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Protein

Plasma serine protease inhibitor

Gene

SERPINA5

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Heparin-dependent serine protease inhibitor acting in body fluids and secretions. Inactivates serine proteases by binding irreversibly to their serine activation site. Involved in the regulation of intravascular and extravascular proteolytic activities. Plays hemostatic roles in the blood plasma. Acts as a procoagulant and proinflammatory factor by inhibiting the anticoagulant activated protein C factor as well as the generation of activated protein C factor by the thrombin/thrombomodulin complex. Acts as an anticoagulant factor by inhibiting blood coagulation factors like prothrombin, factor XI, factor Xa, plasma kallikrein and fibrinolytic enzymes such as tissue- and urinary-type plasminogen activators. In seminal plasma, inactivates several serine proteases implicated in the reproductive system. Inhibits the serpin acrosin; indirectly protects component of the male genital tract from being degraded by excessive released acrosin. Inhibits tissue-and urinary-type plasminogen activator, prostate-specific antigen and kallikrein activities; has a control on the sperm motility and fertilization. Inhibits the activated protein C-catalyzed degradation of SEMG1 and SEMG2; regulates the degradation of semenogelin during the process of transfer of spermatozoa from the male reproductive tract into the female tract. In urine, inhibits urinary-type plasminogen activator and kallikrein activities. Inactivates membrane-anchored serine proteases activities such as MPRSS7 and TMPRSS11E. Inhibits urinary-type plasminogen activator-dependent tumor cell invasion and metastasis. May also play a non-inhibitory role in seminal plasma and urine as a hydrophobic hormone carrier by its binding to retinoic acid.18 Publications

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Its inhibitory activity is greatly enhanced in the presence of glycosaminoglycans, heparin, thrombomodulin and phospholipids vesicles.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei373 – 374Reactive bond2

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

  • blood coagulation Source: Reactome
  • fusion of sperm to egg plasma membrane involved in single fertilization Source: UniProtKB
  • lipid transport Source: UniProtKB-KW
  • negative regulation of endopeptidase activity Source: GO_Central
  • negative regulation of hydrolase activity Source: UniProtKB
  • seminal vesicle development Source: Ensembl
  • spermatogenesis Source: UniProtKB

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHeparin-binding, Protease inhibitor, Serine protease inhibitor
Biological processFertilization, Lipid transport, Transport

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-140837 Intrinsic Pathway of Fibrin Clot Formation
R-HSA-140875 Common Pathway of Fibrin Clot Formation

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P05154

Protein family/group databases

MEROPS protease database

More...
MEROPSi
I04.004

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Plasma serine protease inhibitor
Alternative name(s):
Acrosomal serine protease inhibitor
Plasminogen activator inhibitor 3
Short name:
PAI-3
Short name:
PAI3
Protein C inhibitor
Short name:
PCI
Serpin A5
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:SERPINA5
Synonyms:PCI, PLANH3, PROCI
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 14

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
HostDB:ENSG00000188488.13

Human Gene Nomenclature Database

More...
HGNCi
HGNC:8723 SERPINA5

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
601841 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P05154

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi248R → E: Does not change the rate of thrombin or activated protein C/F5 inhibition in the presence or absence of heparin. Strongly reduces the rate of thrombin inhibition in the presence of heparin. 1 Publication1
Mutagenesisi253R → E: Inhibits strongly thrombomodulin-enhanced rate of thrombin inhibition in presence of heparin. 1 Publication1
Mutagenesisi272E → K: Does not inhibit thrombomodulin-enhanced rate of thrombin inhibition in presence of heparin. 1 Publication1
Mutagenesisi274K → E: Does not inhibit thrombomodulin-enhanced rate of thrombin inhibition in presence of heparin. 1 Publication1
Mutagenesisi285K → E: Does not change the rate of thrombin or activated protein C/F5 inhibition in the presence or absence of heparin. Slightly reduces the rate of thrombin inhibition in the presence of heparin. Does not inhibit thrombomodulin-enhanced rate of thrombin inhibition in presence of heparin. 2 Publications1
Mutagenesisi288R → E: Does not change the rate of thrombin or activated protein C/F5 inhibition in the presence or absence of heparin. Slightly reduces the rate of thrombin inhibition in the presence of heparin. Does not inhibit thrombomodulin-enhanced rate of thrombin inhibition in presence of heparin. 2 Publications1
Mutagenesisi289K → E: Does not change the rate of thrombin or activated protein C/F5 inhibition in the presence or absence of heparin. Slightly reduces the rate of thrombin inhibition in the presence of heparin. Inhibits weakly thrombomodulin-enhanced rate of thrombin inhibition in presence of heparin. 2 Publications1
Mutagenesisi292K → E: Does not change the rate of thrombin or activated protein C/F5 inhibition in the presence or absence of heparin. Slightly reduces the rate of thrombin inhibition in the presence of heparin. Does not inhibit thrombomodulin-enhanced rate of thrombin inhibition in presence of heparin. 2 Publications1
Mutagenesisi360T → R: Inhibits heterodimer formation with TMPRSS11E. 1 Publication1
Mutagenesisi371T → R: Increases inhibition of activated protein C/F5 and factor XI/F11 activities. Decreases inhibition of thrombin activity. 1 Publication1
Mutagenesisi372F → P or G: Increases inhibition of thrombin activity. 1 Publication1
Mutagenesisi373R → P: Increases inhibition of thrombin activity. Inhibits heterodimer formation with TMPRSS11E. 2 Publications1
Mutagenesisi376R → P: Does not change inhibition of thrombin, activated protein C/F5 and factor XI/F11 activities. 1 Publication1
Mutagenesisi381R → E: Does not inhibit thrombomodulin-enhanced rate of thrombin inhibition in presence of heparin. 1 Publication1

Organism-specific databases

DisGeNET

More...
DisGeNETi
5104

Open Targets

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OpenTargetsi
ENSG00000188488

Chemistry databases

Drug and drug target database

More...
DrugBanki
DB00055 Drotrecogin alfa
DB05413 T-1249
DB00013 Urokinase

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
SERPINA5

Domain mapping of disease mutations (DMDM)

More...
DMDMi
322510122

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 191 PublicationAdd BLAST19
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_000041409120 – 25Removed in mature form6
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000003242726 – 406Plasma serine protease inhibitorAdd BLAST381

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi39O-linked (GalNAc...) threonine2 Publications1
Glycosylationi249N-linked (GlcNAc...) asparagine2 Publications1
Glycosylationi262N-linked (GlcNAc...) asparagine3 Publications1
Glycosylationi338N-linked (GlcNAc...) asparagine2 Publications1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

N- and O-glycosylated. N-glycosylation consists of a mixture of sialylated bi- (including sialyl-Lewis X epitopes), tri- and tetra-antennary complex-type chains; affects the maximal heparin- and thrombomodulin-enhanced rates of thrombin inhibition. O-glycosylated with core 1 or possibly core 8 glycans. Further modified with 2 sialic acid residues.6 Publications
Proteolytically cleaved. Inhibition of proteases is accompanied by formation of a stable enzyme-inhibitor complex and by degradation of the serpin to lower molecular weight derivatives. Proteolytically cleaved at the N-terminus; inhibits slightly the heparin- and thrombomodulin-enhanced rates of thrombin inhibition.2 Publications

Keywords - PTMi

Glycoprotein

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P05154

MaxQB - The MaxQuant DataBase

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MaxQBi
P05154

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P05154

PeptideAtlas

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PeptideAtlasi
P05154

PRoteomics IDEntifications database

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PRIDEi
P05154

ProteomicsDB human proteome resource

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ProteomicsDBi
51805

PTM databases

GlyConnect protein glycosylation platform

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GlyConnecti
663

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P05154

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
P05154

UniCarbKB; an annotated and curated database of glycan structures

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UniCarbKBi
P05154

Miscellaneous databases

CutDB - Proteolytic event database

More...
PMAP-CutDBi
P05154

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Predominantly expressed in the epithelium of seminal vesicles. Expressed in the proximal tubular epithelium of the kidney. Expressed in the superficial and more differentiated epidermal keratinocytes of the skin. Expressed in megakaryocytes and platelets. Expressed poorly in kidney tumor cells compared to non tumor kidney tissues. Expressed in spermatozoa. Present in very high concentration in seminal plasma. Present in high concentration in plasma, synovial and Graaf follicle fluids. Present in low concentration in breast milk and in amniotic fluids. Present in very low concentration in urine, cerebrospinal fluids, saliva and tears (at protein level). Strongly expressed in liver. Expressed in kidney, spleen, pancreas, skeletal muscle, heart, testes, ovary, interstitial Leydig cells, epididymal glands, seminal vesicles and prostate.7 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000188488 Expressed in 161 organ(s), highest expression level in right testis

CleanEx database of gene expression profiles

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CleanExi
HS_SERPINA5

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P05154 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P05154 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
HPA056919

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Forms protease inhibiting heterodimers in extracellular body fluids with serine proteases such as activated protein C/coagulation factor V/F5, acrosin/ACR, chymotrypsinogen B/CTRB1, prothrombin/F2, factor Xa/F10, factor XI/F11, kallikrein/KLKB1, tissue kallikrein, trypsin/PRSS1, prostate specific antigen/KLK3, tissue plasminogen activator/PLAT and urinary plasminogen activator/PLAU. Forms membrane-anchored serine proteases inhibiting heterodimers with TMPRSS7 and TMPRSS11E. Interacts with SEMG2.2 Publications

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
111135, 24 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P05154

Database of interacting proteins

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DIPi
DIP-29869N

Protein interaction database and analysis system

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IntActi
P05154, 9 interactors

STRING: functional protein association networks

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STRINGi
9606.ENSP00000333203

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1406
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LQ8X-ray2.40A/C/E/G30-375[»]
B/D/F/H376-406[»]
1PAImodel-A20-373[»]
B374-406[»]
2HI9X-ray2.30A/B/C44-406[»]
2OL2X-ray2.00A/B36-406[»]
2PAImodel-A20-373[»]
B374-406[»]
3DY0X-ray1.55A37-372[»]
B379-406[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P05154

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P05154

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P05154

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The reactive center loop (RCL) extends out from the body of the protein and directs binding to the target protease. The protease cleaves the serpin at the reactive site within the RCL, establishing a covalent linkage between the carboxyl group of the serpin reactive site and the serine hydroxyl of the protease. The resulting inactive serpin-protease complex is highly stable.

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the serpin family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG2392 Eukaryota
COG4826 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000162217

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000238521

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG005957

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P05154

KEGG Orthology (KO)

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KOi
K03913

Identification of Orthologs from Complete Genome Data

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OMAi
VMVNYIF

Database of Orthologous Groups

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OrthoDBi
755773at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P05154

TreeFam database of animal gene trees

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TreeFami
TF343201

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR023795 Serpin_CS
IPR023796 Serpin_dom
IPR000215 Serpin_fam
IPR036186 Serpin_sf

The PANTHER Classification System

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PANTHERi
PTHR11461 PTHR11461, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF00079 Serpin, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00093 SERPIN, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF56574 SSF56574, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00284 SERPIN, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 8 potential isoforms that are computationally mapped.Show allAlign All

P05154-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MQLFLLLCLV LLSPQGASLH RHHPREMKKR VEDLHVGATV APSSRRDFTF
60 70 80 90 100
DLYRALASAA PSQSIFFSPV SISMSLAMLS LGAGSSTKMQ ILEGLGLNLQ
110 120 130 140 150
KSSEKELHRG FQQLLQELNQ PRDGFQLSLG NALFTDLVVD LQDTFVSAMK
160 170 180 190 200
TLYLADTFPT NFRDSAGAMK QINDYVAKQT KGKIVDLLKN LDSNAVVIMV
210 220 230 240 250
NYIFFKAKWE TSFNHKGTQE QDFYVTSETV VRVPMMSRED QYHYLLDRNL
260 270 280 290 300
SCRVVGVPYQ GNATALFILP SEGKMQQVEN GLSEKTLRKW LKMFKKRQLE
310 320 330 340 350
LYLPKFSIEG SYQLEKVLPS LGISNVFTSH ADLSGISNHS NIQVSEMVHK
360 370 380 390 400
AVVEVDESGT RAAAATGTIF TFRSARLNSQ RLVFNRPFLM FIVDNNILFL

GKVNRP
Length:406
Mass (Da):45,675
Last modified:February 8, 2011 - v3
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i2A8FF3DC33C77E04
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 8 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
G3V2M1G3V2M1_HUMAN
Plasma serine protease inhibitor
SERPINA5
231Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
G3V5Q9G3V5Q9_HUMAN
Plasma serine protease inhibitor
SERPINA5
301Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
G3V482G3V482_HUMAN
Plasma serine protease inhibitor
SERPINA5
144Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
G3V265G3V265_HUMAN
Plasma serine protease inhibitor
SERPINA5
157Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
G3V264G3V264_HUMAN
Plasma serine protease inhibitor
SERPINA5
172Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
G3V4B4G3V4B4_HUMAN
Plasma serine protease inhibitor
SERPINA5
86Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
G3V3F5G3V3F5_HUMAN
Plasma serine protease inhibitor
SERPINA5
90Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
G3V3Y3G3V3Y3_HUMAN
Plasma serine protease inhibitor
SERPINA5
24Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti28K → E in CAB45766 (PubMed:17974005).Curated1
Sequence conflicti221Q → L in AAB26244 (PubMed:8471250).Curated1
Sequence conflicti335G → R in AAA35688 (PubMed:3027058).Curated1
Sequence conflicti335G → R in AAB26244 (PubMed:8471250).Curated1
Sequence conflicti384F → S in AAB26244 (PubMed:8471250).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_01308044S → G1 PublicationCorresponds to variant dbSNP:rs2069975Ensembl.1
Natural variantiVAR_00710055A → V in allele PCI*B. 3 PublicationsCorresponds to variant dbSNP:rs6118Ensembl.1
Natural variantiVAR_01308164S → N9 PublicationsCorresponds to variant dbSNP:rs6115Ensembl.1
Natural variantiVAR_01308294G → V1 PublicationCorresponds to variant dbSNP:rs2069976Ensembl.1
Natural variantiVAR_007101105K → E in allele PCI*B. 3 PublicationsCorresponds to variant dbSNP:rs6119Ensembl.1
Natural variantiVAR_013083115L → P1 PublicationCorresponds to variant dbSNP:rs2069999Ensembl.1
Natural variantiVAR_013900121P → A1 PublicationCorresponds to variant dbSNP:rs6120Ensembl.1
Natural variantiVAR_013084217G → R2 PublicationsCorresponds to variant dbSNP:rs6114Ensembl.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
J02639 mRNA Translation: AAA35688.1
M68516 Genomic DNA Translation: AAA02811.1
S69366
, S69364, S69574, S69365 Genomic DNA Translation: AAB30461.1
U35464 mRNA Translation: AAB60386.1
AF361796 Genomic DNA Translation: AAK27240.1
AL049839 Genomic DNA No translation available.
BC008915 mRNA Translation: AAH08915.1
S58545 mRNA Translation: AAB26244.2
AL080185 mRNA Translation: CAB45766.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS9928.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A39339

NCBI Reference Sequences

More...
RefSeqi
NP_000615.3, NM_000624.5

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.159628
Hs.741309

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000329597; ENSP00000333203; ENSG00000188488
ENST00000553780; ENSP00000450837; ENSG00000188488
ENST00000554276; ENSP00000451610; ENSG00000188488
ENST00000554866; ENSP00000451126; ENSG00000188488

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
5104

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:5104

UCSC genome browser

More...
UCSCi
uc001ydm.3 human

Keywords - Coding sequence diversityi

Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

SeattleSNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02639 mRNA Translation: AAA35688.1
M68516 Genomic DNA Translation: AAA02811.1
S69366
, S69364, S69574, S69365 Genomic DNA Translation: AAB30461.1
U35464 mRNA Translation: AAB60386.1
AF361796 Genomic DNA Translation: AAK27240.1
AL049839 Genomic DNA No translation available.
BC008915 mRNA Translation: AAH08915.1
S58545 mRNA Translation: AAB26244.2
AL080185 mRNA Translation: CAB45766.1
CCDSiCCDS9928.1
PIRiA39339
RefSeqiNP_000615.3, NM_000624.5
UniGeneiHs.159628
Hs.741309

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LQ8X-ray2.40A/C/E/G30-375[»]
B/D/F/H376-406[»]
1PAImodel-A20-373[»]
B374-406[»]
2HI9X-ray2.30A/B/C44-406[»]
2OL2X-ray2.00A/B36-406[»]
2PAImodel-A20-373[»]
B374-406[»]
3DY0X-ray1.55A37-372[»]
B379-406[»]
ProteinModelPortaliP05154
SMRiP05154
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111135, 24 interactors
CORUMiP05154
DIPiDIP-29869N
IntActiP05154, 9 interactors
STRINGi9606.ENSP00000333203

Chemistry databases

DrugBankiDB00055 Drotrecogin alfa
DB05413 T-1249
DB00013 Urokinase

Protein family/group databases

MEROPSiI04.004

PTM databases

GlyConnecti663
iPTMnetiP05154
PhosphoSitePlusiP05154
UniCarbKBiP05154

Polymorphism and mutation databases

BioMutaiSERPINA5
DMDMi322510122

Proteomic databases

jPOSTiP05154
MaxQBiP05154
PaxDbiP05154
PeptideAtlasiP05154
PRIDEiP05154
ProteomicsDBi51805

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
5104
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000329597; ENSP00000333203; ENSG00000188488
ENST00000553780; ENSP00000450837; ENSG00000188488
ENST00000554276; ENSP00000451610; ENSG00000188488
ENST00000554866; ENSP00000451126; ENSG00000188488
GeneIDi5104
KEGGihsa:5104
UCSCiuc001ydm.3 human

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
5104
DisGeNETi5104
EuPathDBiHostDB:ENSG00000188488.13

GeneCards: human genes, protein and diseases

More...
GeneCardsi
SERPINA5

H-Invitational Database, human transcriptome db

More...
H-InvDBi
HIX0079547
HGNCiHGNC:8723 SERPINA5
HPAiHPA056919
MIMi601841 gene
neXtProtiNX_P05154
OpenTargetsiENSG00000188488

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG2392 Eukaryota
COG4826 LUCA
GeneTreeiENSGT00940000162217
HOGENOMiHOG000238521
HOVERGENiHBG005957
InParanoidiP05154
KOiK03913
OMAiVMVNYIF
OrthoDBi755773at2759
PhylomeDBiP05154
TreeFamiTF343201

Enzyme and pathway databases

ReactomeiR-HSA-140837 Intrinsic Pathway of Fibrin Clot Formation
R-HSA-140875 Common Pathway of Fibrin Clot Formation
SABIO-RKiP05154

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
SERPINA5 human
EvolutionaryTraceiP05154

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
Protein_C_inhibitor

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
5104
PMAP-CutDBiP05154

Protein Ontology

More...
PROi
PR:P05154

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000188488 Expressed in 161 organ(s), highest expression level in right testis
CleanExiHS_SERPINA5
ExpressionAtlasiP05154 baseline and differential
GenevisibleiP05154 HS

Family and domain databases

InterProiView protein in InterPro
IPR023795 Serpin_CS
IPR023796 Serpin_dom
IPR000215 Serpin_fam
IPR036186 Serpin_sf
PANTHERiPTHR11461 PTHR11461, 1 hit
PfamiView protein in Pfam
PF00079 Serpin, 1 hit
SMARTiView protein in SMART
SM00093 SERPIN, 1 hit
SUPFAMiSSF56574 SSF56574, 1 hit
PROSITEiView protein in PROSITE
PS00284 SERPIN, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiIPSP_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P05154
Secondary accession number(s): Q07616, Q9UG30
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: February 8, 2011
Last modified: January 16, 2019
This is version 204 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

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

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  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. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
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