENSRNOP00000064104; -.
DR   MEROPS; I04.005; -.
DR   GlyCosmos; Q62975; 6 sites, No reported glycans.
DR   GlyGen; Q62975; 6 sites.
DR   PhosphoSitePlus; Q62975; -.
DR   PaxDb; 10116-ENSRNOP00000064104; -.
DR   Ensembl; ENSRNOT00000073709.2; ENSRNOP00000064104.1; ENSRNOG00000050761.2.
DR   GeneID; 171154; -.
DR   KEGG; rno:171154; -.
DR   UCSC; RGD:621220; rat.
DR   AGR; RGD:621220; -.
DR   CTD; 51156; -.
DR   RGD; 621220; Serpina10.
DR   eggNOG; KOG2392; Eukaryota.
DR   GeneTree; ENSGT00940000159462; -.
DR   HOGENOM; CLU_023330_2_1_1; -.
DR   InParanoid; Q62975; -.
DR   OMA; METFHIN; -.
DR   OrthoDB; 3218836at2759; -.
DR   PhylomeDB; Q62975; -.
DR   TreeFam; TF343094; -.
DR   Reactome; R-RNO-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR   Reactome; R-RNO-8957275; Post-translational protein phosphorylation.
DR   PRO; PR:Q62975; -.
DR   Proteomes; UP000002494; Chromosome 6.
DR   Bgee; ENSRNOG00000048988; Expressed in liver and 10 other cell types or tissues.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IBA:GO_Central.
DR   GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
DR   GO; GO:0097421; P:liver regeneration; IEP:RGD.
DR   CDD; cd02055; serpinA10_PZI; 1.
DR   Gene3D; 2.30.39.10; Alpha-1-antitrypsin, domain 1; 1.
DR   Gene3D; 3.30.497.10; Antithrombin, subunit I, domain 2; 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:SF191; PROTEIN Z-DEPENDENT PROTEASE INHIBITOR; 1.
DR   PANTHER; PTHR11461; SERINE PROTEASE INHIBITOR, SERPIN; 1.
DR   Pfam; PF00079; Serpin; 1.
DR   PRINTS; PR00780; LEUSERPINII.
DR   SMART; SM00093; SERPIN; 1.
DR   SUPFAM; SSF56574; Serpins; 1.
DR   Genevisible; Q62975; RN.
PE   2: Evidence at transcript level;
KW   Blood coagulation; Glycoprotein; Hemostasis; Heparin-binding;
KW   Protease inhibitor; Reference proteome; Secreted;
KW   Serine protease inhibitor; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..436
FT                   /note="Protein Z-dependent protease inhibitor"
FT                   /id="PRO_0000032485"
FT   REGION          128..145
FT                   /note="Heparin-binding"
FT                   /evidence="ECO:0000250"
FT   SITE            253
FT                   /note="Essential for interaction with PROZ"
FT                   /evidence="ECO:0000250"
FT   SITE            306
FT                   /note="Essential for interaction with PROZ"
FT                   /evidence="ECO:0000250"
FT   SITE            400..401
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        23
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        42
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        69
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        172
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        189
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        287
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        28
FT                   /note="S -> T (in Ref. 1; AAC52624)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        422
FT                   /note="Q -> R (in Ref. 1; AAC52624)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   436 AA;  50244 MW;  4AAE8B3DB9F520CE CRC64;
     MRVVSSLFLP VLLAEVWLVS SFNLSSHSPE APIRLVSQDY ENQTWEEYEW ADPRDDNEYW
     LRASQQLSNE TSSFGFSLLR KISMRHDGNV IFSPFGLSVA MVNLMLGAKG ETKVQVENGL
     NLQALSQAGP LILPALFKRV KETFSSNKKL GLTQGSFAFI HKDFEIKKTY FNLSTMYFDT
     EYVPTNFRNS SQARGLMNHY INKETEGKIP KLFDEINPET KLILVDYILF KGKWLTPFDP
     IFTEADTFHL DKYKAVKVPM MYREGNFAST FDKKFRCHIL KLPYQGNATM LVVLMEKSGD
     HLALEDYLTT DLVEMWLQDM KTRKMEVFFP KFKLNQRYEM HELLKQVGIR RIFSTSADLS
     ELSAVARNLQ VSKVVQQSVL EVDERGTEVV SGTVSEITAY CMPPVIKVDR PFHFIIYEEM
     SQMLLFLGRV VNPTVL
//