TRFE_XENTR
ID TRFE_XENTR Reviewed; 703 AA.
AC Q501K5;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Serotransferrin;
DE Flags: Precursor;
GN Name=tf;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAY-2005) 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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Plasma.
CC -!- SIMILARITY: Belongs to the transferrin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00741}.
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DR EMBL; BC096012; AAH96012.1; -; mRNA.
DR RefSeq; NP_001027487.1; NM_001032316.1.
DR AlphaFoldDB; Q501K5; -.
DR SMR; Q501K5; -.
DR MEROPS; S60.970; -.
DR PRIDE; Q501K5; -.
DR GeneID; 613079; -.
DR KEGG; xtr:613079; -.
DR CTD; 7018; -.
DR Xenbase; XB-GENE-480506; tf.
DR InParanoid; Q501K5; -.
DR OrthoDB; 232859at2759; -.
DR Reactome; R-XTR-114608; Platelet degranulation.
DR Reactome; R-XTR-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-XTR-6798695; Neutrophil degranulation.
DR Reactome; R-XTR-6799990; Metal sequestration by antimicrobial proteins.
DR Reactome; R-XTR-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-XTR-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-XTR-8957275; Post-translational protein phosphorylation.
DR Reactome; R-XTR-917937; Iron uptake and transport.
DR Reactome; R-XTR-917977; Transferrin endocytosis and recycling.
DR Proteomes; UP000008143; Chromosome 5.
DR Proteomes; UP000790000; Unplaced.
DR GO; GO:0005769; C:early endosome; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0055037; C:recycling endosome; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019731; P:antibacterial humoral response; IBA:GO_Central.
DR GO; GO:0055072; P:iron ion homeostasis; IEA:UniProtKB-KW.
DR GO; GO:0006826; P:iron ion transport; IBA:GO_Central.
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; 1.
DR PROSITE; PS00207; TRANSFERRIN_LIKE_3; 2.
DR PROSITE; PS51408; TRANSFERRIN_LIKE_4; 2.
PE 2: Evidence at transcript level;
KW Disulfide bond; Ion transport; Iron; Iron transport; Metal-binding;
KW Reference proteome; Repeat; Secreted; Signal; Transport.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..703
FT /note="Serotransferrin"
FT /id="PRO_0000305242"
FT DOMAIN 27..341
FT /note="Transferrin-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DOMAIN 354..686
FT /note="Transferrin-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT REGION 341..350
FT /note="Connecting region"
FT /evidence="ECO:0000250"
FT BINDING 80
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 112
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
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 141
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 143
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 212
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 268
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 404
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 443
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 468
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 472
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 474
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
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 539
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 607
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 30..65
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 40..56
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 135..218
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 180..193
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 246..260
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 357..389
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 367..380
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 414..698
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 432..659
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 466..545
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 490..687
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 500..514
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 511..528
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 585..599
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
SQ SEQUENCE 703 AA; 77317 MW; FDFC00F02E808B8D CRC64;
MDLSLHVALC LGMLALCLAM PPKEKQVRWC AKSKSEFSKC RDLVNTCKNK EITLSCVEKS
STDECLTAIQ NDRADAICVD GGDVYKGSLQ PYNLKPIMAE NYGSHTEPDT CYYAVAVVKK
SSTFTFDELR DKRSCHTGIG KTAGWNVIIG LLLEKQLLKW EGPDTESLEK AVSKFFKASC
VPGAKEPKLC QQCAGKKEHK CARSNNEPYY NYAGAFKCLQ DDKGDVAFVK HSTVPEELHK
DYELLCPDNT RKPISDYKNC NLAKVPAHSV LARARDDKSK DIIAFLQEAQ KTKECKLFSS
QHGKDLLFKD TAVSLVPLPP TIDGFLFLGA VYYQEIHALK EGVKEDDLAA PSKVRWCTQS
KAEKTKCDDW TTISGGSIEC TEAATAEDCI LQILKGDADA VTLDGGYMYT AGQCGLVPVM
GEYYDLDDLT PCQRRSSQAK GVYYAVAIAK KGTKVSWKNL RGVKTCHTAV GRTAGWNIPV
GLITNETNNC DFASYVGESC APGSDVKSNL CKLCIGDPAK PLDSAKKCSP SASEAYHGYS
GAFRCLVEKG DVCFAKHTTV FENTDGKNPA AWAKDLKSDD YELLCPDGSR APINDFKRCN
LAEVPAHSVV TLPGKRKPVV EILVNQQSLY GRKGFQKDIF QMFQSKDGKD LLFKDSTQCL
LEISEKTTMQ EFLGDKYYTA VTSLNKCSNT KSGLLSSCTF HSC
