ID   LEG4_RAT                Reviewed;         324 AA.
AC   P38552;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=Galectin-4;
DE            Short=Gal-4;
DE   AltName: Full=L-36 lactose-binding protein;
DE            Short=L36LBP;
DE   AltName: Full=Lactose-binding lectin 4;
GN   Name=Lgals4;
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   TISSUE=Intestine;
RX   PubMed=8449956; DOI=10.1016/s0021-9258(18)53409-8;
RA   Oda Y., Herrmann J., Gitt M., Turck C.W., Burlingame A.L., Barondes S.H.,
RA   Leffler H.;
RT   "Soluble lactose-binding lectin from rat intestine with two different
RT   carbohydrate-binding domains in the same peptide chain.";
RL   J. Biol. Chem. 268:5929-5939(1993).
RN   [2]
RP   PROTEIN SEQUENCE OF 13-37 AND 44-66.
RX   PubMed=7867792; DOI=10.1016/0014-5793(95)00025-5;
RA   Tardy F., Deviller P., Louisot P., Martin A.;
RT   "Purification and characterization of the N-terminal domain of galectin-4
RT   from rat small intestine.";
RL   FEBS Lett. 359:169-172(1995).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-259, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Galectin that binds lactose and a related range of sugars.
CC   -!- SUBUNIT: Monomer.
CC   -!- TISSUE SPECIFICITY: Highly expressed in full-length form in small and
CC       large intestine and stomach but was not detected in other tissues
CC       including lung, liver, kidney and spleen.
CC   -!- DOMAIN: Contains two homologous but distinct carbohydrate-binding
CC       domains.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M73553; AAA41505.1; -; mRNA.
DR   PIR; A46631; A46631.
DR   RefSeq; NP_037107.1; NM_012975.1.
DR   AlphaFoldDB; P38552; -.
DR   SMR; P38552; -.
DR   STRING; 10116.ENSRNOP00000047505; -.
DR   iPTMnet; P38552; -.
DR   PhosphoSitePlus; P38552; -.
DR   PaxDb; P38552; -.
DR   PRIDE; P38552; -.
DR   Ensembl; ENSRNOT00000041205; ENSRNOP00000047505; ENSRNOG00000020338.
DR   GeneID; 25474; -.
DR   KEGG; rno:25474; -.
DR   UCSC; RGD:3003; rat.
DR   CTD; 3960; -.
DR   RGD; 3003; Lgals4.
DR   eggNOG; KOG3587; Eukaryota.
DR   GeneTree; ENSGT00940000160378; -.
DR   HOGENOM; CLU_037794_1_0_1; -.
DR   InParanoid; P38552; -.
DR   OMA; HWGGRFY; -.
DR   OrthoDB; 829777at2759; -.
DR   PRO; PR:P38552; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000020338; Expressed in jejunum and 15 other tissues.
DR   Genevisible; P38552; RN.
DR   GO; GO:0005615; C:extracellular space; ISO:RGD.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   GO; GO:0016936; F:galactoside binding; ISO:RGD.
DR   GO; GO:0002780; P:antibacterial peptide biosynthetic process; IEA:Ensembl.
DR   CDD; cd00070; GLECT; 2.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR044156; Galectin-like.
DR   InterPro; IPR015533; Galectin4/6.
DR   InterPro; IPR001079; Galectin_CRD.
DR   PANTHER; PTHR11346; PTHR11346; 1.
DR   PANTHER; PTHR11346:SF32; PTHR11346:SF32; 1.
DR   Pfam; PF00337; Gal-bind_lectin; 2.
DR   SMART; SM00908; Gal-bind_lectin; 2.
DR   SMART; SM00276; GLECT; 2.
DR   SUPFAM; SSF49899; SSF49899; 2.
DR   PROSITE; PS51304; GALECTIN; 2.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Lectin; Phosphoprotein; Reference proteome;
KW   Repeat.
FT   CHAIN           1..324
FT                   /note="Galectin-4"
FT                   /id="PRO_0000076937"
FT   DOMAIN          19..150
FT                   /note="Galectin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00639"
FT   DOMAIN          196..324
FT                   /note="Galectin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00639"
FT   BINDING         257..263
FT                   /ligand="a beta-D-galactoside"
FT                   /ligand_id="ChEBI:CHEBI:28034"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         259
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
SQ   SEQUENCE   324 AA;  36347 MW;  478024D7322AFE7B CRC64;
     MAYVPAPGYQ PTYNPTLPYK RPIPGGLSVG MSIYIQGIAK DNMRRFHVNF AVGQDEGADI
     AFHFNPRFDG WDKVVFNTMQ SGQWGKEEKK KSMPFQKGHH FELVFMVMSE HYKVVVNGTP
     FYEYGHRLPL QMVTHLQVDG DLELQSINFL GGQPAASQYP GTMTIPAYPS AGYNPPQMNS
     LPVMAGPPIF NPPVPYVGTL QGGLTARRTI IIKGYVLPTA KNLIINFKVG STGDIAFHMN
     PRIGDCVVRN SYMNGSWGSE ERKIPYNPFG AGQFFDLSIR CGTDRFKVFA NGQHLFDFSH
     RFQAFQRVDM LEIKGDITLS YVQI