ID   TCO2_RAT                Reviewed;         427 AA.
AC   Q9R0D6;
DT   13-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Transcobalamin-2;
DE            Short=TC-2;
DE   AltName: Full=Transcobalamin II;
DE            Short=TC II;
DE            Short=TCII;
DE   Flags: Precursor;
GN   Name=Tcn2;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Kidney;
RX   PubMed=15488467; DOI=10.1016/j.abb.2004.08.011;
RA   Kalra S., Li N., Yammani R.R., Seetharam S., Seetharam B.;
RT   "Cobalamin (vitamin B12) binding, phylogeny, and synteny of human
RT   transcobalamin.";
RL   Arch. Biochem. Biophys. 431:189-196(2004).
CC   -!- FUNCTION: Primary vitamin B12-binding and transport protein. Delivers
CC       cobalamin to cells. {ECO:0000250|UniProtKB:P20062}.
CC   -!- SUBUNIT: Interacts with CD320 (via LDL-receptor class A domains).
CC       {ECO:0000250|UniProtKB:P20062}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P20062}.
CC   -!- SIMILARITY: Belongs to the eukaryotic cobalamin transport proteins
CC       family. {ECO:0000305}.
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DR   EMBL; AF054810; AAD55672.1; -; mRNA.
DR   AlphaFoldDB; Q9R0D6; -.
DR   SMR; Q9R0D6; -.
DR   STRING; 10116.ENSRNOP00000005934; -.
DR   PaxDb; Q9R0D6; -.
DR   UCSC; RGD:620681; rat.
DR   RGD; 620681; Tcn2.
DR   eggNOG; ENOG502QSED; Eukaryota.
DR   InParanoid; Q9R0D6; -.
DR   PhylomeDB; Q9R0D6; -.
DR   Reactome; R-RNO-9758890; Transport of RCbl within the body.
DR   PRO; PR:Q9R0D6; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
DR   GO; GO:0005615; C:extracellular space; IDA:RGD.
DR   GO; GO:0140355; F:cargo receptor ligand activity; ISO:RGD.
DR   GO; GO:0031419; F:cobalamin binding; IDA:RGD.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009235; P:cobalamin metabolic process; ISO:RGD.
DR   GO; GO:0015889; P:cobalamin transport; ISS:UniProtKB.
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   2: Evidence at transcript level;
KW   Cobalt; Cobalt transport; Disulfide bond; Ion transport; Metal-binding;
KW   Reference proteome; Secreted; Signal; Transport.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000250"
FT   CHAIN           19..427
FT                   /note="Transcobalamin-2"
FT                   /id="PRO_0000005567"
FT   BINDING         152..156
FT                   /ligand="cob(II)alamin"
FT                   /ligand_id="ChEBI:CHEBI:16304"
FT                   /evidence="ECO:0000250"
FT   BINDING         193..197
FT                   /ligand="cob(II)alamin"
FT                   /ligand_id="ChEBI:CHEBI:16304"
FT                   /evidence="ECO:0000250"
FT   BINDING         193
FT                   /ligand="cob(II)alamin"
FT                   /ligand_id="ChEBI:CHEBI:16304"
FT                   /ligand_part="Co"
FT                   /ligand_part_id="ChEBI:CHEBI:27638"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250"
FT   BINDING         245
FT                   /ligand="cob(II)alamin"
FT                   /ligand_id="ChEBI:CHEBI:16304"
FT                   /evidence="ECO:0000250"
FT   BINDING         248
FT                   /ligand="cob(II)alamin"
FT                   /ligand_id="ChEBI:CHEBI:16304"
FT                   /evidence="ECO:0000250"
FT   BINDING         292
FT                   /ligand="cob(II)alamin"
FT                   /ligand_id="ChEBI:CHEBI:16304"
FT                   /evidence="ECO:0000250"
FT   BINDING         395..397
FT                   /ligand="cob(II)alamin"
FT                   /ligand_id="ChEBI:CHEBI:16304"
FT                   /evidence="ECO:0000250"
FT   DISULFID        21..268
FT                   /evidence="ECO:0000250"
FT   DISULFID        116..310
FT                   /evidence="ECO:0000250"
FT   DISULFID        165..208
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   427 AA;  47420 MW;  BA7E1351667BDF0C CRC64;
     MELLKALLLL SGVLGALAEF CVIPKMDGQL VEKLGQRLLP WMDRLSSEQL NPSIYVGLRL
     SSMQAGTKEN LYLHNLKLHY QQCLLRSTSS DDNSGCQTKI SGGSLALYLL ALRANCELLG
     SRKGDRMVSQ LKWFLEDEKK AIGHHHEGHP HTSYYQYGLS ILALCVHRKR VHDSVVGKLL
     YAVEHDYFTY QGHLSVDTEA MAGLAFTCLE RFNFNSDLRP RITTAIETVR EKILKAQAPE
     GYFGNIYSTP LALQMLMTSP GVGLGPACLK ARKSLLLSLQ DGAFQNPMMI SQLLPVLNHK
     TYLNLISPDC QAPRVMLVPA TEDPVHLSEV SVTLKVSSVL PPYERTVSVF AGASLEDVLN
     RARDLGEFTY GTQASLSGPY LTSVLGKEAG DREYWQLLRV PDTPLLQGIA DYKPKNGETI
     ELRLVKM