TCO2_PONAB
ID TCO2_PONAB Reviewed; 427 AA.
AC Q5REL7;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 68.
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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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; CR857507; CAH89790.1; -; mRNA.
DR RefSeq; NP_001124823.1; NM_001131351.1.
DR AlphaFoldDB; Q5REL7; -.
DR SMR; Q5REL7; -.
DR STRING; 9601.ENSPPYP00000013071; -.
DR GeneID; 100171681; -.
DR KEGG; pon:100171681; -.
DR CTD; 6948; -.
DR eggNOG; ENOG502QSED; Eukaryota.
DR InParanoid; Q5REL7; -.
DR OrthoDB; 1233171at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0031419; F:cobalamin binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 Pfam; PF01122; Cobalamin_bind; 1.
DR PROSITE; PS00468; COBALAMIN_BINDING; 1.
PE 2: Evidence at transcript 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..427
FT /note="Transcobalamin-2"
FT /id="PRO_0000005566"
FT BINDING 104
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000250"
FT BINDING 152..156
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000250"
FT BINDING 190..194
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000250"
FT BINDING 190
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 242
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000250"
FT BINDING 245
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000250"
FT BINDING 291
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000250"
FT BINDING 395..397
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000250"
FT DISULFID 21..267
FT /evidence="ECO:0000250"
FT DISULFID 116..309
FT /evidence="ECO:0000250"
FT DISULFID 165..205
FT /evidence="ECO:0000250"
SQ SEQUENCE 427 AA; 47391 MW; 273EF51BCCCFA6A4 CRC64;
MRHLGALLFL LGVLGALAEI CEIPEVDSHL VEKLGQHLLP WMDRLSLEHL NPSIYVDLRL
SSLQAGTKEE LYLHSLKLGY QQCLLGSAFS EDDGDCQGKP SMGQLALYLL ALRANCEFVR
GHKGDKLVSQ LKRFLEDEKR AIGHDHKGHP HTSYYQYGLG ILALCLHQKR VHDSVVDKLL
YALEPFHQGH HSVDTAAMAG LAFTCLKRSN FNPGRRQRIT MAVRTVREKI LKAQTPEGHF
GNVYSTPLAL QFLMTSPMPG AELGTACLKA RVALFASLQD GAFQNALMIS QLLPVLNHKT
YIDLIFPDCL APRVMLEPAA ETIPQAQEII SVTLQVLSLL PPYRQSISVL AGSTVEDVLK
KAHELGGFTY ETQASLSGPY LISVMGKAAG EREFWQLLRD PNTPLLQGIA DYRPKDGETI
ELRLVSW