LXN_HUMAN
ID LXN_HUMAN Reviewed; 222 AA.
AC Q9BS40; Q96PN2; Q9NQS6;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Latexin;
DE AltName: Full=Endogenous carboxypeptidase inhibitor;
DE Short=ECI;
DE AltName: Full=Protein MUM;
DE AltName: Full=Tissue carboxypeptidase inhibitor;
DE Short=TCI;
GN Name=LXN;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], VARIANT ARG-53, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Fetal brain;
RX PubMed=11455960; DOI=10.1023/a:1010971219806;
RA Liu Q., Yu L., Gao J., Fu Q., Zhang J., Zhang P., Chen J., Zhao S.;
RT "Cloning, tissue expression pattern and genomic organization of latexin, a
RT human homologue of rat carboxypeptidase A inhibitor.";
RL Mol. Biol. Rep. 27:241-246(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Ke Y., Ning T., Lu Z., Guo M., Zhao H.;
RT "1G10 and gastric cancer.";
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin, and Urinary bladder;
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 ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-55, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH CPA4, AND FUNCTION.
RX PubMed=15738388; DOI=10.1073/pnas.0500678102;
RA Pallares I., Bonet R., Garcia-Castellanos R., Ventura S., Aviles F.X.,
RA Vendrell J., Gomis-Rueth F.-X.;
RT "Structure of human carboxypeptidase A4 with its endogenous protein
RT inhibitor, latexin.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:3978-3983(2005).
CC -!- FUNCTION: Hardly reversible, non-competitive, and potent inhibitor of
CC CPA1, CPA2 and CPA4. May play a role in inflammation.
CC {ECO:0000269|PubMed:15738388}.
CC -!- INTERACTION:
CC Q9BS40; Q96DN7: BOC; NbExp=3; IntAct=EBI-1044504, EBI-12208129;
CC Q9BS40; P07451: CA3; NbExp=3; IntAct=EBI-1044504, EBI-12208965;
CC Q9BS40; P12074: COX6A1; NbExp=3; IntAct=EBI-1044504, EBI-2115950;
CC Q9BS40; Q9BQA9: CYBC1; NbExp=3; IntAct=EBI-1044504, EBI-2680384;
CC Q9BS40; Q9NVH1: DNAJC11; NbExp=3; IntAct=EBI-1044504, EBI-1055336;
CC Q9BS40; Q12882: DPYD; NbExp=3; IntAct=EBI-1044504, EBI-2839838;
CC Q9BS40; A0A1W2PQB1: FCGR3A; NbExp=3; IntAct=EBI-1044504, EBI-17709451;
CC Q9BS40; Q6UXU4: GSG1L; NbExp=3; IntAct=EBI-1044504, EBI-10297401;
CC Q9BS40; Q5DX21-2: IGSF11; NbExp=3; IntAct=EBI-1044504, EBI-12178037;
CC Q9BS40; P43361: MAGEA8; NbExp=3; IntAct=EBI-1044504, EBI-10182930;
CC Q9BS40; Q4G0Z9: MCMDC2; NbExp=3; IntAct=EBI-1044504, EBI-14506480;
CC Q9BS40; Q6X4W1-2: NSMF; NbExp=3; IntAct=EBI-1044504, EBI-12028784;
CC Q9BS40; P26367: PAX6; NbExp=3; IntAct=EBI-1044504, EBI-747278;
CC Q9BS40; Q9UQK1: PPP1R3C; NbExp=3; IntAct=EBI-1044504, EBI-2506727;
CC Q9BS40; P78317: RNF4; NbExp=3; IntAct=EBI-1044504, EBI-2340927;
CC Q9BS40; Q8TBC3: SHKBP1; NbExp=3; IntAct=EBI-1044504, EBI-724292;
CC Q9BS40; O75391: SPAG7; NbExp=3; IntAct=EBI-1044504, EBI-348464;
CC Q9BS40; Q9Y6G1: TMEM14A; NbExp=3; IntAct=EBI-1044504, EBI-2800360;
CC Q9BS40; Q9BWF2: TRAIP; NbExp=3; IntAct=EBI-1044504, EBI-1756205;
CC Q9BS40; Q9HCM9: TRIM39; NbExp=3; IntAct=EBI-1044504, EBI-739510;
CC Q9BS40; Q5BJH7-5: YIF1B; NbExp=3; IntAct=EBI-1044504, EBI-12158885;
CC Q9BS40; Q9NP64: ZCCHC17; NbExp=3; IntAct=EBI-1044504, EBI-746345;
CC Q9BS40; Q969J2: ZKSCAN4; NbExp=6; IntAct=EBI-1044504, EBI-2818641;
CC Q9BS40; Q2NKJ9: ZNF430; NbExp=3; IntAct=EBI-1044504, EBI-12298837;
CC Q9BS40; Q8IYX0: ZNF679; NbExp=3; IntAct=EBI-1044504, EBI-745567;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Highly expressed in heart, prostate, ovary, kidney,
CC pancreas, and colon, moderate or low in other tissues including brain.
CC {ECO:0000269|PubMed:11455960}.
CC -!- SIMILARITY: Belongs to the protease inhibitor I47 (latexin) family.
CC {ECO:0000305}.
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DR EMBL; AF087851; AAP97162.1; -; mRNA.
DR EMBL; AF282626; AAF82807.1; -; mRNA.
DR EMBL; AF303587; AAL09331.1; -; Genomic_DNA.
DR EMBL; AF282594; AAK69518.1; -; mRNA.
DR EMBL; AC025033; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC080013; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC005346; AAH05346.1; -; mRNA.
DR EMBL; BC008438; AAH08438.1; -; mRNA.
DR CCDS; CCDS3183.1; -.
DR RefSeq; NP_064554.3; NM_020169.3.
DR PDB; 2BO9; X-ray; 1.60 A; B/D=1-222.
DR PDBsum; 2BO9; -.
DR AlphaFoldDB; Q9BS40; -.
DR SMR; Q9BS40; -.
DR BioGRID; 121252; 39.
DR IntAct; Q9BS40; 26.
DR STRING; 9606.ENSP00000264265; -.
DR MEROPS; I47.001; -.
DR GlyGen; Q9BS40; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9BS40; -.
DR MetOSite; Q9BS40; -.
DR PhosphoSitePlus; Q9BS40; -.
DR SwissPalm; Q9BS40; -.
DR BioMuta; LXN; -.
DR DMDM; 146345452; -.
DR EPD; Q9BS40; -.
DR jPOST; Q9BS40; -.
DR MassIVE; Q9BS40; -.
DR MaxQB; Q9BS40; -.
DR PaxDb; Q9BS40; -.
DR PeptideAtlas; Q9BS40; -.
DR PRIDE; Q9BS40; -.
DR ProteomicsDB; 78864; -.
DR Antibodypedia; 2121; 655 antibodies from 36 providers.
DR DNASU; 56925; -.
DR Ensembl; ENST00000264265.4; ENSP00000264265.3; ENSG00000079257.8.
DR GeneID; 56925; -.
DR KEGG; hsa:56925; -.
DR MANE-Select; ENST00000264265.4; ENSP00000264265.3; NM_020169.4; NP_064554.3.
DR UCSC; uc003fch.3; human.
DR CTD; 56925; -.
DR DisGeNET; 56925; -.
DR GeneCards; LXN; -.
DR HGNC; HGNC:13347; LXN.
DR HPA; ENSG00000079257; Tissue enhanced (urinary).
DR MIM; 609305; gene.
DR neXtProt; NX_Q9BS40; -.
DR OpenTargets; ENSG00000079257; -.
DR PharmGKB; PA134991999; -.
DR VEuPathDB; HostDB:ENSG00000079257; -.
DR eggNOG; ENOG502RYUY; Eukaryota.
DR GeneTree; ENSGT00530000063813; -.
DR HOGENOM; CLU_083048_0_0_1; -.
DR InParanoid; Q9BS40; -.
DR OMA; MWQNSTE; -.
DR OrthoDB; 1129396at2759; -.
DR PhylomeDB; Q9BS40; -.
DR TreeFam; TF332787; -.
DR PathwayCommons; Q9BS40; -.
DR SignaLink; Q9BS40; -.
DR BioGRID-ORCS; 56925; 10 hits in 1064 CRISPR screens.
DR ChiTaRS; LXN; human.
DR EvolutionaryTrace; Q9BS40; -.
DR GenomeRNAi; 56925; -.
DR Pharos; Q9BS40; Tbio.
DR PRO; PR:Q9BS40; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9BS40; protein.
DR Bgee; ENSG00000079257; Expressed in germinal epithelium of ovary and 177 other tissues.
DR ExpressionAtlas; Q9BS40; baseline and differential.
DR Genevisible; Q9BS40; HS.
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; IBA:GO_Central.
DR GO; GO:0050965; P:detection of temperature stimulus involved in sensory perception of pain; IEA:Ensembl.
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; Heparin-binding;
KW Inflammatory response; Metalloenzyme inhibitor; Metalloprotease inhibitor;
KW Protease inhibitor; Reference proteome; Repeat.
FT CHAIN 1..222
FT /note="Latexin"
FT /id="PRO_0000191343"
FT REGION 1..97
FT /note="Cystatin-like fold 1"
FT /evidence="ECO:0000250"
FT REGION 98..117
FT /note="Alpha-helical linker"
FT /evidence="ECO:0000250"
FT REGION 118..222
FT /note="Cystatin-like fold 2"
FT /evidence="ECO:0000250"
FT MOD_RES 55
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT VARIANT 53
FT /note="H -> R (in dbSNP:rs8455)"
FT /evidence="ECO:0000269|PubMed:11455960"
FT /id="VAR_019117"
FT VARIANT 134
FT /note="T -> M (in dbSNP:rs59718588)"
FT /id="VAR_062139"
FT HELIX 8..25
FT /evidence="ECO:0007829|PDB:2BO9"
FT STRAND 32..45
FT /evidence="ECO:0007829|PDB:2BO9"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:2BO9"
FT STRAND 49..60
FT /evidence="ECO:0007829|PDB:2BO9"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:2BO9"
FT STRAND 67..77
FT /evidence="ECO:0007829|PDB:2BO9"
FT STRAND 86..93
FT /evidence="ECO:0007829|PDB:2BO9"
FT HELIX 100..112
FT /evidence="ECO:0007829|PDB:2BO9"
FT STRAND 118..123
FT /evidence="ECO:0007829|PDB:2BO9"
FT HELIX 131..151
FT /evidence="ECO:0007829|PDB:2BO9"
FT STRAND 158..169
FT /evidence="ECO:0007829|PDB:2BO9"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:2BO9"
FT STRAND 176..186
FT /evidence="ECO:0007829|PDB:2BO9"
FT TURN 187..189
FT /evidence="ECO:0007829|PDB:2BO9"
FT STRAND 192..202
FT /evidence="ECO:0007829|PDB:2BO9"
FT TURN 203..205
FT /evidence="ECO:0007829|PDB:2BO9"
FT STRAND 206..214
FT /evidence="ECO:0007829|PDB:2BO9"
SQ SEQUENCE 222 AA; 25750 MW; 7D557BEDA0E1F60C CRC64;
MEIPPTNYPA SRAALVAQNY INYQQGTPHR VFEVQKVKQA SMEDIPGRGH KYHLKFAVEE
IIQKQVKVNC TAEVLYPSTG QETAPEVNFT FEGETGKNPD EEDNTFYQRL KSMKEPLEAQ
NIPDNFGNVS PEMTLVLHLA WVACGYIIWQ NSTEDTWYKM VKIQTVKQVQ RNDDFIELDY
TILLHNIASQ EIIPWQMQVL WHPQYGTKVK HNSRLPKEVQ LE
