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Q02596 (GLCM1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glycosylation-dependent cell adhesion molecule 1

Short name=GlyCAM-1
Alternative name(s):
Endothelial ligand FOR L-selectin
MC26
SGP50
Sulfated 50 kDa glycoprotein
Gene names
Name:Glycam1
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length151 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Adhesion molecule that accomplishes cell binding by presenting carbohydrate(s) to the lectin domain of L-selectin.

Subcellular location

Cell membrane.

Tissue specificity

Lymph nodes. Associated with the lumenal surface of the high endothelial venules of peripheral lymph nodes.

Post-translational modification

Extensively O-glycosylated. Ref.6

Sequence similarities

Belongs to the PP3/GlyCAM-1 family.

Ontologies

Keywords
   Biological processCell adhesion
   Cellular componentCell membrane
Membrane
   DomainSignal
   PTMGlycoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological processcell adhesion

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentextracellular region

Inferred from direct assay. Source: MGI

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncell adhesion molecule binding

Inferred from physical interaction. Source: MGI

sulfate binding

Inferred from direct assay. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Ref.1
Chain20 – 151132Glycosylation-dependent cell adhesion molecule 1
PRO_0000025406

Regions

Compositional bias42 – 6322Ser/Thr-rich
Compositional bias93 – 12230Ser/Thr-rich

Amino acid modifications

Glycosylation1151N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q02596 [UniParc].

Last modified July 1, 1993. Version 1.
Checksum: 274E66AA05534A77

FASTA15116,209
        10         20         30         40         50         60 
MKFFTVLLFV SLAATSLALL PGSKDELQMK TQPTDAIPAA QSTPTSYTSE ESTSSKDLSK 

        70         80         90        100        110        120 
EPSIFREELI SKDNVVIEST KPENQEAQDG LRSGSSQLEE TTRPTTSAAT TSEENLTKSS 

       130        140        150 
QTVEEELGKI IEGFVTGAED IISGASRITK S 

« Hide

References

« Hide 'large scale' references
[1]"An endothelial ligand for L-selectin is a novel mucin-like molecule."
Lasky L.A., Singer M.S., Dowbenko D., Imai Y., Henzel W.J., Grimley C., Fennie C., Gillett N., Watson S.R., Rosen S.D.
Cell 69:927-938(1992) [PubMed: 1376638] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PROTEIN SEQUENCE OF 20-41.
Tissue: Lymph node.
[2]"Structure and chromosomal localization of the murine gene encoding GLYCAM 1. A mucin-like endothelial ligand for L selectin."
Dowbenko D., Andalibi A., Young P.E., Lusis A.J., Lasky L.A.
J. Biol. Chem. 268:4525-4529(1993) [PubMed: 7680041] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Liver.
[3]"Expression of the mC26 gene encoding GlyCAM-1 in the lactating mouse mammary gland."
Nishimura T., Takeshita N., Satow H., Kohmoto K.
J. Biochem. 114:567-569(1993) [PubMed: 8276769] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: BALB/c.
Tissue: Liver.
[4]"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. expand/collapse author list , 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: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Mammary gland.
[5]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[6]"Structure of the O-glycans in GlyCAM-1, an endothelial-derived ligand for L-selectin."
Hemmerich S., Leffler H., Rosen S.D.
J. Biol. Chem. 270:12035-12047(1995) [PubMed: 7538131] [Abstract]
Cited for: STRUCTURE OF CARBOHYDRATES.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L08101 Genomic DNA. Translation: AAA79887.1.
M93428 mRNA. Translation: AAA37710.1.
D16108 Genomic DNA. Translation: BAA03682.1.
AK021358 mRNA. Translation: BAB32385.1.
BC145832 mRNA. Translation: AAI45833.1.
BC145858 mRNA. Translation: AAI45859.1.
IPIIPI00129509.
PIRA41908.
RefSeqNP_032160.1. NM_008134.2.
UniGeneMm.219621.

3D structure databases

ProteinModelPortalQ02596.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ02596.

PTM databases

PhosphoSiteQ02596.

Proteomic databases

PRIDEQ02596.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000023134; ENSMUSP00000023134; ENSMUSG00000022491.
GeneID14663.
KEGGmmu:14663.
UCSCuc007xyk.1. mouse.

Organism-specific databases

CTD644076.
MGIMGI:95759. Glycam1.

Phylogenomic databases

GeneTreeENSGT00520000060242.
HOVERGENHBG106667.
InParanoidQ02596.
OMAEAQDGLR.
OrthoDBEOG41RPWQ.

Gene expression databases

ArrayExpressQ02596.
BgeeQ02596.
CleanExMM_GLYCAM1.
GenevestigatorQ02596.
GermOnlineENSMUSG00000022491. Mus musculus.

Family and domain databases

InterProIPR007906. GLYCAM-1.
[Graphical view]
KOK06815.
PANTHERPTHR17389. GLYCAM-1. 1 hit.
PfamPF05242. GLYCAM-1. 1 hit.
[Graphical view]
ProDomPD012695. PD012695. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetSearch...

Other

NextBio286538.
SOURCESearch...

Entry information

Entry nameGLCM1_MOUSE
AccessionPrimary (citable) accession number: Q02596
Secondary accession number(s): A6H6D0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: November 16, 2011
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families