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Protein

Vitamin K-dependent protein S

Gene

Pros1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Anticoagulant plasma protein; it is a cofactor to activated protein C in the degradation of coagulation factors Va and VIIIa. It helps to prevent coagulation and stimulating fibrinolysis.

GO - Molecular functioni

  • calcium ion binding Source: InterPro
  • protein complex binding Source: RGD

GO - Biological processi

  • blood coagulation Source: UniProtKB-KW
  • fibrinolysis Source: UniProtKB-KW
  • negative regulation of coagulation Source: RGD
  • positive regulation of phagocytosis Source: RGD
  • response to lipopolysaccharide Source: RGD
Complete GO annotation...

Keywords - Biological processi

Blood coagulation, Fibrinolysis, Hemostasis

Keywords - Ligandi

Calcium

Names & Taxonomyi

Protein namesi
Recommended name:
Vitamin K-dependent protein S
Gene namesi
Name:Pros1
Synonyms:Pros
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi620971. Pros1.

Subcellular locationi

GO - Cellular componenti

  • extracellular space Source: RGD
  • protein complex Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424By similarityAdd
BLAST
Propeptidei25 – 4117By similarityPRO_0000022127Add
BLAST
Chaini42 – 675634Vitamin K-dependent protein SPRO_0000022128Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei47 – 4714-carboxyglutamatePROSITE-ProRule annotationBy similarity
Modified residuei48 – 4814-carboxyglutamatePROSITE-ProRule annotationBy similarity
Modified residuei55 – 5514-carboxyglutamatePROSITE-ProRule annotationBy similarity
Modified residuei57 – 5714-carboxyglutamatePROSITE-ProRule annotationBy similarity
Disulfide bondi58 ↔ 63By similarity
Modified residuei60 – 6014-carboxyglutamatePROSITE-ProRule annotationBy similarity
Modified residuei61 – 6114-carboxyglutamatePROSITE-ProRule annotationBy similarity
Modified residuei66 – 6614-carboxyglutamatePROSITE-ProRule annotationBy similarity
Modified residuei67 – 6714-carboxyglutamatePROSITE-ProRule annotationBy similarity
Modified residuei70 – 7014-carboxyglutamatePROSITE-ProRule annotationBy similarity
Modified residuei73 – 7314-carboxyglutamatePROSITE-ProRule annotationBy similarity
Modified residuei77 – 7714-carboxyglutamatePROSITE-ProRule annotationBy similarity
Disulfide bondi121 ↔ 134By similarity
Disulfide bondi126 ↔ 143By similarity
Modified residuei136 – 1361(3R)-3-hydroxyaspartateBy similarity
Disulfide bondi145 ↔ 154By similarity
Disulfide bondi161 ↔ 175By similarity
Disulfide bondi171 ↔ 184By similarity
Disulfide bondi186 ↔ 199By similarity
Disulfide bondi205 ↔ 217By similarity
Disulfide bondi212 ↔ 226By similarity
Disulfide bondi228 ↔ 241By similarity
Disulfide bondi247 ↔ 256By similarity
Disulfide bondi252 ↔ 265By similarity
Disulfide bondi267 ↔ 282By similarity
Disulfide bondi449 ↔ 475By similarity
Glycosylationi499 – 4991N-linked (GlcNAc...)Sequence analysis
Glycosylationi509 – 5091N-linked (GlcNAc...)Sequence analysis

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, Zymogen

Proteomic databases

PaxDbiP53813.
PRIDEiP53813.

Expressioni

Tissue specificityi

Plasma.

Interactioni

GO - Molecular functioni

  • protein complex binding Source: RGD

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000064737.

Structurei

3D structure databases

ProteinModelPortaliP53813.
SMRiP53813. Positions 46-86, 200-283.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini42 – 8746GlaPROSITE-ProRule annotationAdd
BLAST
Domaini117 – 15539EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini157 – 20044EGF-like 2; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini201 – 24242EGF-like 3; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini243 – 28341EGF-like 4; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini299 – 475177Laminin G-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini484 – 665182Laminin G-like 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni88 – 11629Thrombin-sensitiveAdd
BLAST

Sequence similaritiesi

Contains 4 EGF-like domains.PROSITE-ProRule annotation
Contains 1 Gla (gamma-carboxy-glutamate) domain.PROSITE-ProRule annotation
Contains 2 laminin G-like domains.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiENOG410IGF6. Eukaryota.
ENOG410ZTGU. LUCA.
HOVERGENiHBG051702.
InParanoidiP53813.
PhylomeDBiP53813.

Family and domain databases

Gene3Di2.60.120.200. 2 hits.
4.10.740.10. 1 hit.
InterProiIPR017857. Coagulation_fac_subgr_Gla_dom.
IPR013320. ConA-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR000294. GLA_domain.
IPR009030. Growth_fac_rcpt_.
IPR001791. Laminin_G.
IPR033189. PROS1.
[Graphical view]
PANTHERiPTHR24040:SF0. PTHR24040:SF0. 1 hit.
PfamiPF00008. EGF. 1 hit.
PF07645. EGF_CA. 3 hits.
PF00594. Gla. 1 hit.
PF00054. Laminin_G_1. 1 hit.
[Graphical view]
PRINTSiPR00001. GLABLOOD.
SMARTiSM00181. EGF. 4 hits.
SM00179. EGF_CA. 4 hits.
SM00069. GLA. 1 hit.
SM00282. LamG. 2 hits.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 2 hits.
SSF57184. SSF57184. 1 hit.
SSF57630. SSF57630. 1 hit.
PROSITEiPS00010. ASX_HYDROXYL. 4 hits.
PS00022. EGF_1. 1 hit.
PS01186. EGF_2. 3 hits.
PS50026. EGF_3. 4 hits.
PS01187. EGF_CA. 3 hits.
PS00011. GLA_1. 1 hit.
PS50998. GLA_2. 1 hit.
PS50025. LAM_G_DOMAIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P53813-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRVLSVRFRV LLACLALVLP NSETNFLSKE RASQVLVRKR RANTLLEETK
60 70 80 90 100
KGNLERECIE ELCNKEEARE VFENNPETDY FYPKYLGCLG AFRVGAFSAA
110 120 130 140 150
RQSANAYPDL RSCVNAIPDQ CDPMPCNEDG YLSCKDGQGA FTCICKPGWQ
160 170 180 190 200
GDKCQFDINE CKDPSNINGG CSQTCDNTPG SYHCSCKIGF AMLTNKKDCK
210 220 230 240 250
DVDECSLKPS VCGTAVCKNI PGDFECECPN GYRYDPSSKS CKDVDECSEN
260 270 280 290 300
TCAQLCVNYP GGYSCYCDGK KGFKLAQDQR SCEGIPVCLS LDLDKNYELL
310 320 330 340 350
YLAEQFAGVV LYLKFRLPDI TRFSAEFDFR TYDSEGIILY AESLDHSNWL
360 370 380 390 400
LIALREGKIE VQFKNEFSTQ ITTGGNVINN GIWNMVSVEE LDDSVSIKIA
410 420 430 440 450
KEAVMNINKL GSLFKPTDGF LDTKIYFAGL PRKVESALIK PINPRLDGCI
460 470 480 490 500
RGWNLMKQGA LGAKEIVEGK QNKHCFLTVE KGSYYPGSGI AQFSIDYNNV
510 520 530 540 550
TNAEGWQINV TLNIRPSTGT GVMLALVSGD TVPFALSLVD SGSGTSQDIL
560 570 580 590 600
VFVENSVAAH LEAITLCSEQ PSQLKCNINR NGLELWTPVR KDVIYSKDLQ
610 620 630 640 650
RQLAILDKTM KGTVATYLGG VPDISFSATP VNAFYSGCME VNINGVQLDL
660 670
DEAISKHNDI RAHSCPSVRK IQKNF
Length:675
Mass (Da):74,627
Last modified:October 1, 1996 - v1
Checksum:iB4338F756B486075
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S78744 mRNA. Translation: AAC60704.1.
PIRiJC4180. KXRTS.
UniGeneiRn.2888.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S78744 mRNA. Translation: AAC60704.1.
PIRiJC4180. KXRTS.
UniGeneiRn.2888.

3D structure databases

ProteinModelPortaliP53813.
SMRiP53813. Positions 46-86, 200-283.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000064737.

Proteomic databases

PaxDbiP53813.
PRIDEiP53813.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

RGDi620971. Pros1.

Phylogenomic databases

eggNOGiENOG410IGF6. Eukaryota.
ENOG410ZTGU. LUCA.
HOVERGENiHBG051702.
InParanoidiP53813.
PhylomeDBiP53813.

Miscellaneous databases

PROiP53813.

Family and domain databases

Gene3Di2.60.120.200. 2 hits.
4.10.740.10. 1 hit.
InterProiIPR017857. Coagulation_fac_subgr_Gla_dom.
IPR013320. ConA-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR000294. GLA_domain.
IPR009030. Growth_fac_rcpt_.
IPR001791. Laminin_G.
IPR033189. PROS1.
[Graphical view]
PANTHERiPTHR24040:SF0. PTHR24040:SF0. 1 hit.
PfamiPF00008. EGF. 1 hit.
PF07645. EGF_CA. 3 hits.
PF00594. Gla. 1 hit.
PF00054. Laminin_G_1. 1 hit.
[Graphical view]
PRINTSiPR00001. GLABLOOD.
SMARTiSM00181. EGF. 4 hits.
SM00179. EGF_CA. 4 hits.
SM00069. GLA. 1 hit.
SM00282. LamG. 2 hits.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 2 hits.
SSF57184. SSF57184. 1 hit.
SSF57630. SSF57630. 1 hit.
PROSITEiPS00010. ASX_HYDROXYL. 4 hits.
PS00022. EGF_1. 1 hit.
PS01186. EGF_2. 3 hits.
PS50026. EGF_3. 4 hits.
PS01187. EGF_CA. 3 hits.
PS00011. GLA_1. 1 hit.
PS50998. GLA_2. 1 hit.
PS50025. LAM_G_DOMAIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPROS_RAT
AccessioniPrimary (citable) accession number: P53813
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: May 11, 2016
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 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.