TCO2_MOUSE
ID TCO2_MOUSE Reviewed; 430 AA.
AC O88968; Q3TD34; Q3UP69; Q5SQ21;
DT 13-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Transcobalamin-2;
DE Short=TC-2;
DE AltName: Full=Transcobalamin II;
DE Short=TC II;
DE Short=TCII;
DE Flags: Precursor;
GN Name=Tcn2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT GLU-102.
RC STRAIN=BALB/cJ, and NZB; TISSUE=Liver;
RA Hasegawa M., Foote S.;
RT "Mouse transcobalamin II: polymorphism in NZB.";
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Head, Kidney, and Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Primary vitamin B12-binding and transport protein. Delivers
CC cobalamin to cells. {ECO:0000250|UniProtKB:P20062}.
CC -!- SUBUNIT: Interacts with CD320 (via LDL-receptor class A domains).
CC {ECO:0000250|UniProtKB:P20062}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P20062}.
CC -!- SIMILARITY: Belongs to the eukaryotic cobalamin transport proteins
CC family. {ECO:0000305}.
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DR EMBL; AF090686; AAC61868.1; -; mRNA.
DR EMBL; AK133707; BAE21792.1; -; mRNA.
DR EMBL; AK143761; BAE25528.1; -; mRNA.
DR EMBL; AK147176; BAE27739.1; -; mRNA.
DR EMBL; AK161618; BAE36496.1; -; mRNA.
DR EMBL; AK170401; BAE41770.1; -; mRNA.
DR EMBL; AL807241; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL807395; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466574; EDL40449.1; -; Genomic_DNA.
DR EMBL; BC003720; AAH03720.1; -; mRNA.
DR CCDS; CCDS24371.1; -.
DR RefSeq; NP_001123930.1; NM_001130458.1.
DR RefSeq; NP_001123931.1; NM_001130459.1.
DR RefSeq; NP_056564.1; NM_015749.3.
DR RefSeq; XP_006514673.1; XM_006514610.3.
DR RefSeq; XP_006514674.1; XM_006514611.3.
DR RefSeq; XP_006514675.1; XM_006514612.3.
DR RefSeq; XP_006514676.1; XM_006514613.3.
DR AlphaFoldDB; O88968; -.
DR SMR; O88968; -.
DR BioGRID; 204042; 1.
DR STRING; 10090.ENSMUSP00000105620; -.
DR CPTAC; non-CPTAC-3619; -.
DR jPOST; O88968; -.
DR MaxQB; O88968; -.
DR PaxDb; O88968; -.
DR PeptideAtlas; O88968; -.
DR PRIDE; O88968; -.
DR ProteomicsDB; 263262; -.
DR Antibodypedia; 206; 236 antibodies from 27 providers.
DR DNASU; 21452; -.
DR Ensembl; ENSMUST00000020710; ENSMUSP00000020710; ENSMUSG00000020432.
DR Ensembl; ENSMUST00000109988; ENSMUSP00000105615; ENSMUSG00000020432.
DR Ensembl; ENSMUST00000109989; ENSMUSP00000105616; ENSMUSG00000020432.
DR Ensembl; ENSMUST00000109990; ENSMUSP00000105617; ENSMUSG00000020432.
DR Ensembl; ENSMUST00000109991; ENSMUSP00000105618; ENSMUSG00000020432.
DR Ensembl; ENSMUST00000109992; ENSMUSP00000105619; ENSMUSG00000020432.
DR Ensembl; ENSMUST00000109993; ENSMUSP00000105620; ENSMUSG00000020432.
DR GeneID; 21452; -.
DR KEGG; mmu:21452; -.
DR UCSC; uc007htx.2; mouse.
DR CTD; 6948; -.
DR MGI; MGI:98534; Tcn2.
DR VEuPathDB; HostDB:ENSMUSG00000020432; -.
DR eggNOG; ENOG502QSED; Eukaryota.
DR GeneTree; ENSGT00530000063370; -.
DR HOGENOM; CLU_052188_1_0_1; -.
DR InParanoid; O88968; -.
DR OMA; QCVKDSG; -.
DR OrthoDB; 1233171at2759; -.
DR PhylomeDB; O88968; -.
DR TreeFam; TF333092; -.
DR Reactome; R-MMU-9758890; Transport of RCbl within the body.
DR BioGRID-ORCS; 21452; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Tcn2; mouse.
DR PRO; PR:O88968; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; O88968; protein.
DR Bgee; ENSMUSG00000020432; Expressed in parotid gland and 266 other tissues.
DR Genevisible; O88968; MM.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0140355; F:cargo receptor ligand activity; IDA:MGI.
DR GO; GO:0031419; F:cobalamin binding; IDA:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009235; P:cobalamin metabolic process; IDA:MGI.
DR GO; GO:0015889; P:cobalamin transport; ISS:UniProtKB.
DR GO; GO:0006824; P:cobalt ion transport; IEA:UniProtKB-KW.
DR InterPro; IPR002157; Cbl-bd_prot.
DR InterPro; IPR027954; DUF4430.
DR Pfam; PF01122; Cobalamin_bind; 1.
DR Pfam; PF14478; DUF4430; 1.
DR PROSITE; PS00468; COBALAMIN_BINDING; 1.
PE 1: Evidence at protein level;
KW Cobalt; Cobalt transport; Disulfide bond; Ion transport; Metal-binding;
KW Reference proteome; Secreted; Signal; Transport.
FT SIGNAL 1..18
FT /evidence="ECO:0000250"
FT CHAIN 19..430
FT /note="Transcobalamin-2"
FT /id="PRO_0000005565"
FT BINDING 152..156
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000250"
FT BINDING 193..197
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000250"
FT BINDING 193
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /ligand_part="Co"
FT /ligand_part_id="ChEBI:CHEBI:27638"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 245
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000250"
FT BINDING 248
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000250"
FT BINDING 294
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000250"
FT BINDING 398..400
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000250"
FT DISULFID 21..270
FT /evidence="ECO:0000250"
FT DISULFID 116..312
FT /evidence="ECO:0000250"
FT DISULFID 165..208
FT /evidence="ECO:0000250"
FT VARIANT 102
FT /note="G -> E (in strain: NZB)"
FT /evidence="ECO:0000269|Ref.1"
FT CONFLICT 19
FT /note="E -> G (in Ref. 2; BAE25528)"
FT /evidence="ECO:0000305"
FT CONFLICT 291
FT /note="M -> V (in Ref. 2; BAE41770)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 430 AA; 47586 MW; 2EFF1427E48480A5 CRC64;
MELLKALLLL SGVFGALAEF CVIPRIDSQL VEKLGQRLLP WMDRLSSEQL NPSVFVGLRL
SSMQAGTKED LYLHSLKIHY QQCLLRSTSS DDNSSCQPKL SGGSLALYLL ALRANCEFFG
SRKGDRLISQ LKWFLEDEKK AIGHNHEGHP NTNYYQYGLS ILALCVHQKR LHDSVVGKLL
YAVEHDYFTY QGHVSVDTEA MAGLALTCLE RFNFNSDLRP RITMAIETVR EKILKSQAPE
GYFGNIYSTP LALQMLMTSP ASGVGLGTAC IKAGTSLLLS LQDGAFQNPL MISQLLPILN
HKTYLDLIFP DCQASRVMLV PAVEDPVHIS EVISVTLKVA SALSPYEQTF FVFAGSSLED
VLKLAQDGGG FTYGTQASLS GPYLTSVLGK DAGDREYWQL LRAPDTPLLQ GIADYKPQDG
ETIELRLVRW
