GLCM1_MOUSE
ID GLCM1_MOUSE Reviewed; 151 AA.
AC Q02596; A6H6D0;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Glycosylation-dependent cell adhesion molecule 1;
DE Short=GlyCAM-1;
DE AltName: Full=Endothelial ligand FOR L-selectin;
DE AltName: Full=MC26;
DE AltName: Full=SGP50;
DE AltName: Full=Sulfated 50 kDa glycoprotein;
DE Flags: Precursor;
GN Name=Glycam1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND PROTEIN SEQUENCE OF 20-41.
RC TISSUE=Lymph node;
RX PubMed=1376638; DOI=10.1016/0092-8674(92)90612-g;
RA Lasky L.A., Singer M.S., Dowbenko D., Imai Y., Henzel W.J., Grimley C.,
RA Fennie C., Gillett N., Watson S.R., Rosen S.D.;
RT "An endothelial ligand for L-selectin is a novel mucin-like molecule.";
RL Cell 69:927-938(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Liver;
RX PubMed=7680041; DOI=10.1016/s0021-9258(18)53641-3;
RA Dowbenko D., Andalibi A., Young P.E., Lusis A.J., Lasky L.A.;
RT "Structure and chromosomal localization of the murine gene encoding GLYCAM
RT 1. A mucin-like endothelial ligand for L selectin.";
RL J. Biol. Chem. 268:4525-4529(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=8276769; DOI=10.1093/oxfordjournals.jbchem.a124217;
RA Nishimura T., Takeshita N., Satow H., Kohmoto K.;
RT "Expression of the mC26 gene encoding GlyCAM-1 in the lactating mouse
RT mammary gland.";
RL J. Biochem. 114:567-569(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 STRUCTURE OF CARBOHYDRATES.
RX PubMed=7538131; DOI=10.1074/jbc.270.20.12035;
RA Hemmerich S., Leffler H., Rosen S.D.;
RT "Structure of the O-glycans in GlyCAM-1, an endothelial-derived ligand for
RT L-selectin.";
RL J. Biol. Chem. 270:12035-12047(1995).
CC -!- FUNCTION: Adhesion molecule that accomplishes cell binding by
CC presenting carbohydrate(s) to the lectin domain of L-selectin.
CC -!- SUBCELLULAR LOCATION: Cell membrane.
CC -!- TISSUE SPECIFICITY: Lymph nodes. Associated with the lumenal surface of
CC the high endothelial venules of peripheral lymph nodes.
CC -!- PTM: Extensively O-glycosylated.
CC -!- SIMILARITY: Belongs to the PP3/GlyCAM-1 family. {ECO:0000305}.
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DR EMBL; L08101; AAA79887.1; -; Genomic_DNA.
DR EMBL; M93428; AAA37710.1; -; mRNA.
DR EMBL; D16108; BAA03682.1; -; Genomic_DNA.
DR EMBL; AK021358; BAB32385.1; -; mRNA.
DR EMBL; BC145832; AAI45833.1; -; mRNA.
DR EMBL; BC145858; AAI45859.1; -; mRNA.
DR CCDS; CCDS27905.1; -.
DR PIR; A41908; A41908.
DR RefSeq; NP_032160.1; NM_008134.3.
DR AlphaFoldDB; Q02596; -.
DR STRING; 10090.ENSMUSP00000023134; -.
DR GlyGen; Q02596; 1 site.
DR PhosphoSitePlus; Q02596; -.
DR CPTAC; non-CPTAC-3711; -.
DR MaxQB; Q02596; -.
DR PaxDb; Q02596; -.
DR PRIDE; Q02596; -.
DR ProteomicsDB; 271228; -.
DR DNASU; 14663; -.
DR Ensembl; ENSMUST00000023134; ENSMUSP00000023134; ENSMUSG00000022491.
DR GeneID; 14663; -.
DR KEGG; mmu:14663; -.
DR UCSC; uc007xyk.2; mouse.
DR CTD; 644076; -.
DR MGI; MGI:95759; Glycam1.
DR VEuPathDB; HostDB:ENSMUSG00000022491; -.
DR eggNOG; ENOG502TDVV; Eukaryota.
DR GeneTree; ENSGT00520000060242; -.
DR HOGENOM; CLU_137449_0_0_1; -.
DR InParanoid; Q02596; -.
DR OMA; PHAYEVT; -.
DR OrthoDB; 1585143at2759; -.
DR PhylomeDB; Q02596; -.
DR TreeFam; TF339780; -.
DR BioGRID-ORCS; 14663; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Glycam1; mouse.
DR PRO; PR:Q02596; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q02596; protein.
DR Bgee; ENSMUSG00000022491; Expressed in peripheral lymph node and 62 other tissues.
DR ExpressionAtlas; Q02596; baseline and differential.
DR Genevisible; Q02596; MM.
DR GO; GO:0005576; C:extracellular region; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0050839; F:cell adhesion molecule binding; IPI:MGI.
DR GO; GO:0043199; F:sulfate binding; IDA:MGI.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0009617; P:response to bacterium; IEP:MGI.
DR InterPro; IPR007906; GLYCAM-1.
DR Pfam; PF05242; GLYCAM-1; 1.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell membrane; Direct protein sequencing; Glycoprotein;
KW Membrane; Phosphoprotein; Reference proteome; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:1376638"
FT CHAIN 20..151
FT /note="Glycosylation-dependent cell adhesion molecule 1"
FT /id="PRO_0000025406"
FT REGION 29..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..74
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 54
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P80195"
FT MOD_RES 59
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P80195"
FT MOD_RES 63
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P80195"
FT MOD_RES 71
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P80195"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 151 AA; 16209 MW; 274E66AA05534A77 CRC64;
MKFFTVLLFV SLAATSLALL PGSKDELQMK TQPTDAIPAA QSTPTSYTSE ESTSSKDLSK
EPSIFREELI SKDNVVIEST KPENQEAQDG LRSGSSQLEE TTRPTTSAAT TSEENLTKSS
QTVEEELGKI IEGFVTGAED IISGASRITK S
