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O88968 (TCO2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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-2

Short name=TC-2
Alternative name(s):
Transcobalamin II
Short name=TC II
Short name=TCII
Gene names
Name:Tcn2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length430 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Primary vitamin B12-binding and transport protein. Delivers cobalamin to cells By similarity.

Subcellular location

Secreted.

Sequence similarities

Belongs to the eukaryotic cobalamin transport proteins family.

Ontologies

Keywords
   Biological processCobalt transport
Ion transport
Transport
   Cellular componentSecreted
   Coding sequence diversityPolymorphism
   DomainSignal
   LigandCobalt
Metal-binding
   PTMDisulfide bond
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcobalamin metabolic process

Inferred from Biological aspect of Ancestor. Source: RefGenome

cobalamin transport

Inferred from electronic annotation. Source: InterPro

cobalt ion transport

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncobalamin binding

Inferred from sequence or structural similarity. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 By similarity
Chain19 – 430412Transcobalamin-2
PRO_0000005565

Regions

Region152 – 1565Cobalamin binding By similarity
Region193 – 1975Cobalamin binding By similarity
Region398 – 4003Cobalamin binding By similarity

Sites

Metal binding1931Cobalt (cobalamin axial ligand) By similarity
Binding site2451Cobalamin By similarity
Binding site2481Cobalamin By similarity
Binding site2941Cobalamin By similarity

Amino acid modifications

Disulfide bond21 ↔ 270 By similarity
Disulfide bond116 ↔ 312 By similarity
Disulfide bond165 ↔ 208 By similarity

Natural variations

Natural variant1021G → E in strain: NZB. Ref.1

Experimental info

Sequence conflict191E → G in BAE25528. Ref.2
Sequence conflict2911M → V in BAE41770. Ref.2

Sequences

Sequence LengthMass (Da)Tools
O88968 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 2EFF1427E48480A5

FASTA43047,586
        10         20         30         40         50         60 
MELLKALLLL SGVFGALAEF CVIPRIDSQL VEKLGQRLLP WMDRLSSEQL NPSVFVGLRL 

        70         80         90        100        110        120 
SSMQAGTKED LYLHSLKIHY QQCLLRSTSS DDNSSCQPKL SGGSLALYLL ALRANCEFFG 

       130        140        150        160        170        180 
SRKGDRLISQ LKWFLEDEKK AIGHNHEGHP NTNYYQYGLS ILALCVHQKR LHDSVVGKLL 

       190        200        210        220        230        240 
YAVEHDYFTY QGHVSVDTEA MAGLALTCLE RFNFNSDLRP RITMAIETVR EKILKSQAPE 

       250        260        270        280        290        300 
GYFGNIYSTP LALQMLMTSP ASGVGLGTAC IKAGTSLLLS LQDGAFQNPL MISQLLPILN 

       310        320        330        340        350        360 
HKTYLDLIFP DCQASRVMLV PAVEDPVHIS EVISVTLKVA SALSPYEQTF FVFAGSSLED 

       370        380        390        400        410        420 
VLKLAQDGGG FTYGTQASLS GPYLTSVLGK DAGDREYWQL LRAPDTPLLQ GIADYKPQDG 

       430 
ETIELRLVRW 

« Hide

References

« Hide 'large scale' references
[1]"Mouse transcobalamin II: polymorphism in NZB."
Hasegawa M., Foote S.
Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT GLU-102.
Strain: BALB/c and NZB.
Tissue: Liver.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J and NOD.
Tissue: Head, Kidney and Spleen.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[4]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF090686 mRNA. Translation: AAC61868.1.
AK133707 mRNA. Translation: BAE21792.1.
AK143761 mRNA. Translation: BAE25528.1.
AK147176 mRNA. Translation: BAE27739.1.
AK161618 mRNA. Translation: BAE36496.1.
AK170401 mRNA. Translation: BAE41770.1.
AL807395, AL807241 Genomic DNA. Translation: CAI26040.1.
AL807241, AL807395 Genomic DNA. Translation: CAI51997.1.
CH466574 Genomic DNA. Translation: EDL40449.1.
BC003720 mRNA. Translation: AAH03720.1.
CCDSCCDS24371.1.
RefSeqNP_001123930.1. NM_001130458.1.
NP_001123931.1. NM_001130459.1.
NP_056564.1. NM_015749.3.
XP_006514673.1. XM_006514610.1.
XP_006514674.1. XM_006514611.1.
XP_006514675.1. XM_006514612.1.
XP_006514676.1. XM_006514613.1.
UniGeneMm.20948.

3D structure databases

ProteinModelPortalO88968.
SMRO88968. Positions 19-430.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteO88968.

Proteomic databases

MaxQBO88968.
PaxDbO88968.
PRIDEO88968.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000020710; ENSMUSP00000020710; ENSMUSG00000020432.
ENSMUST00000109988; ENSMUSP00000105615; ENSMUSG00000020432.
ENSMUST00000109989; ENSMUSP00000105616; ENSMUSG00000020432.
ENSMUST00000109990; ENSMUSP00000105617; ENSMUSG00000020432.
ENSMUST00000109991; ENSMUSP00000105618; ENSMUSG00000020432.
ENSMUST00000109992; ENSMUSP00000105619; ENSMUSG00000020432.
ENSMUST00000109993; ENSMUSP00000105620; ENSMUSG00000020432.
GeneID21452.
KEGGmmu:21452.
UCSCuc007htx.2. mouse.

Organism-specific databases

CTD6948.
MGIMGI:98534. Tcn2.

Phylogenomic databases

eggNOGNOG47054.
GeneTreeENSGT00530000063370.
HOGENOMHOG000074060.
HOVERGENHBG001328.
InParanoidQ3TD34.
KOK14619.
OMAGHKGDRL.
OrthoDBEOG79GT6F.
PhylomeDBO88968.
TreeFamTF333092.

Gene expression databases

BgeeO88968.
CleanExMM_TCN2.
GenevestigatorO88968.

Family and domain databases

InterProIPR002157. Cbl-bd_transpt_euk.
IPR019554. Soluble_ligand-bd.
[Graphical view]
PANTHERPTHR10559. PTHR10559. 1 hit.
PfamPF01122. Cobalamin_bind. 1 hit.
PF10531. SLBB. 1 hit.
[Graphical view]
PROSITEPS00468. COBALAMIN_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio300812.
PROO88968.
SOURCESearch...

Entry information

Entry nameTCO2_MOUSE
AccessionPrimary (citable) accession number: O88968
Secondary accession number(s): Q3TD34, Q3UP69, Q5SQ21
Entry history
Integrated into UniProtKB/Swiss-Prot: December 13, 2001
Last sequence update: November 1, 1998
Last modified: July 9, 2014
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot