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Transcobalamin-2 (TC-2) (Transcobalamin II) (TC II) (TCII)

 TCO2_HUMAN              Reviewed;         427 AA.
P20062; Q96FD4; Q9BVI8; Q9UCI5; Q9UCI6; Q9UDM0;
01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
03-MAR-2009, sequence version 3.
07-NOV-2018, entry version 185.
RecName: Full=Transcobalamin-2;
Short=TC-2;
AltName: Full=Transcobalamin II;
Short=TC II;
Short=TCII;
Flags: Precursor;
Name=TCN2; Synonyms=TC2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS THR-198; LEU-219;
PRO-259 AND SER-376.
PubMed=1708393;
Platica O., Janeczko R., Quadros E.V., Regec A., Romain R.,
Rothenberg S.P.;
"The cDNA sequence and the deduced amino acid sequence of human
transcobalamin II show homology with rat intrinsic factor and human
transcobalamin I.";
J. Biol. Chem. 266:7860-7863(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=8439564; DOI=10.1016/0167-4781(93)90264-E;
Li N., Seetharam S., Lindemans J., Alpers D.H., Arwert F.,
Seetharam B.;
"Isolation and sequence analysis of variant forms of human
transcobalamin II.";
Biochim. Biophys. Acta 1172:21-30(1993).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=7742531;
Regec A., Quadros E.V., Platica O., Rothenberg S.P.;
"The cloning and characterization of the human transcobalamin II
gene.";
Blood 85:2711-2719(1995).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
PRO-259.
PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
Beare D.M., Dunham I.;
"A genome annotation-driven approach to cloning the human ORFeome.";
Genome Biol. 5:R84.1-R84.11(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=10591208; DOI=10.1038/990031;
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
Khan A.S., Lane L., Tilahun Y., Wright H.;
"The DNA sequence of human chromosome 22.";
Nature 402:489-495(1999).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
GLN-227.
TISSUE=Brain, and Eye;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PROTEIN SEQUENCE OF 19-37, AND SUBCELLULAR LOCATION.
PubMed=3782074;
Quadros E.V., Rothenberg S.P., Pan Y.C.E., Stein S.;
"Purification and molecular characterization of human transcobalamin
II.";
J. Biol. Chem. 261:15455-15460(1986).
[8]
PARTIAL PROTEIN SEQUENCE, FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=8443384;
Quadros E.V., Sai P., Rothenberg S.P.;
"Functional human transcobalamin II isoproteins are secreted by insect
cells using the baculovirus expression system.";
Blood 81:1239-1245(1993).
[9]
X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 19-427 IN COMPLEX WITH
COBALAMIN, AND DISULFIDE BONDS.
PubMed=16537422; DOI=10.1073/pnas.0509099103;
Wuerges J., Garau G., Geremia S., Fedosov S.N., Petersen T.E.,
Randaccio L.;
"Structural basis for mammalian vitamin B12 transport by
transcobalamin.";
Proc. Natl. Acad. Sci. U.S.A. 103:4386-4391(2006).
[10] {ECO:0000244|PDB:4ZRP, ECO:0000244|PDB:4ZRQ}
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 19-427 IN COMPLEX WITH
COBALAMIN AND CD320, INTERACTION WITH CD320, AND DISULFIDE BONDS.
PubMed=27411955; DOI=10.1038/ncomms12100;
Alam A., Woo J.S., Schmitz J., Prinz B., Root K., Chen F., Bloch J.S.,
Zenobi R., Locher K.P.;
"Structural basis of transcobalamin recognition by human CD320
receptor.";
Nat. Commun. 7:12100-12100(2016).
[11]
VARIANT PRO-259, AND POLYMORPHISM.
PubMed=11159542; DOI=10.1182/blood.V97.4.1092;
Namour F., Olivier J., Abdelmouttaleb I., Adjalla C., Debard R.,
Salvat C., Gueant J.;
"Transcobalamin codon 259 polymorphism in HT-29 and Caco-2 cells and
in Caucasians: relation to transcobalamin and homocysteine
concentration in blood.";
Blood 97:1092-1098(2001).
-!- FUNCTION: Primary vitamin B12-binding and transport protein.
Delivers cobalamin to cells. {ECO:0000269|PubMed:8443384}.
-!- SUBUNIT: Interacts with CD320 (via LDL-receptor class A domains).
{ECO:0000269|PubMed:27411955}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:3782074,
ECO:0000269|PubMed:8443384}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P20062-1; Sequence=Displayed;
Name=2;
IsoId=P20062-2; Sequence=VSP_043711;
Note=No experimental confirmation available.;
-!- POLYMORPHISM: Pro/Arg-259 polymorphism affects TCN2 plasma
concentration and may interfere in vitamin B(12) cellular
availability and homocysteine metabolism (PubMed:11159542).
{ECO:0000269|PubMed:11159542}.
-!- DISEASE: Transcobalamin II deficiency (TCN2 deficiency)
[MIM:275350]: Results in various forms of anemia. Note=The disease
is caused by mutations affecting the gene represented in this
entry.
-!- SIMILARITY: Belongs to the eukaryotic cobalamin transport proteins
family. {ECO:0000305}.
-!- WEB RESOURCE: Name=TCN2base; Note=TCN2 mutation db;
URL="http://structure.bmc.lu.se/idbase/TCN2base/";
-----------------------------------------------------------------------
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EMBL; M60396; AAA61054.1; -; mRNA.
EMBL; L02647; AAA61056.1; -; mRNA.
EMBL; L02648; AAA61057.1; -; mRNA.
EMBL; AF047576; AAC05491.1; -; Genomic_DNA.
EMBL; CR456591; CAG30477.1; -; mRNA.
EMBL; AC005006; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC001176; AAH01176.1; -; mRNA.
EMBL; BC011239; AAH11239.1; -; mRNA.
CCDS; CCDS13881.1; -. [P20062-1]
CCDS; CCDS54519.1; -. [P20062-2]
PIR; A39744; A39744.
RefSeq; NP_000346.2; NM_000355.3. [P20062-1]
RefSeq; NP_001171655.1; NM_001184726.1. [P20062-2]
UniGene; Hs.417948; -.
PDB; 2BB5; X-ray; 3.20 A; A/B=19-427.
PDB; 4ZRP; X-ray; 2.10 A; A/B=19-427.
PDB; 4ZRQ; X-ray; 2.60 A; A/B=19-427.
PDB; 5NO0; X-ray; 1.57 A; A=325-427.
PDB; 5NP4; X-ray; 1.43 A; A=325-427.
PDB; 5NRP; X-ray; 1.57 A; A=325-427.
PDB; 5NSA; X-ray; 1.27 A; A=325-427.
PDBsum; 2BB5; -.
PDBsum; 4ZRP; -.
PDBsum; 4ZRQ; -.
PDBsum; 5NO0; -.
PDBsum; 5NP4; -.
PDBsum; 5NRP; -.
PDBsum; 5NSA; -.
ProteinModelPortal; P20062; -.
SMR; P20062; -.
BioGrid; 112808; 5.
IntAct; P20062; 2.
STRING; 9606.ENSP00000215838; -.
DrugBank; DB00115; Cyanocobalamin.
DrugBank; DB00200; Hydroxocobalamin.
BioMuta; TCN2; -.
DMDM; 224471876; -.
PaxDb; P20062; -.
PeptideAtlas; P20062; -.
PRIDE; P20062; -.
ProteomicsDB; 53720; -.
ProteomicsDB; 53721; -. [P20062-2]
DNASU; 6948; -.
Ensembl; ENST00000215838; ENSP00000215838; ENSG00000185339. [P20062-1]
Ensembl; ENST00000407817; ENSP00000384914; ENSG00000185339. [P20062-2]
GeneID; 6948; -.
KEGG; hsa:6948; -.
UCSC; uc003aip.3; human. [P20062-1]
CTD; 6948; -.
DisGeNET; 6948; -.
EuPathDB; HostDB:ENSG00000185339.8; -.
GeneCards; TCN2; -.
HGNC; HGNC:11653; TCN2.
HPA; HPA000837; -.
MalaCards; TCN2; -.
MIM; 275350; phenotype.
MIM; 613441; gene.
neXtProt; NX_P20062; -.
OpenTargets; ENSG00000185339; -.
Orphanet; 859; Transcobalamin deficiency.
PharmGKB; PA36404; -.
eggNOG; ENOG410IDZK; Eukaryota.
eggNOG; ENOG410XSU1; LUCA.
GeneTree; ENSGT00530000063370; -.
HOGENOM; HOG000074060; -.
HOVERGEN; HBG001328; -.
InParanoid; P20062; -.
KO; K14619; -.
OMA; PSIYVGL; -.
OrthoDB; EOG091G095C; -.
PhylomeDB; P20062; -.
TreeFam; TF333092; -.
Reactome; R-HSA-196741; Cobalamin (Cbl, vitamin B12) transport and metabolism.
Reactome; R-HSA-3359454; Defective TCN2 causes hereditary megaloblastic anemia.
Reactome; R-HSA-3359485; Defective CD320 causes methylmalonic aciduria.
SABIO-RK; P20062; -.
ChiTaRS; TCN2; human.
EvolutionaryTrace; P20062; -.
GenomeRNAi; 6948; -.
PRO; PR:P20062; -.
Proteomes; UP000005640; Chromosome 22.
Bgee; ENSG00000185339; Expressed in 136 organ(s), highest expression level in esophagus.
CleanEx; HS_TCN2; -.
ExpressionAtlas; P20062; baseline and differential.
Genevisible; P20062; HS.
GO; GO:0005768; C:endosome; TAS:Reactome.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0043202; C:lysosomal lumen; TAS:Reactome.
GO; GO:0031419; F:cobalamin binding; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0009235; P:cobalamin metabolic process; TAS:Reactome.
GO; GO:0015889; P:cobalamin transport; IDA:UniProtKB.
GO; GO:0006824; P:cobalt ion transport; IEA:UniProtKB-KW.
InterPro; IPR002157; Cbl-bd_prot.
InterPro; IPR027954; DUF4430.
InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
Pfam; PF01122; Cobalamin_bind; 1.
Pfam; PF14478; DUF4430; 1.
SUPFAM; SSF48239; SSF48239; 1.
PROSITE; PS00468; COBALAMIN_BINDING; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cobalt; Cobalt transport;
Complete proteome; Direct protein sequencing; Disulfide bond;
Ion transport; Metal-binding; Polymorphism; Reference proteome;
Secreted; Signal; Transport.
SIGNAL 1 18 {ECO:0000269|PubMed:3782074}.
CHAIN 19 427 Transcobalamin-2.
/FTId=PRO_0000005564.
REGION 152 156 Cobalamin binding.
{ECO:0000269|PubMed:27411955}.
REGION 190 194 Cobalamin binding.
{ECO:0000269|PubMed:27411955}.
REGION 395 397 Cobalamin binding.
{ECO:0000269|PubMed:27411955}.
METAL 190 190 Cobalt (cobalamin axial ligand).
BINDING 104 104 Cobalamin. {ECO:0000269|PubMed:16537422,
ECO:0000269|PubMed:27411955}.
BINDING 242 242 Cobalamin. {ECO:0000269|PubMed:16537422}.
BINDING 245 245 Cobalamin. {ECO:0000269|PubMed:16537422,
ECO:0000269|PubMed:27411955}.
BINDING 291 291 Cobalamin. {ECO:0000269|PubMed:16537422}.
DISULFID 21 267 {ECO:0000244|PDB:2BB5,
ECO:0000244|PDB:4ZRP,
ECO:0000244|PDB:4ZRQ,
ECO:0000269|PubMed:16537422,
ECO:0000269|PubMed:27411955}.
DISULFID 83 96 {ECO:0000244|PDB:4ZRP,
ECO:0000244|PDB:4ZRQ,
ECO:0000269|PubMed:27411955}.
DISULFID 116 309 {ECO:0000244|PDB:2BB5,
ECO:0000244|PDB:4ZRP,
ECO:0000244|PDB:4ZRQ,
ECO:0000269|PubMed:16537422,
ECO:0000269|PubMed:27411955}.
DISULFID 165 205 {ECO:0000244|PDB:2BB5,
ECO:0000244|PDB:4ZRP,
ECO:0000244|PDB:4ZRQ,
ECO:0000269|PubMed:16537422,
ECO:0000269|PubMed:27411955}.
VAR_SEQ 116 143 CEFVRGHKGDRLVSQLKWFLEDEKRAIG -> W (in
isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_043711.
VARIANT 23 23 I -> V (in dbSNP:rs9606756).
/FTId=VAR_054539.
VARIANT 89 89 F -> L (in dbSNP:rs35915865).
/FTId=VAR_054540.
VARIANT 198 198 M -> T. {ECO:0000269|PubMed:1708393}.
/FTId=VAR_001638.
VARIANT 215 215 R -> W (in dbSNP:rs35838082).
/FTId=VAR_054541.
VARIANT 219 219 I -> L. {ECO:0000269|PubMed:1708393}.
/FTId=VAR_001639.
VARIANT 227 227 R -> Q (in dbSNP:rs17849434).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_054542.
VARIANT 259 259 R -> P (in dbSNP:rs1801198).
{ECO:0000269|PubMed:11159542,
ECO:0000269|PubMed:15461802,
ECO:0000269|PubMed:1708393}.
/FTId=VAR_001640.
VARIANT 348 348 S -> F (in dbSNP:rs9621049).
/FTId=VAR_054543.
VARIANT 376 376 L -> S (in dbSNP:rs1131603).
{ECO:0000269|PubMed:1708393}.
/FTId=VAR_001641.
VARIANT 399 399 R -> Q (in dbSNP:rs4820889).
/FTId=VAR_054544.
HELIX 28 38 {ECO:0000244|PDB:4ZRP}.
HELIX 39 43 {ECO:0000244|PDB:4ZRP}.
TURN 47 49 {ECO:0000244|PDB:4ZRP}.
HELIX 52 59 {ECO:0000244|PDB:4ZRP}.
STRAND 61 64 {ECO:0000244|PDB:4ZRP}.
HELIX 67 85 {ECO:0000244|PDB:4ZRP}.
HELIX 102 114 {ECO:0000244|PDB:4ZRP}.
HELIX 121 142 {ECO:0000244|PDB:4ZRP}.
STRAND 144 146 {ECO:0000244|PDB:4ZRP}.
HELIX 154 166 {ECO:0000244|PDB:4ZRP}.
HELIX 173 183 {ECO:0000244|PDB:4ZRP}.
STRAND 184 186 {ECO:0000244|PDB:4ZRQ}.
HELIX 193 208 {ECO:0000244|PDB:4ZRP}.
HELIX 213 215 {ECO:0000244|PDB:4ZRP}.
HELIX 216 232 {ECO:0000244|PDB:4ZRP}.
STRAND 240 242 {ECO:0000244|PDB:4ZRP}.
TURN 243 245 {ECO:0000244|PDB:4ZRP}.
HELIX 246 253 {ECO:0000244|PDB:4ZRP}.
HELIX 263 279 {ECO:0000244|PDB:4ZRP}.
HELIX 286 296 {ECO:0000244|PDB:4ZRP}.
HELIX 301 304 {ECO:0000244|PDB:4ZRP}.
STRAND 328 336 {ECO:0000244|PDB:5NSA}.
STRAND 338 341 {ECO:0000244|PDB:5NSA}.
STRAND 343 350 {ECO:0000244|PDB:5NSA}.
HELIX 355 365 {ECO:0000244|PDB:5NSA}.
STRAND 370 373 {ECO:0000244|PDB:5NSA}.
STRAND 380 384 {ECO:0000244|PDB:5NSA}.
STRAND 393 399 {ECO:0000244|PDB:5NSA}.
TURN 400 402 {ECO:0000244|PDB:5NSA}.
TURN 409 411 {ECO:0000244|PDB:5NSA}.
STRAND 419 426 {ECO:0000244|PDB:5NSA}.
SEQUENCE 427 AA; 47535 MW; FD04A110941989DB CRC64;
MRHLGAFLFL LGVLGALTEM CEIPEMDSHL VEKLGQHLLP WMDRLSLEHL NPSIYVGLRL
SSLQAGTKED LYLHSLKLGY QQCLLGSAFS EDDGDCQGKP SMGQLALYLL ALRANCEFVR
GHKGDRLVSQ LKWFLEDEKR AIGHDHKGHP HTSYYQYGLG ILALCLHQKR VHDSVVDKLL
YAVEPFHQGH HSVDTAAMAG LAFTCLKRSN FNPGRRQRIT MAIRTVREEI LKAQTPEGHF
GNVYSTPLAL QFLMTSPMRG AELGTACLKA RVALLASLQD GAFQNALMIS QLLPVLNHKT
YIDLIFPDCL APRVMLEPAA ETIPQTQEII SVTLQVLSLL PPYRQSISVL AGSTVEDVLK
KAHELGGFTY ETQASLSGPY LTSVMGKAAG EREFWQLLRD PNTPLLQGIA DYRPKDGETI
ELRLVSW


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