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   24-JAN-2024, entry version 133.
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   GlyCosmos; P80195; 4 sites, 5 glycans.
DR   iPTMnet; P80195; -.
DR   PaxDb; 9913-ENSBTAP00000017854; -.
DR   PeptideAtlas; P80195; -.
DR   Ensembl; ENSBTAT00000017854.3; ENSBTAP00000017854.2; ENSBTAG00000013417.3.
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; SEEETHW; -.
DR   OrthoDB; 4995077at2759; -.
DR   TreeFam; TF339780; -.
DR   Proteomes; UP000009136; Chromosome 5.
DR   Bgee; ENSBTAG00000013417; Expressed in milk and 21 other cell types or tissues.
DR   ExpressionAtlas; P80195; baseline and differential.
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
//