LXN_MOUSE
ID LXN_MOUSE Reviewed; 222 AA.
AC P70202; Q3UDQ0; Q8CCS8;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Latexin;
DE AltName: Full=Endogenous carboxypeptidase inhibitor;
DE Short=ECI;
DE AltName: Full=Tissue carboxypeptidase inhibitor;
DE Short=TCI;
GN Name=Lxn;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9119386; DOI=10.1006/geno.1996.4469;
RA Jin M.-H., Uratani Y., Arimatsu Y.;
RT "Mapping to mouse chromosome 3 of the gene encoding latexin (Lxn) expressed
RT in neocortical neurons in a region-specific manner.";
RL Genomics 39:419-421(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, and Olfactory bulb;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP PROTEIN SEQUENCE OF 13-42 AND 160-167, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS), INDUCTION, CYSTATIN-LIKE REGIONS,
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15698574; DOI=10.1016/j.str.2004.12.013;
RA Aagaard A., Listwan P., Cowieson N., Huber T., Ravasi T., Wells C.A.,
RA Flanagan J.U., Kellie S., Hume D.A., Kobe B., Martin J.L.;
RT "An inflammatory role for the mammalian carboxypeptidase inhibitor latexin:
RT relationship to cystatins and the tumor suppressor TIG1.";
RL Structure 13:309-317(2005).
CC -!- FUNCTION: Hardly reversible, non-competitive, and potent inhibitor of
CC CPA1, CPA2 and CPA4 (By similarity). May play a role in inflammation.
CC {ECO:0000250, ECO:0000269|PubMed:15698574}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Highly enriched in macrophages.
CC {ECO:0000269|PubMed:15698574}.
CC -!- INDUCTION: By CSF1 and lipopolysaccharides (LPS).
CC {ECO:0000269|PubMed:15698574}.
CC -!- SIMILARITY: Belongs to the protease inhibitor I47 (latexin) family.
CC {ECO:0000305}.
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DR EMBL; D88769; BAA13700.1; -; mRNA.
DR EMBL; AK032170; BAC27739.1; -; mRNA.
DR EMBL; AK149981; BAE29211.1; -; mRNA.
DR CCDS; CCDS17397.1; -.
DR RefSeq; NP_058033.2; NM_016753.4.
DR PDB; 1WNH; X-ray; 1.83 A; A=1-222.
DR PDBsum; 1WNH; -.
DR AlphaFoldDB; P70202; -.
DR PCDDB; P70202; -.
DR SMR; P70202; -.
DR BioGRID; 201231; 1.
DR STRING; 10090.ENSMUSP00000060732; -.
DR MEROPS; I47.001; -.
DR iPTMnet; P70202; -.
DR PhosphoSitePlus; P70202; -.
DR SwissPalm; P70202; -.
DR UCD-2DPAGE; P70202; -.
DR EPD; P70202; -.
DR PaxDb; P70202; -.
DR PeptideAtlas; P70202; -.
DR PRIDE; P70202; -.
DR ProteomicsDB; 292056; -.
DR Antibodypedia; 2121; 655 antibodies from 36 providers.
DR DNASU; 17035; -.
DR Ensembl; ENSMUST00000058981; ENSMUSP00000060732; ENSMUSG00000047557.
DR GeneID; 17035; -.
DR KEGG; mmu:17035; -.
DR UCSC; uc008pln.1; mouse.
DR CTD; 56925; -.
DR MGI; MGI:107633; Lxn.
DR VEuPathDB; HostDB:ENSMUSG00000047557; -.
DR eggNOG; ENOG502RYUY; Eukaryota.
DR GeneTree; ENSGT00530000063813; -.
DR HOGENOM; CLU_083048_0_0_1; -.
DR InParanoid; P70202; -.
DR OMA; MWQNSTE; -.
DR OrthoDB; 1129396at2759; -.
DR PhylomeDB; P70202; -.
DR TreeFam; TF332787; -.
DR BioGRID-ORCS; 17035; 4 hits in 70 CRISPR screens.
DR ChiTaRS; Lxn; mouse.
DR EvolutionaryTrace; P70202; -.
DR PRO; PR:P70202; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; P70202; protein.
DR Bgee; ENSMUSG00000047557; Expressed in facial nucleus and 262 other tissues.
DR ExpressionAtlas; P70202; baseline and differential.
DR Genevisible; P70202; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR GO; GO:0008191; F:metalloendopeptidase inhibitor activity; IMP:MGI.
DR GO; GO:0050965; P:detection of temperature stimulus involved in sensory perception of pain; IMP:MGI.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR InterPro; IPR046350; Cystatin_sf.
DR InterPro; IPR009684; Prot_inh_latexin.
DR PANTHER; PTHR28591; PTHR28591; 1.
DR Pfam; PF06907; Latexin; 1.
DR PIRSF; PIRSF011132; Prot_inh_latexin; 1.
DR SUPFAM; SSF54403; SSF54403; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW Heparin-binding; Inflammatory response; Metalloenzyme inhibitor;
KW Metalloprotease inhibitor; Protease inhibitor; Reference proteome; Repeat.
FT CHAIN 1..222
FT /note="Latexin"
FT /id="PRO_0000191344"
FT REGION 1..97
FT /note="Cystatin-like fold 1"
FT REGION 98..117
FT /note="Alpha-helical linker"
FT REGION 118..222
FT /note="Cystatin-like fold 2"
FT MOD_RES 55
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9BS40"
FT CONFLICT 18
FT /note="E -> K (in Ref. 1; BAA13700)"
FT /evidence="ECO:0000305"
FT CONFLICT 95
FT /note="I -> V (in Ref. 1; BAA13700)"
FT /evidence="ECO:0000305"
FT HELIX 8..25
FT /evidence="ECO:0007829|PDB:1WNH"
FT STRAND 32..45
FT /evidence="ECO:0007829|PDB:1WNH"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:1WNH"
FT STRAND 49..60
FT /evidence="ECO:0007829|PDB:1WNH"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:1WNH"
FT STRAND 67..76
FT /evidence="ECO:0007829|PDB:1WNH"
FT STRAND 86..93
FT /evidence="ECO:0007829|PDB:1WNH"
FT HELIX 100..112
FT /evidence="ECO:0007829|PDB:1WNH"
FT STRAND 118..123
FT /evidence="ECO:0007829|PDB:1WNH"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:1WNH"
FT HELIX 134..151
FT /evidence="ECO:0007829|PDB:1WNH"
FT STRAND 158..169
FT /evidence="ECO:0007829|PDB:1WNH"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:1WNH"
FT STRAND 176..186
FT /evidence="ECO:0007829|PDB:1WNH"
FT TURN 187..190
FT /evidence="ECO:0007829|PDB:1WNH"
FT STRAND 191..202
FT /evidence="ECO:0007829|PDB:1WNH"
FT TURN 203..205
FT /evidence="ECO:0007829|PDB:1WNH"
FT STRAND 206..214
FT /evidence="ECO:0007829|PDB:1WNH"
SQ SEQUENCE 222 AA; 25492 MW; 2A7686E6206C9766 CRC64;
MEIPPTHYAA SRAASVAENC INYQQGTPHK LFLVQTVQQA SKEDIPGRGH KYHLKFSVEE
IIQKQVTVNC TAEVLYPQMG QGSAPEVNFT FEGEIGKNPD EEDNTFYQSL MSLKRPLEAQ
DIPDNFGNVS PQMKPVQHLA WVACGYVMWQ NSTEDTWYKM LKIQTVKQVQ RNDDFIELDY
TILLHDIASQ EIIPWQMQVL WHPQYGTKVK HNSRLPKEGQ AE
