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P20061 (TCO1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 132. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transcobalamin-1

Short name=TC-1
Alternative name(s):
Haptocorrin
Short name=HC
Protein R
Transcobalamin I
Short name=TC I
Short name=TCI
Gene names
Name:TCN1
Synonyms:TC1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length433 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binds vitamin B12 with femtomolar affinity and protects it from the acidic environment of the stomach.

Subcellular location

Secreted.

Tissue specificity

Produced by the salivary glands of the oral cavity, in response to ingestion of food. Major constituent of secondary granules in neutrophils. Ref.1

Post-translational modification

Contains about 30% carbohydrates.

Sequence similarities

Belongs to the eukaryotic cobalamin transport proteins family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323
Chain24 – 433410Transcobalamin-1
PRO_0000005561

Regions

Region24 – 310287Globular N-terminal alpha domain
Region142 – 1465Cobalamin binding
Region182 – 1865Cobalamin binding
Region311 – 33222Flexible linker
Region333 – 433101Globular C-terminal beta domain
Region402 – 4043Cobalamin binding

Sites

Binding site2401Cobalamin
Binding site2431Cobalamin
Binding site2891Cobalamin
Binding site4331Cobalamin

Amino acid modifications

Glycosylation1601N-linked (GlcNAc...) Potential
Glycosylation2161N-linked (GlcNAc...) Ref.5 Ref.6 Ref.7
Glycosylation3161N-linked (GlcNAc...) Ref.7
Glycosylation3371N-linked (GlcNAc...) Ref.7
Glycosylation3431N-linked (GlcNAc...) Ref.7
Glycosylation3491N-linked (GlcNAc...) Ref.7
Glycosylation3541N-linked (GlcNAc...) Ref.7
Glycosylation3691N-linked (GlcNAc...) Ref.6 Ref.7
Disulfide bond26 ↔ 265 Ref.7
Disulfide bond105 ↔ 308 Ref.7
Disulfide bond155 ↔ 197 Ref.7
Disulfide bond388 ↔ 393 Ref.7

Natural variations

Natural variant351R → H.
Corresponds to variant rs34528912 [ dbSNP | Ensembl ].
VAR_031923
Natural variant3011D → Y.
Corresponds to variant rs34324219 [ dbSNP | Ensembl ].
VAR_031924

Experimental info

Sequence conflict1191I → T in AAA61058. Ref.1

Secondary structure

............................................................... 433
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P20061 [UniParc].

Last modified May 1, 2007. Version 2.
Checksum: CF1052BE3DBA929A

FASTA43348,207
        10         20         30         40         50         60 
MRQSHQLPLV GLLLFSFIPS QLCEICEVSE ENYIRLKPLL NTMIQSNYNR GTSAVNVVLS 

        70         80         90        100        110        120 
LKLVGIQIQT LMQKMIQQIK YNVKSRLSDV SSGELALIIL ALGVCRNAEE NLIYDYHLID 

       130        140        150        160        170        180 
KLENKFQAEI ENMEAHNGTP LTNYYQLSLD VLALCLFNGN YSTAEVVNHF TPENKNYYFG 

       190        200        210        220        230        240 
SQFSVDTGAM AVLALTCVKK SLINGQIKAD EGSLKNISIY TKSLVEKILS EKKENGLIGN 

       250        260        270        280        290        300 
TFSTGEAMQA LFVSSDYYNE NDWNCQQTLN TVLTEISQGA FSNPNAAAQV LPALMGKTFL 

       310        320        330        340        350        360 
DINKDSSCVS ASGNFNISAD EPITVTPPDS QSYISVNYSV RINETYFTNV TVLNGSVFLS 

       370        380        390        400        410        420 
VMEKAQKMND TIFGFTMEER SWGPYITCIQ GLCANNNDRT YWELLSGGEP LSQGAGSYVV 

       430 
RNGENLEVRW SKY 

« Hide

References

« Hide 'large scale' references
[1]"Structure of the cDNA encoding transcobalamin I, a neutrophil granule protein."
Johnston J., Bollekens J., Allen R.H., Berliner N.
J. Biol. Chem. 264:15754-15757(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Trachea.
[3]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-216.
Tissue: Plasma.
[6]"Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry."
Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T., Loo J.A.
J. Proteome Res. 5:1493-1503(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-216 AND ASN-369.
Tissue: Saliva.
[7]"Structural basis for universal corrinoid recognition by the cobalamin transport protein haptocorrin."
Furger E., Frei D.C., Schibli R., Fischer E., Prota A.E.
J. Biol. Chem. 288:25466-25476(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) IN COMPLEX WITH CYANOCOBALAMIN, DISULFIDE BONDS, COBALAMIN-BINDING SITES, GLYCOSYLATION AT ASN-216; ASN-316; ASN-337; ASN-343; ASN-349; ASN-354 AND ASN-369.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J05068 mRNA. Translation: AAA61058.1.
AK292990 mRNA. Translation: BAF85679.1.
AP002347 Genomic DNA. No translation available.
CH471076 Genomic DNA. Translation: EAW73861.1.
CCDSCCDS7978.1.
PIRA34227.
RefSeqNP_001053.2. NM_001062.3.
UniGeneHs.2012.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2CKVmodel-Y24-433[»]
4KKIX-ray2.35A1-433[»]
4KKJX-ray3.00A1-433[»]
ProteinModelPortalP20061.
SMRP20061. Positions 24-433.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112807. 2 interactions.
IntActP20061. 1 interaction.
STRING9606.ENSP00000257264.

Chemistry

DrugBankDB00115. Cyanocobalamin.
DB00200. Hydroxocobalamin.

PTM databases

PhosphoSiteP20061.

Polymorphism databases

DMDM146345530.

Proteomic databases

PaxDbP20061.
PRIDEP20061.

Protocols and materials databases

DNASU6947.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000257264; ENSP00000257264; ENSG00000134827.
GeneID6947.
KEGGhsa:6947.
UCSCuc001noj.2. human.

Organism-specific databases

CTD6947.
GeneCardsGC11M059620.
H-InvDBHIX0009662.
HGNCHGNC:11652. TCN1.
HPAHPA041631.
MIM189905. gene.
neXtProtNX_P20061.
PharmGKBPA36403.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG79743.
HOGENOMHOG000013214.
HOVERGENHBG094393.
InParanoidP20061.
OMAENLEVRW.
OrthoDBEOG771277.
PhylomeDBP20061.
TreeFamTF333092.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.

Gene expression databases

BgeeP20061.
CleanExHS_TCN1.
GenevestigatorP20061.

Family and domain databases

InterProIPR002157. Cbl-bd_transpt_euk.
IPR027954. DUF4430.
[Graphical view]
PANTHERPTHR10559. PTHR10559. 1 hit.
PfamPF01122. Cobalamin_bind. 1 hit.
PF14478. DUF4430. 1 hit.
[Graphical view]
PROSITEPS00468. COBALAMIN_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiHaptocorrin.
GenomeRNAi6947.
NextBio27199.
PROP20061.
SOURCESearch...

Entry information

Entry nameTCO1_HUMAN
AccessionPrimary (citable) accession number: P20061
Secondary accession number(s): A8KAC5, Q8WV77
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: May 1, 2007
Last modified: July 9, 2014
This is version 132 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM