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Protein

Neuroserpin

Gene

SERPINI1

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

Functioni

Serine protease inhibitor that inhibits plasminogen activators and plasmin but not thrombin (PubMed:9442076, PubMed:26329378, PubMed:19265707, PubMed:19285087, PubMed:11880376). May be involved in the formation or reorganization of synaptic connections as well as for synaptic plasticity in the adult nervous system. May protect neurons from cell damage by tissue-type plasminogen activator (Probable).Curated5 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei362 – 363Reactive bond1 Publication1 Publication2

GO - Molecular functioni

  • serine-type endopeptidase inhibitor activity Source: UniProtKB

GO - Biological processi

  • central nervous system development Source: ProtInc
  • peripheral nervous system development Source: ProtInc
  • positive regulation of neuron projection development Source: Ensembl
  • regulation of cell adhesion Source: Ensembl

Keywordsi

Molecular functionProtease inhibitor, Serine protease inhibitor

Protein family/group databases

MEROPSiI04.025.

Names & Taxonomyi

Protein namesi
Recommended name:
Neuroserpin
Alternative name(s):
Peptidase inhibitor 12
Short name:
PI-12
Serpin I1
Gene namesi
Name:SERPINI1
Synonyms:PI12
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

EuPathDBiHostDB:ENSG00000163536.12.
HGNCiHGNC:8943. SERPINI1.

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

Cytoplasmic vesicle, Secreted

Pathology & Biotechi

Involvement in diseasei

Encephalopathy, familial, with neuroserpin inclusion bodies (FENIB)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA neurodegenerative disease clinically characterized by dementia. Additional features include intellectual decline, psychic seizures, progressive myoclonic epilepsy, and cerebral atrophy. Histologically, it is characterized by the presence of eosinophilic inclusion bodies (called Collins bodies) throughout the deeper layers of the cerebral cortex, leading to neuronal death.
See also OMIM:604218
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00852049S → P in FENIB; Syracuse; decreased protein stability; decreased proteinase inhibitor activity; increased tendency to form polymers. 2 PublicationsCorresponds to variant dbSNP:rs121909051Ensembl.1
Natural variantiVAR_00852152S → R in FENIB; Portland. 1 Publication1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi161N → G: Increases protein stability and abolishes tendency to form polymers. No effect on inhibitory activity. 1 Publication1
Mutagenesisi162L → K: Increases protein stability and abolishes tendency to form polymers. No effect on inhibitory activity. 1 Publication1
Mutagenesisi163V → I: Increases protein stability and decreases tendency to form polymers. No effect on inhibitory activity. 1 Publication1
Mutagenesisi289E → A: Slightly decreases inhibitory activity. No effect on thermal stability. 1 Publication1
Mutagenesisi340S → A: Increases protein stability and decreases tendency to form polymers. No effect on inhibitory activity. 1 Publication1

Keywords - Diseasei

Disease mutation, Neurodegeneration

Organism-specific databases

DisGeNETi5274.
MalaCardsiSERPINI1.
MIMi604218. phenotype.
OpenTargetsiENSG00000163536.
Orphaneti85110. Familial encephalopathy with neuroserpin inclusion bodies.
PharmGKBiPA35511.

Polymorphism and mutation databases

BioMutaiSERPINI1.
DMDMi3183087.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 16Sequence analysisAdd BLAST16
ChainiPRO_000003252117 – 410NeuroserpinAdd BLAST394

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi157N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi321N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi401N-linked (GlcNAc...) asparagineSequence analysis1

Keywords - PTMi

Glycoprotein

Proteomic databases

EPDiQ99574.
MaxQBiQ99574.
PaxDbiQ99574.
PeptideAtlasiQ99574.
PRIDEiQ99574.

PTM databases

iPTMnetiQ99574.
PhosphoSitePlusiQ99574.

Miscellaneous databases

PMAP-CutDBiQ99574.

Expressioni

Tissue specificityi

Detected in brain cortex and hippocampus pyramidal neurons (at protein level) (PubMed:17040209). Predominantly expressed in the brain (PubMed:9070919).2 Publications

Gene expression databases

BgeeiENSG00000163536.
CleanExiHS_SERPINI1.
ExpressionAtlasiQ99574. baseline and differential.
GenevisibleiQ99574. HS.

Organism-specific databases

HPAiCAB026059.
HPA001565.
HPA056092.

Interactioni

Subunit structurei

Monomer. Has a tendency to form large polymers already at 41 and 45 degrees Celsius (in vitro).2 Publications

Protein-protein interaction databases

BioGridi111292. 3 interactors.
IntActiQ99574. 1 interactor.
STRINGi9606.ENSP00000295777.

Structurei

Secondary structure

1410
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi25 – 40Combined sources16
Beta strandi46 – 48Combined sources3
Helixi50 – 63Combined sources14
Helixi66 – 76Combined sources11
Helixi86 – 91Combined sources6
Turni101 – 103Combined sources3
Beta strandi105 – 115Combined sources11
Helixi122 – 132Combined sources11
Beta strandi135 – 139Combined sources5
Helixi144 – 157Combined sources14
Turni158 – 161Combined sources4
Helixi169 – 171Combined sources3
Beta strandi176 – 192Combined sources17
Helixi196 – 198Combined sources3
Beta strandi200 – 205Combined sources6
Beta strandi211 – 229Combined sources19
Beta strandi238 – 246Combined sources9
Beta strandi249 – 257Combined sources9
Helixi264 – 267Combined sources4
Helixi268 – 270Combined sources3
Helixi273 – 282Combined sources10
Beta strandi284 – 293Combined sources10
Beta strandi295 – 302Combined sources8
Helixi303 – 310Combined sources8
Helixi314 – 316Combined sources3
Turni323 – 325Combined sources3
Beta strandi331 – 344Combined sources14
Beta strandi346 – 361Combined sources16
Beta strandi369 – 371Combined sources3
Beta strandi376 – 382Combined sources7
Turni383 – 385Combined sources3
Beta strandi388 – 395Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3F02X-ray1.80A/B17-362[»]
C/D363-410[»]
3F5NX-ray3.15A/B/C/D/E17-410[»]
3FGQX-ray2.09A/B17-400[»]
ProteinModelPortaliQ99574.
SMRiQ99574.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ99574.

Family & Domainsi

Sequence similaritiesi

Belongs to the serpin family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG2392. Eukaryota.
COG4826. LUCA.
GeneTreeiENSGT00900000140788.
HOGENOMiHOG000238519.
HOVERGENiHBG005957.
InParanoidiQ99574.
OMAiVQNGFHV.
OrthoDBiEOG091G0ION.
PhylomeDBiQ99574.
TreeFamiTF352620.

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.

Sequencei

Sequence statusi: Complete.

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

Q99574-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAFLGLFSLL VLQSMATGAT FPEEAIADLS VNMYNRLRAT GEDENILFSP
60 70 80 90 100
LSIALAMGMM ELGAQGSTQK EIRHSMGYDS LKNGEEFSFL KEFSNMVTAK
110 120 130 140 150
ESQYVMKIAN SLFVQNGFHV NEEFLQMMKK YFNAAVNHVD FSQNVAVANY
160 170 180 190 200
INKWVENNTN NLVKDLVSPR DFDAATYLAL INAVYFKGNW KSQFRPENTR
210 220 230 240 250
TFSFTKDDES EVQIPMMYQQ GEFYYGEFSD GSNEAGGIYQ VLEIPYEGDE
260 270 280 290 300
ISMMLVLSRQ EVPLATLEPL VKAQLVEEWA NSVKKQKVEV YLPRFTVEQE
310 320 330 340 350
IDLKDVLKAL GITEIFIKDA NLTGLSDNKE IFLSKAIHKS FLEVNEEGSE
360 370 380 390 400
AAAVSGMIAI SRMAVLYPQV IVDHPFFFLI RNRRTGTILF MGRVMHPETM
410
NTSGHDFEEL
Length:410
Mass (Da):46,427
Last modified:May 1, 1997 - v1
Checksum:iD966E9036BB21943
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti70K → E in AAH18043 (PubMed:15489334).Curated1
Sequence conflicti326S → Y in AAH18043 (PubMed:15489334).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00852049S → P in FENIB; Syracuse; decreased protein stability; decreased proteinase inhibitor activity; increased tendency to form polymers. 2 PublicationsCorresponds to variant dbSNP:rs121909051Ensembl.1
Natural variantiVAR_00852152S → R in FENIB; Portland. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z81326 mRNA. Translation: CAB03626.1.
AF248246, AF248244, AF248245 Genomic DNA. Translation: AAG01089.1.
AK290082 mRNA. Translation: BAF82771.1.
CR627434 mRNA. Translation: CAH10520.1.
CH471052 Genomic DNA. Translation: EAW78571.1.
CH471052 Genomic DNA. Translation: EAW78572.1.
CH471052 Genomic DNA. Translation: EAW78573.1.
BC018043 mRNA. Translation: AAH18043.1.
CCDSiCCDS3203.1.
RefSeqiNP_001116224.1. NM_001122752.1.
NP_005016.1. NM_005025.4.
XP_016862107.1. XM_017006618.1.
UniGeneiHs.478153.

Genome annotation databases

EnsembliENST00000295777; ENSP00000295777; ENSG00000163536.
ENST00000446050; ENSP00000397373; ENSG00000163536.
GeneIDi5274.
KEGGihsa:5274.
UCSCiuc003ffa.5. human.

Similar proteinsi

Entry informationi

Entry nameiNEUS_HUMAN
AccessioniPrimary (citable) accession number: Q99574
Secondary accession number(s): A8K217, D3DNP1, Q6AHZ4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: May 1, 1997
Last modified: October 25, 2017
This is version 158 of the entry and version 1 of the sequence. See 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: 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. SIMILARITY comments
    Index of protein domains and families