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   24-JAN-2024, entry version 155.
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; 10090-ENSMUSP00000105620; -.
DR   PeptideAtlas; O88968; -.
DR   ProteomicsDB; 263262; -.
DR   Antibodypedia; 206; 265 antibodies from 27 providers.
DR   DNASU; 21452; -.
DR   Ensembl; ENSMUST00000020710.11; ENSMUSP00000020710.5; ENSMUSG00000020432.13.
DR   Ensembl; ENSMUST00000109988.2; ENSMUSP00000105615.2; ENSMUSG00000020432.13.
DR   Ensembl; ENSMUST00000109989.10; ENSMUSP00000105616.4; ENSMUSG00000020432.13.
DR   Ensembl; ENSMUST00000109990.8; ENSMUSP00000105617.2; ENSMUSG00000020432.13.
DR   Ensembl; ENSMUST00000109991.8; ENSMUSP00000105618.2; ENSMUSG00000020432.13.
DR   Ensembl; ENSMUST00000109992.8; ENSMUSP00000105619.2; ENSMUSG00000020432.13.
DR   Ensembl; ENSMUST00000109993.9; ENSMUSP00000105620.3; ENSMUSG00000020432.13.
DR   GeneID; 21452; -.
DR   KEGG; mmu:21452; -.
DR   UCSC; uc007htx.2; mouse.
DR   AGR; MGI:98534; -.
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; 5354110at2759; -.
DR   PhylomeDB; O88968; -.
DR   TreeFam; TF333092; -.
DR   Reactome; R-MMU-9758890; Transport of RCbl within the body.
DR   BioGRID-ORCS; 21452; 4 hits in 78 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 270 other cell types or tissues.
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:0015889; P:cobalamin transport; IDA:MGI.
DR   GO; GO:0006824; P:cobalt ion transport; IEA:UniProtKB-KW.
DR   Gene3D; 1.50.10.20; -; 1.
DR   Gene3D; 2.170.130.30; -; 1.
DR   InterPro; IPR002157; Cbl-bd_prot.
DR   InterPro; IPR027954; Transcobalamin-like_C.
DR   PANTHER; PTHR10559; TRANSCOBALAMIN-1/GASTRIC INTRINSIC FACTOR; 1.
DR   PANTHER; PTHR10559:SF14; TRANSCOBALAMIN-2; 1.
DR   Pfam; PF01122; Cobalamin_bind; 1.
DR   Pfam; PF14478; DUF4430; 1.
DR   PROSITE; PS00468; COBALAMIN_BINDING; 1.
DR   Genevisible; O88968; MM.
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
//