PROZ_MOUSE
ID PROZ_MOUSE Reviewed; 399 AA.
AC Q9CQW3;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Vitamin K-dependent protein Z;
DE Flags: Precursor;
GN Name=Proz;
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=C57BL/6J; TISSUE=Liver, and Stomach;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-230.
RC STRAIN=C57BL/6J; TISSUE=Plasma;
RX PubMed=17330941; DOI=10.1021/pr0604559;
RA Bernhard O.K., Kapp E.A., Simpson R.J.;
RT "Enhanced analysis of the mouse plasma proteome using cysteine-containing
RT tryptic glycopeptides.";
RL J. Proteome Res. 6:987-995(2007).
CC -!- FUNCTION: Appears to assist hemostasis by binding thrombin and
CC promoting its association with phospholipid vesicles. Inhibits activity
CC of the coagulation protease factor Xa in the presence of SERPINA10,
CC calcium and phospholipids (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Plasma.
CC -!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate
CC and asparagine is (R) stereospecific within EGF domains. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
CC -!- CAUTION: Although homologous with the vitamin K-dependent clotting
CC factors, it has lost two of the essential catalytic residues and has no
CC enzymatic activity. {ECO:0000305}.
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DR EMBL; AK005011; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK008819; BAB25912.1; -; mRNA.
DR CCDS; CCDS22105.1; -.
DR RefSeq; NP_080110.1; NM_025834.3.
DR AlphaFoldDB; Q9CQW3; -.
DR SMR; Q9CQW3; -.
DR STRING; 10090.ENSMUSP00000033822; -.
DR MEROPS; S01.996; -.
DR GlyGen; Q9CQW3; 4 sites.
DR iPTMnet; Q9CQW3; -.
DR PhosphoSitePlus; Q9CQW3; -.
DR MaxQB; Q9CQW3; -.
DR PaxDb; Q9CQW3; -.
DR PRIDE; Q9CQW3; -.
DR ProteomicsDB; 291889; -.
DR Antibodypedia; 25847; 209 antibodies from 27 providers.
DR DNASU; 66901; -.
DR Ensembl; ENSMUST00000033822; ENSMUSP00000033822; ENSMUSG00000031445.
DR GeneID; 66901; -.
DR KEGG; mmu:66901; -.
DR UCSC; uc009kwu.1; mouse.
DR CTD; 8858; -.
DR MGI; MGI:1860488; Proz.
DR VEuPathDB; HostDB:ENSMUSG00000031445; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000154505; -.
DR HOGENOM; CLU_006842_19_5_1; -.
DR InParanoid; Q9CQW3; -.
DR OMA; NTARYMI; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; Q9CQW3; -.
DR TreeFam; TF327329; -.
DR Reactome; R-MMU-159740; Gamma-carboxylation of protein precursors.
DR Reactome; R-MMU-159763; Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
DR Reactome; R-MMU-159782; Removal of aminoterminal propeptides from gamma-carboxylated proteins.
DR BioGRID-ORCS; 66901; 2 hits in 73 CRISPR screens.
DR PRO; PR:Q9CQW3; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q9CQW3; protein.
DR Bgee; ENSMUSG00000031445; Expressed in liver and 56 other tissues.
DR ExpressionAtlas; Q9CQW3; baseline and differential.
DR Genevisible; Q9CQW3; MM.
DR GO; GO:0005576; C:extracellular region; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; TAS:MGI.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0007596; P:blood coagulation; IDA:MGI.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 2.40.10.10; -; 2.
DR Gene3D; 4.10.740.10; -; 1.
DR InterPro; IPR017857; Coagulation_fac-like_Gla_dom.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR035972; GLA-like_dom_SF.
DR InterPro; IPR000294; GLA_domain.
DR InterPro; IPR012224; Pept_S1A_FX.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001254; Trypsin_dom.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF00594; Gla; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PIRSF; PIRSF001143; Factor_X; 1.
DR PRINTS; PR00001; GLABLOOD.
DR SMART; SM00181; EGF; 2.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00069; GLA; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF57630; SSF57630; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS00011; GLA_1; 1.
DR PROSITE; PS50998; GLA_2; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
PE 1: Evidence at protein level;
KW Blood coagulation; Calcium; Cleavage on pair of basic residues;
KW Disulfide bond; EGF-like domain; Gamma-carboxyglutamic acid; Glycoprotein;
KW Hemostasis; Hydroxylation; Reference proteome; Repeat; Secreted;
KW Serine protease homolog; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..40
FT /evidence="ECO:0000250"
FT /id="PRO_0000028490"
FT CHAIN 41..399
FT /note="Vitamin K-dependent protein Z"
FT /id="PRO_0000028491"
FT DOMAIN 41..86
FT /note="Gla"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT DOMAIN 87..123
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 125..166
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 172..399
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT MOD_RES 47
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00744,
FT ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 48
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00744,
FT ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 55
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00744,
FT ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 57
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00744,
FT ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 60
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00744,
FT ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 61
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00744,
FT ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 66
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00744,
FT ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 67
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00744,
FT ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 70
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00744,
FT ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 73
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00744,
FT ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 80
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00744,
FT ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 104
FT /note="(3R)-3-hydroxyaspartate"
FT /evidence="ECO:0000250"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 230
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17330941"
FT CARBOHYD 305
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 331
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 58..63
FT /evidence="ECO:0000250"
FT DISULFID 91..102
FT /evidence="ECO:0000250"
FT DISULFID 96..111
FT /evidence="ECO:0000250"
FT DISULFID 113..122
FT /evidence="ECO:0000250"
FT DISULFID 129..141
FT /evidence="ECO:0000250"
FT DISULFID 137..150
FT /evidence="ECO:0000250"
FT DISULFID 152..165
FT /evidence="ECO:0000250"
FT DISULFID 208..224
FT /evidence="ECO:0000250"
FT DISULFID 326..340
FT /evidence="ECO:0000250"
SQ SEQUENCE 399 AA; 44304 MW; 4FC85C9598F27E03 CRC64;
MAGCILLLRG FILTLILHQV ELSVFLPAPK ANNVLRRWRR GSSYFLEEIF QGNLEKECYE
EVCNYEEARE VFENDVITDE FWRQYGGGSP CVSQPCLNNG TCEDHIRSYS CTCSPGYEGK
TCAMAKNECH LERTDGCQHF CHPGQSSYMC SCAKGYKLGK DQKSCGPSDK CACGALTSEH
IRMTKSSQSQ PSFPWQVRLT NSEGEDFCAG VLLQEDFVLT TAKCSLLHSN ISVKANVDQR
IRIKSTHVHM RYDEESGEND VSLLQLEEPL QCPSSGLPVC VPERDFAEHV LIPGTEGLLS
GWMLNGTHLA TTPMLLSVTQ ADGEECGQTL NVTVTTRTSC EKGSVVMGPW VEGSVVTREH
KGTWFLTGIL GSPPPPGQSQ MLLLTAVPRY SMWFKQIMK
