ID   TCO1_PIG                Reviewed;         417 AA.
AC   P17630;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   11-JUN-2014, sequence version 2.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Transcobalamin-1;
DE            Short=TC-1;
DE   AltName: Full=Cobalophilin;
DE   AltName: Full=Haptocorrin;
DE   AltName: Full=Protein R;
DE   AltName: Full=Transcobalamin I;
DE            Short=TC I;
DE            Short=TCI;
DE   Flags: Precursor;
GN   Name=TCN1;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 2-417, AND PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Stomach;
RX   PubMed=2331993; DOI=10.1111/j.1432-1033.1990.tb15468.x;
RA   Hewitt J.E., Seetharam B., Leykam J.F., Alpers D.H.;
RT   "Isolation and characterization of a cDNA encoding porcine gastric
RT   haptocorrin.";
RL   Eur. J. Biochem. 189:125-130(1990).
CC   -!- FUNCTION: Binds vitamin B12 with femtomolar affinity and protects it
CC       from the acidic environment of the stomach (By similarity). Binds to
CC       cobalamin and to cobalamin analogs such as cobinamide. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Haptocorrins are a family of cobalamin-binding
CC       glycoproteins found in blood, salivary and mucosal secretions.
CC   -!- PTM: Contains about 30% carbohydrates.
CC   -!- SIMILARITY: Belongs to the eukaryotic cobalamin transport proteins
CC       family. {ECO:0000305}.
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DR   EMBL; X52566; CAA36800.1; -; mRNA.
DR   PIR; S09334; S09334.
DR   AlphaFoldDB; P17630; -.
DR   SMR; P17630; -.
DR   PaxDb; P17630; -.
DR   PeptideAtlas; P17630; -.
DR   InParanoid; P17630; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0031419; F:cobalamin binding; IBA:GO_Central.
DR   GO; GO:0015889; P:cobalamin transport; IBA:GO_Central.
DR   GO; GO:0006824; P:cobalt ion transport; IEA:UniProtKB-KW.
DR   InterPro; IPR002157; Cbl-bd_prot.
DR   InterPro; IPR027954; DUF4430.
DR   Pfam; PF01122; Cobalamin_bind; 1.
DR   Pfam; PF14478; DUF4430; 1.
DR   PROSITE; PS00468; COBALAMIN_BINDING; 1.
PE   1: Evidence at protein level;
KW   Cobalt; Cobalt transport; Direct protein sequencing; Disulfide bond;
KW   Glycoprotein; Ion transport; Reference proteome; Secreted; Signal;
KW   Transport.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000305"
FT   CHAIN           26..417
FT                   /note="Transcobalamin-1"
FT                   /id="PRO_0000005562"
FT   REGION          24..308
FT                   /note="Globular N-terminal alpha domain"
FT                   /evidence="ECO:0000250"
FT   REGION          309..327
FT                   /note="Flexible linker"
FT                   /evidence="ECO:0000250"
FT   REGION          328..417
FT                   /note="Globular C-terminal beta domain"
FT                   /evidence="ECO:0000250"
FT   BINDING         143..147
FT                   /ligand="cyanocob(III)alamin"
FT                   /ligand_id="ChEBI:CHEBI:17439"
FT                   /evidence="ECO:0000250|UniProtKB:P20061"
FT   BINDING         187
FT                   /ligand="cyanocob(III)alamin"
FT                   /ligand_id="ChEBI:CHEBI:17439"
FT                   /evidence="ECO:0000250|UniProtKB:P20061"
FT   BINDING         287
FT                   /ligand="cyanocob(III)alamin"
FT                   /ligand_id="ChEBI:CHEBI:17439"
FT                   /evidence="ECO:0000250|UniProtKB:P20061"
FT   BINDING         376..377
FT                   /ligand="cyanocob(III)alamin"
FT                   /ligand_id="ChEBI:CHEBI:17439"
FT                   /evidence="ECO:0000250|UniProtKB:P20061"
FT   BINDING         393..395
FT                   /ligand="cyanocob(III)alamin"
FT                   /ligand_id="ChEBI:CHEBI:17439"
FT                   /evidence="ECO:0000250|UniProtKB:P20061"
FT   CARBOHYD        90
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        161
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        166
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        179
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        312
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        328
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        345
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        360
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        156..198
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   417 AA;  47095 MW;  C629088F1D13D623 CRC64;
     MRQSHQLPLV GLLLFSLIPS QLCQSCVVSE KDYSHLRLLI SAMDNLEQIR GIYGASILLS
     QRLAGIQNPS LEEELSQRIQ DDMNRRDMSN LTSGQLALII LAFGACKTPD VRFIHDHHLV
     EKLGEKFKEE IKNMEIHNSN PLTNYYQLSF DVLTLCLFRG NYSISNVTHY FNPENKNFNL
     SGHFSVDTGA VAVLALTCVK RSISNGKIKA AIKDSDTIQK YIESLVHKIQ SEKMVVSLET
     RIAQEKLCRL SLSHQTITKM NQIAKKLWTR CLTHSQGVFR LPIAAAQILP ALLGKTYLDV
     TKLLLVPKVQ VNITDEPVPV VPTLSPENIS VIYCVKINEI SNCINITVFL DVMKAAQEKN
     STIYGFTMTE TPWGPYITSV QGIWANNNER TYWEHSEQQQ ITKPRSMGIM LSKMESI