TRFE_ONCKI
ID TRFE_ONCKI Reviewed; 687 AA.
AC P79815;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Serotransferrin;
DE Flags: Precursor;
GN Name=tf;
OS Oncorhynchus kisutch (Coho salmon) (Salmo kisutch).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Oncorhynchus.
OX NCBI_TaxID=8019;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Lee J., Tange N., Yamashita H., Hirono I., Aoki T.;
RT "Cloning and characterization of transferrin cDNA from coho salmon
RT (Oncorhynchus kisutch).";
RL Fish Pathol. 30:271-277(1996).
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; D89084; BAA13759.1; -; mRNA.
DR AlphaFoldDB; P79815; -.
DR SMR; P79815; -.
DR MEROPS; S60.970; -.
DR Proteomes; UP000694557; Unplaced.
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; Reference proteome; Repeat; Secreted; Signal; Transport.
FT SIGNAL 1..18
FT /evidence="ECO:0000250"
FT CHAIN 19..687
FT /note="Serotransferrin"
FT /id="PRO_0000035721"
FT DOMAIN 25..329
FT /note="Transferrin-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DOMAIN 340..670
FT /note="Transferrin-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 74
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 104
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 129
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 136
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 137
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 201
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 257
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 524
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 592
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT CARBOHYD 169
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 673
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 28..50
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 127..207
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 172..186
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 235..249
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..682
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 419..643
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 451..530
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 475..671
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 485..499
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 496..513
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 570..584
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
SQ SEQUENCE 687 AA; 74800 MW; E9754B12858EE100 CRC64;
MKLLLVSALL GCFATVYAAP AEGMVRWCVK SEKELKKCHD LAANVAGFSC VRRDDSLECI
QAIKREEADA ITLDGGDIYI AGLHNYNLQP IIAEDYGEDS DTCYYAVAVA KKGTEFGFLD
LRGKKSCHTG LGKSAGWNIP IGTLVTVGQI QWAGIEDRPV ESAVSDFFNA SCAPGANRDS
QLCQLCMGDC SRSHNEPYYD YSGAFQCLKD GAGEVAFIKH LTVPAAEKAS YELLCKDNTR
APIDSYKTCH LARVPAHAVV SRKDPRLANL IYSKLMAVTN FNLFSSDGYA AKNLMFKDST
QNLVQLPMTT DSFLYLGAEY MSTIRSLTKA QATGVTSRAI KWCAVGHKEK VKCDAWTINS
FTDGDSRIEC QDAPTVDECI KKIMRKEADA IAVDGGEVFT AGKCGLVPVM VEQYDEVRCS
APGEASSYFA VAVAKRGSGL TWTTLKGKRS CHTGLGRTAG WNIPMGLIHR RTMNCDFTTY
FSKGCAPGFE VDSPFCAQCK GSGKSVGGDG SKCKASSEEQ YYGYNGAFRC LVEDAGDVAF
IKHTIVPEMT DGSGPVWAQN LMSSDFELLC QDGTTKPVTH FRECHLAKVP AHAVITRPES
RGEVVSILLE QQARFGSSGS DSSFNMFKPD FGKNLLFKDS TKCLQEIPSG TKFQGFLGEE
YMIAMQSLRE CSNSTSDLEK ACTFHSC
