TRFE_BOVIN
ID TRFE_BOVIN Reviewed; 704 AA.
AC Q29443; Q0IIK2;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Serotransferrin;
DE Short=Transferrin;
DE AltName: Full=Beta-1 metal-binding globulin;
DE AltName: Full=Siderophilin;
DE Flags: Precursor;
GN Name=TF;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=8557646; DOI=10.1074/jbc.271.2.1166;
RA Retzer M.D., Kabani A., Button L.L., Yu R.H., Schryvers A.B.;
RT "Production and characterization of chimeric transferrins for the
RT determination of the binding domains for bacterial transferrin receptors.";
RL J. Biol. Chem. 271:1166-1173(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hippocampus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Transferrins are iron binding transport proteins which can
CC bind two Fe(3+) ions in association with the binding of an anion,
CC usually bicarbonate. It is responsible for the transport of iron from
CC sites of absorption and heme degradation to those of storage and
CC utilization. Serum transferrin may also have a further role in
CC stimulating cell proliferation.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.
CC -!- SIMILARITY: Belongs to the transferrin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00741}.
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DR EMBL; U02564; AAA96735.1; -; mRNA.
DR EMBL; BC122602; AAI22603.1; -; mRNA.
DR PIR; A60166; A60166.
DR RefSeq; NP_803450.2; NM_177484.3.
DR AlphaFoldDB; Q29443; -.
DR SMR; Q29443; -.
DR IntAct; Q29443; 1.
DR STRING; 9913.ENSBTAP00000009564; -.
DR MEROPS; S60.970; -.
DR PaxDb; Q29443; -.
DR PeptideAtlas; Q29443; -.
DR PRIDE; Q29443; -.
DR GeneID; 280705; -.
DR KEGG; bta:280705; -.
DR CTD; 7018; -.
DR eggNOG; ENOG502QT0C; Eukaryota.
DR InParanoid; Q29443; -.
DR OrthoDB; 232859at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0008199; F:ferric iron binding; IEA:InterPro.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IEA:InterPro.
DR GO; GO:0006826; P:iron ion transport; IEA:InterPro.
DR InterPro; IPR030685; Serotransferrin_mammal.
DR InterPro; IPR016357; Transferrin.
DR InterPro; IPR001156; Transferrin-like_dom.
DR InterPro; IPR018195; Transferrin_Fe_BS.
DR Pfam; PF00405; Transferrin; 2.
DR PIRSF; PIRSF500682; Serotransferrin; 1.
DR PIRSF; PIRSF002549; Transferrin; 1.
DR PRINTS; PR00422; TRANSFERRIN.
DR SMART; SM00094; TR_FER; 2.
DR PROSITE; PS00205; TRANSFERRIN_LIKE_1; 1.
DR PROSITE; PS00206; TRANSFERRIN_LIKE_2; 2.
DR PROSITE; PS00207; TRANSFERRIN_LIKE_3; 1.
DR PROSITE; PS51408; TRANSFERRIN_LIKE_4; 2.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Ion transport; Iron; Iron transport;
KW Metal-binding; Methylation; Phosphoprotein; Reference proteome; Repeat;
KW Secreted; Signal; Transport.
FT SIGNAL 1..19
FT /evidence="ECO:0000250"
FT CHAIN 20..704
FT /note="Serotransferrin"
FT /id="PRO_0000035713"
FT DOMAIN 25..351
FT /note="Transferrin-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DOMAIN 364..689
FT /note="Transferrin-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 81
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 113
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 138
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 142
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 144
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 145
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 211
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 272
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 414
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 449
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 475
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 479
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 481
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 482
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 543
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 611
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT MOD_RES 42
FT /note="Dimethylated arginine"
FT /evidence="ECO:0000250|UniProtKB:P12346"
FT MOD_RES 691
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02787"
FT CARBOHYD 514
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 28..66
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 38..57
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 136..217
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 176..192
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 179..200
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 189..202
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 250..264
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 362..622
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 367..399
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 377..390
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 424..699
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 441..663
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 473..549
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 497..690
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 507..521
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 518..532
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 589..603
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 641..646
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT CONFLICT 151
FT /note="A -> G (in Ref. 2; AAI22603)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 704 AA; 77753 MW; D87BB2AFE46C708D CRC64;
MRPAVRALLA CAVLGLCLAD PERTVRWCTI STHEANKCAS FRENVLRILE SGPFVSCVKK
TSHMDCIKAI SNNEADAVTL DGGLVYEAGL KPNNLKPVVA EFHGTKDNPQ THYYAVAVVK
KDTDFKLNEL RGKKSCHTGL GRSAGWNIPM AKLYKELPDP QESIQRAAAN FFSASCVPCA
DQSSFPKLCQ LCAGKGTDKC ACSNHEPYFG YSGAFKCLME GAGDVAFVKH STVFDNLPNP
EDRKNYELLC GDNTRKSVDD YQECYLAMVP SHAVVARTVG GKEDVIWELL NHAQEHFGKD
KPDNFQLFQS PHGKDLLFKD SADGFLKIPS KMDFELYLGY EYVTALQNLR ESKPPDSSKD
ECMVKWCAIG HQERTKCDRW SGFSGGAIEC ETAENTEECI AKIMKGEADA MSLDGGYLYI
AGKCGLVPVL AENYKTEGES CKNTPEKGYL AVAVVKTSDA NINWNNLKDK KSCHTAVDRT
AGWNIPMGLL YSKINNCKFD EFFSAGCAPG SPRNSSLCAL CIGSEKGTGK ECVPNSNERY
YGYTGAFRCL VEKGDVAFVK DQTVIQNTDG NNNEAWAKNL KKENFEVLCK DGTRKPVTDA
ENCHLARGPN HAVVSRKDKA TCVEKILNKQ QDDFGKSVTD CTSNFCLFQS NSKDLLFRDD
TKCLASIAKK TYDSYLGDDY VRAMTNLRQC STSKLLEACT FHKP
