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O88968

- TCO2_MOUSE

UniProt

O88968 - TCO2_MOUSE

Protein

Transcobalamin-2

Gene

Tcn2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 103 (01 Oct 2014)
      Sequence version 1 (01 Nov 1998)
      Previous versions | rss
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    Functioni

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi193 – 1931Cobalt (cobalamin axial ligand)By similarity
    Binding sitei245 – 2451CobalaminBy similarity
    Binding sitei248 – 2481CobalaminBy similarity
    Binding sitei294 – 2941CobalaminBy similarity

    GO - Molecular functioni

    1. cobalamin binding Source: UniProtKB
    2. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. cobalamin metabolic process Source: RefGenome
    2. cobalamin transport Source: InterPro
    3. cobalt ion transport Source: UniProtKB-KW

    Keywords - Biological processi

    Cobalt transport, Ion transport, Transport

    Keywords - Ligandi

    Cobalt, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_189098. Defective CD320 causes methylmalonic aciduria.
    REACT_189114. Defective TCN2 causes hereditary megaloblastic anemia.
    REACT_189118. Cobalamin (Cbl, vitamin B12) transport and metabolism.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Transcobalamin-2
    Short name:
    TC-2
    Alternative name(s):
    Transcobalamin II
    Short name:
    TC II
    Short name:
    TCII
    Gene namesi
    Name:Tcn2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 11

    Organism-specific databases

    MGIiMGI:98534. Tcn2.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1818By similarityAdd
    BLAST
    Chaini19 – 430412Transcobalamin-2PRO_0000005565Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi21 ↔ 270By similarity
    Disulfide bondi116 ↔ 312By similarity
    Disulfide bondi165 ↔ 208By similarity

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    MaxQBiO88968.
    PaxDbiO88968.
    PRIDEiO88968.

    PTM databases

    PhosphoSiteiO88968.

    Expressioni

    Gene expression databases

    BgeeiO88968.
    CleanExiMM_TCN2.
    GenevestigatoriO88968.

    Structurei

    3D structure databases

    ProteinModelPortaliO88968.
    SMRiO88968. Positions 19-430.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni152 – 1565Cobalamin bindingBy similarity
    Regioni193 – 1975Cobalamin bindingBy similarity
    Regioni398 – 4003Cobalamin bindingBy similarity

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG47054.
    GeneTreeiENSGT00530000063370.
    HOGENOMiHOG000074060.
    HOVERGENiHBG001328.
    InParanoidiQ3TD34.
    KOiK14619.
    OMAiGHKGDRL.
    OrthoDBiEOG79GT6F.
    PhylomeDBiO88968.
    TreeFamiTF333092.

    Family and domain databases

    InterProiIPR002157. Cbl-bd_transpt_euk.
    IPR019554. Soluble_ligand-bd.
    [Graphical view]
    PANTHERiPTHR10559. PTHR10559. 1 hit.
    PfamiPF01122. Cobalamin_bind. 1 hit.
    PF10531. SLBB. 1 hit.
    [Graphical view]
    PROSITEiPS00468. COBALAMIN_BINDING. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    O88968-1 [UniParc]FASTAAdd to Basket

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    MELLKALLLL SGVFGALAEF CVIPRIDSQL VEKLGQRLLP WMDRLSSEQL    50
    NPSVFVGLRL SSMQAGTKED LYLHSLKIHY QQCLLRSTSS DDNSSCQPKL 100
    SGGSLALYLL ALRANCEFFG SRKGDRLISQ LKWFLEDEKK AIGHNHEGHP 150
    NTNYYQYGLS ILALCVHQKR LHDSVVGKLL YAVEHDYFTY QGHVSVDTEA 200
    MAGLALTCLE RFNFNSDLRP RITMAIETVR EKILKSQAPE GYFGNIYSTP 250
    LALQMLMTSP ASGVGLGTAC IKAGTSLLLS LQDGAFQNPL MISQLLPILN 300
    HKTYLDLIFP DCQASRVMLV PAVEDPVHIS EVISVTLKVA SALSPYEQTF 350
    FVFAGSSLED VLKLAQDGGG FTYGTQASLS GPYLTSVLGK DAGDREYWQL 400
    LRAPDTPLLQ GIADYKPQDG ETIELRLVRW 430
    Length:430
    Mass (Da):47,586
    Last modified:November 1, 1998 - v1
    Checksum:i2EFF1427E48480A5
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti19 – 191E → G in BAE25528. (PubMed:16141072)Curated
    Sequence conflicti291 – 2911M → V in BAE41770. (PubMed:16141072)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti102 – 1021G → E in strain: NZB. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS24371.1.
    RefSeqiNP_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.
    UniGeneiMm.20948.

    Genome annotation databases

    EnsembliENSMUST00000020710; ENSMUSP00000020710; ENSMUSG00000020432.
    ENSMUST00000109988; ENSMUSP00000105615; ENSMUSG00000020432.
    ENSMUST00000109989; ENSMUSP00000105616; ENSMUSG00000020432.
    ENSMUST00000109990; ENSMUSP00000105617; ENSMUSG00000020432.
    ENSMUST00000109991; ENSMUSP00000105618; ENSMUSG00000020432.
    ENSMUST00000109992; ENSMUSP00000105619; ENSMUSG00000020432.
    ENSMUST00000109993; ENSMUSP00000105620; ENSMUSG00000020432.
    GeneIDi21452.
    KEGGimmu:21452.
    UCSCiuc007htx.2. mouse.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS24371.1.
    RefSeqi NP_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.
    UniGenei Mm.20948.

    3D structure databases

    ProteinModelPortali O88968.
    SMRi O88968. Positions 19-430.
    ModBasei Search...
    MobiDBi Search...

    PTM databases

    PhosphoSitei O88968.

    Proteomic databases

    MaxQBi O88968.
    PaxDbi O88968.
    PRIDEi O88968.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000020710 ; ENSMUSP00000020710 ; ENSMUSG00000020432 .
    ENSMUST00000109988 ; ENSMUSP00000105615 ; ENSMUSG00000020432 .
    ENSMUST00000109989 ; ENSMUSP00000105616 ; ENSMUSG00000020432 .
    ENSMUST00000109990 ; ENSMUSP00000105617 ; ENSMUSG00000020432 .
    ENSMUST00000109991 ; ENSMUSP00000105618 ; ENSMUSG00000020432 .
    ENSMUST00000109992 ; ENSMUSP00000105619 ; ENSMUSG00000020432 .
    ENSMUST00000109993 ; ENSMUSP00000105620 ; ENSMUSG00000020432 .
    GeneIDi 21452.
    KEGGi mmu:21452.
    UCSCi uc007htx.2. mouse.

    Organism-specific databases

    CTDi 6948.
    MGIi MGI:98534. Tcn2.

    Phylogenomic databases

    eggNOGi NOG47054.
    GeneTreei ENSGT00530000063370.
    HOGENOMi HOG000074060.
    HOVERGENi HBG001328.
    InParanoidi Q3TD34.
    KOi K14619.
    OMAi GHKGDRL.
    OrthoDBi EOG79GT6F.
    PhylomeDBi O88968.
    TreeFami TF333092.

    Enzyme and pathway databases

    Reactomei REACT_189098. Defective CD320 causes methylmalonic aciduria.
    REACT_189114. Defective TCN2 causes hereditary megaloblastic anemia.
    REACT_189118. Cobalamin (Cbl, vitamin B12) transport and metabolism.

    Miscellaneous databases

    NextBioi 300812.
    PROi O88968.
    SOURCEi Search...

    Gene expression databases

    Bgeei O88968.
    CleanExi MM_TCN2.
    Genevestigatori O88968.

    Family and domain databases

    InterProi IPR002157. Cbl-bd_transpt_euk.
    IPR019554. Soluble_ligand-bd.
    [Graphical view ]
    PANTHERi PTHR10559. PTHR10559. 1 hit.
    Pfami PF01122. Cobalamin_bind. 1 hit.
    PF10531. SLBB. 1 hit.
    [Graphical view ]
    PROSITEi PS00468. COBALAMIN_BINDING. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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].

    Entry informationi

    Entry nameiTCO2_MOUSE
    AccessioniPrimary (citable) accession number: O88968
    Secondary accession number(s): Q3TD34, Q3UP69, Q5SQ21
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 13, 2001
    Last sequence update: November 1, 1998
    Last modified: October 1, 2014
    This is version 103 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3