Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Latexin

Gene

Lxn

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Hardly reversible, non-competitive, and potent inhibitor of CPA1, CPA2 and CPA4 (By similarity). May play a role in inflammation.By similarity1 Publication

GO - Molecular functioni

  • heparin binding Source: UniProtKB-KW
  • metalloendopeptidase inhibitor activity Source: MGI

GO - Biological processi

  • detection of temperature stimulus involved in sensory perception of pain Source: MGI
  • inflammatory response Source: UniProtKB-KW
  • negative regulation of endopeptidase activity Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Metalloenzyme inhibitor, Metalloprotease inhibitor, Protease inhibitor

Keywords - Biological processi

Inflammatory response

Keywords - Ligandi

Heparin-binding

Protein family/group databases

MEROPSiI47.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Latexin
Alternative name(s):
Endogenous carboxypeptidase inhibitor
Short name:
ECI
Tissue carboxypeptidase inhibitor
Short name:
TCI
Gene namesi
Name:Lxn
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:107633. Lxn.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 222222LatexinPRO_0000191344Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei55 – 551N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP70202.
PaxDbiP70202.
PRIDEiP70202.

2D gel databases

UCD-2DPAGEP70202.

PTM databases

iPTMnetiP70202.
PhosphoSiteiP70202.

Expressioni

Tissue specificityi

Highly enriched in macrophages.1 Publication

Inductioni

By CSF1 and lipopolysaccharides (LPS).1 Publication

Gene expression databases

BgeeiP70202.
CleanExiMM_LXN.
ExpressionAtlasiP70202. baseline and differential.
GenevisibleiP70202. MM.

Interactioni

Protein-protein interaction databases

IntActiP70202. 1 interaction.
MINTiMINT-4100751.
STRINGi10090.ENSMUSP00000060732.

Structurei

Secondary structure

1
222
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi8 – 2518Combined sources
Beta strandi32 – 4514Combined sources
Turni46 – 483Combined sources
Beta strandi49 – 6012Combined sources
Turni61 – 633Combined sources
Beta strandi67 – 7610Combined sources
Beta strandi86 – 938Combined sources
Helixi100 – 11213Combined sources
Beta strandi118 – 1236Combined sources
Helixi131 – 1333Combined sources
Helixi134 – 15118Combined sources
Beta strandi158 – 16912Combined sources
Beta strandi172 – 1743Combined sources
Beta strandi176 – 18611Combined sources
Turni187 – 1904Combined sources
Beta strandi191 – 20212Combined sources
Turni203 – 2053Combined sources
Beta strandi206 – 2149Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WNHX-ray1.83A1-222[»]
ProteinModelPortaliP70202.
SMRiP70202. Positions 1-217.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP70202.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 9797Cystatin-like fold 1Add
BLAST
Regioni98 – 11720Alpha-helical linkerAdd
BLAST
Regioni118 – 222105Cystatin-like fold 2Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG410IHYK. Eukaryota.
ENOG4111KGW. LUCA.
HOGENOMiHOG000113410.
HOVERGENiHBG052373.
InParanoidiP70202.
OMAiCLKFSVE.
OrthoDBiEOG783MWF.
PhylomeDBiP70202.
TreeFamiTF332787.

Family and domain databases

InterProiIPR009684. Prot_inh_latexin.
[Graphical view]
PfamiPF06907. Latexin. 1 hit.
[Graphical view]
PIRSFiPIRSF011132. Prot_inh_latexin. 1 hit.
ProDomiPD023134. Prot_inh_latexin. 1 hit.
[Graphical view] [Entries sharing at least one domain]

Sequencei

Sequence statusi: Complete.

P70202-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEIPPTHYAA SRAASVAENC INYQQGTPHK LFLVQTVQQA SKEDIPGRGH
60 70 80 90 100
KYHLKFSVEE IIQKQVTVNC TAEVLYPQMG QGSAPEVNFT FEGEIGKNPD
110 120 130 140 150
EEDNTFYQSL MSLKRPLEAQ DIPDNFGNVS PQMKPVQHLA WVACGYVMWQ
160 170 180 190 200
NSTEDTWYKM LKIQTVKQVQ RNDDFIELDY TILLHDIASQ EIIPWQMQVL
210 220
WHPQYGTKVK HNSRLPKEGQ AE
Length:222
Mass (Da):25,492
Last modified:July 5, 2004 - v2
Checksum:i2A7686E6206C9766
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti18 – 181E → K in BAA13700 (PubMed:9119386).Curated
Sequence conflicti95 – 951I → V in BAA13700 (PubMed:9119386).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D88769 mRNA. Translation: BAA13700.1.
AK032170 mRNA. Translation: BAC27739.1.
AK149981 mRNA. Translation: BAE29211.1.
CCDSiCCDS17397.1.
RefSeqiNP_058033.2. NM_016753.4.
UniGeneiMm.2632.

Genome annotation databases

EnsembliENSMUST00000058981; ENSMUSP00000060732; ENSMUSG00000047557.
GeneIDi17035.
KEGGimmu:17035.
UCSCiuc008pln.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D88769 mRNA. Translation: BAA13700.1.
AK032170 mRNA. Translation: BAC27739.1.
AK149981 mRNA. Translation: BAE29211.1.
CCDSiCCDS17397.1.
RefSeqiNP_058033.2. NM_016753.4.
UniGeneiMm.2632.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WNHX-ray1.83A1-222[»]
ProteinModelPortaliP70202.
SMRiP70202. Positions 1-217.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP70202. 1 interaction.
MINTiMINT-4100751.
STRINGi10090.ENSMUSP00000060732.

Protein family/group databases

MEROPSiI47.001.

PTM databases

iPTMnetiP70202.
PhosphoSiteiP70202.

2D gel databases

UCD-2DPAGEP70202.

Proteomic databases

EPDiP70202.
PaxDbiP70202.
PRIDEiP70202.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000058981; ENSMUSP00000060732; ENSMUSG00000047557.
GeneIDi17035.
KEGGimmu:17035.
UCSCiuc008pln.1. mouse.

Organism-specific databases

CTDi56925.
MGIiMGI:107633. Lxn.

Phylogenomic databases

eggNOGiENOG410IHYK. Eukaryota.
ENOG4111KGW. LUCA.
HOGENOMiHOG000113410.
HOVERGENiHBG052373.
InParanoidiP70202.
OMAiCLKFSVE.
OrthoDBiEOG783MWF.
PhylomeDBiP70202.
TreeFamiTF332787.

Miscellaneous databases

EvolutionaryTraceiP70202.
NextBioi291144.
PROiP70202.
SOURCEiSearch...

Gene expression databases

BgeeiP70202.
CleanExiMM_LXN.
ExpressionAtlasiP70202. baseline and differential.
GenevisibleiP70202. MM.

Family and domain databases

InterProiIPR009684. Prot_inh_latexin.
[Graphical view]
PfamiPF06907. Latexin. 1 hit.
[Graphical view]
PIRSFiPIRSF011132. Prot_inh_latexin. 1 hit.
ProDomiPD023134. Prot_inh_latexin. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Mapping to mouse chromosome 3 of the gene encoding latexin (Lxn) expressed in neocortical neurons in a region-specific manner."
    Jin M.-H., Uratani Y., Arimatsu Y.
    Genomics 39:419-421(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Bone marrow and Olfactory bulb.
  3. Lubec G., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 13-42 AND 160-167, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6J.
    Tissue: Brain.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen and Testis.
  5. "An inflammatory role for the mammalian carboxypeptidase inhibitor latexin: relationship to cystatins and the tumor suppressor TIG1."
    Aagaard A., Listwan P., Cowieson N., Huber T., Ravasi T., Wells C.A., Flanagan J.U., Kellie S., Hume D.A., Kobe B., Martin J.L.
    Structure 13:309-317(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS), INDUCTION, CYSTATIN-LIKE REGIONS, FUNCTION, TISSUE SPECIFICITY.

Entry informationi

Entry nameiLXN_MOUSE
AccessioniPrimary (citable) accession number: P70202
Secondary accession number(s): Q3UDQ0, Q8CCS8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2004
Last sequence update: July 5, 2004
Last modified: March 16, 2016
This is version 109 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

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

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.