TCO2_BOVIN
ID TCO2_BOVIN Reviewed; 432 AA.
AC Q9XSC9; Q0V8P0; Q1RMV8; Q58CR7; Q58DL8; Q9TR25;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 135.
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 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], PARTIAL PROTEIN SEQUENCE, AND DISULFIDE BONDS.
RC TISSUE=Mammary gland, and Milk;
RX PubMed=10473547; DOI=10.1074/jbc.274.37.26015;
RA Fedosov S.N., Berglund L., Nexo E., Petersen T.E.;
RT "Sequence, S-S bridges, and spectra of bovine transcobalamin expressed in
RT Pichia pastoris.";
RL J. Biol. Chem. 274:26015-26020(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PRO-47.
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PRO-47.
RC STRAIN=Hereford; TISSUE=Uterus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PROTEIN SEQUENCE OF 19-44, AND SUBCELLULAR LOCATION.
RC TISSUE=Milk;
RX PubMed=8547333; DOI=10.1016/0167-4838(95)00173-5;
RA Fedosov S.N., Petersen T.E., Nexo E.;
RT "Transcobalamin from cow milk: isolation and physico-chemical properties.";
RL Biochim. Biophys. Acta 1292:113-119(1996).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 19-432 IN COMPLEX WITH COBALAMIN,
RP AND DISULFIDE BONDS.
RX PubMed=16537422; DOI=10.1073/pnas.0509099103;
RA Wuerges J., Garau G., Geremia S., Fedosov S.N., Petersen T.E.,
RA Randaccio L.;
RT "Structural basis for mammalian vitamin B12 transport by transcobalamin.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:4386-4391(2006).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.73 ANGSTROMS) OF 19-432 IN COMPLEX WITH COBALAMIN,
RP AND DISULFIDE BONDS.
RX PubMed=17943552; DOI=10.1080/15216540701673413;
RA Wuerges J., Geremia S., Fedosov S.N., Randaccio L.;
RT "Vitamin B12 transport proteins: crystallographic analysis of beta-axial
RT ligand substitutions in cobalamin bound to transcobalamin.";
RL IUBMB Life 59:722-729(2007).
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:0000269|PubMed:8547333}.
CC -!- TISSUE SPECIFICITY: Expressed in mammary gland, kidney, lymphatic nodes
CC and liver.
CC -!- SIMILARITY: Belongs to the eukaryotic cobalamin transport proteins
CC family. {ECO:0000305}.
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DR EMBL; AF121289; AAD23829.1; -; mRNA.
DR EMBL; BT021579; AAX46426.1; -; mRNA.
DR EMBL; BT021659; AAX46506.1; -; mRNA.
DR EMBL; BT021880; AAX46727.1; -; mRNA.
DR EMBL; BT021899; AAX46746.1; -; mRNA.
DR EMBL; BT026178; ABG67017.1; -; mRNA.
DR EMBL; BT026282; ABG81438.1; -; mRNA.
DR EMBL; BC114678; AAI14679.1; -; mRNA.
DR PIR; S62672; S62672.
DR RefSeq; NP_776620.2; NM_174195.3.
DR PDB; 2BB6; X-ray; 2.00 A; A/B/C/D=19-432.
DR PDB; 2BBC; X-ray; 2.40 A; A=19-432.
DR PDB; 2V3N; X-ray; 2.73 A; A=19-432.
DR PDB; 2V3P; X-ray; 2.90 A; A=19-432.
DR PDBsum; 2BB6; -.
DR PDBsum; 2BBC; -.
DR PDBsum; 2V3N; -.
DR PDBsum; 2V3P; -.
DR AlphaFoldDB; Q9XSC9; -.
DR SMR; Q9XSC9; -.
DR STRING; 9913.ENSBTAP00000029446; -.
DR PaxDb; Q9XSC9; -.
DR PRIDE; Q9XSC9; -.
DR Ensembl; ENSBTAT00000029446; ENSBTAP00000029446; ENSBTAG00000002770.
DR GeneID; 281518; -.
DR KEGG; bta:281518; -.
DR CTD; 6948; -.
DR VEuPathDB; HostDB:ENSBTAG00000002770; -.
DR VGNC; VGNC:35699; TCN2.
DR eggNOG; ENOG502QSED; Eukaryota.
DR GeneTree; ENSGT00530000063370; -.
DR HOGENOM; CLU_052188_1_0_1; -.
DR InParanoid; Q9XSC9; -.
DR OMA; QCVKDSG; -.
DR OrthoDB; 1233171at2759; -.
DR TreeFam; TF333092; -.
DR Reactome; R-BTA-9758890; Transport of RCbl within the body.
DR EvolutionaryTrace; Q9XSC9; -.
DR Proteomes; UP000009136; Chromosome 17.
DR Bgee; ENSBTAG00000002770; Expressed in cortex of kidney and 107 other tissues.
DR ExpressionAtlas; Q9XSC9; baseline.
DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0140355; F:cargo receptor ligand activity; IEA:Ensembl.
DR GO; GO:0031419; F:cobalamin binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009235; P:cobalamin metabolic process; IEA:Ensembl.
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 Pfam; PF01122; Cobalamin_bind; 1.
DR PROSITE; PS00468; COBALAMIN_BINDING; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cobalt; Cobalt transport; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Ion transport; Metal-binding;
KW Reference proteome; Secreted; Signal; Transport.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:8547333"
FT CHAIN 19..432
FT /note="Transcobalamin-2"
FT /id="PRO_0000005563"
FT BINDING 104
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000269|PubMed:16537422,
FT ECO:0000269|PubMed:17943552"
FT BINDING 152..156
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT BINDING 193..197
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
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 BINDING 245
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000269|PubMed:16537422,
FT ECO:0000269|PubMed:17943552"
FT BINDING 248
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000269|PubMed:16537422,
FT ECO:0000269|PubMed:17943552"
FT BINDING 294
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000269|PubMed:16537422,
FT ECO:0000269|PubMed:17943552"
FT BINDING 400..402
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 21..270
FT DISULFID 116..312
FT DISULFID 165..208
FT VARIANT 47
FT /note="Q -> P"
FT /evidence="ECO:0000269|PubMed:16305752, ECO:0000269|Ref.3"
FT CONFLICT 124
FT /note="G -> A (in Ref. 2; AAX46426)"
FT /evidence="ECO:0000305"
FT CONFLICT 413
FT /note="G -> S (in Ref. 2; ABG67017)"
FT /evidence="ECO:0000305"
FT HELIX 28..38
FT /evidence="ECO:0007829|PDB:2BB6"
FT HELIX 39..43
FT /evidence="ECO:0007829|PDB:2BB6"
FT TURN 47..49
FT /evidence="ECO:0007829|PDB:2BB6"
FT HELIX 52..59
FT /evidence="ECO:0007829|PDB:2BB6"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:2BB6"
FT HELIX 68..84
FT /evidence="ECO:0007829|PDB:2BB6"
FT TURN 91..93
FT /evidence="ECO:0007829|PDB:2V3P"
FT HELIX 102..114
FT /evidence="ECO:0007829|PDB:2BB6"
FT HELIX 121..142
FT /evidence="ECO:0007829|PDB:2BB6"
FT STRAND 144..147
FT /evidence="ECO:0007829|PDB:2BB6"
FT HELIX 154..166
FT /evidence="ECO:0007829|PDB:2BB6"
FT HELIX 173..184
FT /evidence="ECO:0007829|PDB:2BB6"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:2BB6"
FT TURN 192..194
FT /evidence="ECO:0007829|PDB:2BB6"
FT HELIX 195..212
FT /evidence="ECO:0007829|PDB:2BB6"
FT HELIX 216..218
FT /evidence="ECO:0007829|PDB:2BB6"
FT HELIX 219..235
FT /evidence="ECO:0007829|PDB:2BB6"
FT STRAND 243..245
FT /evidence="ECO:0007829|PDB:2BB6"
FT TURN 246..248
FT /evidence="ECO:0007829|PDB:2BB6"
FT HELIX 249..256
FT /evidence="ECO:0007829|PDB:2BB6"
FT HELIX 264..281
FT /evidence="ECO:0007829|PDB:2BB6"
FT TURN 282..284
FT /evidence="ECO:0007829|PDB:2BB6"
FT HELIX 289..298
FT /evidence="ECO:0007829|PDB:2BB6"
FT TURN 299..301
FT /evidence="ECO:0007829|PDB:2BB6"
FT HELIX 304..308
FT /evidence="ECO:0007829|PDB:2BB6"
FT STRAND 312..314
FT /evidence="ECO:0007829|PDB:2BB6"
FT STRAND 334..346
FT /evidence="ECO:0007829|PDB:2BB6"
FT STRAND 348..355
FT /evidence="ECO:0007829|PDB:2BB6"
FT HELIX 360..369
FT /evidence="ECO:0007829|PDB:2BB6"
FT STRAND 370..372
FT /evidence="ECO:0007829|PDB:2BB6"
FT STRAND 375..378
FT /evidence="ECO:0007829|PDB:2BB6"
FT STRAND 385..389
FT /evidence="ECO:0007829|PDB:2BB6"
FT STRAND 398..404
FT /evidence="ECO:0007829|PDB:2BB6"
FT TURN 405..407
FT /evidence="ECO:0007829|PDB:2BB6"
FT TURN 414..416
FT /evidence="ECO:0007829|PDB:2BB6"
FT STRAND 424..431
FT /evidence="ECO:0007829|PDB:2BB6"
SQ SEQUENCE 432 AA; 47958 MW; 5690AB18AC62DA11 CRC64;
MGHLGALLFL LGGLGALANI CEITEVDSTL VERLGQRLLP WMDRLSQEQL NPSIYVGLRL
SSLQAGAKEA HYLHSLKLSY QQSLLRPASN KDDNDSEAKP SMGQLALYLL ALRANCEFIG
GRKGDRLVSQ LKRFLEDEKR AIGHNHQGHP RTSYYQYSLG ILALCVHQKR VHDSVVGKLL
YAVEHKPHLL QDHVSVDTMA MAGMAFSCLE LSNLNPKQRN RINLALKRVQ EKILKAQTPE
GYFGNVYSTP LALQLLMGSL RPSVELGTAC LKAKAALQAS LQHKTFQNPL MISQLLPVLN
QKSYVDLISP DCQAPRALLE PALETPPQAK VPKFIDVLLK VSGISPSYRH SVSVPAGSSL
EDILKNAQEH GRFRFRTQAS LSGPFLTSVL GRKAGEREFW QVLRDPDTPL QQGIADYRPK
DGETIELRLV GW
