O88968 (TCO2_MOUSE) 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

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	430 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	Cobalt transport Ion transport Transport
Cellular component	Secreted
Coding sequence diversity	Polymorphism
Domain	Signal
Ligand	Cobalt Metal-binding
PTM	Disulfide bond
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cobalamin 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_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	cobalamin 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 18	18	By similarity
	Chain	19 – 430	412	Transcobalamin-2		PRO_0000005565
Regions
	Region	152 – 156	5	Cobalamin binding By similarity
	Region	193 – 197	5	Cobalamin binding By similarity
	Region	398 – 400	3	Cobalamin binding By similarity
Sites
	Metal binding	193	1	Cobalt (cobalamin axial ligand) By similarity
	Binding site	245	1	Cobalamin By similarity
	Binding site	248	1	Cobalamin By similarity
	Binding site	294	1	Cobalamin By similarity
Amino acid modifications
	Disulfide bond	21 ↔ 270		By similarity
	Disulfide bond	116 ↔ 312		By similarity
	Disulfide bond	165 ↔ 208		By similarity
Natural variations
	Natural variant	102	1	G → E in strain: NZB. Ref.1
Experimental info
	Sequence conflict	19	1	E → G in BAE25528. Ref.2
	Sequence conflict	291	1	M → V in BAE41770. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	O88968 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: 2EFF1427E48480A5	FASTA	430	47,586
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.
IPI	IPI00136556.
RefSeq	NP_001123930.1. NM_001130458.1. NP_001123931.1. NM_001130459.1. NP_056564.1. NM_015749.3.
UniGene	Mm.20948.
3D structure databases
ProteinModelPortal	O88968.
SMR	O88968. Positions 19-430.
ModBase	Search...
PTM databases
PhosphoSite	O88968.
Proteomic databases
PaxDb	O88968.
PRIDE	O88968.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000020710; ENSMUSP00000020710; ENSMUSG00000020432. ENSMUST00000109988; ENSMUSP00000105615; ENSMUSG00000020432. ENSMUST00000109989; ENSMUSP00000105616; ENSMUSG00000020432. ENSMUST00000109990; ENSMUSP00000105617; ENSMUSG00000020432. ENSMUST00000109991; ENSMUSP00000105618; ENSMUSG00000020432. ENSMUST00000109992; ENSMUSP00000105619; ENSMUSG00000020432. ENSMUST00000109993; ENSMUSP00000105620; ENSMUSG00000020432.
GeneID	21452.
KEGG	mmu:21452.
UCSC	uc007htx.2. mouse.
Organism-specific databases
CTD	6948.
MGI	MGI:98534. Tcn2.
Phylogenomic databases
eggNOG	NOG47054.
GeneTree	ENSGT00530000063370.
HOGENOM	HOG000074060.
HOVERGEN	HBG001328.
InParanoid	Q3TD34.
KO	K14619.
OMA	KAQTPEG.
OrthoDB	EOG4VDPZJ.
Gene expression databases
Bgee	O88968.
CleanEx	MM_TCN2.
Genevestigator	O88968.
GermOnline	ENSMUSG00000020432. Mus musculus.
Family and domain databases
InterPro	IPR002157. Cbl-bd_transpt_euk. IPR019554. Soluble_ligand-bd. [Graphical view]
PANTHER	PTHR10559. PTHR10559. 1 hit.
Pfam	PF01122. Cobalamin_bind. 1 hit. PF10531. SLBB. 1 hit. [Graphical view]
PROSITE	PS00468. COBALAMIN_BINDING. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	300812.
SOURCE	Search...

Entry information

Entry name

TCO2_MOUSE

Accession

Primary (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:	April 3, 2013
This is version 92 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program