ID   GT253_MOUSE             Reviewed;         592 AA.
AC   A3KGW5;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Inactive glycosyltransferase 25 family member 3;
DE   AltName: Full=Cerebral endothelial cell adhesion molecule;
DE   Flags: Precursor;
GN   Name=Cercam; Synonyms=Ceecam1, Glt25d3;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- FUNCTION: Probable cell adhesion protein involved in leukocyte
CC       transmigration across the blood-brain barrier. Does not express any
CC       beta-galactosyltransferase activity in vitro.
CC       {ECO:0000250|UniProtKB:Q5T4B2}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-
CC       ProRule:PRU10138}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 25 family.
CC       {ECO:0000305}.
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DR   EMBL; AL928926; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS15860.1; -.
DR   RefSeq; NP_997181.1; NM_207298.2.
DR   AlphaFoldDB; A3KGW5; -.
DR   SMR; A3KGW5; -.
DR   BioGRID; 221195; 4.
DR   STRING; 10090.ENSMUSP00000041622; -.
DR   CAZy; GT25; Glycosyltransferase Family 25.
DR   GlyGen; A3KGW5; 4 sites.
DR   iPTMnet; A3KGW5; -.
DR   PhosphoSitePlus; A3KGW5; -.
DR   PaxDb; A3KGW5; -.
DR   PeptideAtlas; A3KGW5; -.
DR   PRIDE; A3KGW5; -.
DR   ProteomicsDB; 271111; -.
DR   Antibodypedia; 17470; 114 antibodies from 23 providers.
DR   DNASU; 99151; -.
DR   Ensembl; ENSMUST00000047521; ENSMUSP00000041622; ENSMUSG00000039787.
DR   GeneID; 99151; -.
DR   KEGG; mmu:99151; -.
DR   UCSC; uc008jai.1; mouse.
DR   CTD; 51148; -.
DR   MGI; MGI:2139134; Cercam.
DR   VEuPathDB; HostDB:ENSMUSG00000039787; -.
DR   eggNOG; KOG4179; Eukaryota.
DR   GeneTree; ENSGT01030000234558; -.
DR   HOGENOM; CLU_024037_2_0_1; -.
DR   InParanoid; A3KGW5; -.
DR   OMA; NRQRQGC; -.
DR   OrthoDB; 931915at2759; -.
DR   PhylomeDB; A3KGW5; -.
DR   TreeFam; TF313826; -.
DR   BioGRID-ORCS; 99151; 2 hits in 73 CRISPR screens.
DR   ChiTaRS; Cercam; mouse.
DR   PRO; PR:A3KGW5; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; A3KGW5; protein.
DR   Bgee; ENSMUSG00000039787; Expressed in ascending aorta and 154 other tissues.
DR   ExpressionAtlas; A3KGW5; baseline and differential.
DR   Genevisible; A3KGW5; MM.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0007155; P:cell adhesion; ISO:MGI.
DR   CDD; cd06532; Glyco_transf_25; 1.
DR   Gene3D; 3.90.550.10; -; 1.
DR   InterPro; IPR002654; Glyco_trans_25.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   Pfam; PF01755; Glyco_transf_25; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
DR   PROSITE; PS00014; ER_TARGET; 1.
PE   3: Inferred from homology;
KW   Cell adhesion; Endoplasmic reticulum; Glycoprotein; Reference proteome;
KW   Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..592
FT                   /note="Inactive glycosyltransferase 25 family member 3"
FT                   /id="PRO_0000309545"
FT   REGION          540..592
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           589..592
FT                   /note="Prevents secretion from ER"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT   COMPBIAS        540..568
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        72
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        150
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        234
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        357
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   592 AA;  67672 MW;  8DB0093ACCCA8CB1 CRC64;
     MHVARLLPLL LLLGQQLRAA SVTEPTLPTV VLAILARNAE HSLPHYLGAL ERLDYPRARL
     ALWCATDHNM DNTTGMLREW LAAVGRDYAT VVWKPEEEAR SYPDEQGPKH WTKERHQFLM
     ELRQEALAFA RDWGADYILF ADTDNILTNN QTLKLLIDRQ LPVVAPMLDS QTYYSNFWCG
     ITPQGYYRRT AEYFPTKNRQ RQGCFRVPMV HSTFLLSLQT EETARLAFYP PHPNYSWPFD
     DIIVFAYACQ AAGVSMHVCN DHRYGYMNVV VKPHQSLEEE KTNFIHLILE ALVDGPPMLA
     SAHVSRPPKK LSKMGFDEVF VISLARRPQR RARMLSSLWE MEISAQVVDA VDGRTLNSSI
     LKHLGVDLLP GYQDPYSGHT LTKGEVGCFL SHYSIWEEVV ARGLARVVVF EDDVRFKDNF
     RRRLERLMED VLIQKLSWDL IYLGRKQVNP EEEVAVEGLP GLVVAGYSYW TLAYTLSLAG
     ARKLLASQPL HRMLPVDEFL PVMFDRHPND QYKAYFWPRD LQAFSARPLL ASPTHYSGDA
     EWLSDTETSS PWDDDSGRLI SQTGSQKALR GPHLHLTGSS GHSLHPHHRD EL