(data stored in ACNUC19913 zone)

HOGENOM: MOUSE8_PE169

ID   MOUSE8_PE169                         STANDARD;      PRT;   399 AA.
AC   MOUSE8_PE169; Q9CQW3;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Vitamin K-dependent protein Z;Flags: Precursor;
DE   (MOUSE8.PE169).
GN   Name=Proz;
OS   MUS MUSCULUS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae;
OC   Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS MOUSE8.PE169.
CC       Mus musculus chromosome 8 NCBIM37  sequence 1..131738871 annotated by
CC       Ensembl
CC   -!- ANNOTATIONS ORIGIN:PROZ_MOUSE
CC   -!- FUNCTION: Appears to assist hemostasis by binding thrombin and
CC       promoting its association with phospholipid vesicles (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Plasma.
CC   -!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of
CC       aspartate and asparagine is (R) stereospecific within EGF domains
CC       (By similarity).
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC   -!- SIMILARITY: Contains 2 EGF-like domains.
CC   -!- SIMILARITY: Contains 1 Gla (gamma-carboxy-glutamate) domain.
CC   -!- SIMILARITY: Contains 1 peptidase S1 domain.
CC   -!- CAUTION: Although homologous with the vitamin K-dependent clotting
CC       factors, it has lost two of the essential catalytic residues and
CC       has no enzymatic activity.
CC   -!- GENE_FAMILY: HOG000251821 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Mus_musculus;ENSMUSG00000031445;ENSMUST00000033822;ENSMUSP00000033822.
DR   EMBL; AK005011; - ;
DR   EMBL; AK008819; - ;
DR   EMBL; BC024104; - ;
DR   EMBL; BC038045; - ;
DR   EMBL; CH466566; - ;
DR   UniProtKB/Swiss-Prot; Q9CQW3; -.
DR   EMBL; AK005011; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AK008819; BAB25912.1; -; mRNA.
DR   IPI; IPI00133222; -.
DR   RefSeq; NP_080110.1; NM_025834.3.
DR   UniGene; Mm.441140; -.
DR   ProteinModelPortal; Q9CQW3; -.
DR   SMR; Q9CQW3; 46-85, 89-398.
DR   STRING; Q9CQW3; -.
DR   PRIDE; Q9CQW3; -.
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   GeneTree; ENSGT00560000076714; -.
DR   InParanoid; Q9CQW3; -.
DR   OMA; WFLTGIL; -.
DR   OrthoDB; EOG45756N; -.
DR   PhylomeDB; Q9CQW3; -.
DR   NextBio; 322969; -.
DR   ArrayExpress; Q9CQW3; -.
DR   Bgee; Q9CQW3; -.
DR   Genevestigator; Q9CQW3; -.
DR   GermOnline; ENSMUSG00000031445; Mus musculus.
DR   GO; GO:0005576; C:extracellular region; IDA:MGI.
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   InterPro; IPR017857; Coagulation_fac_subgr_Gla_dom.
DR   InterPro; IPR006209; EGF.
DR   InterPro; IPR006210; EGF-like.
DR   InterPro; IPR013032; EGF-like_reg_CS.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR000742; EGF_3.
DR   InterPro; IPR000294; GLA_domain.
DR   InterPro; IPR009003; Pept_cys/ser_Trypsin-like.
DR   InterPro; IPR012224; Pept_S1A_FX.
DR   InterPro; IPR001254; Peptidase_S1_S6.
DR   Gene3D; G3DSA:4.10.740.10; Coagulation_factor_Gla; 1.
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; SM00069; GLA; 1.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; Pept_Ser_Cys; 1.
DR   SUPFAM; SSF57630; VitK_dep_GLA; 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.
DR   HOGENOMDNA; MOUSE8.PE169; -.
KW   ENSMUSG000000314455old_1320000031; ENSMUSP000000338221old_1320000031;
KW   Q05CL2_MOUSE; Q8CI01_MOUSE; AK005011; AK008819; BC024104; BC038045;
KW   CH466566;
KW   Blood coagulation; Calcium; Cleavage on pair of basic residues;
KW   Complete proteome; Disulfide bond; EGF-like domain;
KW   Gamma-carboxyglutamic acid; Glycoprotein; Hydroxylation;
KW   Reference proteome; Repeat; Secreted; Serine protease homolog; Signal.
SQ   SEQUENCE   399 AA;  UNKNOWN MW;  UNKNOWN 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
//

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