Q9XSC9 (TCO2_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Transcobalamin-2
Short name=TC-2

Alternative name(s):
Transcobalamin II
Short name=TC II
Short name=TCII

Gene names

Name:

TCN2

Organism

Bos taurus (Bovine) [Reference proteome]

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	432 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Primary vitamin B12-binding and transport protein. Delivers cobalamin to cells.
Subcellular location	Secreted.
Tissue specificity	Expressed in mammary gland, kidney, lymphatic nodes and liver.
Sequence similarities	Belongs to the eukaryotic cobalamin transport proteins family.

Ontologies

Keywords
Biological process	Cobalt transport Ion transport Transport
Cellular component	Secreted
Coding sequence diversity	Polymorphism
Domain	Signal
Ligand	Cobalt Metal-binding
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cobalamin metabolic process Inferred from sequence or structural similarity. Source: RefGenome cobalamin transport Inferred from electronic annotation. Source: InterPro cobalt ion transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	cobalamin binding Inferred from direct assay Ref.5. Source: UniProtKB metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 18

18

Ref.4

Chain

19 – 432

414

Transcobalamin-2

PRO_0000005563

Regions

Region

152 – 156

5

Cobalamin binding

Region

193 – 197

5

Cobalamin binding

Region

400 – 402

3

Cobalamin binding

Sites

Metal binding

193

1

Cobalt (cobalamin axial ligand)

Binding site

104

1

Cobalamin

Binding site

245

1

Cobalamin

Binding site

248

1

Cobalamin

Binding site

294

1

Cobalamin

Amino acid modifications

Glycosylation

94

1

N-linked (GlcNAc...) Potential

Disulfide bond

21 ↔ 270

Ref.1 Ref.5 Ref.6

Disulfide bond

116 ↔ 312

Ref.1 Ref.5 Ref.6

Disulfide bond

165 ↔ 208

Ref.1 Ref.5 Ref.6

Natural variations

Natural variant

47

1

Q → P. Ref.2 Ref.3

Experimental info

Sequence conflict

124

1

G → A in AAX46426. Ref.2

Sequence conflict

413

1

G → S in ABG67017. Ref.2

Secondary structure

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432

Helix Strand Turn

Details...

Helix

28 – 38

11

Helix

39 – 43

5

Turn

47 – 49

3

Helix

52 – 59

8

Beta strand

61 – 64

4

Helix

68 – 84

17

Turn

91 – 93

3

Helix

102 – 114

13

Helix

121 – 142

22

Beta strand

144 – 147

4

Helix

154 – 166

13

Helix

173 – 184

12

Beta strand

185 – 187

3

Turn

192 – 194

3

Helix

195 – 212

18

Helix

216 – 218

3

Helix

219 – 235

17

Beta strand

243 – 245

3

Turn

246 – 248

3

Helix

249 – 256

8

Helix

264 – 281

18

Turn

282 – 284

3

Helix

289 – 298

10

Turn

299 – 301

3

Helix

304 – 308

5

Beta strand

312 – 314

3

Beta strand

334 – 346

13

Beta strand

348 – 355

8

Helix

360 – 369

10

Beta strand

370 – 372

3

Beta strand

375 – 378

4

Beta strand

385 – 389

5

Beta strand

398 – 404

7

Turn

405 – 407

3

Turn

414 – 416

3

Beta strand

424 – 431

8

Sequences

	Sequence		Length	Mass (Da)
	Q9XSC9 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: 5690AB18AC62DA11	FASTA	432	47,958
	10 20 30 40 50 60 MGHLGALLFL LGGLGALANI CEITEVDSTL VERLGQRLLP WMDRLSQEQL NPSIYVGLRL 70 80 90 100 110 120 SSLQAGAKEA HYLHSLKLSY QQSLLRPASN KDDNDSEAKP SMGQLALYLL ALRANCEFIG 130 140 150 160 170 180 GRKGDRLVSQ LKRFLEDEKR AIGHNHQGHP RTSYYQYSLG ILALCVHQKR VHDSVVGKLL 190 200 210 220 230 240 YAVEHKPHLL QDHVSVDTMA MAGMAFSCLE LSNLNPKQRN RINLALKRVQ EKILKAQTPE 250 260 270 280 290 300 GYFGNVYSTP LALQLLMGSL RPSVELGTAC LKAKAALQAS LQHKTFQNPL MISQLLPVLN 310 320 330 340 350 360 QKSYVDLISP DCQAPRALLE PALETPPQAK VPKFIDVLLK VSGISPSYRH SVSVPAGSSL 370 380 390 400 410 420 EDILKNAQEH GRFRFRTQAS LSGPFLTSVL GRKAGEREFW QVLRDPDTPL QQGIADYRPK 430 DGETIELRLV GW

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence, S-S bridges, and spectra of bovine transcobalamin expressed in Pichia pastoris." Fedosov S.N., Berglund L., Nexo E., Petersen T.E. J. Biol. Chem. 274:26015-26020(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, DISULFIDE BONDS. Tissue: Mammary gland and Milk.
[2]	"Characterization of 954 bovine full-CDS cDNA sequences." Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L. BMC Genomics 6:166-166(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT PRO-47.
[3]	NIH - Mammalian Gene Collection (MGC) project Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT PRO-47. Strain: Hereford. Tissue: Uterus.
[4]	"Transcobalamin from cow milk: isolation and physico-chemical properties." Fedosov S.N., Petersen T.E., Nexo E. Biochim. Biophys. Acta 1292:113-119(1996) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 19-44. Tissue: Milk.
[5]	"Structural basis for mammalian vitamin B12 transport by transcobalamin." Wuerges J., Garau G., Geremia S., Fedosov S.N., Petersen T.E., Randaccio L. Proc. Natl. Acad. Sci. U.S.A. 103:4386-4391(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 19-432 IN COMPLEX WITH COBALAMIN, DISULFIDE BONDS.
[6]	"Vitamin B12 transport proteins: crystallographic analysis of beta-axial ligand substitutions in cobalamin bound to transcobalamin." Wuerges J., Geremia S., Fedosov S.N., Randaccio L. IUBMB Life 59:722-729(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.73 ANGSTROMS) OF 19-432 IN COMPLEX WITH COBALAMIN, DISULFIDE BONDS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF121289 mRNA. Translation: AAD23829.1.
BT021579 mRNA. Translation: AAX46426.1.
BT021659 mRNA. Translation: AAX46506.1.
BT021880 mRNA. Translation: AAX46727.1.
BT021899 mRNA. Translation: AAX46746.1.
BT026178 mRNA. Translation: ABG67017.1.
BT026282 mRNA. Translation: ABG81438.1.
BC114678 mRNA. Translation: AAI14679.1.

IPI

IPI00718019.

PIR

S62672.

RefSeq

NP_776620.2. NM_174195.3.

UniGene

Bt.44412.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2BB6	X-ray	2.00	A/B/C/D	19-432	[»]
2BBC	X-ray	2.40	A	19-432	[»]
2V3N	X-ray	2.73	A	19-432	[»]
2V3P	X-ray	2.90	A	19-432	[»]

ProteinModelPortal

Q9XSC9.

SMR

Q9XSC9. Positions 19-432.

ModBase

Search...

Protein-protein interaction databases

STRING

9913.ENSBTAP00000029446.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSBTAT00000029446; ENSBTAP00000029446; ENSBTAG00000002770.

GeneID

281518.

KEGG

bta:281518.

Organism-specific databases

CTD

6948.

Phylogenomic databases

eggNOG

NOG47054.

GeneTree

ENSGT00530000063370.

HOGENOM

HOG000074060.

HOVERGEN

HBG001328.

InParanoid

Q9XSC9.

KO

K14619.

OMA

KAQTPEG.

OrthoDB

EOG4VDPZJ.

Gene expression databases

ArrayExpress

Q9XSC9.

Family and domain databases

InterPro

IPR002157. Cbl-bd_transpt_euk.
[Graphical view]

PANTHER

PTHR10559. PTHR10559. 1 hit.

Pfam

PF01122. Cobalamin_bind. 1 hit.
[Graphical view]

PROSITE

PS00468. COBALAMIN_BINDING. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q9XSC9.

NextBio

20805483.

Entry information

Entry name

TCO2_BOVIN

Accession

Primary (citable) accession number: Q9XSC9
Secondary accession number(s): Q0V8P0 , Q1RMV8, Q58CR7, Q58DL8, Q9TR25

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 27, 2001
Last sequence update:	November 1, 1999
Last modified:	April 3, 2013
This is version 89 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program