TRFE_PAROL
ID TRFE_PAROL Reviewed; 685 AA.
AC O93429;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Serotransferrin;
DE Flags: Precursor;
GN Name=tf;
OS Paralichthys olivaceus (Bastard halibut) (Hippoglossus olivaceus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Paralichthyidae;
OC Paralichthys.
OX NCBI_TaxID=8255;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Kim Y., Lee J., Hong Y., Hirono I., Aoki T.;
RT "Molecular cloning and sequence analysis of transferrin cDNA from Japanese
RT flounder Paralichthys olivaceus.";
RL Submitted (NOV-1996) 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.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the transferrin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00741}.
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DR EMBL; D88801; BAA28944.1; -; mRNA.
DR AlphaFoldDB; O93429; -.
DR SMR; O93429; -.
DR MEROPS; S60.970; -.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR GO; GO:0055072; P:iron ion homeostasis; IEA:UniProtKB-KW.
DR InterPro; IPR016357; Transferrin.
DR InterPro; IPR001156; Transferrin-like_dom.
DR InterPro; IPR018195; Transferrin_Fe_BS.
DR Pfam; PF00405; Transferrin; 2.
DR PIRSF; PIRSF002549; Transferrin; 1.
DR PRINTS; PR00422; TRANSFERRIN.
DR SMART; SM00094; TR_FER; 2.
DR PROSITE; PS00205; TRANSFERRIN_LIKE_1; 2.
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; Repeat; Secreted; Signal; Transport.
FT SIGNAL 1..16
FT /evidence="ECO:0000250"
FT CHAIN 17..685
FT /note="Serotransferrin"
FT /id="PRO_0000035723"
FT DOMAIN 23..329
FT /note="Transferrin-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DOMAIN 340..666
FT /note="Transferrin-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 72
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 102
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 127
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 131
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 133
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 134
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 200
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 256
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 394
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 428
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 453
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 457
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 459
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 460
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 520
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 588
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT CARBOHYD 476
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 26..48
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 125..206
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 170..184
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 234..248
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 343..379
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 353..370
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 404..678
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 419..639
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 451..526
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 475..667
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 485..499
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 496..509
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 566..580
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
SQ SEQUENCE 685 AA; 74655 MW; 5A6F622AD7D5B662 CRC64;
MKPLLLLPLL GCLATIASCI DTVKWCVTST KENLKCTALA AAAPVFSCVA RASITDCLTA
IKAGEADAIT LDGGEIYTAG LDEYKLHPII AEQYGTSTDT CYYAVAVAKK NTGFGLHQLM
GKKSCHTGVG KSAGWNIPIG TLLSMDFIKW KGSDDKKLEE VVGEFFHSSC APGATDSANL
CKLCIGDCSK SSETEPYYNY HGAFQCLKDG KGDVAFVKHL TVPEEEKNDY ELLCKDNTRK
PIDQFENCDL AKVPSHAVVT RKDNEELAQF IWQSLSSVKN FNLFSSTPYG GKNLMFKDST
TTLVQLPLNV DHTMYLGPHY LESVKALKIV NIPSTTSDAM KWCAVGRSES DKCDSWSVAS
LVQDGTTIDC IKGNTVDDCL KKIMHKEADA MAVDGGQVYT AGKCGLVPAM VEQYDQGQCS
APGAARLYYA VAVIKKGSGV TWENLRNKRS CHTGIGRNAG WNIPMGLIYE QTKNCNFSAF
FSSSCAPGAD PSSQLCAQCA GNAESINKCK ASNEERYYAY AGAFRCLAEG KGDVAFVKHS
IVKENTDGQG PEWAKAFLSN DYELICPSKG PVSVENFMSC NLAKVNAHAV VTRPEIRTKV
VTFLNNQQSH FGNSASEESF KMFTSPDGEN LLFKYSTKCL QEIPAHLDYK GFLGQEYMTV
MSSLRTCKES TSDLEQLCTY NMCQT
