TRFEB_XENLA
ID TRFEB_XENLA Reviewed; 701 AA.
AC Q6PGT3; Q7ZTQ7;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Serotransferrin-B;
DE Flags: Precursor;
GN Name=tf-b;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2003) 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH43632.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC043632; AAH43632.1; ALT_INIT; mRNA.
DR EMBL; BC056840; AAH56840.1; -; mRNA.
DR RefSeq; NP_001083070.1; NM_001089601.1.
DR AlphaFoldDB; Q6PGT3; -.
DR SMR; Q6PGT3; -.
DR MEROPS; S60.970; -.
DR PRIDE; Q6PGT3; -.
DR DNASU; 398723; -.
DR GeneID; 398723; -.
DR KEGG; xla:398723; -.
DR CTD; 398723; -.
DR Xenbase; XB-GENE-865383; tf.L.
DR OrthoDB; 232859at2759; -.
DR Proteomes; UP000186698; Chromosome 5L.
DR Bgee; 398723; Expressed in liver and 16 other tissues.
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; 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..701
FT /note="Serotransferrin-B"
FT /id="PRO_0000305241"
FT DOMAIN 26..338
FT /note="Transferrin-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DOMAIN 352..684
FT /note="Transferrin-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT REGION 338..348
FT /note="Connecting region"
FT /evidence="ECO:0000250"
FT BINDING 79
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 111
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
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 140
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 143
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 267
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 402
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 441
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 466
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 470
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 473
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 537
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 605
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 29..64
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 39..55
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 134..217
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 179..192
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 245..259
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 355..387
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 365..378
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 412..696
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 430..657
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 464..543
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 488..685
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 498..512
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 509..526
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 583..597
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
SQ SEQUENCE 701 AA; 76857 MW; 5533B32DDF05B33F CRC64;
MDLALRVALC LSMLALCLAM PKEKQVRWCV KSKSELNKCR DLVNTCKNKE ITLSCVEKPN
TDECLTAIQE DRADAICVDG GDVYKGSLQP YNLKPIMAEN YGSQTETDTC YYAVAVVKKS
STFTFDELKD KRSCHTGIGK TAGWNIIIGL LLEKKLLSWG GPDTESLEKA VSRFFKASCV
PGAKEPNLCQ QCAGKKEHKC SRSNNEPYYN YAGAFKCLQD DKGDVAFVKQ STVPEAFHKD
YELLCPDNTR KPIKDYKKCN LAKVPAHAVL TRSRDDKTKD IIAFLQEAQK ECKLFSSQYG
KDLIFKNSAV SLIPLPPSMD GFLFLGADYS NAIQALKEGV KEDEVPAAET KVRWCTQSKA
EKNKCDDWTT ISGGAIECTE AASAEDCIVQ ILKGDADAVT LDGGYMYTAG QCGLVPVMGE
YYDQDDLTPC QRRSSGTKGV YYAVAIAKKG TKVSWSNLRG VKTCHTAVGR TAGWNIPVGL
ITNETKNCDF ASYVGQSCAP GSDVKSKLCA LCIGDPEKRL ESSKKCSPSA SEAYYGYSGA
FRCLVEKGQV AFAKHTTVFE NTDGKNPAGW AKDLKSGDFE LLCPDGSRAP VTDYKSCNLA
EVPAHAVVTL PEKRTFVAEI VVNQQSLYGR KGFQKDIFQM FESTGGKDLL FKDSTQCLLE
IPKKTTMQEF LGDKYHTAVT SLNKCSTTKS GLLASCTFHS C
