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Protein

Galectin-1

Gene

Lgals1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Lectin that binds beta-galactoside and a wide array of complex carbohydrates. Plays a role in regulating apoptosis, cell proliferation and cell differentiation. Inhibits CD45 protein phosphatase activity and therefore the dephosphorylation of Lyn kinase. Strong inducer of T-cell apoptosis.By similarity1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei53 – 531Beta-galactosideBy similarity
Binding sitei62 – 621Beta-galactosideBy similarity

GO - Molecular functioni

  • carbohydrate binding Source: MGI
  • galactose binding Source: UniProtKB
  • lactose binding Source: Ensembl
  • poly(A) RNA binding Source: MGI
  • signal transducer activity Source: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Apoptosis

Keywords - Ligandi

Lectin

Names & Taxonomyi

Protein namesi
Recommended name:
Galectin-1
Short name:
Gal-1
Alternative name(s):
14 kDa lectin
Beta-galactoside-binding lectin L-14-I
Galaptin
Lactose-binding lectin 1
Lectin galactoside-binding soluble 1
S-Lac lectin 1
Gene namesi
Name:Lgals1
Synonyms:Gbp
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:96777. Lgals1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 135134Galectin-1PRO_0000076918Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei13 – 131N6-acetyllysineCombined sources
Modified residuei19 – 191N6-acetyllysineCombined sources
Modified residuei29 – 291N6-acetyllysineCombined sources
Modified residuei30 – 301PhosphoserineBy similarity
Modified residuei108 – 1081N6-acetyllysine; alternateCombined sources
Modified residuei108 – 1081N6-succinyllysine; alternateCombined sources
Modified residuei128 – 1281N6-acetyllysineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP16045.
MaxQBiP16045.
PaxDbiP16045.
PRIDEiP16045.
TopDownProteomicsiP16045.

2D gel databases

REPRODUCTION-2DPAGEIPI00229517.
P16045.
SWISS-2DPAGEP16045.
UCD-2DPAGEP16045.

PTM databases

iPTMnetiP16045.
PhosphoSiteiP16045.
SwissPalmiP16045.

Expressioni

Gene expression databases

BgeeiP16045.
CleanExiMM_LGALS1.
GenevisibleiP16045. MM.

Interactioni

Subunit structurei

Homodimer. Binds LGALS3BP. Interacts with CD2, CD3, CD4, CD6, CD7, CD43, ALCAM and CD45. Interacts with laminin (via poly-N-acetyllactosamine). Interacts with SUSD2.By similarity

Protein-protein interaction databases

BioGridi201142. 2 interactions.
IntActiP16045. 5 interactions.
MINTiMINT-4100323.
STRINGi10090.ENSMUSP00000086795.

Structurei

Secondary structure

1
135
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 83Combined sources
Beta strandi17 – 248Combined sources
Beta strandi33 – 386Combined sources
Beta strandi41 – 499Combined sources
Beta strandi58 – 658Combined sources
Beta strandi73 – 753Combined sources
Beta strandi84 – 929Combined sources
Beta strandi94 – 1007Combined sources
Beta strandi106 – 1105Combined sources
Beta strandi120 – 1234Combined sources
Beta strandi127 – 1359Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4LBQX-ray2.40A/B/C/D1-135[»]
ProteinModelPortaliP16045.
SMRiP16045. Positions 3-135.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 135132GalectinPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni45 – 495Beta-galactoside bindingBy similarity
Regioni69 – 724Beta-galactoside bindingBy similarity

Sequence similaritiesi

Contains 1 galectin domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3587. Eukaryota.
ENOG4111EA0. LUCA.
GeneTreeiENSGT00440000034263.
HOVERGENiHBG006255.
InParanoidiP16045.
KOiK06830.
OMAiCNSKEDG.
OrthoDBiEOG7NKKN0.
PhylomeDBiP16045.
TreeFamiTF315551.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR001079. Galectin_CRD.
[Graphical view]
PfamiPF00337. Gal-bind_lectin. 1 hit.
[Graphical view]
SMARTiSM00908. Gal-bind_lectin. 1 hit.
SM00276. GLECT. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS51304. GALECTIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P16045-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MACGLVASNL NLKPGECLKV RGEVASDAKS FVLNLGKDSN NLCLHFNPRF
60 70 80 90 100
NAHGDANTIV CNTKEDGTWG TEHREPAFPF QPGSITEVCI TFDQADLTIK
110 120 130
LPDGHEFKFP NRLNMEAINY MAADGDFKIK CVAFE
Length:135
Mass (Da):14,866
Last modified:January 23, 2007 - v3
Checksum:iFD6967C1F4117122
GO

Sequence cautioni

The sequence AAA37313.1 differs from that shown. Reason: Frameshift at several positions. Curated
The sequence AK004298 differs from that shown. Reason: Frameshift at position 117. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti78 – 781F → S in AAA37667 (PubMed:1986871).Curated
Sequence conflicti86 – 861T → I in AAH02063 (PubMed:15489334).Curated
Sequence conflicti131 – 1344CVAF → VRGL in AAA36172 (PubMed:3020551).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15986 mRNA. Translation: CAA34117.1.
X53067 mRNA. Translation: CAA37242.1.
X51577, X51578, X51579 Genomic DNA. Translation: CAA35930.1.
M57470 mRNA. Translation: AAA37667.1.
X66532 mRNA. Translation: CAA47143.1.
AK004298 mRNA. No translation available.
BC002063 mRNA. Translation: AAH02063.1.
BC099479 mRNA. Translation: AAH99479.1.
X51903 mRNA. Translation: CAA36183.1.
M33214 mRNA. Translation: AAA37313.1. Frameshift.
M14087 mRNA. Translation: AAA36172.1.
CCDSiCCDS27628.1.
PIRiB26495.
S07162.
S11718. LNMSGB.
RefSeqiNP_032521.1. NM_008495.2.
UniGeneiMm.43831.

Genome annotation databases

EnsembliENSMUST00000089377; ENSMUSP00000086795; ENSMUSG00000068220.
GeneIDi16852.
KEGGimmu:16852.
UCSCiuc007wrv.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15986 mRNA. Translation: CAA34117.1.
X53067 mRNA. Translation: CAA37242.1.
X51577, X51578, X51579 Genomic DNA. Translation: CAA35930.1.
M57470 mRNA. Translation: AAA37667.1.
X66532 mRNA. Translation: CAA47143.1.
AK004298 mRNA. No translation available.
BC002063 mRNA. Translation: AAH02063.1.
BC099479 mRNA. Translation: AAH99479.1.
X51903 mRNA. Translation: CAA36183.1.
M33214 mRNA. Translation: AAA37313.1. Frameshift.
M14087 mRNA. Translation: AAA36172.1.
CCDSiCCDS27628.1.
PIRiB26495.
S07162.
S11718. LNMSGB.
RefSeqiNP_032521.1. NM_008495.2.
UniGeneiMm.43831.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4LBQX-ray2.40A/B/C/D1-135[»]
ProteinModelPortaliP16045.
SMRiP16045. Positions 3-135.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201142. 2 interactions.
IntActiP16045. 5 interactions.
MINTiMINT-4100323.
STRINGi10090.ENSMUSP00000086795.

PTM databases

iPTMnetiP16045.
PhosphoSiteiP16045.
SwissPalmiP16045.

2D gel databases

REPRODUCTION-2DPAGEIPI00229517.
P16045.
SWISS-2DPAGEP16045.
UCD-2DPAGEP16045.

Proteomic databases

EPDiP16045.
MaxQBiP16045.
PaxDbiP16045.
PRIDEiP16045.
TopDownProteomicsiP16045.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000089377; ENSMUSP00000086795; ENSMUSG00000068220.
GeneIDi16852.
KEGGimmu:16852.
UCSCiuc007wrv.1. mouse.

Organism-specific databases

CTDi3956.
MGIiMGI:96777. Lgals1.

Phylogenomic databases

eggNOGiKOG3587. Eukaryota.
ENOG4111EA0. LUCA.
GeneTreeiENSGT00440000034263.
HOVERGENiHBG006255.
InParanoidiP16045.
KOiK06830.
OMAiCNSKEDG.
OrthoDBiEOG7NKKN0.
PhylomeDBiP16045.
TreeFamiTF315551.

Miscellaneous databases

NextBioi290788.
PROiP16045.
SOURCEiSearch...

Gene expression databases

BgeeiP16045.
CleanExiMM_LGALS1.
GenevisibleiP16045. MM.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR001079. Galectin_CRD.
[Graphical view]
PfamiPF00337. Gal-bind_lectin. 1 hit.
[Graphical view]
SMARTiSM00908. Gal-bind_lectin. 1 hit.
SM00276. GLECT. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS51304. GALECTIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The sequence of the mouse 14 kDa beta-galactoside-binding lectin and evidence for its synthesis on free cytoplasmic ribosomes."
    Wilson T.J.G., Firth M.N., Powell J.T., Harrison F.L.
    Biochem. J. 261:847-852(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
    Strain: C3H/HeJ.
    Tissue: Skeletal muscle.
  2. "Structure and expression of the negative growth factor mouse beta-galactoside binding protein gene."
    Chiariotti L., Wells V., Bruni C.B., Mallucci L.
    Biochim. Biophys. Acta 1089:54-60(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: BALB/cJ.
    Tissue: Liver.
  3. "Identification of an autocrine negative growth factor: mouse beta-galactoside-binding protein is a cytostatic factor and cell growth regulator."
    Wells V., Mallucci L.
    Cell 64:91-97(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "Expression of the L14 lectin during mouse embryogenesis suggests multiple roles during pre- and post-implantation development."
    Poirier F., Timmons P.M., Chan C.T., Guenet J.-L., Rigby P.W.
    Development 115:143-155(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  5. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Embryo.
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Czech II and NIH Black Swiss.
    Tissue: Mammary gland and Thyroid.
  7. "Evidence for export of a muscle lectin from cytosol to extracellular matrix and for a novel secretory mechanism."
    Cooper D.N.W., Barondes S.H.
    J. Cell Biol. 110:1681-1691(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-107.
    Tissue: Skeletal muscle.
  8. "Expression of two different endogenous galactoside-binding lectins sharing sequence homology."
    Raz A., Carmi P., Pazerni G.
    Cancer Res. 48:645-649(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-105.
  9. "Evidence that a human soluble beta-galactoside-binding lectin is encoded by a family of genes."
    Gitt M.A., Barondes S.H.
    Proc. Natl. Acad. Sci. U.S.A. 83:7603-7607(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 68-134.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  11. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-13; LYS-19; LYS-29; LYS-108 AND LYS-128, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-108, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiLEG1_MOUSE
AccessioniPrimary (citable) accession number: P16045
Secondary accession number(s): P05163
, P11946, P17601, Q4FZH4, Q99M27, Q9D0X0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: May 11, 2016
This is version 159 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

Was originally thought to originate from human.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.