GLCM1_BOVIN
ID GLCM1_BOVIN Reviewed; 153 AA.
AC P80195; P35451; Q32P62;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Glycosylation-dependent cell adhesion molecule 1;
DE Short=GlyCAM-1;
DE AltName: Full=28 kDa milk glycoprotein PP3;
DE AltName: Full=Lactophorin;
DE AltName: Full=Proteose-peptone component 3;
DE Short=PP3;
DE Flags: Precursor;
GN Name=GLYCAM1;
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 [MRNA].
RC TISSUE=Milk;
RA Kuriki H., Motoshima H., Minagawa E., Tsukasaki F., Kanno C.;
RT "cDNA cloning of lactophorin from bovine milk.";
RL Submitted (DEC-1993) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7999787; DOI=10.1016/0167-4781(94)00195-9;
RA Johnsen L.B., Soerensen E.S., Petersen T.E., Berglund L.;
RT "Characterization of a bovine mammary gland PP3 cDNA reveals homology with
RT mouse and rat adhesion molecule GlyCAM-1.";
RL Biochim. Biophys. Acta 1260:116-118(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Lactating mammary gland;
RX PubMed=7607540; DOI=10.1016/0378-1119(95)00138-v;
RA Groenen M.A., Dijkhof R.J., der Poel J.J.;
RT "Characterization of a GlyCAM1-like gene (glycosylation-dependent cell
RT adhesion molecule 1) which is highly and specifically expressed in the
RT lactating bovine mammary gland.";
RL Gene 158:189-195(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PROTEIN SEQUENCE OF 19-153, PHOSPHORYLATION AT SER-47; SER-52; SER-56;
RP SER-58 AND SER-64, AND GLYCOSYLATION AT THR-34; ASN-95 AND THR-104.
RC TISSUE=Milk;
RX PubMed=8294608; DOI=10.1017/s0022029900027886;
RA Soerensen E.S., Petersen T.E.;
RT "Phosphorylation, glycosylation and amino acid sequence of component PP3
RT from the proteose peptone fraction of bovine milk.";
RL J. Dairy Res. 60:535-542(1993).
RN [6]
RP PROTEIN SEQUENCE OF 19-48 AND 72-91.
RC TISSUE=Milk;
RX PubMed=8320368; DOI=10.1017/s0022029900027503;
RA Soerensen E.S., Petersen T.E.;
RT "Purification and characterization of three proteins isolated from the
RT proteose peptone fraction of bovine milk.";
RL J. Dairy Res. 60:189-197(1993).
RN [7]
RP PHOSPHORYLATION AT SER-47; SER-52; SER-56; SER-58 AND SER-64, AND
RP GLYCOSYLATION AT THR-34; SER-78; ASN-95 AND THR-104.
RC TISSUE=Milk;
RX PubMed=12918977; DOI=10.1021/ac026295b;
RA Kjeldsen F., Haselmann K.F., Budnik B.A., Sorensen E.S., Zubarev R.A.;
RT "Complete characterization of posttranslational modification sites in the
RT bovine milk protein PP3 by tandem mass spectrometry with electron capture
RT dissociation as the last stage.";
RL Anal. Chem. 75:2355-2361(2003).
CC -!- INTERACTION:
CC P80195; P80195: GLYCAM1; NbExp=4; IntAct=EBI-7562491, EBI-7562491;
CC -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein.
CC -!- TISSUE SPECIFICITY: Highly and specifically expressed in the lactating
CC mammary gland.
CC -!- SIMILARITY: Belongs to the PP3/GlyCAM-1 family. {ECO:0000305}.
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DR EMBL; D26176; BAA05164.1; -; mRNA.
DR EMBL; L36854; AAA79330.1; -; mRNA.
DR EMBL; X79406; CAA55943.1; -; mRNA.
DR EMBL; X83391; CAA58309.1; -; Genomic_DNA.
DR EMBL; BC108244; AAI08245.1; -; mRNA.
DR PIR; S52083; S52083.
DR RefSeq; NP_777253.1; NM_174828.2.
DR AlphaFoldDB; P80195; -.
DR SMR; P80195; -.
DR MINT; P80195; -.
DR STRING; 9913.ENSBTAP00000017854; -.
DR GlyConnect; 318; 3 O-Linked glycans (1 site).
DR iPTMnet; P80195; -.
DR PaxDb; P80195; -.
DR PeptideAtlas; P80195; -.
DR PRIDE; P80195; -.
DR Ensembl; ENSBTAT00000017854; ENSBTAP00000017854; ENSBTAG00000013417.
DR GeneID; 282430; -.
DR KEGG; bta:282430; -.
DR CTD; 644076; -.
DR VEuPathDB; HostDB:ENSBTAG00000013417; -.
DR VGNC; VGNC:108932; GLYCAM1.
DR eggNOG; ENOG502TDVV; Eukaryota.
DR GeneTree; ENSGT00520000060242; -.
DR HOGENOM; CLU_137449_0_0_1; -.
DR InParanoid; P80195; -.
DR OMA; PHAYEVT; -.
DR OrthoDB; 1585143at2759; -.
DR TreeFam; TF339780; -.
DR Proteomes; UP000009136; Chromosome 5.
DR Bgee; ENSBTAG00000013417; Expressed in milk and 21 other tissues.
DR ExpressionAtlas; P80195; baseline.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR InterPro; IPR007906; GLYCAM-1.
DR Pfam; PF05242; GLYCAM-1; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Glycoprotein; Membrane; Phosphoprotein;
KW Reference proteome; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:8294608,
FT ECO:0000269|PubMed:8320368"
FT CHAIN 19..153
FT /note="Glycosylation-dependent cell adhesion molecule 1"
FT /id="PRO_0000025408"
FT REGION 95..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 47
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:12918977,
FT ECO:0000269|PubMed:7999787, ECO:0000269|PubMed:8294608"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:12918977,
FT ECO:0000269|PubMed:7999787, ECO:0000269|PubMed:8294608"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:12918977,
FT ECO:0000269|PubMed:7999787, ECO:0000269|PubMed:8294608"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:12918977,
FT ECO:0000269|PubMed:7999787, ECO:0000269|PubMed:8294608"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:12918977,
FT ECO:0000269|PubMed:7999787, ECO:0000269|PubMed:8294608"
FT CARBOHYD 34
FT /note="O-linked (GalNAc...) threonine; partial"
FT /evidence="ECO:0000269|PubMed:12918977,
FT ECO:0000269|PubMed:7999787, ECO:0000269|PubMed:8294608"
FT CARBOHYD 78
FT /note="O-linked (HexNAc...) serine"
FT /evidence="ECO:0000269|PubMed:12918977"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12918977,
FT ECO:0000269|PubMed:7999787, ECO:0000269|PubMed:8294608"
FT CARBOHYD 104
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:12918977,
FT ECO:0000269|PubMed:8294608"
FT /id="CAR_000158"
SQ SEQUENCE 153 AA; 17152 MW; 6679E5F1F99CB886 CRC64;
MKFLCVLLLA SLAATSLAIL NKPEDETHLE AQPTDASAQF IRNLQISNED LSKEPSISRE
DLISKEQIVI RSSRQPQSQN PKLPLSILKE KHLRNATLGS EETTEHTPSD ASTTEGKLME
LGHKIMRNLE NTVKETIKYL KSLFSHAFEV VKT
