ID   GT253_BOVIN             Reviewed;         595 AA.
AC   A7MB73;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Probable inactive glycosyltransferase 25 family member 3;
DE   AltName: Full=Cerebral endothelial cell adhesion molecule;
DE   Flags: Precursor;
GN   Name=CERCAM; Synonyms=CEECAM1, GLT25D3;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal muscle;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
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; BC151373; AAI51374.1; -; mRNA.
DR   RefSeq; NP_001095505.1; NM_001102035.1.
DR   AlphaFoldDB; A7MB73; -.
DR   SMR; A7MB73; -.
DR   STRING; 9913.ENSBTAP00000004595; -.
DR   CAZy; GT25; Glycosyltransferase Family 25.
DR   PaxDb; A7MB73; -.
DR   Ensembl; ENSBTAT00000004595; ENSBTAP00000004595; ENSBTAG00000038139.
DR   GeneID; 516122; -.
DR   KEGG; bta:516122; -.
DR   CTD; 51148; -.
DR   VEuPathDB; HostDB:ENSBTAG00000038139; -.
DR   VGNC; VGNC:27222; CERCAM.
DR   eggNOG; KOG4179; Eukaryota.
DR   GeneTree; ENSGT01030000234558; -.
DR   HOGENOM; CLU_024037_2_0_1; -.
DR   InParanoid; A7MB73; -.
DR   OMA; NRQRQGC; -.
DR   OrthoDB; 931915at2759; -.
DR   Proteomes; UP000009136; Chromosome 11.
DR   Bgee; ENSBTAG00000038139; Expressed in thyroid gland and 99 other tissues.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
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   2: Evidence at transcript level;
KW   Cell adhesion; Endoplasmic reticulum; Glycoprotein; Reference proteome;
KW   Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..595
FT                   /note="Probable inactive glycosyltransferase 25 family
FT                   member 3"
FT                   /id="PRO_0000309543"
FT   REGION          576..595
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           592..595
FT                   /note="Prevents secretion from ER"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT   CARBOHYD        75
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        153
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        237
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        360
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   595 AA;  67466 MW;  B95DF9D68F1C9460 CRC64;
     MRAAPAAPLL QLLLLLGPRP EAAGVAEPPL PTVVLAILAR NAEHSLPHYL GALERLDYPR
     ARLALWCATD HNVDNTTAML REWLAAVGDN YAAVVWRPEG EPRSYPDEEG PKHWTKERHQ
     FLMELKQEAL TFARDWGADY ILFADTDNIL TNNQTLRLLI EPGLPVVAPM LDSQTYYSNF
     WCGITPQGYY RRTADYFPTK NRQRRGCFRV PMVHSTFLVS LRAEGTGQLA FYPPHPNYTW
     PFDDIIVFAY ACQAAGVAVH VCNEQRYGYL NVPVKSHQGL EDERVNFIHL ILEALVDGPP
     MWASAHVSRP PKRPSKMGFD EVFVISLARR PDRRERMLTS LWEMEISGRV VDAVDGRMLN
     SSVMRTLGVD LLPGYQDPYS GRTLTKGEVG CFLSHYSIWE EVVTRGLAQV VVFEDDVRFE
     SNFKGRLEQL MEEVEAEKLP WDLIYLGRKQ VNPEEEAVVE GLPHLVAAGY SYWTLAYVLS
     LAGARKLLAS QPLRRMLPVD EFLPIMFDQH PNEQYKAHFW PRDLQAFSAR PLLAAPTHYA
     GDSEWLSDTE TSSPWDDDSG RLISWTGSYK TLRGPRLDLA GGSGHSLRPH PRDEL