LXN_RAT
ID LXN_RAT Reviewed; 223 AA.
AC Q64361;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 118.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=7524963; DOI=10.1111/j.1460-9568.1994.tb00592.x;
RA Hatanaka Y., Uratani Y., Takiguchi-Hayashi K., Omori A., Sato K.,
RA Miyamoto M., Arimatsu Y.;
RT "Intracortical regionality represented by specific transcription for a
RT novel protein, latexin.";
RL Eur. J. Neurosci. 6:973-982(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND FUNCTION.
RC TISSUE=Hypothalamus;
RX PubMed=8618874; DOI=10.1073/pnas.92.26.12225;
RA Normant E., Martres M.P., Schwartz J.C., Gros C.;
RT "Purification, cDNA cloning, functional expression, and characterization of
RT a 26-kDa endogenous mammalian carboxypeptidase inhibitor.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:12225-12229(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=10350638; DOI=10.1016/s0169-328x(99)00107-2;
RA Miyasaka N., Hatanaka Y., Jin M.H., Arimatsu Y.;
RT "Genomic organization and regulatory elements of the rat latexin gene,
RT which is expressed in a cell type-specific manner in both central and
RT peripheral nervous systems.";
RL Brain Res. Mol. Brain Res. 69:62-72(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 14-31; 66-79 AND 99-110, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Spinal cord;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (NOV-2006) to UniProtKB.
CC -!- FUNCTION: Hardly reversible, non-competitive, and potent inhibitor of
CC CPA1, CPA2 and CPA4. May play a role in inflammation (By similarity).
CC {ECO:0000250, ECO:0000269|PubMed:8618874}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the protease inhibitor I47 (latexin) family.
CC {ECO:0000305}.
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DR EMBL; X76985; CAA54290.1; -; mRNA.
DR EMBL; U40260; AAC52381.1; -; mRNA.
DR EMBL; Y18435; CAA77175.2; -; Genomic_DNA.
DR EMBL; BC081763; AAH81763.1; -; mRNA.
DR PIR; S41286; S41286.
DR RefSeq; NP_113843.1; NM_031655.1.
DR AlphaFoldDB; Q64361; -.
DR SMR; Q64361; -.
DR BioGRID; 248715; 2.
DR IntAct; Q64361; 1.
DR STRING; 10116.ENSRNOP00000018402; -.
DR MEROPS; I47.001; -.
DR iPTMnet; Q64361; -.
DR PhosphoSitePlus; Q64361; -.
DR jPOST; Q64361; -.
DR PaxDb; Q64361; -.
DR PRIDE; Q64361; -.
DR Ensembl; ENSRNOT00000018402; ENSRNOP00000018402; ENSRNOG00000013572.
DR GeneID; 59073; -.
DR KEGG; rno:59073; -.
DR UCSC; RGD:68361; rat.
DR CTD; 56925; -.
DR RGD; 68361; Lxn.
DR eggNOG; ENOG502RYUY; Eukaryota.
DR GeneTree; ENSGT00530000063813; -.
DR HOGENOM; CLU_083048_0_0_1; -.
DR InParanoid; Q64361; -.
DR OMA; MWQNSTE; -.
DR OrthoDB; 1129396at2759; -.
DR PhylomeDB; Q64361; -.
DR TreeFam; TF332787; -.
DR PRO; PR:Q64361; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000013572; Expressed in duodenum and 20 other tissues.
DR Genevisible; Q64361; RN.
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; ISO:RGD.
DR GO; GO:0050965; P:detection of temperature stimulus involved in sensory perception of pain; ISO:RGD.
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 Acetylation; Cytoplasm; Direct protein sequencing; Heparin-binding;
KW Inflammatory response; Metalloenzyme inhibitor; Metalloprotease inhibitor;
KW Protease inhibitor; Reference proteome; Repeat.
FT CHAIN 1..223
FT /note="Latexin"
FT /id="PRO_0000191345"
FT REGION 1..97
FT /note="Cystatin-like fold 1"
FT /evidence="ECO:0000250"
FT REGION 98..118
FT /note="Alpha-helical linker"
FT /evidence="ECO:0000250"
FT REGION 119..223
FT /note="Cystatin-like fold 2"
FT /evidence="ECO:0000250"
FT MOD_RES 56
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9BS40"
SQ SEQUENCE 223 AA; 25580 MW; 763E10679A9F0F8A CRC64;
MEEIPPTHYA ASRAASVAEN CINYQQGTPN KVFKVQTVQQ ASKEDIPGRG HKYHLKFSVE
EIIQKQVTVS CTAEVLYPRM GQGSAPEVNF TFEGEIGKNP DEEDNTFYQR LMSMKEPLQA
QNIPDNFGNV SPQMKPVHHL AWVACGYVMW QNSTEDTWYK MAKIQTVKQV QRNDDFIELD
YTVLLHDVAS QEIIPWQMQV LWHPQYGTKV KHNSRLPKEA PAE
