PP13_HUMAN
ID PP13_HUMAN Reviewed; 139 AA.
AC Q9UHV8; C5HZ15;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Galactoside-binding soluble lectin 13;
DE AltName: Full=Galectin-13;
DE Short=Gal-13;
DE AltName: Full=Placental tissue protein 13;
DE Short=PP13;
DE Short=Placental protein 13;
GN Name=LGALS13; Synonyms=PLAC8;
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 [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Placenta;
RX PubMed=10527825; DOI=10.1053/plac.1999.0436;
RA Than N.G., Sumegi B., Than G.N., Berente Z., Bohn H.;
RT "Isolation and sequence analysis of a cDNA encoding human placental tissue
RT protein 13 (PP13), a new lysophospholipase, homologue of human eosinophil
RT Charcot-Leyden crystal protein.";
RL Placenta 20:703-710(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Placenta;
RA Admon A., Paltieli Y., Slotky R., Mandel S.;
RT "Placental protein 13 (PP13), a serum marker for pregnancy disorders.";
RL Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Placenta;
RX PubMed=19497882; DOI=10.1073/pnas.0903568106;
RA Than N.G., Romero R., Goodman M., Weckle A., Xing J., Dong Z., Xu Y.,
RA Tarquini F., Szilagyi A., Gal P., Hou Z., Tarca A.L., Kim C.J., Kim J.S.,
RA Haidarian S., Uddin M., Bohn H., Benirschke K., Santolaya-Forgas J.,
RA Grossman L.I., Erez O., Hassan S.S., Zavodszky P., Papp Z., Wildman D.E.;
RT "A primate subfamily of galectins expressed at the maternal-fetal interface
RT that promote immune cell death.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:9731-9736(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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 [6]
RP SUBUNIT.
RC TISSUE=Placenta;
RX PubMed=6856484;
RA Bohn H., Kraus W., Winckler W.;
RT "Purification and characterization of two new soluble placental tissue
RT proteins (PP13 and PP17).";
RL Oncodev. Biol. Med. 4:343-350(1983).
RN [7]
RP 3D-STRUCTURE MODELING.
RX PubMed=11742106; DOI=10.1093/protein/14.11.875;
RA Visegrady B., Than N.G., Kilar F., Suemegi B., Than G.N., Bohn H.;
RT "Homology modelling and molecular dynamics studies of human placental
RT tissue protein 13 (galectin-13).";
RL Protein Eng. 14:875-880(2001).
RN [8] {ECO:0007744|PDB:5XG7, ECO:0007744|PDB:5XG8, ECO:0007744|PDB:5Y03}
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 2-139 OF WILD TYPE AND MUTANT
RP HIS-53, FUNCTION, DISULFIDE BOND, SUBUNIT, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF ARG-53; CYS-136 AND CYS-138.
RX PubMed=29343868; DOI=10.1038/s41598-018-19465-0;
RA Su J., Wang Y., Si Y., Gao J., Song C., Cui L., Wu R., Tai G., Zhou Y.;
RT "Galectin-13, a different prototype galectin, does not bind beta-galacto-
RT sides and forms dimers via intermolecular disulfide bridges between Cys-136
RT and Cys-138.";
RL Sci. Rep. 8:980-980(2018).
CC -!- FUNCTION: Binds beta-galactoside and lactose. Strong inducer of T-cell
CC apoptosis (PubMed:10527825, PubMed:19497882). Has hemagglutinating
CC activity towards chicken erythrocytes (PubMed:29343868).
CC {ECO:0000269|PubMed:10527825, ECO:0000269|PubMed:19497882,
CC ECO:0000269|PubMed:29343868}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000269|PubMed:29343868,
CC ECO:0000269|PubMed:6856484}.
CC -!- INTERACTION:
CC Q9UHV8; Q02930-3: CREB5; NbExp=3; IntAct=EBI-3957707, EBI-10192698;
CC Q9UHV8; P49639: HOXA1; NbExp=6; IntAct=EBI-3957707, EBI-740785;
CC Q9UHV8; Q7Z417: NUFIP2; NbExp=3; IntAct=EBI-3957707, EBI-1210753;
CC Q9UHV8; P32242: OTX1; NbExp=3; IntAct=EBI-3957707, EBI-740446;
CC Q9UHV8; Q9UKS6: PACSIN3; NbExp=3; IntAct=EBI-3957707, EBI-77926;
CC Q9UHV8; A2BDE7: PHLDA1; NbExp=3; IntAct=EBI-3957707, EBI-14084211;
CC Q9UHV8; Q12837: POU4F2; NbExp=3; IntAct=EBI-3957707, EBI-17236143;
CC Q9UHV8; P09022: Hoxa1; Xeno; NbExp=3; IntAct=EBI-3957707, EBI-3957603;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:29343868}. Nucleus
CC matrix {ECO:0000269|PubMed:29343868}.
CC -!- TISSUE SPECIFICITY: Detected in adult and fetal spleen, fetal kidney,
CC adult urinary bladder and placenta. Placental expression originates
CC predominantly from the syncytiotrophoblast.
CC {ECO:0000269|PubMed:10527825, ECO:0000269|PubMed:19497882}.
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DR EMBL; AF117383; AAF22001.1; -; mRNA.
DR EMBL; AY055826; AAL09162.1; -; mRNA.
DR EMBL; FJ613336; ACR09638.1; -; mRNA.
DR EMBL; FJ613337; ACR09639.1; -; mRNA.
DR EMBL; FJ613338; ACR09640.1; -; mRNA.
DR EMBL; CH471126; EAW56910.1; -; Genomic_DNA.
DR EMBL; BC066304; AAH66304.1; -; mRNA.
DR EMBL; BC069312; AAH69312.1; -; mRNA.
DR CCDS; CCDS33024.1; -.
DR RefSeq; NP_037400.1; NM_013268.2.
DR PDB; 5XG7; X-ray; 1.55 A; A=1-139.
DR PDB; 5XG8; X-ray; 1.55 A; A=2-139.
DR PDB; 5Y03; X-ray; 2.12 A; A=1-139.
DR PDB; 6A62; X-ray; 2.03 A; A=2-139.
DR PDB; 6A63; X-ray; 1.63 A; A=2-139.
DR PDB; 6A64; X-ray; 1.63 A; A=2-139.
DR PDB; 6A65; X-ray; 1.77 A; A=2-139.
DR PDB; 6A66; X-ray; 1.40 A; A=2-139.
DR PDB; 6KJW; X-ray; 1.36 A; A=1-139.
DR PDB; 6KJX; X-ray; 1.53 A; A=1-139.
DR PDB; 6KJY; X-ray; 1.50 A; A=1-139.
DR PDBsum; 5XG7; -.
DR PDBsum; 5XG8; -.
DR PDBsum; 5Y03; -.
DR PDBsum; 6A62; -.
DR PDBsum; 6A63; -.
DR PDBsum; 6A64; -.
DR PDBsum; 6A65; -.
DR PDBsum; 6A66; -.
DR PDBsum; 6KJW; -.
DR PDBsum; 6KJX; -.
DR PDBsum; 6KJY; -.
DR AlphaFoldDB; Q9UHV8; -.
DR SMR; Q9UHV8; -.
DR BioGRID; 118889; 16.
DR IntAct; Q9UHV8; 14.
DR MINT; Q9UHV8; -.
DR STRING; 9606.ENSP00000221797; -.
DR UniLectin; Q9UHV8; -.
DR BioMuta; LGALS13; -.
DR DMDM; 41017510; -.
DR MassIVE; Q9UHV8; -.
DR PaxDb; Q9UHV8; -.
DR PeptideAtlas; Q9UHV8; -.
DR PRIDE; Q9UHV8; -.
DR ProteomicsDB; 84418; -.
DR Antibodypedia; 16851; 447 antibodies from 21 providers.
DR DNASU; 29124; -.
DR Ensembl; ENST00000221797.5; ENSP00000221797.3; ENSG00000105198.12.
DR GeneID; 29124; -.
DR KEGG; hsa:29124; -.
DR MANE-Select; ENST00000221797.5; ENSP00000221797.3; NM_013268.3; NP_037400.1.
DR UCSC; uc002omb.4; human.
DR CTD; 29124; -.
DR DisGeNET; 29124; -.
DR GeneCards; LGALS13; -.
DR HGNC; HGNC:15449; LGALS13.
DR HPA; ENSG00000105198; Tissue enriched (placenta).
DR MIM; 608717; gene.
DR neXtProt; NX_Q9UHV8; -.
DR OpenTargets; ENSG00000105198; -.
DR PharmGKB; PA134923011; -.
DR VEuPathDB; HostDB:ENSG00000105198; -.
DR eggNOG; KOG3587; Eukaryota.
DR GeneTree; ENSGT00940000162909; -.
DR HOGENOM; CLU_037794_4_0_1; -.
DR InParanoid; Q9UHV8; -.
DR OMA; DIAFCFR; -.
DR OrthoDB; 829777at2759; -.
DR PhylomeDB; Q9UHV8; -.
DR TreeFam; TF315551; -.
DR PathwayCommons; Q9UHV8; -.
DR SignaLink; Q9UHV8; -.
DR BioGRID-ORCS; 29124; 9 hits in 1031 CRISPR screens.
DR GeneWiki; LGALS13; -.
DR GenomeRNAi; 29124; -.
DR Pharos; Q9UHV8; Tbio.
DR PRO; PR:Q9UHV8; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9UHV8; protein.
DR Bgee; ENSG00000105198; Expressed in placenta and 34 other tissues.
DR ExpressionAtlas; Q9UHV8; baseline and differential.
DR Genevisible; Q9UHV8; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0016363; C:nuclear matrix; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0004622; F:lysophospholipase activity; TAS:ProtInc.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0006644; P:phospholipid metabolic process; TAS:ProtInc.
DR GO; GO:0070234; P:positive regulation of T cell apoptotic process; IEA:InterPro.
DR CDD; cd00070; GLECT; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR044156; Galectin-like.
DR InterPro; IPR030653; Galectin_13.
DR InterPro; IPR001079; Galectin_CRD.
DR PANTHER; PTHR11346; PTHR11346; 1.
DR PANTHER; PTHR11346:SF120; PTHR11346:SF120; 1.
DR Pfam; PF00337; Gal-bind_lectin; 1.
DR SMART; SM00908; Gal-bind_lectin; 1.
DR SMART; SM00276; GLECT; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS51304; GALECTIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Apoptosis; Cytoplasm; Disulfide bond; Hemagglutinin; Lectin;
KW Nucleus; Reference proteome.
FT CHAIN 1..139
FT /note="Galactoside-binding soluble lectin 13"
FT /id="PRO_0000076963"
FT DOMAIN 6..138
FT /note="Galectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00639"
FT DISULFID 136
FT /note="Interchain (with C-138)"
FT /evidence="ECO:0000269|PubMed:29343868"
FT DISULFID 138
FT /note="Interchain (with C-136)"
FT /evidence="ECO:0000269|PubMed:29343868"
FT MUTAGEN 53
FT /note="R->H: No effect on its haemagglutinating activity."
FT /evidence="ECO:0000269|PubMed:29343868"
FT MUTAGEN 136
FT /note="C->S: Loss of homodimerization; when associated with
FT S-138."
FT /evidence="ECO:0000269|PubMed:29343868"
FT MUTAGEN 138
FT /note="C->S: Loss of homodimerization; when associated with
FT S-136."
FT /evidence="ECO:0000269|PubMed:29343868"
FT STRAND 6..11
FT /evidence="ECO:0007829|PDB:6KJW"
FT STRAND 19..26
FT /evidence="ECO:0007829|PDB:6KJW"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:6KJW"
FT STRAND 35..45
FT /evidence="ECO:0007829|PDB:6KJW"
FT STRAND 50..57
FT /evidence="ECO:0007829|PDB:6KJW"
FT TURN 58..60
FT /evidence="ECO:0007829|PDB:6KJW"
FT STRAND 61..68
FT /evidence="ECO:0007829|PDB:6KJW"
FT STRAND 76..79
FT /evidence="ECO:0007829|PDB:6KJW"
FT STRAND 89..95
FT /evidence="ECO:0007829|PDB:6KJW"
FT STRAND 97..104
FT /evidence="ECO:0007829|PDB:6KJW"
FT STRAND 107..113
FT /evidence="ECO:0007829|PDB:6KJW"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:6KJW"
FT STRAND 123..137
FT /evidence="ECO:0007829|PDB:6KJW"
SQ SEQUENCE 139 AA; 16119 MW; D1FE26D66C1F5FD0 CRC64;
MSSLPVPYKL PVSLSVGSCV IIKGTPIHSF INDPQLQVDF YTDMDEDSDI AFRFRVHFGN
HVVMNRREFG IWMLEETTDY VPFEDGKQFE LCIYVHYNEY EIKVNGIRIY GFVHRIPPSF
VKMVQVSRDI SLTSVCVCN
