ID   GLCM1_RAT               Reviewed;         146 AA.
AC   Q04807;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   25-MAY-2022, entry version 104.
DE   RecName: Full=Glycosylation-dependent cell adhesion molecule 1;
DE            Short=GlyCAM-1;
DE   AltName: Full=Endothelial ligand FOR L-selectin;
DE   AltName: Full=SGP50;
DE   AltName: Full=Sulfated 50 kDa glycoprotein;
DE   Flags: Precursor;
GN   Name=Glycam1;
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].
RX   PubMed=8100229; DOI=10.1016/s0021-9258(19)85253-5;
RA   Dowbenko D., Watson S.R., Lasky L.A.;
RT   "Cloning of a rat homologue of mouse GlyCAM 1 reveals conservation of
RT   structural domains.";
RL   J. Biol. Chem. 268:14399-14403(1993).
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. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PP3/GlyCAM-1 family. {ECO:0000305}.
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DR   EMBL; L08100; AAA41249.1; -; mRNA.
DR   PIR; A47167; A47167.
DR   RefSeq; NP_036926.1; NM_012794.1.
DR   AlphaFoldDB; Q04807; -.
DR   STRING; 10116.ENSRNOP00000052145; -.
DR   PhosphoSitePlus; Q04807; -.
DR   PaxDb; Q04807; -.
DR   GeneID; 25258; -.
DR   KEGG; rno:25258; -.
DR   UCSC; RGD:2712; rat.
DR   CTD; 644076; -.
DR   RGD; 2712; Glycam1.
DR   eggNOG; ENOG502TDVV; Eukaryota.
DR   InParanoid; Q04807; -.
DR   OrthoDB; 1585143at2759; -.
DR   PhylomeDB; Q04807; -.
DR   PRO; PR:Q04807; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0007155; P:cell adhesion; TAS:RGD.
DR   InterPro; IPR007906; GLYCAM-1.
DR   Pfam; PF05242; GLYCAM-1; 1.
PE   2: Evidence at transcript level;
KW   Cell adhesion; Cell membrane; Glycoprotein; Membrane; Phosphoprotein;
KW   Reference proteome; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..146
FT                   /note="Glycosylation-dependent cell adhesion molecule 1"
FT                   /id="PRO_0000025407"
FT   REGION          25..112
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        34..52
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        53..67
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        72..112
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         71
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P80195"
SQ   SEQUENCE   146 AA;  15440 MW;  37D32683B9AE8245 CRC64;
     MKFFTVLLFA SLAATSLAAV PGSKDELHLR TQPTDAIPAS QFTPSSHISK ESTSSKDLSK
     ESFIFNEELV SEDNVGTEST KPQSQEAQDG LRSGSSQQEE TTSAATSEGK LTMLSQAVQK
     ELGKVIEGFI SGVEDIISGA SGTVRP