TRFEA_XENLA
ID TRFEA_XENLA Reviewed; 702 AA.
AC P20233; Q7SYA2;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 3.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Serotransferrin-A;
DE Flags: Precursor;
GN Name=tf-a; Synonyms=tf;
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 [MRNA].
RC TISSUE=Liver;
RX PubMed=2235503; DOI=10.1093/nar/18.20.6135;
RA Moskaitis J.E., Pastori R.L., Schoenberg D.R.;
RT "The nucleotide sequence of Xenopus laevis transferrin mRNA.";
RL Nucleic Acids Res. 18:6135-6135(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Tadpole;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUL-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=AAH54950.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA38396.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X54530; CAA38396.1; ALT_FRAME; mRNA.
DR EMBL; BC054950; AAH54950.1; ALT_FRAME; mRNA.
DR PIR; S12100; S12100.
DR RefSeq; NP_001079812.1; NM_001086343.1.
DR AlphaFoldDB; P20233; -.
DR SMR; P20233; -.
DR MEROPS; S60.970; -.
DR PRIDE; P20233; -.
DR DNASU; 379502; -.
DR GeneID; 379502; -.
DR KEGG; xla:379502; -.
DR CTD; 379502; -.
DR Xenbase; XB-GENE-6255495; tf.S.
DR OrthoDB; 232859at2759; -.
DR Proteomes; UP000186698; Chromosome 5S.
DR Bgee; 379502; 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..702
FT /note="Serotransferrin-A"
FT /id="PRO_0000035720"
FT DOMAIN 26..340
FT /note="Transferrin-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DOMAIN 353..685
FT /note="Transferrin-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT REGION 340..349
FT /note="Connecting region"
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 403
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 442
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 467
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 471
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 474
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 538
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 606
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 356..388
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 366..379
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 413..697
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 431..658
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 465..544
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 489..686
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 499..513
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 510..527
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 584..598
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT CONFLICT 3
FT /note="L -> F (in Ref. 1; CAA38396)"
FT /evidence="ECO:0000305"
FT CONFLICT 154
FT /note="K -> R (in Ref. 1; CAA38396)"
FT /evidence="ECO:0000305"
FT CONFLICT 167..169
FT /note="LEK -> WRN (in Ref. 1; CAA38396)"
FT /evidence="ECO:0000305"
FT CONFLICT 189
FT /note="C -> S (in Ref. 1; CAA38396)"
FT /evidence="ECO:0000305"
FT CONFLICT 273
FT /note="V -> G (in Ref. 1; CAA38396)"
FT /evidence="ECO:0000305"
FT CONFLICT 301..303
FT /note="YGK -> VWGR (in Ref. 1; CAA38396)"
FT /evidence="ECO:0000305"
FT CONFLICT 435
FT /note="S -> C (in Ref. 1; CAA38396)"
FT /evidence="ECO:0000305"
FT CONFLICT 487
FT /note="G -> A (in Ref. 1; CAA38396)"
FT /evidence="ECO:0000305"
FT CONFLICT 523..524
FT /note="SA -> RE (in Ref. 1; CAA38396)"
FT /evidence="ECO:0000305"
FT CONFLICT 597
FT /note="K -> R (in Ref. 1; CAA38396)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 702 AA; 76948 MW; F94EB75AB3C8EC74 CRC64;
MDLSLRVALC LSMLALCLAI QKEKQVRWCV KSNSELKKCK DLVDTCKNKE IKLSCVEKSN
TDECFTAIQE DHADAICVDG GDVYKGSLQP YNLKPIMAEN YGSHTETDTC YYAVAVVKKS
SKFTFDELKD KKSCHTGIGK TAGWNIIIGL LLEKKLLKWA GPDSETLEKA VSKFFKASCV
PGAKEPKLCQ LCAGIKEHKC SRSNNEPYYN YAGAFKCLQD DQGDVAFVKQ STVPEEFHKD
YELLCPDNTR KSIKEYKNCN LAKVPAHAVL TRVRDDKSKD IIEFLQEAQK TQECKLFSSP
YGKDLIFKDS AVSLIPLPSS MDSFLFLGAD YSNAIQALKE GVKEDDSAAQ VKVRWCTQSK
AEKTKCDDWT TISGGAIECT EASTAEECIV QILKGDADAV TLDGGYMYTA GLCGLVPVMG
EYYDQDDLTP CQRSSSQAKG VYYAVAIVKK GTQVSWSNLR GVKTCHTAVG RTAGWNIPVG
LITSETGNCD FASYVGESCA PGSDVKSNLC ALCIGDPEKL SESAKKCSPS ASEAYYGYSG
AFRCLVEKGQ VGFAKHTTVF ENTDGKNPAG WAKDLKSEDF ELLCPDGSRA PVTDYKKCNL
AEVPAHAVVT LPDKREQVAK IVVNQQSLYG RKGFQKDIFQ MFQSTGGKDL LFKDSTQCLL
EIPSKTTMQE FLGDKYHTAV TSLNKCSTSK SGLLAACTFH SC
