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   27-MAR-2024, entry version 182.
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; 9606-ENSP00000221797; -.
DR   PeptideAtlas; Q9UHV8; -.
DR   ProteomicsDB; 84418; -.
DR   Antibodypedia; 16851; 483 antibodies from 22 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   AGR; HGNC:15449; -.
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; SDIAFCF; -.
DR   OrthoDB; 2874391at2759; -.
DR   PhylomeDB; Q9UHV8; -.
DR   TreeFam; TF315551; -.
DR   PathwayCommons; Q9UHV8; -.
DR   SignaLink; Q9UHV8; -.
DR   BioGRID-ORCS; 29124; 9 hits in 1108 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 cell types or tissues.
DR   ExpressionAtlas; Q9UHV8; baseline and differential.
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   CDD; cd00070; GLECT; 1.
DR   Gene3D; 2.60.120.200; -; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR044156; Galectin-like.
DR   InterPro; IPR001079; Galectin_CRD.
DR   PANTHER; PTHR11346:SF120; GALACTOSIDE-BINDING SOLUBLE LECTIN 13; 1.
DR   PANTHER; PTHR11346; GALECTIN; 1.
DR   Pfam; PF00337; Gal-bind_lectin; 1.
DR   SMART; SM00908; Gal-bind_lectin; 1.
DR   SMART; SM00276; GLECT; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   PROSITE; PS51304; GALECTIN; 1.
DR   Genevisible; Q9UHV8; HS.
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
//