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 04-NOV-2026, entry version 152. 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 IN COMPLEX WITH COBALAMIN, 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 IN COMPLEX WITH COBALAMIN, 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 AlphaFoldDB; Q9XSC9; -. DR SMR; Q9XSC9; -. DR FunCoup; Q9XSC9; 396. DR STRING; 9913.ENSBTAP00000029446; -. DR GlyCosmos; Q9XSC9; 1 site, No reported glycans. DR GlyGen; Q9XSC9; 1 site. DR PaxDb; 9913-ENSBTAP00000029446; -. DR GeneID; 281518; -. DR KEGG; bta:281518; -. DR CTD; 6948; -. DR VEuPathDB; HostDB:ENSBTAG00000002770; -. DR VGNC; VGNC:35699; TCN2. DR eggNOG; ENOG502QSED; Eukaryota. DR HOGENOM; CLU_052188_1_0_1; -. DR InParanoid; Q9XSC9; -. DR OMA; AACHNMD; -. DR OrthoDB; 9440006at2759; -. 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 cell types or tissues. DR ExpressionAtlas; Q9XSC9; baseline. DR GO; GO:0005576; C:extracellular region; EXP:UniProtKB. DR GO; GO:0031419; F:cobalamin binding; IDA:UniProtKB. DR GO; GO:0015889; P:cobalamin transport; ISS:UniProtKB. DR FunFam; 1.50.10.20:FF:000013; Transcobalamin-2; 1. DR FunFam; 2.170.130.30:FF:000002; Transcobalamin-2; 1. DR Gene3D; 1.50.10.20; -; 1. DR Gene3D; 2.170.130.30; -; 1. DR InterPro; IPR002157; Cbl-bd_prot. DR InterPro; IPR051588; Cobalamin_Transport. DR PANTHER; PTHR10559; TRANSCOBALAMIN-1/GASTRIC INTRINSIC FACTOR; 1. DR PANTHER; PTHR10559:SF14; TRANSCOBALAMIN-2; 1. 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 98..101 FT /evidence="ECO:0007829|PDB:2V3N" 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 //