ZPI_RAT
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 03-AUG-2022, entry version 144.
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 GlyGen; Q62975; 6 sites.
DR PaxDb; Q62975; -.
DR Ensembl; ENSRNOT00000073709; ENSRNOP00000064104; ENSRNOG00000050761.
DR GeneID; 171154; -.
DR KEGG; rno:171154; -.
DR UCSC; RGD:621220; rat.
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; SKQYFDM; -.
DR OrthoDB; 1124079at2759; -.
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 tissues.
DR Genevisible; Q62975; RN.
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 GO; GO:0010951; P:negative regulation of endopeptidase activity; IBA:GO_Central.
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 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
