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Protein

Vitamin K-dependent protein Z

Gene

PROZ

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Appears to assist hemostasis by binding thrombin and promoting its association with phospholipid vesicles. Inhibits activity of the coagulation protease factor Xa in the presence of SERPINA10, calcium and phospholipids.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Serine protease homolog

Keywords - Biological processi

Blood coagulation, Hemostasis

Keywords - Ligandi

Calcium

Enzyme and pathway databases

ReactomeiR-HSA-159740. Gamma-carboxylation of protein precursors.
R-HSA-159763. Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
R-HSA-159782. Removal of aminoterminal propeptides from gamma-carboxylated proteins.

Protein family/group databases

MEROPSiS01.979.

Names & Taxonomyi

Protein namesi
Recommended name:
Vitamin K-dependent protein Z
Gene namesi
Name:PROZ
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 13

Organism-specific databases

HGNCiHGNC:9460. PROZ.

Subcellular locationi

GO - Cellular componenti

  • endoplasmic reticulum lumen Source: Reactome
  • extracellular exosome Source: UniProtKB
  • Golgi lumen Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

MalaCardsiPROZ.
Orphaneti329217. Cerebral sinovenous thrombosis.
PharmGKBiPA33813.

Chemistry

DrugBankiDB00170. Menadione.

Polymorphism and mutation databases

BioMutaiPROZ.
DMDMi131092.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Add
BLAST
Propeptidei24 – 4017PRO_0000028488Add
BLAST
Chaini41 – 400360Vitamin K-dependent protein Z1 PublicationPRO_0000028489Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei47 – 4714-carboxyglutamatePROSITE-ProRule annotation1 Publication
Modified residuei48 – 4814-carboxyglutamatePROSITE-ProRule annotation1 Publication
Modified residuei51 – 5114-carboxyglutamatePROSITE-ProRule annotation1 Publication
Modified residuei55 – 5514-carboxyglutamatePROSITE-ProRule annotation1 Publication
Modified residuei57 – 5714-carboxyglutamatePROSITE-ProRule annotation1 Publication
Disulfide bondi58 ↔ 63By similarity
Modified residuei60 – 6014-carboxyglutamatePROSITE-ProRule annotation1 Publication
Modified residuei61 – 6114-carboxyglutamatePROSITE-ProRule annotation1 Publication
Modified residuei66 – 6614-carboxyglutamatePROSITE-ProRule annotation1 Publication
Modified residuei67 – 6714-carboxyglutamatePROSITE-ProRule annotation1 Publication
Modified residuei70 – 7014-carboxyglutamatePROSITE-ProRule annotation1 Publication
Modified residuei73 – 7314-carboxyglutamatePROSITE-ProRule annotation1 Publication
Modified residuei75 – 7514-carboxyglutamatePROSITE-ProRule annotation1 Publication
Modified residuei80 – 8014-carboxyglutamatePROSITE-ProRule annotation1 Publication
Disulfide bondi91 ↔ 102
Glycosylationi93 – 931O-linked (Glc...)
Disulfide bondi96 ↔ 111
Glycosylationi99 – 991N-linked (GlcNAc...)1 Publication
Modified residuei104 – 1041(3R)-3-hydroxyaspartateBy similarity
Disulfide bondi113 ↔ 122
Disulfide bondi129 ↔ 141
Disulfide bondi137 ↔ 150
Disulfide bondi152 ↔ 165
Disulfide bondi203 ↔ 219
Glycosylationi225 – 2251N-linked (GlcNAc...)1 Publication
Glycosylationi233 – 2331N-linked (GlcNAc...)2 Publications
Glycosylationi306 – 3061N-linked (GlcNAc...)Sequence analysis
Disulfide bondi327 ↔ 341
Glycosylationi332 – 3321N-linked (GlcNAc...)1 Publication

Post-translational modificationi

The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains.By similarity

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Gamma-carboxyglutamic acid, Glycoprotein, Hydroxylation

Proteomic databases

PaxDbiP22891.
PRIDEiP22891.

PTM databases

iPTMnetiP22891.
PhosphoSiteiP22891.
UniCarbKBiP22891.

Expressioni

Tissue specificityi

Plasma.

Gene expression databases

BgeeiP22891.
CleanExiHS_PROZ.
GenevisibleiP22891. HS.

Organism-specific databases

HPAiHPA016503.

Interactioni

Subunit structurei

Interacts with SERPINA10.2 Publications

Protein-protein interaction databases

BioGridi114382. 31 interactions.
STRINGi9606.ENSP00000364697.

Structurei

Secondary structure

1
400
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni97 – 993Combined sources
Beta strandi106 – 1083Combined sources
Beta strandi114 – 1163Combined sources
Beta strandi119 – 1224Combined sources
Beta strandi126 – 1283Combined sources
Beta strandi134 – 1363Combined sources
Beta strandi138 – 1403Combined sources
Beta strandi145 – 1473Combined sources
Beta strandi149 – 1513Combined sources
Beta strandi156 – 1583Combined sources
Beta strandi165 – 1673Combined sources
Beta strandi191 – 1955Combined sources
Beta strandi197 – 1993Combined sources
Beta strandi201 – 2099Combined sources
Beta strandi212 – 2154Combined sources
Helixi217 – 2204Combined sources
Beta strandi227 – 2304Combined sources
Beta strandi240 – 24910Combined sources
Turni255 – 2584Combined sources
Beta strandi263 – 2697Combined sources
Turni273 – 2764Combined sources
Helixi285 – 2906Combined sources
Turni291 – 2955Combined sources
Beta strandi298 – 3025Combined sources
Beta strandi309 – 3113Combined sources
Beta strandi315 – 3228Combined sources
Helixi324 – 3318Combined sources
Beta strandi339 – 3435Combined sources
Helixi348 – 3503Combined sources
Beta strandi356 – 3605Combined sources
Beta strandi365 – 3717Combined sources
Helixi376 – 3783Combined sources
Beta strandi380 – 3878Combined sources
Helixi388 – 3914Combined sources
Helixi392 – 3998Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3F1SX-ray2.30B125-400[»]
3H5CX-ray3.26B84-400[»]
ProteinModelPortaliP22891.
SMRiP22891. Positions 46-85, 89-400.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP22891.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini41 – 8646GlaPROSITE-ProRule annotationAdd
BLAST
Domaini87 – 12337EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini125 – 16642EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini175 – 400226Peptidase S1PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase S1 family.PROSITE-ProRule annotation
Contains 2 EGF-like domains.PROSITE-ProRule annotation
Contains 1 Gla (gamma-carboxy-glutamate) domain.PROSITE-ProRule annotation
Contains 1 peptidase S1 domain.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiKOG3627. Eukaryota.
COG5640. LUCA.
GeneTreeiENSGT00760000118890.
HOGENOMiHOG000251821.
HOVERGENiHBG013304.
InParanoidiP22891.
OMAiWFLTGIL.
OrthoDBiEOG761BTN.
PhylomeDBiP22891.
TreeFamiTF327329.

Family and domain databases

Gene3Di4.10.740.10. 1 hit.
InterProiIPR017857. Coagulation_fac_subgr_Gla_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR000294. GLA_domain.
IPR012224. Pept_S1A_FX.
IPR009003. Peptidase_S1_PA.
IPR001254. Trypsin_dom.
[Graphical view]
PfamiPF00008. EGF. 1 hit.
PF00594. Gla. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFiPIRSF001143. Factor_X. 1 hit.
PRINTSiPR00001. GLABLOOD.
SMARTiSM00181. EGF. 2 hits.
SM00179. EGF_CA. 2 hits.
SM00069. GLA. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
SSF57630. SSF57630. 1 hit.
PROSITEiPS00010. ASX_HYDROXYL. 1 hit.
PS00022. EGF_1. 1 hit.
PS01186. EGF_2. 2 hits.
PS50026. EGF_3. 1 hit.
PS00011. GLA_1. 1 hit.
PS50998. GLA_2. 1 hit.
PS50240. TRYPSIN_DOM. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P22891-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAGCVPLLQG LVLVLALHRV EPSVFLPASK ANDVLVRWKR AGSYLLEELF
60 70 80 90 100
EGNLEKECYE EICVYEEARE VFENEVVTDE FWRRYKGGSP CISQPCLHNG
110 120 130 140 150
SCQDSIWGYT CTCSPGYEGS NCELAKNECH PERTDGCQHF CLPGQESYTC
160 170 180 190 200
SCAQGYRLGE DHKQCVPHDQ CACGVLTSEK RAPDLQDLPW QVKLTNSEGK
210 220 230 240 250
DFCGGVIIRE NFVLTTAKCS LLHRNITVKT YFNRTSQDPL MIKITHVHVH
260 270 280 290 300
MRYDADAGEN DLSLLELEWP IQCPGAGLPV CTPEKDFAEH LLIPRTRGLL
310 320 330 340 350
SGWARNGTDL GNSLTTRPVT LVEGEECGQV LNVTVTTRTY CERSSVAAMH
360 370 380 390 400
WMDGSVVTRE HRGSWFLTGV LGSQPVGGQA HMVLVTKVSR YSLWFKQIMN
Length:400
Mass (Da):44,744
Last modified:November 1, 1991 - v2
Checksum:i7EBD2DCC48860268
GO
Isoform 2 (identifier: P22891-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     24-24: V → ATSLKERHGLHSDSACTGVQESL

Show »
Length:422
Mass (Da):47,053
Checksum:iB8824CE1ECAEEEAE
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti70 – 701E → K.1 Publication
Corresponds to variant rs3024778 [ dbSNP | Ensembl ].
VAR_013124
Natural varianti295 – 2951R → H.1 Publication
Corresponds to variant rs3024772 [ dbSNP | Ensembl ].
VAR_013125

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei24 – 241V → ATSLKERHGLHSDSACTGVQ ESL in isoform 2. CuratedVSP_005415

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M55670 mRNA. Translation: AAA36500.1.
M55671 mRNA. Translation: AAA36501.1.
AB033749 Genomic DNA. Translation: BAA85763.1.
AB033749 Genomic DNA. Translation: BAA85764.1.
AF440358 Genomic DNA. Translation: AAL27631.1.
EF445049 Genomic DNA. Translation: ACA06105.1.
AL137002 Genomic DNA. Translation: CAI41389.1.
AL137002 Genomic DNA. Translation: CAI41388.1.
CH471085 Genomic DNA. Translation: EAX09186.1.
CH471085 Genomic DNA. Translation: EAX09187.1.
BC074906 mRNA. Translation: AAH74906.1.
BC074907 mRNA. Translation: AAH74907.1.
M59303 mRNA. Translation: AAA36499.1.
CCDSiCCDS58300.1. [P22891-2]
CCDS9531.1. [P22891-1]
PIRiA36244. KXHUZ.
RefSeqiNP_001243063.1. NM_001256134.1. [P22891-2]
NP_003882.1. NM_003891.2. [P22891-1]
UniGeneiHs.1011.

Genome annotation databases

EnsembliENST00000342783; ENSP00000344458; ENSG00000126231. [P22891-2]
ENST00000375547; ENSP00000364697; ENSG00000126231. [P22891-1]
GeneIDi8858.
KEGGihsa:8858.
UCSCiuc001vta.3. human. [P22891-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

SeattleSNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M55670 mRNA. Translation: AAA36500.1.
M55671 mRNA. Translation: AAA36501.1.
AB033749 Genomic DNA. Translation: BAA85763.1.
AB033749 Genomic DNA. Translation: BAA85764.1.
AF440358 Genomic DNA. Translation: AAL27631.1.
EF445049 Genomic DNA. Translation: ACA06105.1.
AL137002 Genomic DNA. Translation: CAI41389.1.
AL137002 Genomic DNA. Translation: CAI41388.1.
CH471085 Genomic DNA. Translation: EAX09186.1.
CH471085 Genomic DNA. Translation: EAX09187.1.
BC074906 mRNA. Translation: AAH74906.1.
BC074907 mRNA. Translation: AAH74907.1.
M59303 mRNA. Translation: AAA36499.1.
CCDSiCCDS58300.1. [P22891-2]
CCDS9531.1. [P22891-1]
PIRiA36244. KXHUZ.
RefSeqiNP_001243063.1. NM_001256134.1. [P22891-2]
NP_003882.1. NM_003891.2. [P22891-1]
UniGeneiHs.1011.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3F1SX-ray2.30B125-400[»]
3H5CX-ray3.26B84-400[»]
ProteinModelPortaliP22891.
SMRiP22891. Positions 46-85, 89-400.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114382. 31 interactions.
STRINGi9606.ENSP00000364697.

Chemistry

DrugBankiDB00170. Menadione.

Protein family/group databases

MEROPSiS01.979.

PTM databases

iPTMnetiP22891.
PhosphoSiteiP22891.
UniCarbKBiP22891.

Polymorphism and mutation databases

BioMutaiPROZ.
DMDMi131092.

Proteomic databases

PaxDbiP22891.
PRIDEiP22891.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000342783; ENSP00000344458; ENSG00000126231. [P22891-2]
ENST00000375547; ENSP00000364697; ENSG00000126231. [P22891-1]
GeneIDi8858.
KEGGihsa:8858.
UCSCiuc001vta.3. human. [P22891-1]

Organism-specific databases

CTDi8858.
GeneCardsiPROZ.
H-InvDBHIX0037352.
HGNCiHGNC:9460. PROZ.
HPAiHPA016503.
MalaCardsiPROZ.
MIMi176895. gene.
neXtProtiNX_P22891.
Orphaneti329217. Cerebral sinovenous thrombosis.
PharmGKBiPA33813.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3627. Eukaryota.
COG5640. LUCA.
GeneTreeiENSGT00760000118890.
HOGENOMiHOG000251821.
HOVERGENiHBG013304.
InParanoidiP22891.
OMAiWFLTGIL.
OrthoDBiEOG761BTN.
PhylomeDBiP22891.
TreeFamiTF327329.

Enzyme and pathway databases

ReactomeiR-HSA-159740. Gamma-carboxylation of protein precursors.
R-HSA-159763. Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
R-HSA-159782. Removal of aminoterminal propeptides from gamma-carboxylated proteins.

Miscellaneous databases

EvolutionaryTraceiP22891.
GenomeRNAii8858.
PROiP22891.
SOURCEiSearch...

Gene expression databases

BgeeiP22891.
CleanExiHS_PROZ.
GenevisibleiP22891. HS.

Family and domain databases

Gene3Di4.10.740.10. 1 hit.
InterProiIPR017857. Coagulation_fac_subgr_Gla_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR000294. GLA_domain.
IPR012224. Pept_S1A_FX.
IPR009003. Peptidase_S1_PA.
IPR001254. Trypsin_dom.
[Graphical view]
PfamiPF00008. EGF. 1 hit.
PF00594. Gla. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFiPIRSF001143. Factor_X. 1 hit.
PRINTSiPR00001. GLABLOOD.
SMARTiSM00181. EGF. 2 hits.
SM00179. EGF_CA. 2 hits.
SM00069. GLA. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
SSF57630. SSF57630. 1 hit.
PROSITEiPS00010. ASX_HYDROXYL. 1 hit.
PS00022. EGF_1. 1 hit.
PS01186. EGF_2. 2 hits.
PS50026. EGF_3. 1 hit.
PS00011. GLA_1. 1 hit.
PS50998. GLA_2. 1 hit.
PS50240. TRYPSIN_DOM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Amino acid sequence of human protein Z, a vitamin K-dependent plasma glycoprotein."
    Ichinose A., Takeya H., Espling E., Iwanaga S., Kisiel W., Davie E.W.
    Biochem. Biophys. Res. Commun. 172:1139-1144(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], GAMMA-CARBOXYGLUTAMATION AT GLU-47; GLU-48; GLU-51; GLU-55; GLU-57; GLU-60; GLU-61; GLU-66; GLU-67; GLU-70; GLU-73; GLU-75 AND GLU-80, PARTIAL PROTEIN SEQUENCE.
    Tissue: Liver.
  2. "The gene for human protein Z is localized to chromosome 13 at band q34 and is coded by eight regular exons and one alternative exon."
    Fujimaki K., Yamazaki T., Taniwaki M., Ichinose A.
    Biochemistry 37:6838-6846(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING.
  3. SeattleSNPs variation discovery resource
    Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LYS-70 AND HIS-295.
  4. NHLBI resequencing and genotyping service (RS&G)
    Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "The DNA sequence and analysis of human chromosome 13."
    Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
    Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  8. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 81-400, PROTEIN SEQUENCE OF 63-103.
  9. "Identification of a disaccharide (Xyl-Glc) and a trisaccharide (Xyl2-Glc) O-glycosidically linked to a serine residue in the first epidermal growth factor-like domain of human factors VII and IX and protein Z and bovine protein Z."
    Nishimura H., Kawabata S., Kisiel W., Hase S., Ikenaka T., Takao T., Shimonishi Y., Iwanaga S.
    J. Biol. Chem. 264:20320-20325(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE OF CARBOHYDRATE ON SER-93.
  10. "A new trisaccharide sugar chain linked to a serine residue in the first EGF-like domain of clotting factors VII and IX and protein Z."
    Iwanaga S., Nishimura H., Kawabata S., Kisiel W., Hase S., Ikenaka T.
    Adv. Exp. Med. Biol. 281:121-131(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE OF CARBOHYDRATE ON SER-93.
  11. "Crystal structure of protein Z-dependent inhibitor complex shows how protein Z functions as a cofactor in the membrane inhibition of factor X."
    Wei Z., Yan Y., Carrell R.W., Zhou A.
    Blood 114:3662-3667(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 125-400 IN COMPLEX WITH SERPINA10, GLYCOSYLATION AT ASN-233, DISULFIDE BONDS, SUBUNIT.
  12. "Basis for the specificity and activation of the serpin protein Z-dependent proteinase inhibitor (ZPI) as an inhibitor of membrane-associated factor Xa."
    Huang X., Dementiev A., Olson S.T., Gettins P.G.
    J. Biol. Chem. 285:20399-20409(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.26 ANGSTROMS) OF 84-400 IN COMPLEX WITH SERPINA10, GLYCOSYLATION AT ASN-99; ASN-225; ASN-233 AND ASN-332, DISULFIDE BONDS, SUBUNIT.

Entry informationi

Entry nameiPROZ_HUMAN
AccessioniPrimary (citable) accession number: P22891
Secondary accession number(s): A6NMB4
, Q15213, Q5JVF5, Q5JVF6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: November 1, 1991
Last modified: June 8, 2016
This is version 177 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Caution

Although related to peptidase S1 family vitamin K-dependent clotting factors, it has lost two of the essential catalytic residues and therefore lacks protease activity.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 13
    Human chromosome 13: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Peptidase families
    Classification of peptidase families and list of entries
  7. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.